GLUCOSAMINE A M EDICAL D ICTIONARY , B IBLIOGRAPHY , AND A NNOTATED R ESEARCH G UIDE TO I NTERNET R EFERENCES
J AMES N. P ARKER , M.D. AND P HILIP M. P ARKER , P H .D., E DITORS
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ICON Health Publications ICON Group International, Inc. 4370 La Jolla Village Drive, 4th Floor San Diego, CA 92122 USA Copyright ©2004 by ICON Group International, Inc. Copyright ©2004 by ICON Group International, Inc. All rights reserved. This book is protected by copyright. No part of it may be reproduced, stored in a retrieval system, or transmitted in any form or by any means, electronic, mechanical, photocopying, recording, or otherwise, without written permission from the publisher. Printed in the United States of America. Last digit indicates print number: 10 9 8 7 6 4 5 3 2 1
Publisher, Health Care: Philip Parker, Ph.D. Editor(s): James Parker, M.D., Philip Parker, Ph.D. Publisher's note: The ideas, procedures, and suggestions contained in this book are not intended for the diagnosis or treatment of a health problem. As new medical or scientific information becomes available from academic and clinical research, recommended treatments and drug therapies may undergo changes. The authors, editors, and publisher have attempted to make the information in this book up to date and accurate in accord with accepted standards at the time of publication. The authors, editors, and publisher are not responsible for errors or omissions or for consequences from application of the book, and make no warranty, expressed or implied, in regard to the contents of this book. Any practice described in this book should be applied by the reader in accordance with professional standards of care used in regard to the unique circumstances that may apply in each situation. The reader is advised to always check product information (package inserts) for changes and new information regarding dosage and contraindications before prescribing any drug or pharmacological product. Caution is especially urged when using new or infrequently ordered drugs, herbal remedies, vitamins and supplements, alternative therapies, complementary therapies and medicines, and integrative medical treatments. Cataloging-in-Publication Data Parker, James N., 1961Parker, Philip M., 1960Glucosamine: A Medical Dictionary, Bibliography, and Annotated Research Guide to Internet References / James N. Parker and Philip M. Parker, editors p. cm. Includes bibliographical references, glossary, and index. ISBN: 0-597-83961-1 1. Glucosamine-Popular works. I. Title.
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Disclaimer This publication is not intended to be used for the diagnosis or treatment of a health problem. It is sold with the understanding that the publisher, editors, and authors are not engaging in the rendering of medical, psychological, financial, legal, or other professional services. References to any entity, product, service, or source of information that may be contained in this publication should not be considered an endorsement, either direct or implied, by the publisher, editors, or authors. ICON Group International, Inc., the editors, and the authors are not responsible for the content of any Web pages or publications referenced in this publication.
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Acknowledgements The collective knowledge generated from academic and applied research summarized in various references has been critical in the creation of this book which is best viewed as a comprehensive compilation and collection of information prepared by various official agencies which produce publications on glucosamine. Books in this series draw from various agencies and institutions associated with the United States Department of Health and Human Services, and in particular, the Office of the Secretary of Health and Human Services (OS), the Administration for Children and Families (ACF), the Administration on Aging (AOA), the Agency for Healthcare Research and Quality (AHRQ), the Agency for Toxic Substances and Disease Registry (ATSDR), the Centers for Disease Control and Prevention (CDC), the Food and Drug Administration (FDA), the Healthcare Financing Administration (HCFA), the Health Resources and Services Administration (HRSA), the Indian Health Service (IHS), the institutions of the National Institutes of Health (NIH), the Program Support Center (PSC), and the Substance Abuse and Mental Health Services Administration (SAMHSA). In addition to these sources, information gathered from the National Library of Medicine, the United States Patent Office, the European Union, and their related organizations has been invaluable in the creation of this book. Some of the work represented was financially supported by the Research and Development Committee at INSEAD. This support is gratefully acknowledged. Finally, special thanks are owed to Tiffany Freeman for her excellent editorial support.
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About the Editors James N. Parker, M.D. Dr. James N. Parker received his Bachelor of Science degree in Psychobiology from the University of California, Riverside and his M.D. from the University of California, San Diego. In addition to authoring numerous research publications, he has lectured at various academic institutions. Dr. Parker is the medical editor for health books by ICON Health Publications. Philip M. Parker, Ph.D. Philip M. Parker is the Eli Lilly Chair Professor of Innovation, Business and Society at INSEAD (Fontainebleau, France and Singapore). Dr. Parker has also been Professor at the University of California, San Diego and has taught courses at Harvard University, the Hong Kong University of Science and Technology, the Massachusetts Institute of Technology, Stanford University, and UCLA. Dr. Parker is the associate editor for ICON Health Publications.
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About ICON Health Publications To discover more about ICON Health Publications, simply check with your preferred online booksellers, including Barnes&Noble.com and Amazon.com which currently carry all of our titles. Or, feel free to contact us directly for bulk purchases or institutional discounts: ICON Group International, Inc. 4370 La Jolla Village Drive, Fourth Floor San Diego, CA 92122 USA Fax: 858-546-4341 Web site: www.icongrouponline.com/health
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Table of Contents FORWARD .......................................................................................................................................... 1 CHAPTER 1. STUDIES ON GLUCOSAMINE.......................................................................................... 3 Overview........................................................................................................................................ 3 The Combined Health Information Database................................................................................. 3 Federally Funded Research on Glucosamine.................................................................................. 5 E-Journals: PubMed Central ....................................................................................................... 28 The National Library of Medicine: PubMed ................................................................................ 31 CHAPTER 2. NUTRITION AND GLUCOSAMINE ................................................................................ 73 Overview...................................................................................................................................... 73 Finding Nutrition Studies on Glucosamine ................................................................................ 73 Federal Resources on Nutrition ................................................................................................... 78 Additional Web Resources ........................................................................................................... 78 CHAPTER 3. ALTERNATIVE MEDICINE AND GLUCOSAMINE ......................................................... 81 Overview...................................................................................................................................... 81 The Combined Health Information Database............................................................................... 81 National Center for Complementary and Alternative Medicine.................................................. 82 Additional Web Resources ........................................................................................................... 90 General References ....................................................................................................................... 93 CHAPTER 4. DISSERTATIONS ON GLUCOSAMINE ........................................................................... 95 Overview...................................................................................................................................... 95 Dissertations on Glucosamine ..................................................................................................... 95 Keeping Current .......................................................................................................................... 95 CHAPTER 5. CLINICAL TRIALS AND GLUCOSAMINE ...................................................................... 97 Overview...................................................................................................................................... 97 Recent Trials on Glucosamine ..................................................................................................... 97 Keeping Current on Clinical Trials ............................................................................................. 99 CHAPTER 6. PATENTS ON GLUCOSAMINE .................................................................................... 101 Overview.................................................................................................................................... 101 Patents on Glucosamine............................................................................................................. 101 Patent Applications on Glucosamine......................................................................................... 126 Keeping Current ........................................................................................................................ 153 CHAPTER 7. BOOKS ON GLUCOSAMINE ........................................................................................ 155 Overview.................................................................................................................................... 155 Book Summaries: Federal Agencies............................................................................................ 155 Book Summaries: Online Booksellers......................................................................................... 156 Chapters on Glucosamine .......................................................................................................... 156 CHAPTER 8. PERIODICALS AND NEWS ON GLUCOSAMINE .......................................................... 159 Overview.................................................................................................................................... 159 News Services and Press Releases.............................................................................................. 159 Newsletters on Glucosamine...................................................................................................... 161 Newsletter Articles .................................................................................................................... 162 Academic Periodicals covering Glucosamine ............................................................................. 163 APPENDIX A. PHYSICIAN RESOURCES .......................................................................................... 167 Overview.................................................................................................................................... 167 NIH Guidelines.......................................................................................................................... 167 NIH Databases........................................................................................................................... 169 Other Commercial Databases..................................................................................................... 172 The Genome Project and Glucosamine....................................................................................... 172 APPENDIX B. PATIENT RESOURCES ............................................................................................... 177 Overview.................................................................................................................................... 177 Patient Guideline Sources.......................................................................................................... 177
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Finding Associations.................................................................................................................. 180 APPENDIX C. FINDING MEDICAL LIBRARIES ................................................................................ 183 Overview.................................................................................................................................... 183 Preparation................................................................................................................................. 183 Finding a Local Medical Library................................................................................................ 183 Medical Libraries in the U.S. and Canada ................................................................................. 183 ONLINE GLOSSARIES................................................................................................................ 189 Online Dictionary Directories ................................................................................................... 189 GLUCOSAMINE DICTIONARY................................................................................................ 191 INDEX .............................................................................................................................................. 271
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FORWARD In March 2001, the National Institutes of Health issued the following warning: "The number of Web sites offering health-related resources grows every day. Many sites provide valuable information, while others may have information that is unreliable or misleading."1 Furthermore, because of the rapid increase in Internet-based information, many hours can be wasted searching, selecting, and printing. Since only the smallest fraction of information dealing with glucosamine is indexed in search engines, such as www.google.com or others, a non-systematic approach to Internet research can be not only time consuming, but also incomplete. This book was created for medical professionals, students, and members of the general public who want to know as much as possible about glucosamine, using the most advanced research tools available and spending the least amount of time doing so. In addition to offering a structured and comprehensive bibliography, the pages that follow will tell you where and how to find reliable information covering virtually all topics related to glucosamine, from the essentials to the most advanced areas of research. Public, academic, government, and peer-reviewed research studies are emphasized. Various abstracts are reproduced to give you some of the latest official information available to date on glucosamine. Abundant guidance is given on how to obtain free-of-charge primary research results via the Internet. While this book focuses on the field of medicine, when some sources provide access to non-medical information relating to glucosamine, these are noted in the text. E-book and electronic versions of this book are fully interactive with each of the Internet sites mentioned (clicking on a hyperlink automatically opens your browser to the site indicated). If you are using the hard copy version of this book, you can access a cited Web site by typing the provided Web address directly into your Internet browser. You may find it useful to refer to synonyms or related terms when accessing these Internet databases. NOTE: At the time of publication, the Web addresses were functional. However, some links may fail due to URL address changes, which is a common occurrence on the Internet. For readers unfamiliar with the Internet, detailed instructions are offered on how to access electronic resources. For readers unfamiliar with medical terminology, a comprehensive glossary is provided. For readers without access to Internet resources, a directory of medical libraries, that have or can locate references cited here, is given. We hope these resources will prove useful to the widest possible audience seeking information on glucosamine. The Editors
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From the NIH, National Cancer Institute (NCI): http://www.cancer.gov/cancerinfo/ten-things-to-know.
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CHAPTER 1. STUDIES ON GLUCOSAMINE Overview In this chapter, we will show you how to locate peer-reviewed references and studies on glucosamine.
The Combined Health Information Database The Combined Health Information Database summarizes studies across numerous federal agencies. To limit your investigation to research studies and glucosamine, you will need to use the advanced search options. First, go to http://chid.nih.gov/index.html. From there, select the “Detailed Search” option (or go directly to that page with the following hyperlink: http://chid.nih.gov/detail/detail.html). The trick in extracting studies is found in the drop boxes at the bottom of the search page where “You may refine your search by.” Select the dates and language you prefer, and the format option “Journal Article.” At the top of the search form, select the number of records you would like to see (we recommend 100) and check the box to display “whole records.” We recommend that you type “glucosamine” (or synonyms) into the “For these words:” box. Consider using the option “anywhere in record” to make your search as broad as possible. If you want to limit the search to only a particular field, such as the title of the journal, then select this option in the “Search in these fields” drop box. The following is what you can expect from this type of search: •
Determining the Efficacy of Glucosamine and Chondroitin for Osteoarthritis Source: Nurse Practitioner, The. 26(6): 44-46,49-52. June 2001. Summary: This journal article provides health professionals with information on the use of glucosamine and chondroitin in the treatment of osteoarthritis (OA). Although OA was once regarded as a simple consequence of aging and cartilage degeneration, researchers now believe that OA may be a group of overlapping diseases rather than a single disorder. The functional properties of articular cartilage are the core of OA pathogenesis. Components of articular cartilage are water, collagen, proteoglycans, chondrocytes, and other matrix components. Over time, the catabolism of proteoglycans and the increased loss of glycosaminoglycans result in the abrasion of cartilage and the formation of new bone within the joint. In healthy people, a balance of cartilage matrix turnover is maintained through synthesis and degradation. The failure to maintain this
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homeostatic balance because of reduced formation or increased catabolism is a possible explanation for OA. Treatment modalities focus on primary and secondary prevention. Primary prevention involves educating patients about joint protection, exercise, weight reduction, and the dangers of repetitive motion. Secondary prevention is mainly palliative and involves both nonpharmacologic and pharmacologic therapies to minimize pain. Glucosamine sulfate and chondroitin sulfate are being used by many patients for the treatment of OA. The article reviews human and animal studies on the use of these agents in treating OA. Despite findings in many of these studies supporting the efficacy of these agents for palliation of joint pain in patients with OA, the American College of Rheumatology Subcommittee on OA believes that it is too early to issue recommendations for use. Currently, the National Institute for Arthritis and Musculoskeletal and Skin Diseases, in collaboration with the National Center for Complementary and Alternative Medicine has begun a pivotal study to thoroughly evaluate these agents. 36 references. (AA-M). •
Glucosamine and Osteoarthritis Source: Nurse Practitioner. 25(9): 96-97. September 2000. Summary: This journal article provides nurses with information on the use of glucosamine to manage osteoarthritis. Current osteoarthritis treatment is largely palliative. Nonpharmacologic methods include weight loss and exercise. Pharmacologic options include acetaminophen, nonsteroidal antiinflammatory drugs, steroid injections, and surgery. In recent years, glucosamine, a nutritional supplement, has received much publicity as a treatment for osteoarthritis. Glucosamine is present as a natural compound in most human tissue. In vitro, it has been shown to stimulate the production of proteoglycans, which promote the building of cartilage. Although no rigorous long term studies have been conducted to evaluate the therapeutic benefits or adverse effects of glucosamine in patients with osteoarthritis, several clinical trials have demonstrated its efficacy in relieving pain and increasing movement. Glucosamine is classified as a dietary supplement and, as such, is not subject to Food and Drug Administration approval. Therefore, product purity may be questionable. 13 references.
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Glucosamine and Chondroitin Source: Arthritis Today. 12(5): 46-48,51. September-October 1998. Summary: This journal article provides people who have arthritis with information on the dietary supplements glucosamine and chondroitin. Both glucosamine and chondroitin are substances found in the body and needed in the metabolism of cartilage. The supplements have been lauded as cures for osteoarthritis (OA). There is increasing evidence that they actually relieve the pain of OA in some people. Results from more than a dozen European studies on humans reveal that about half of the participants with mild to moderate OA who took either of the supplements reported some pain relief. Although more research is needed, there is even some evidence that the supplements may slow down loss of cartilage. Despite this evidence, most researchers and doctors, even those who are using the supplements themselves, are wary of the hype and commercialism surrounding them. There is no quality control of glucosamine and chondroitin products because they are sold as dietary supplements and are therefore not regulated by the Food and Drug Administration. Only long-term, scientifically controlled studies will prove the effectiveness and safety of these supplements. People who decide to try them should consult their doctor first, continue to take their prescription medications unless their doctor tells them to stop, be sure that OA is the cause of their pain, avoid the supplements if they are pregnant or could become
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pregnant, check their blood sugar levels frequently if they have diabetes, check their blood-clotting time frequently if they are taking a blood-thinning medication or daily aspirin and chondroitin, and continue proven pain management techniques.
Federally Funded Research on Glucosamine The U.S. Government supports a variety of research studies relating to glucosamine. These studies are tracked by the Office of Extramural Research at the National Institutes of Health.2 CRISP (Computerized Retrieval of Information on Scientific Projects) is a searchable database of federally funded biomedical research projects conducted at universities, hospitals, and other institutions. Search the CRISP Web site at http://crisp.cit.nih.gov/crisp/crisp_query.generate_screen. You will have the option to perform targeted searches by various criteria, including geography, date, and topics related to glucosamine. For most of the studies, the agencies reporting into CRISP provide summaries or abstracts. As opposed to clinical trial research using patients, many federally funded studies use animals or simulated models to explore glucosamine. The following is typical of the type of information found when searching the CRISP database for glucosamine: •
Project Title: ALLOSTERIC CONFORMATIONAL CHANGE OF GLUCOSAMINE 6 PHOSPHATE DEAMINASE Principal Investigator & Institution: Horjales, Eduardo; Stanford University Stanford, Ca 94305 Timing: Fiscal Year 2001 Summary: GlcN6P deaminase is an allosteric enzyme and kinetic evidence shows that it undergoes a concerted allosteric transition. The current knowledge about the kinetics of this enzyme and its easy expression and purification indicate that GlcN6P deaminase may be a useful system for the study of allosteric transitions. A main interest in these results derives from enhancing the resolution to be able to determine the conformation of a particular motif of 30 aminoacids linking the allosteric and the active sites. The conformation of this structural part seems to be responsible for the activation of the enzyme and resulted partially disordered in the present structure. SR should provide information on the conformation of this motif which can be essential for the understanding of the allosteric mechanism of this enzyme. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen
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Project Title: BIOBEHAVIORAL RESEARCH CENTER(BRC) Principal Investigator & Institution: Yucha, Carolyn B.; Professor and Associate Dean for Researc; Adult and Elderly Nursing; University of Florida Gainesville, Fl 32611 Timing: Fiscal Year 2001; Project Start 01-AUG-2001; Project End 31-JUL-2004 Summary: (from applicant's Abstract) The goal of the Biobehavioral Research Center (BRC) in the University of Florida College of Nursing is to provide the infrastructure for
2 Healthcare projects are funded by the National Institutes of Health (NIH), Substance Abuse and Mental Health Services (SAMHSA), Health Resources and Services Administration (HRSA), Food and Drug Administration (FDA), Centers for Disease Control and Prevention (CDCP), Agency for Healthcare Research and Quality (AHRQ), and Office of Assistant Secretary of Health (OASH).
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faculty to develop state-of-the-art interdisciplinary research that integrates biological and behavioral sciences. The long-term goal of the BRC is to advance our understanding of biobehavioral aspects of health promotion, disease prevention, and nursing interventions for acute and chronic illness across the lifespan. The specific aims of the BRC are: (1) Develop a cadre of nurse scientists with expertise in the integration of biological and behavioral sciences, (2) Develop programs of Biobehavioral research that promote health, prevent disease and improve nursing care, and, (3) Disseminate research findings that interpret biological and behavioral sciences to impact nursing care. These aims will be supported by the Administrative and Pilot Cores, which will work together to provide fiscal oversight; allocation of shared resources including space, equipment and statistical consultation; provision of educational programs and mentoring opportunities, and, patient safety oversight. Five biobehavioral pilot studies are proposed: (1) GlutenFree & Casein-Free Dietary Treatment in Autism, (2) Exercise, Bone Density & Balance in Postmenopausal Women, (3) Effect of Immune Mediators on Quality of Life in Allergy, (4) Promoting Adherence: Theory-based Asthma Education, and (5) Managing OA Symptoms: Glucosamine and Chondroitin Sulfate. The CON is positioned to rapidly expand its research mission and profile. The BRC will facilitate this growth by augmenting the current research support infrastructure and enhancing the development of interdisciplinary collaboration in the Health Science Center and the University at large. The BRC is supported by the extensive resources and environment at the University of Florida and by substantial financial support provided by the University and the College of Nursing. At the end of three years, at least twelve nurse scientists with expertise in biobehavioral research will be developed, and a minimum of ten pilot studies will be funded, half of which will develop into programs of biobehavioral research leading to greater extramural funding. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: BIOCHEMISTRY AND MOLECULAR GENETICS OF MITOMYCIN BIOSYNT Principal Investigator & Institution: Sherman, David H.; Research Associate; Biotechnology Institute; University of Minnesota Twin Cities 200 Oak Street Se Minneapolis, Mn 554552070 Timing: Fiscal Year 2001; Project Start 01-JAN-2000; Project End 31-DEC-2003 Summary: The overall aim of the proposed research is to understand the molecular mechanisms controlling the biosynthesis of and cellular resistance to the antitumor antibiotic, mitomycin C. This important chemotherapeutic agent is biosynthetically derived from a shikimate pathway metabolite (3-amino-5-hydroxybenzoic acid) and Dglucosamine. In this work, molecular genetic, biochemical and chemical approaches will be used to obtain information on the functional role of the set of genes and enzymes involved in constructing this important anticancer drug. Our initial work demonstrated that Streptomyces lavendulae (the mitomycin producer) had at least two genetic loci (mcr and mrd) that specify resistance to mitomycin. Identification of cosmid clones containing DNA adjacent to the resistance genes revealed that mitomycin biosynthetic genes are clustered around the mitomycin resistance determinant (mrd). Using probes for shikimate pathway genes, homologs to the dehydroquinase, dehydroquinate synthase, 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) synthase and 3amino-5-hydroxybenzoic acid synthase (AHBAS) were identified among a total of 47 genes within the 55 kb cluster. With this information in hand, gene disruption/replacement, mutant complementation, and biochemical experiments will be performed to probe the precise function of the individual mitomycin biosynthetic
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enzymes. This information will be used to identify and characterize the mechanism and specificity of the enzyme(s) responsible for coupling the AHBA precursor to the Dglucosamine sugar moiety. Subsequently, studies will be initiated to understand and manipulate enzymes involved in establishing the core mitosane structure and the specificity of tailoring enzymes that provide molecular diversity to this significant class of metabolites. Concurrently, our work will continue on the resistance mechanisms that provide cellular self-protection against mitomycins in the producing organism. Overall, this work will provide an important theoretical and experimental base for future combinatorial biology-based production of novel AHBA-derived natural products using molecular genetic technology. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: BIOSYNTHESIS OF MEMBRANE GLYCOLIPIDS IN RHIZOBIUM Principal Investigator & Institution: Raetz, Christian R.; Professor & Chairman; Biochemistry; Duke University Durham, Nc 27706 Timing: Fiscal Year 2001; Project Start 01-JUL-1995; Project End 30-JUN-2004 Summary: Lipopolysaccharides (LPSs) are remarkable glycolipids that comprise the outer surfaces of Gram-negative bacteria, including the symbiotic organism, Rhizobium leguminosarum. In Escherichia coli, the lipid A anchor of LPS is a hexa-acylated disaccharide of glucosamine, bearing phosphate moieties at positions 1 and 4'. The minimal LPS required for a growth of E.coli consists of lipid A and two extra sugars. Emerging genomic sequences indicate that the enzymes that make lipid A in E. coli are present in most other Gram-negative bacteria. Lipid A (often termed endotoxin) is also the active component of LPS responsible for the clinical complications of Gram-negative sepsis. Minor modifications in the structure of lipid A can have profound effects on pathogenesis. Some lipid A analogs are actually potent endotoxin antagonists. Compared to E. coli, the chemical structures of the lipid A and core domains of R. leguminosarum LPS are very unusual. R. leguminosarum lipid A lacks the and 4'phosphates, but is modified with galacturonic acid at position 4'. It is acylated with a peculiar 28 carbon fatty acid, and contains 2-deoxy-2-aminogluconate in place of the proximal glucosamine. The structure of R. leguminosarum LPS indicates the existence of novel enzymes for generating diverse lipid A and core species. It is now established that the first seven enzymes of lipid A biosynthesis are in fact the same in E. coli and R. leguminosarum. The differences arise in the later stages of the pathway. To date, enzymes identified as unique to R. leguminosarum include a 4'-phosphatase that is also a phosphotransferase, a 1-phosphatase, a long chain acyltransferase with its own acyl carrier protein, and three distinct core glycosyltransferases. Characterization of the R. leguminosarum system should provide insights into the function of lipid A-like molecules, including special roles during symbiosis in plants, and affords the opportunity to create novel lipid A hybrids that may have interesting adjuvant or antagonist activities. Some structural features of R. leguminosarum lipid A are seen in human pathogens. Legionella pneumophila lipid A contains a C28 chain, while Porphyromonas gingivalis and Helicobacter pylori lipid A lack the 4' phosphate. In the coming grant period, the specific aims are: I) cloning of the C28 acyltransferase of R. leguminosarum; II) analysis of the lipid A 4'-phosphatase/phosphotransferase, especially its ability to synthesize PtdIns-4-P; III) determination of the enzymatic basis for proximal unit diversity in R. leguminosarum lipid A; and IV) characterization of enzymes that incorporate the unique inner core sugars of R. leguminosarum LPS. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen
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Project Title: C-C AND C-N BOND FORMATION IN UNUSUAL SUGAR BIOSYNTHESES Principal Investigator & Institution: Liu, Hung-Wen; George H. Hitchings Regents Chair and Pr; Medicinal Chemistry; University of Texas Austin 101 E. 27Th/Po Box 7726 Austin, Tx 78712 Timing: Fiscal Year 2001; Project Start 01-JUL-1996; Project End 30-JUN-2003 Summary: This abstract is not available. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen
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Project Title: CHITIN BIOSYNTHESIS AND THE MOSQUITO PERITROPHIC MATRIX Principal Investigator & Institution: Christensen, Bruce M.; Professor; Animal Hlth & Biomedical Scis; University of Wisconsin Madison 750 University Ave Madison, Wi 53706 Timing: Fiscal Year 2003; Project Start 01-JAN-1999; Project End 31-JAN-2008 Summary: (provided by the applicant): The resurgence of mosquito-borne diseases places a growing importance on research that will better delineate mechanisms influencing vector competence. Following ingestion with a blood meal, all mosquitoborne pathogens must survive the midgut environment and traverse the peritrophic matrix (PM) and midgut epithelium to reach specific tissues required for development and/or transmission; therefore the PM serves as a barrier that must be circumvented if a pathogen is to be successfully transmitted. The PM is a proteoglycan matrix composed of chitin, proteins and glycoproteins that is produced by the midgut and serves to separate the blood bolus from the midgut epithelium. The focus of this research proposal is aimed at increasing our understanding of midgut chitin biosynthesis required for PM formation in the mosquito, Aedes aegypti. During the previous period of support, studies were initiated on three key enzymes to verify their involvement in chitin synthesis and to begin an assessment of factors controlling their expression. It now is known that glutamine synthetase (GS), glucosamine: fructose-6-phosphate amidotransferase (GFAT) and chitin synthase (CS) play major roles in chitin synthesis in the midgut. A major hurdle to detailed studies of factors responsible for the blood mealinduced upregulation of expression of these genes in midguts has been the proteaseinduced degradation of nuclear proteins during extraction. During the initial period of support, experimental protocols were developed to alleviate this problem; consequently, electrophoretic mobility shift assays (EMSA) now have identified several important cisacting elements and putative trans-acting factors that bind those elements and selectively control GS expression in midgut tissues. However, It still is not known how chitin is trafficked from the cytoplasm of midgut cells to the extracellular space of the midgut lumen where PM formation occurs. Likewise, three additional enzymes, glucosamine-6-phosphate N-acetyltransferase (GNAT), phosphoacetyl glucosamine mutase (AGM), and uridine diphosphate-N-acetylglucosamine pyrophophrylase (UAP) are also involved in this pathway but have never been cloned or characterized in any insect. In this competing continuation application various microscopical, biochemical and molecular techniques will be used with the mosquito, Ae. aegypti, to extend studies on the chitin biosynthetic pathway by (1) cloning and characterizing the genes encoding GNAT, AGM, and UAP and determining temporal and spatial transcription and translation in midguts following blood feeding, (2) identifying key regulatory elements in the GS, GFAT and CS genes that are responsible for midgut-specific up regulation of expression following a blood meal, (3) performing gene silencing studies, using a
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transducing virus system, to obtain direct evidence of the roles these enzymes play in chitin biosynthesis, and (4) obtaining structure-function information to evaluate how chitin is trafficked out of midgut cells and also mechanistically determining the regulatory function of GFAT in feedback inhibition of chitin synthesis. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: CYTOSOLIC O-GLYCOSYLATION AND INSULIN SIGNALING Principal Investigator & Institution: Hart, Gerald W.; Delamar Professor and Director; Biological Chemistry; Johns Hopkins University 3400 N Charles St Baltimore, Md 21218 Timing: Fiscal Year 2002; Project Start 01-MAY-2002; Project End 30-APR-2005 Summary: (provided by applicant): Compelling data from many laboratories have documented an essential role for glucosamine metabolism in the induction of insulinresistance, the underlying cause of type II diabetes. Signaling via the insulin receptor is mediated by a complex, but fairly well studied signal transduction cascade. We and others have described the dynamic O-GlcNAc modification of a myriad of nucleocytoplasmic proteins and its interplay with phosphate on a number of signaling and regulatory proteins. Hyperglycemia induced insulin-resistance is accompanied by a dramatic increase in O-GlcNAc on many proteins. Strikingly, a specific inhibitor of OGlcNAcase, the enzyme that removes O-GlcNAc from proteins, causes insulin-resistance in the absence of hyperglycemia, providing direct evidence that hyper-O-GlcNAcylation itself is sufficient to disrupt insulin signaling. Given the wealth of knowledge of the insulin signaling pathway, our aims are straight-forward. Aim 1 will systematically determine the site(s) in the insulin signaling pathway which are blocked by hyper-OGlcNAcylation. Points of involvement of O-GlcNAc in insulin signaling will be mapped by functional analysis at each known step in the pathway, and by a non-biased proteomic analysis of insulin-responsive O-GlcNAc modified proteins. Aim 2 will biochemically characterize the structure/function, site occupancy, and relationship to 0phosphate of key insulin-signaling proteins that are already known to be O-GlcNAc modified, including GSK3 beta, IRS-1 & 2, Akt/PKB, and PPAR-gamma-RXR. Aim 3 will systematically study the role of insulin-signaling and hyperglycemia in the regulation of the adipocyte enzymes controlling O-GlcNAc cycling, O-GlcNAc Transferase and O-GlcNAcase. The 3T3-L1 adipocyte insulin-signaling system not only provides a great model to elucidate the functions of O-GlcNAc in insulin signaling, but also these studies will likely provide a new understanding of the molecular mechanisms causing diabetes, and may lead to unexpected avenues for its treatment. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen
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Project Title: ENZYME INTERMEDIATE STRUCTURES BY NMR Principal Investigator & Institution: Evans, Jeremy N.; Professor; Biochemistry and Biophysics; Washington State University 423 Neill Hall Pullman, Wa 99164 Timing: Fiscal Year 2001; Project Start 01-AUG-1991; Project End 31-JUL-2003 Summary: This renewal proposal requests funds to continue our studies ont he structure-function relationships for the enzyme 5-enolpyruvylshikimate-3- phosphate (EPSP) synthase, while developing further a new method for the structural characterization of enzymatic reactions in general by time- resolved solid-state NMR spectroscopy. The project will be extended to include uridine diphosphate N-acetylglucosamine enolpyruvyl transferase (UDP-NAG EPT) and 3-deoxy-D-manno-2octulosonate-8-phosphate (KD08P) synthase. The research program is designed to determine, using nuclear magnetic resonance (NMR) spectroscopy, the structure of the
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enzyme-bound intermediates of three enolpyruvyl transfer enzymes; EPSP synthase; UDP- NAG EPT and KD08P synthase. EPSP synthase catalyzes the condensation of shikimate-3-phosphate and phosphoenolpyruvate, and the product, EPSP, is a key intermediate in the biosynthesis of aromatic amino acids. UDP-NAG EPT is a key enzyme in bacterial cell wall biosynthesis, and KD08P synthase is involved in bacterial lipopolysaccharide biosynthesis. The specific aims of this renewal proposal are to: (1) carry out site-directed mutagenesis studies on specific active site residues of EPSP synthase, (2) carry out time-resolved solid-state REDOR NMR measurements on EPSP synthase, measuring longer distances than was originally proposed in GM43215, and (3) extend this approach to two other enolpyruvyl transferase enzymes, UDP-NAG EPT and KD08P synthase, as time permits. We believe that the consequences of these studies are particularly interesting and exciting, not just for extending our understanding of the structure-function relationship of EPSP synthase and related enolpyruvyl transferase enzymes, but also for developing methodologies that can provide detailed time-resolved structural information on enzymatic reactions in general, which even sophisticated techniques like Laue X-ray diffraction have difficulty obtaining. The long-term goal of our research is to collaborate with a Laue X-ray crystallographer, whose structural information of the protein as whole will be crucial, and generate a "move" of the molecular details of an enzyme in action. This might enable the rational of antibacterial agents in the future. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: FACTORS THAT MODIFY INSULIN ACTION Principal Investigator & Institution: Buse, Maria G.; Professor; Medicine; Medical University of South Carolina 171 Ashley Ave Charleston, Sc 29425 Timing: Fiscal Year 2001; Project Start 01-MAY-1978; Project End 31-MAR-2003 Summary: "Glucose toxicity" accounts for insulin resistance in uncontrolled Type I diabetes (IDDM) and contributes to insulin resistance in Type II diabetes (NIDDM). Sustained hyperglycemia or hyperinsulinemia cause insulin resistance; glucose and insulin act synergistically in down- regulating insulin-stimulated glucose transport. A hypothesis to be tested in 3T3-Ll adipocytes is that glucose/insulin induced glucose transport desensitization reflects altered subcellular trafficking of the glucose transporter, GLUT4, which may involve impaired GLUT4 translocation and inappropriate association of GLUT4 containing vesicles (GCV) with the plasma membrane. Products of the hexosamine synthesis pathway (HNSP) have been implicated in glucose-induced insulin resistance; glutamine-fructose-6-P amidotransferase (GFAT) is the rate limiting enzyme and UDP-N-acetyl glucosamine (UDP-GlcNAc) the major product. The role of HNSP will be tested by examining whether conditions which increase or decrease flux via HNSP augment or mitigate, respectively, glucose induced insulin resistance. O-GlcNAcylation is a reversible process, involving O-glycosylation of proteins on Ser/Thr residues with monosaccharide GlcNAc. It usually involves phosphorylation sites and may be regulatory. Based on preliminary data in muscles of a mouse model of insulin resistance, over-expressing GLUTI in muscle, the hypothesis will be tested that increased flux via HNSP promotes O-GlcNAcylation of critical proteins involved in insulin- stimulated glucose transport. These may include GSV-associated proteins, possibly GLUT4 itself and/or proteins associated with GSV docking and fusion. Since adaptive regulation usually involves multiple sites, we will test the hypothesis that glucose-induced insulin resistance represents in part down-regulation of the insulin receptor (IR) signaling cascade, attempt to identify the major regulatory sites and critically assess the possible
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contribution of HNSP to the glucose effect. If warranted, the involvement of modulators of IR signal transduction, I.E. protein kinase C (PKC) isoforms, and candidate protein tyrosine phosphatases (PTP-ases: PTP-1B, SH-PTP2 and LAR) will be examined. GFAT activity is allosterically regulated by UDP-GlcNAc, and is modulated in vivo in muscle by the hormonal and metabolic milieu. The pre- and post-translational regulation of GFAT expression will be studied in muscles of rodent models. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: FEASIBILITY OSTEOARTHRITIS
OF
INTERNET-BASED
TRIALS
FOR
Principal Investigator & Institution: Mcalindon, Timothy E.; Associate Professor; Medicine; Boston University Medical Campus 715 Albany St, 560 Boston, Ma 02118 Timing: Fiscal Year 2001; Project Start 30-SEP-1999; Project End 31-JAN-2003 Summary: The explosive growth in Internet use during the last few years has made it possible to communicate with greater numbers of people on-line than with any other technology. Recent software advances have made it possible to transmit and collect secure data from remote individuals over the Internet in an efficient and interactive manner. Thus, the internet has become an extraordinarily powerful potential resource for performing questionnaire-based research. One of the most enticing, yet unexplored, medical applications of the Internet is the possibility of performing clinical trials entirely on-line. Because of the vast scope of the Internet, it may be possible to study the attributes of various compounds which might otherwise never be evaluable in traditional clinic- based settings. For example, there exist a number of nutritional compounds which may be modestly effective in relieving osteoarthritis symptoms. Because of the large numbers and prohibitive costs involved in detecting efficacy from these compounds, it is unlikely that they will all be adequately evaluated in traditional clinical trials. The Internet, on the other hand, using validated symptom questionnaires, could have great utility in testing these safe compounds in the treatment of osteoarthritis. On the other hand, we need to learn about many factors which are critical to the feasibility of Internet-based trials, such as response rates, demographic characteristics of respondents, willingness of respondents to participate, validity of responses, protocol compliance, and participant retention. Our aim, therefore, is to evaluate aspects of the feasibility, utility and validity of performing a clinical trial using the Internet, by performing a model on-line trial of a glucosamine/chondroitin sulfate nutritional supplement among individuals with symptomatic knee osteoarthritis. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: FLUORESCENT CHEMOSENSORS FOR CARBOHYDRATES Principal Investigator & Institution: Heagy, Michael D.; Chemistry; New Mexico Inst of Mining & Technology 801 Leroy Pl Socorro, Nm 87801 Timing: Fiscal Year 2002; Project Start 01-SEP-1998; Project End 31-AUG-2005 Summary: (provided by applicant) Because of their potential for nondestructive detection and cell permeability, fluorescent chemosensors for carbohydrates can play a critical role in glycobiology. The objectives of this continuing research program involve the application of molecular clefts as fluorogenic sensors suitable for biological studies of monosaccharides and carbohydrate derivatives. The scope of these investigations build on previous results in which novel signal transduction mechanisms were identified and shown to proceed by substituent changes of the fluorophore component. In an effort to significantly augment the fluorescence signal intensity over conventional
12
Glucosamine
Photoinduced Electron Transfer (PET) fluorescence as well as red-shift this response to longer wavelength emission, new sensors are proposed which utilize Resonance Energy Transfer fluorescence (FRET). This research plan begins by investigating intermolecular energy transfer between two donor/acceptor Forster-pairs. Given the calculated distance of separation (14 Angstroms) for one saccharide complexed between two receptor components, well known donor/acceptor dyes that coincide with this Forster distance such as diethylaminocoumarin and fluorescein are incorporated into the sensor design. Subsequent plans utilize rigid aromatic diimide chromophores as nonfluorescent molecular scaffolds to which recognition groups are appended via benzylimide bonds. Cooperative binding of analyte between receptor sites is expected to decrease torsional motion and enhance energy transfer rates between coupled FRET cassettes. In addition to investigating simple monosaccharides via FRET based sensors, carbohydrate derivatives relevant to glucose metabolism and cell membrane carbohydrates are also targeted for fluorimetric detection. Specifically, glucose-6phosphate and N-acetylneuraminic acid via 2-point bifunctional binding sites from phenylboronic acid and guanidinium receptors. Second messenger myo-Inositoltriphosphate via bis- guanidinium groups and glucosamine sensing through crownether coordination are also included in these fluorometry studies. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: GENETIC SYSTEM TO STUDY VIRULENCE IN BACTEROIDES Principal Investigator & Institution: Malamy, Michael H.; Professor; Molecular Biol & Microbiology; Tufts University Boston Boston, Ma 02111 Timing: Fiscal Year 2003; Project Start 01-JAN-1983; Project End 30-APR-2004 Summary: (provided by applicant): This study will focus on factors that allow the obligate anaerobe B.fragilis, although a component of the normal colonic microbiota, to be a successful pathogen. These include its ability to withstand an aerobic environment (aero-tolerance) during early stages of infection; the presence of systems to import heme into the cell for the heme-dependent pathways of central metabolism and defense against reactive oxygen species; the ability of B.fragilis to remove sialic acid residues from host components, and its virtuosity in obtaining nutrients for growth in vivo from complex oligosaccharides and glycoproteins. Specific aims include: 1, to continue to study factors that allow B.fragilis to withstand prolonged oxygen challenge (aerotolerance): We propose that activities in the B.fragilis periplasm serve as the initial line of defense to combat the formation of reactive oxygen species (ROS), protect sensitive targets from ROS challenges and to reverse ROS damage. In addition we have identified specific functions (superoxide dismutase, SOD), and an extensive gene cluster (the Bat operon) that are required for aerotolerance. We will test the hypothesis that the Bat operon plays an important role in exporting reducing potential from the cytoplasm to the periplasm. 2. Acquisition of iron and heme is important for B.fragilis growth in vitro and in vivo. We will study the process of heme uptake in B.fragilis by the heme permease systems whose genes and functions we have described. We will also continue to study the heme-dependent, and Fe-S cluster-containing enzymes in the dual pathways of central metabolism to establish their roles in aerotolerance and in providing energy during oxygen challenge. 3. to investigate the composition, functions and control of operons for the acquisition of growth substrates from the infected host. We will focus on the operon containing the neuraminidase (nanH1) gene and several other glycohydrolases capable of converting the complex Lewis antigen found on the surface of many human cells to individual monosaccharides. We will continue to define the operon for NANA utilization, the NanL1 operon. Is neuraminidase a virulence factor
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because it supplies NANA for B.fragilis growth, or because its activity alters the surface of host cells during infection, or both? 4.We will develop additional tools to define changes in macromolecular synthesis and stability of DNA, proteins and membranes during 9 oxygen challenge. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: GIARDIA ENCYSTMENT: CONTROL OF GA1NAC SYNTHESIS Principal Investigator & Institution: Jarroll, Edward L.; Pharmaceutical Sciences; Northeastern University 360 Huntington Ave Boston, Ma 02115 Timing: Fiscal Year 2000; Project Start 15-AUG-2000; Project End 14-AUG-2004 Summary: Giardia causes is a major intestinal illness in the United States as well as many other countries worldwide. The life cycle is simple and direct requiring a vegetative trophozoite which attaches to the microvillus brush border of the host's intestine and a cyst which passes from host to host by the fecal-oral route. During cyst formation (encystment) induced by bile, Giardia trophozoites form a protective cyst wall filament rich in the cyst wall specific sugar N-acetylgalactosamine (GalNAC, as a novel [GalNAC beta1 yields 3 GalNAc]n homopolymer). GalNAc, undetected in nonencysting trophozoites, is synthesized from glucose during encystment by the activity of five inducible, nonsedimentable enzymes: Glucosamine 6-phosphate isomerase, GPI, glucosamine 6-phosphate N-acetylase (GlcNPA), phosphoacetylglucosamine mutase (PAG1cNM), UDP-N- acetylglucosamine pyrophosphorylase (UDP-GlcNAcPP), and UDP-N- acetylglucosamine 4' epimerase (UDP-GlcNAcE). The goal of our laboratories is an in-depth study of enzyme regulation for, the molecular biology for the control of, and the possible development of new chemotherapeutic agents that can target this pathway thus acting to prevent the formation of cysts and thus aiding in the control of giardiasis. To date GPI, UDP-GlcNAcPP and CWS have been purified (or partially purified) and characterized, and GPI and UDP-GlcNAcPP have been cloned and sequenced. We have shown also that GPI is transcriptionally regulated while UDP-GlcNAcPP is constitutive but unidirectionally activated toward GalNAc synthesis by glucosamine 6-PO4 the anabolic product of GPI. Before more in depth studies of the regulation of this pathway can be undertaken, it is essential to understand more about the three enzymes which have not yet been purified or characterized. Thus, we plan to use molecular techniques coupled with enzyme analyses to 1) determine whether GlcNPA, PAGlcNM, and UDPGlcNAcE activities are induced at a transcriptional level (as is the case with GPI) or at a post- transcriptional level (as is the case with Giardia's UDP-N- acetylglucosamine pyrophosphorylase), and 2) determine if GlcNPA, PAG1cNM, and UDP-GlcNAcE are regulatory enzymes in the GalNAc synthetic pathway by purifying (or expressing) these enzymes and characterizing them with respect to enzyme kinetics, and possible activators and inhibitors. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen
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Project Title: GLUCOSAMINE DEGRADATION
IN
CARTILAGE
HOMEOSTASIS
AND
Principal Investigator & Institution: Shikhman, Alexander R.; Scripps Research Institute Tpc7 La Jolla, Ca 92037 Timing: Fiscal Year 2001; Project Start 01-JUN-2000; Project End 31-MAY-2005 Summary: Glucosamine represents one of the most commonly used over-the- counter drugs to treat osteoarthritis. However, the molecular mechanisms involved in the realization of its anti-arthritic activities are still poorly understood. Recently, we
14
Glucosamine
discovered that glucosamine (GlcN) and its derivative, N-acetylglucosamine (GlcNAc), express a broad range of anti-inflammatory activities in cultured human articular chondrocytes stimulated with interleukin-1beta (IL-1beta). These activities include inhibition of IL-beta induced nitric oxide (NO) production, IL-6 and COX-2 synthesis. In contrast, GlcNAc does not affect constitutively expressed COX-1 protein. These data have allowed us to generate a working hypothesis proposing that GlcN and its derivatives may beneficially affect the impaired cartilage metabolism in OA, which eventually could result in restoration of extracellular cartilage matrix and chondrocyte homeostasis. Therefore, the goal of the proposed project is to analyze the influence of GlcN and GlcNAc on homeostasis of normal and osteoarthritic human articular chondrocytes and to study the effect of these agents on quantitative and qualitative changes in extracellular matrix glycosaminoglycans. The aims of the study are: 1) to study the effect of GlcN and GlcNAc on production of glycosaminoglycans, including hyaluronic acid, chondroitin-6 sulfate, chondroitin-4 sulfate, dermatan sulfate, and keratan sulfate, in cultured human chondrocytes isolated from normal and osteoarthritic joints; 2) to investigate in vitro chondroprotective effect of GlcNAc on glycosaminoglycan degradation induced by IL-1beta; 3) to study the effect of GlcNAc on the activity of selected lysosomal glycosidases in cultured human articular chondrocytes stimulated with IL-1beta; 4) to correlate the biological activities of GlcN and GlcNAc with the age of chondrocyte donors; 5) to analyze the effect of G1cN and GlcNAc on chondrocyte apoptosis; 6) to examine the effect of G1cN and GlcNAc on TGFbeta and IGF-1 production in cultured human articular chondrocytes. Results of the study will broaden our understanding of the mechanisms of chondroprotection, and will serve as a starting platform for the identification of new molecular targets involved in the pathogenesis of osteoarthritis. The potential practical value of this project is that the obtained experimental data could be used as a basis for the design of a new class of the pharmacological agents capable of preventing or may be even restoring cartilage loss in the joints affected by arthritis. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: GLUCOSAMINE, ATHEROSCLEROSIS
PROTEOGLYCAN
SYNTHESIS
AND
Principal Investigator & Institution: Tannock, Lisa R.; Medicine; University of Washington Seattle, Wa 98195 Timing: Fiscal Year 2001; Project Start 18-JUN-2001; Project End 31-MAY-2003 Summary: (APPLICANT'S ABSTRACT): Glucosamine is a nutritional supplement commonly used for the relief of joint pain. However, it is not subject to FDA regulation and its long-term safety is unknown. Glucosamine is used in the synthesis of glycosaminoglycan chains on proteoglycans. Vascular proteoglycans play a key role in atherogenesis due to their retention of atherogenic lipoproteins in the arterial wall. Thus, glucosamine use could potentially be atherogenic. Previous studies have yielded conflicting results with respect to the atherogenic potential of glucosamine. Some studies have suggested that glucosamine may have pro=atherogenic effects, while others suggest an anti-atherogenic effect. This grant proposes to investigate the role of glucosamine in vascular. proteoglycan biosynthesis and lipoprotein retention in vitro, andin vivo. The major hypothesis of this grant is that glucosamine supplementation will result in altered proteoglycan synthesis by vascular-smooth muscle cells, which will in turn result in an altered propensity to atherosclerosis. Depending on the nature of these altered vascular proteoglycans, glucosamine supplementation could either enhance susceptibility to, or protect against, atherosclerosis. This grant proposes to study the
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effect of glucosamine supplementation on the structure and function of proteoglycans synthesized by monkey aortic smooth muscle cells in vitro. Studies will be performed to determine the effect on-degree of sulfation, size, and ratio of classes of proteoglycans synthesized by vascular smooth muscle cells, and the retention of atherogenic lipoproteins by these altered proteoglycans. In addition, this grant proposes to address the effect of glucosamine supplementation in vivo. LDL receptor deficient mice, a mouse model of atherosclerosis that has a human-like lipoprotein profile, will be supplemented with oral glucosamine, and the extent of atherosclerotic lesions will be determined. The findings from the proposed study should provide important insights into the potential effects of glucosamine supplementation on atherosclerotic cardiovascular disease. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: GLYCOCONJUGATES OF LEISHMANIA Principal Investigator & Institution: Turco, Salvatore J.; Professor; Biochemistry; University of Kentucky 109 Kinkead Hall Lexington, Ky 40506 Timing: Fiscal Year 2001; Project Start 01-SEP-1985; Project End 31-AUG-2003 Summary: Leishmaniasis is a major health problem to humans and is caused by protozoan parasites of the genus Leishmania. Lipophosphoglycan (LPG) is an important macromolecule on the surface of the promastigote form of these parasites and is believed to be multifunctional. Structurally, LPG is composed of four domains: (i) a lyso-l-O-alkylphosphatidylinositol anchor, (ii) a phosphosaccharide core, (iii) a polymer of repeating saccharide units linked together by phosphodiester bridges, and (iv) a small, capping oligosaccharide at the terminal, non-reducing end. The lipid anchor and phosphosaccharide core regions of LPG are conserved among various Leishmania species, whereas there is variability of sugar composition and sequence in the repeating phosphorylated saccharide units and the capping structure. While significant progress has been made on structure-function relationships of LPG, much more remains to be learned concerning interspecies differences, and intraspecies developmental modifications of LPG structure. Determining these structural differences along with the biosynthesis and turnover of this important glycoconjugate will also be a focus of our research. The specific aims of this application are as follows: l. Continuation of structural analysis of LPGs. Specifically, the structure of LPG from Indian isolates of L. donovani and from isolates of L. braziliensis and L. amazonensis will be elucidated. 2. Biochemical analysis of LPG biosynthesis. Two key enzymes (mannosylphosphate transferase and arabinosyltransferase) involved in LPG biosynthesis will be purified and characterized. 3. Characterization of LPG turnover. The turnover of LPG by the parasite and the fate of LPG upon infection of macrophages by promastigotes will be investigated. From these studies, we hope to contribute to the understanding of the role LPG plays in the pathogenesis of leishmaniasis and to provide a biochemical rationale for the design of chemotherapeutic regimens that exploit its unique structure. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen
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Project Title: IN VIVO EFFECTOR CELL RESPONSE TO PEPTIDE VACCINATION Principal Investigator & Institution: Cole, David J.; Professor & Chief of Surgery; Surgery; Medical University of South Carolina 171 Ashley Ave Charleston, Sc 29425 Timing: Fiscal Year 2001; Project Start 01-JUL-2001; Project End 30-JUN-2004 Summary: (Applicant's Abstract) The molecular definition of tumor antigens has generated considerable enthusiasm for peptide-based cancer vaccines. However, the
16
Glucosamine
antigen-specific T cell response to peptide-based cancer vaccines remains poorly understood. The applicant has established an effective collaboration at the Medical University of South Carolina to explore the rational development of these vaccines. He has characterized a vaccine delivery system based on the unique polymer poly-N-acetyl glucosamine (designated F2 gel). This highly purified polysaccharide can be formulated into a stable matrix in combination with antigenic peptide and cytokine. F2 gel/peptide matrix vaccine is capable of effectively stimulating an antigen-specific T cell response, and is associated with protection from tumor challenge. Macrophages are critical to the efficacy of this vaccine, as macrophage depletion prior to vaccination abrogates the antigen-specific T cell response. The hypothesis of this application is that vaccination with the F2 gel/peptide/cytokine matrix leads to an effective cell-mediated antitumor response by providing sustained release of antigenic peptide and cytokine in a microenvironment that elicits macrophage activation. In this application, the applicant describes an innovative model based on the adoptive transfer of TCR transgenic OT-1 T cells and the murine tumor E.G7 that will allow him to precisely define in vivo T cell responses to peptide vaccination. He proposes to define whether a peptide-dose tolerance threshold exists which limits T cell antitumor responses and to evaluate whether paracrine cytokine release (Tc cytokines IL-12 and IL-2, or GM-CSF) can enhance the efficacy of his system. In addition, he will evaluate the ability of this unique vaccine delivery system to overcome E.G7 tumor-induced T cell anergy. Parallel studies will investigate the macrophage and dendritic cell response to the F2 gel matrix vaccine. Two unique reagents will facilitate his efforts to define the antigen presenting cell response to vaccination: the Kb/SIINFEKL tetramer, specific for the OT-1 TCR, and the mAb 25-D1.16, specific for the Kb/SIINFEKL complex. The results gained from the proposed studies will contribute to the design of phase I clinical trials. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: INHERITED GLUCORONIDATION
DISORDERS
OF
HEPATIC
BILIRUBIN
Principal Investigator & Institution: Roy-Chowdhury, Namita; Associate Professor; Medicine; Yeshiva University 500 W 185Th St New York, Ny 10033 Timing: Fiscal Year 2003; Project Start 01-JUL-1987; Project End 30-JUN-2007 Summary: (provided by applicant): Bilirubin is the toxic end product of heme breakdown. Efficient biliary excretion of bilirubin requires glucuronidation mediated by uridinediphosphoglucuronate glucuronosyltransferase-1A1 (UGT1A1), the catalytic site of which is located inside the hepatocyte endoplasmic reticulum (ER) lumen. Inherited UGT1A1 deficiency leads to the accumulation of unconjugated bilirubin, causing the potentially lethal Crigler-Najjar syndrome type 1. UGT1A1 also detoxifies estrogen and several drugs and carcinogens. Specific Aim 1 is to characterize the structure-function relationship of UGT1A1. We have shown that UGT1A1 forms dimers, and will test the hypothesis that dimerization is required for activation of the enzyme by stimulation of the import of UDP-glucuronic acid (UDPGA) into the ER lumen by the physiological UGT activator, UDP-N-acetyl glucosamine (UDP-gluc-Nac). We will test whether dimerization explains the dominant negative function of some mutant forms of UGT1A1. Another hypothesis to be tested is that UGT1A1 activity is regulated by phosphorylation. ER localization is important in UGT1A1 function. Therefore, we will delineate the motifs required for membrane incorporation and specific ER localization. Since several drugs cause hyperbilirubinemia by inhibiting UGT1A1 activity, we will delineate domains involved in binding the substrtes, UDPGA and bilirubin. Specific Aim 2 is to characterize UGT1A1 gene expression. We hypothesize that the interaction
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of cis-acting elements within the regulatory upstream region of UGT1A1 with hepatocellular transactivating factors determine the tissue-specificity of UGT1A1 expression, its induction by Phenobarbital and clofibrate, and its down-regulation by thryroid hormone. We will test this DNase foot-printing, electrophoretic mobility shift assays and expression of promoter-reporter constructs in differentiated human hepatoma cells and immortalized human hepatocytes. Successful completion of this study will elucidate the mechanism of UGT1A1 function in health and inherited disorders. Understanding the regulatory mechanisms of UGT1A1 should assist in identifying enzyme-inducing drugs for improved treatment of neonatal hyperbilirubinemia mad incomplete UGT1A1 deficiency (Crigler-Najjar syndrome type 2). Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: INTRAARTICULAR INJECTION OF POLYGLUCOSAMINE FOR KNEE OA Principal Investigator & Institution: Cattaneo, Maurizio V.; Ivrea, Inc. 216 Ricciuti Dr Quincy, Ma 02169 Timing: Fiscal Year 2002; Project Start 30-SEP-2002; Project End 31-MAR-2003 Summary: (provided by applicant): Osteoarthritis (OA) is a common disabling disorder for which no good medical remedy currently exists. As a result, many patients take Glucosamine, a nutritional supplement, for the treatment of their OA symptoms, because of its high level of safety compared to traditional anti-inflammatory medications. However, oral glucosamine is promptly metabolized by the liver during first-pass metabolism. Injectable polyglucosamine (PGA) is a highly viscous sustainedrelease form of glucosamine which may prove a more efficient modality for delivering glucosamine to the joint. The overall goal of this proposed Phase I SBIR is to determine if intraarticular injections of PGA protect against the early stages of joint damage in a rabbit model of OA. The proposed specific aims include: (1) Create a surgical instability of the knee in 14 2 Kg NZW rabbits using a modification of the Hulth technique. (2) Administer the PGA-treated and control groups (n=7 each) 5 weekly injections of PGA or saline respectively into the unstable knee, and maintain the animals for an additional 7 weeks. (3) Examine the extent of lesions in a blind fashion using morphological, histological and biochemical evaluations. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen
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Project Title: LECTIN-LIKE PROPERTIES OF AMELOGENINS Principal Investigator & Institution: Ravindranath, Rajeswari; Ctr/Craniofacial Molec Biol; University of Southern California 2250 Alcazar Street, Csc-219 Los Angeles, Ca 90033 Timing: Fiscal Year 2001; Project Start 01-FEB-2000; Project End 31-JAN-2005 Summary: (adapted from the Investigator's abstract): The long-term objective of this proposal is to determine the nature and function of amelogenins with sugar residues of other enamel proteins, and cell surface glycoconjugates. The central hypothesis is that amelogenins have lectin-like properties, which mediate functional protein-carbohydrate interactions with matrix glycoproteins or cell surface glycoconjugates within the matrix or at the dentine enamel junction (DEJ). Preliminary data from the Principal Investigator's laboratory have established the presence of and amelogenin glyco-binding motif located in the conserved amino terminal region of the molecule. Others have established that a mutation in this region of the amelogenin structure results in the
18
Glucosamine
clinical enamel defect; amelogenesis imperfecta. (Collier et al., 1997). To test this hypothesis the following five specific aims will be investigated. The first aim is to identify specific interactions between amelogenins and structural analogs of N-acetyl glucosamine (GlcNAc) and N-acetyl neuraminic acid (NeuAC) and their glycosidic linkages commonly found in mammalian glycoproteins and glycolipids. Agglutination and competitive inhibition studies of amelogenins with oligosaccharides and glycoconjugates. (2) To identify putative ligands for amelogenin-binding in the extracellular enamel matrix "non-amelogenin" glycoprotein fractions. The lectin histochemistry of non-amelogenin proteins and immunological and radiometric assessment of amelogenin binding to these proteins is studied. (3) To assess the influence of carbohydrate-amelogenin interactions on nanosphere formation. Conjugates of glycoproteins and amelogenins are studied employing electron and atomic-force microscopy. (4) To evaluate the effects of GlcNAc/NeuAc-rich nonamelogenins and glycoprotein analogs on biomineralization in the presence and absence of amelogenin in vitro. The effects of glycoconjugates and amelogenins of apatite biomineralization are assessed. (5) To develop a model for the recognition and binding of amelogenins with cell surface glycoconjugates of odontoblasts and ameloblasts and to determine the effects of amelogenin-derived peptides on amelogenesis in vitro. A fibroblast model is developed and cell-surface amelogenin interactions and the putative role of amelogenin peptides in a feedback-signaling pathway are investigated. These experiments are a logical extension of the newly identified lectin-like properties of amelogenins (Ravindranath et al. Submitted), which are postulated to play a functional role in normal enamel biomineralization. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: MECHANISTIC MANNOSYLTRANSFERASES
STUDIES
OF
PROKARYOTIC
Principal Investigator & Institution: Thorson, Jon S.; Associate Professor; None; University of Wisconsin Madison 750 University Ave Madison, Wi 53706 Timing: Fiscal Year 2001; Project Start 01-AUG-1998; Project End 31-JUL-2003 Summary: There is a fundamental lack of information regarding the chemical mechanisms by which glycosyl transfer and the incorporation of glycosylation patterns into the final target (proteins, cell walls and/or antibiotics) occur due primarily to the restricted availability of glycosyltransferases and their nucleotide diphosphate sugar substrates. While essentially all research in this arena has focused upon eukaryotic transferases, we suggest prokaryotic glycosyltransferases to be a rich alternative source with perhaps better accessibility. Thus we propose a detailed comparison of two prokaryotic model mannosyltransferases which use identical substrates but differ only in the stereochemistry of mannosyltransfer (alpha1 yields 4 or "retaining" versus beta1 yields 4 or "inverting"; Man Talpha4 and Man Tbeta4, respectively). Through a multidisciplinary approach (overexpression and purification of Man Talpha4 and Man Tbeta4; simplified assay systems based upon synthetic "unnatural" acceptors; chemical mechanistic probes including substrate and solvent isotope effects, elucidation/characterization of covalent Man T alpha4- and/or Man Tbeta4- substrate complexes, nucleophilic traps and testing the catalytic competency of synthetic substrate analogs; and Man Talpha4/Man Tbeta4 structural probes including site-directed mutagenesis; in vitro molecular evolution; differential labeling and/or active sitedirected affinity labeling), the proposed work should help define i) the Man Talpha4 and Man Tbeta4 chemical reaction mechanisms and ii) how the Man Talpha4 and Man Tbeta4 scaffold governs these important reactions. Using mannosyl transfer as the
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model, the proposed work will serve to establish a foundation from which a general glycosyltransferase mechanistic consensus can be derived. In addition, the selected reactions (alpha/beta 1 yields 4 mannosyl transfer) are analogous to those found in eukaryotic N-linked glycoprotein biosynthesis and mechanism-based inhibitors based upon these models should lead to altered eukaryotic cell surface glycosylation patterns terminating in N-acetyl-D-glucosamine (GlcNAc) and Man, defining the cell as "nonself" and thus providing therapeutic opportunities. The beta-mannosyl linkage is also particularly difficult to prepare via chemical synthesis and our proposed studies may lead to enzymatic alternatives. Finally, the presented in vitro evolution/selection methodology should contribute to the general synthetic utility of glycosyltransferases (by providing simplified substrates and the potential to screen for essentially any glycosyl transfer event) and possibly lead to future bacterial cell surface engineering towards designed therapeutic vaccines. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: METABOLITE PROBES FOR MOLECULAR OPTICAL IMAGING Principal Investigator & Institution: Rajopadhye, Milind; Visen Medical, Inc. 2 Gill St, Ste E&F Woburn, Ma 01801 Timing: Fiscal Year 2003; Project Start 01-JUL-2003; Project End 30-JUN-2004 Summary: (provided by applicant): There is a growing need in the medical imaging sciences to better detect and characterize abnormal tissue and disease processes. Additionally, definitive and successful imaging modalities allowing the molecular characterization of pathological processes have yet to be obtained. VisEn Medical is developing a broad optical imaging technology platform that will enable noninvasive imaging of molecular events associated with human disease. By utilizing near-infrared emitting fluorochromes (NIRFs) linked to biomolecules (i.e. imaging probe), VisEn can obtain information as to the localization and activity of specific enzymes and metabolites associated with a particular pathology, including cancer. The overall goal of this study is to develop and synthesize NIRF-conjugated metabolite probes capable of imaging the in vivo metabolic function of cancer in real-time. To achieve this objective, VisEn will: 1. Develop monovalent and bivalent NIRF-conjugated glucose biomolecules. Probes will be synthesized by conjugating glucosamine to several different fluorochromes in sufficient quantities for purification, analysis and in vitro characterization. 2. Characterize metabolite-imaging probes by physiochemical and optical metrics. Kinetics and specificity of cellular uptake will be examined to help select the most promising candidates for in vivo analysis. 3. Perform in vivo imaging experiments to demonstrate the ability of the probes to image tumor bearing animal models noninvasive and in real-time. This study represents the first step towards the development of novel, safe and cost-effective clinical agents to image molecular profiles of cancer in vivo. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen
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Project Title: MODIFICATION OF HELICOBACTER PYLORI LIPID A Principal Investigator & Institution: Trent, Michael S.; Microbiology; East Tennessee State University Box 70565 Johnson City, Tn 37601 Timing: Fiscal Year 2003; Project Start 01-APR-2003; Project End 31-MAR-2005 Summary: (provided by applicant): The outer membrane of Gram-negative bacteria consists of a unique molecule known as lipid A that serves as the membrane anchor for lipopolysaccharide (LPS). Lipid A (endotoxin) is the component of LPS responsible for
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Glucosamine
the stimulation of the host innate immune system involved in Gram- negative sepsis. The lipid A of Escherchia coli is a hexa-acylated disaccharide of glucosamine that is substituted at the 1- and 4'- positions with phosphate and glycosylated at the 6' position with two Kdo (3-deoxy-D-manno-octulosonic acid) moieties. Nine enzymes are required for biosynthesis of Kdo2- lipid A, the minimal LPS required for E. coli growth under normal laboratory conditions. Since lipid A is required for bacterial growth, it has become an interesting target for the design of novel antibacterial agents. Although single copies of the lipid A biosynthetic genes are found in nearly all Gram-negative bacterial genomes including those of Helicobacter pylori, the lipid A of the latter is underacylated with the phosphate groups either absent or modified. The primary focus of the present study is the identification of novel enzymes required for the modification of H. plyori lipid A and initial studies to evaluate the importance of such modifications during infection. Secondly, the lipid A structure of Helicobacter heilmannii will be investigated. H. pylori is now considered the causative agent of gastric and duodenal ulcers and H. heilmannii has recently been found associated with human gastritis. The specific aims of the current proposal are: (I) characterization and cloning of lipid A deacylases of H. pylori; (II) characterization and cloning of genes required for modification of the phosphates of H. pylori lipid A; (III) relevance of H. pylori lipid A modifications during infection; and (IV) isolation, purification, and structural characterization of key lipid A species of H. heilmannii. The completion of these aims will not only further the understanding of the lipid A biosynthetic pathway in H. pylori and H. heihnannii but also lay the foundation for new molecular insights into the pathogenesis of these unique organisms. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: N-ACETYLGLUCOSAMINE TREATMENT OF OSTEOARTHRITIS Principal Investigator & Institution: Okumu, Franklin W.; Optimer Pharmaceuticals, Inc. 10110 Sorrento Valley Rd, Ste C San Diego, Ca 921211643 Timing: Fiscal Year 2003; Project Start 15-SEP-2003; Project End 31-AUG-2004 Summary: (provided by applicant): Osteoarthritis (OA) represents the most common joint disease, affecting approximately 40 million Americans. OA is a leading cause of severe activity limitations and disability. Therapies that definitively alter the course of the disease are not available. Pharmacologic management of OA is limited to pain control. Nonsteroidal anti-inflammatory drugs are widely used but are associated with significant adverse reactions. Oral glucosamine and chondroitin sulfate are consumed by a large number of patients. Although some studies suggest that this reduces the rate of joint space narrowing, this conclusion is not uniformly accepted. Viscosupplementation with hyaluronan acid or its derivatives has been approved as a therapy for patients with knee OA and clinical experience demonstrated excellent patient compliance. This establishes the need for second-generation products with improved efficacy towards symptom control and disease modification. The key advantage of intraarticular therapy is in the delivery of high local drug concentrations and a reduced risk for systemic adverse reactions. The following proposal is based on prior research to identify novel effective and safe approaches to this form of OA therapy. We observed chondroprotective activities of the glucosamine derivative,Nacetylglucosamine (GIcNAc). Intraarticular injections of aqueous solutions of GIcNAc in 6 rabbits with experimental OA demonstrated greater efficacy than hyaluronan in reducing not only joint inflammation but also cartilage degradation. Adverse reactions were not observed. Based on these findings we propose the hypothesis that intra articular administration of GIcNAc represents a novel, effective and safe approach to
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chondroprotection. The following aims will address this hypothesis: 1. Prepare formulations of GIcNAc and retention time in rodent joints. 2. Assess therapeutic efficacy of GIcNAc formulations in rabbits with experimentally induced OA. These studies have the potential to provide the basis for a safe and effective chondroprotective therapy for OA. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: PATHWAYS REGULATING AMOEBIC CYST FORMATION Principal Investigator & Institution: Eichinger, Daniel J.; Associate Professor; Medical/Molecular Parasitology; New York University School of Medicine 550 1St Ave New York, Ny 10016 Timing: Fiscal Year 2001; Project Start 01-MAR-2000; Project End 29-FEB-2004 Summary: (Adapted from the Applicant'ps Abstract): Encystation in the human parasite Entamoeba histolytica cannot be studied in vitro. The related reptilian parasite, E. invadens, will encyst in vitro and can be used as model system to study encystation in Entamoeba. Two sugars inhibit the amebic encystation process. Galactose prevents the aggregation of ameba, which precedes encystation while N acetyl glucosamine allows aggregation to occur but still prevents the formation of osmotically resistant cysts. This proposal will study the role of galactose ligands and their receptor in the encystment process. An ortholog of the light subunit of the GalNAc lectin of E. histolytica has been cloned from E. invadens. The E. invadens gene product binds galactose and mucin, appears to be found on the surface of the ameba and likely mediates the initial cellular aggregation step. Gal-terminated glycoconjugates stimulate encystation in a concentration-dependent manner and suggest a role for the lectin in parasite differentiation. The structure of the lectin and a proposed mechanism of regulating encystation will be examined in this proposal. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen
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Project Title: GLUCOSAMINE
PILOT--MANAGING
OSTEOARTHRITIS
SYMPTOMS:
Principal Investigator & Institution: Yoon, Saun-Joo L.; University of Florida Gainesville, Fl 32611 Timing: Fiscal Year 2001; Project Start 01-AUG-2001; Project End 31-JUL-2004 Summary: (from applicant's Abstract) In the millennium, the health care system in the United States will be forced to focus on managing chronic illness and preventing disability in the increasing aging population. Osteoarthritis (OA), particularly of the knee and hip, is the most common chronic condition and the leading cause of disability among older adults. Current treatment regimens either provide only temporary relief with medications or require surgical intervention. Such treatments can be costly in terms of adverse effects and rehabilitation. In addition, more people are spending money to obtain dietary supplements to manage their symptoms related to OA and other chronic illnesses, Although glucosamine and chondroitin sulfate (GCS) has shown some effectiveness in relieving arthritic pain, its use has not been supported by the American College of Rheumatology. The purpose of this study is to determine if oral GCS results in functional, global, and structural improvement. The proposed study is a randomized, double-blinded, and placebo-controlled study with repeated measures. The sample will consist of twenty persons 50 years and older with osteoarthritis in at least one knee. Subjects in experimental and control groups will receive GCS and a placebo, respectively, for six months. Subjects in both groups will be provided with placebo for
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Glucosamine
the 3 months until follow-up assessment to prevent them from crossing over. Dependent measures include: 1) range of motion, gait balance, and strength of the affected knee joint for measuring functional improvement; 2) severity of osteoarthritis, pain distress, and quality of life for measuring global improvement; and 3) MRI of the knee for measuring structural improvement. This study fills an important gap in our knowledge about the effect of glucosamine and chondroitin sulfate and may show effects that will impact intervention in persons with OA in the future. In particular, the proposed study will provide nurses with the data necessary to determine whether or not to recommend GCS as a treatment for their patients with OA. If GCS successfully decreases pain and slows down the joint degenerating process, OA patients may be more likely to comply with non-pharmacological treatments such as exercise. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: PROTEASOME REGULATION BY O-GLYCOSYLATION Principal Investigator & Institution: Kudlow, Jeffrey E.; Division Director; Medicine; University of Alabama at Birmingham Uab Station Birmingham, Al 35294 Timing: Fiscal Year 2003; Project Start 01-AUG-2003; Project End 31-JUL-2008 Summary: (provided by applicant): The laboratory has shown that protein modification with O-linked N-acetylglucosamine (O-GlcNAc) plays a direct role in the function of transcriptional activators and repressors. This modification, which results from glucose metabolism, also modulates the function of the proteasome, the major organelle involved in intracellular degradation of proteins. The chymotryptic activity of 26S proteasomes, but not 20S proteasomes against 4 amino acid peptides (LLVY) is blocked by incubation of the proteasome with O-GlcNAc transferase (OGT). In addition, the ATPase activity of intact proteasomes is blocked by OGT. Physiologically inactivated proteasomes from NRK cells treated with high glucose or glucosamine can be reactivated by recombinant O-GlcNAcase, the enzyme that removes this modification. Labeling studies on purified proteasomes with [3H]-GlcNAc indicate that the modified protein(s) have a molecular mass of about 45 kDa and that this substrate resides in the 19S regulatory cap of the proteasome. Since the proteasome degrades pro-apoptotic factors such as p53 and many of its downstream targets, inhibition of proteasome function might lead to the accumulation of these factors with the induction of apoptosis. The chemotherapeutic agent and GlcNAc analog, streptozotocin, also induces apoptosis through its property as a non-competitive inhibitor of the O-GlcNAcase. The proposed studies are designed to determine the biochemical linkage between the O-GlcNAc pathway and the proteasome. The ability of O-GlcNAc to block proteasomal function may also couple glucose metabolism to amino acid release from muscle wasting. The specific aims are as follows: General goal: Determine the role of O-GlcNAc in proteasomal function. 1. Determine the effect of O-GlcNAc transferase (OGT) and OGlcNAcase on proteasome function in vitro using these enzymes to reversibly modify proteins in the proteasome in vitro. 2. Identify proteasomeassociated protein(s) that contain the O-GlcNAc modification and regulate proteasome function in a reversible manner. 3. Determine how O-GlcNAcylation of the proteasome 19S regulatory subunit modifies the function of the proteasomal peptidase and ATPases. 4. Using transgenic mice, determine the effect of proteasome blockade in vivo on epithelial cell apoptosis and muscle protein wasting. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen
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Project Title: REGULATION OF AMPICILLIN RESISTANCE IN E FACEIUM Principal Investigator & Institution: Rice, Louis B.; Professor; Medicine; Case Western Reserve University 10900 Euclid Ave Cleveland, Oh 44106 Timing: Fiscal Year 2001; Project Start 01-MAR-2001; Project End 28-FEB-2005 Summary: (Verbatim from Applicant's Abstract):The dramatic rise in prevalence of multi-resistant enterococci in United States hospitals over the past decade has limited therapeutic options, affected morbidity and mortality and increased the cost of caring for seriously ill hospitalized patients. The expression of resistance to vancomycin has received the most attention during this time. However, it is equally problematic that virtually all vancomycin-resistant enterococci (VRE) are Enterococcus faecium that express resistance to high levels of ampicillin. While it is clear that ampicillin resistance in E. faecium requires expression of low affinity penicillin-binding protein 5 (PBP5), the correlation between the amounts of detectable PBP5 and the level of ampicillin resistance is not exact. Several point mutations in pbp5 have been identified in strains expressing high-level ampicillin resistance, but the specific contributions of these mutations to the levels of resistance have never been assessed. We have identified the first transferable ampicillin resistance described from E. faecium in a VRE strain from Northeast Ohio. The pbp5 gene conferring resistance in this isolate possesses several mutations that have been associated with high-level ampicillin resistance in other E. faecium isolates. Curiously, levels of ampicillin resistance expressed by transconjugant E. faecium strains are not equivalent to those expressed by the donor, despite documentation that equivalent amounts of PBP5 are produced. In the past two years, we have acquired evidence that levels of ampicillin resistance expressed correlate with transcription (but not necessarily translation) of an upstream open reading frame designated ftsWEf. The specific aims of this proposal are to: 1) perform site directed mutagenesis of E. faecium pbp5 to determine the functional (MIC, affinity) and structural importance of specific mutations. With collaborations in France and Switzerland, we now possess the molecular expertise to create the mutants and analyze their functional impact and determine the crystal structure; 2) to investigate the role of the putative upstream repressor psr in regulating expression of ampicillin resistance in E. faecium; 3) to investigate the mechanisms by which transcription of ftsWEf impacts the levels of ampicillin resistance expressed by E. faecium; 4) to assess whether upstream open reading frames designated nanE-Ef and ywrF-Ef affect levels of ampicillin resistance expressed and 5) to determine whether the peptidoglycan precursors differ in sensitive and resistant strains. These investigations will yield new insights into what is arguably the most resistant nosocomial pathogen of our time by providing important structure-function correlations for PBP5, correlations which may be important for the development of newer and better inhibitory compounds. They will also yield important new information on mechanisms of cell wall synthesis in E. faecium and other Gram-positive bacteria as well as on the mechanisms by which ampicillin resistance in E. faecium is regulated. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen
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Project Title: ROLE OF NUTRIENTS IN AGE-RELATED INSULIN RESISTANCE Principal Investigator & Institution: Hawkins, Meredith A.; Assistant Professor; Yeshiva University 500 W 185Th St New York, Ny 10033 Timing: Fiscal Year 2003; Project Start 01-DEC-2002; Project End 30-NOV-2007 Summary: Nutrient excess and obesity play a central role in the pathogenesis of the insulin resistance syndrome, with important age-related sequelae including accelerated
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atherosclerosis and type 2 diabetes mellitus (T2DM), and is the subject of this Program Project. This proposal will study the interrelationships of aging, obesity and the hexosamine biosynthetic pathway (HBP) in the induction of nutrient-induced insulin resistance in humans. The HBP provides cellular "satiety" signals with increased circulating levels of such nutrients as glucose and free fatty acids, and increases glycosylation of important intracellular factors including transcription factors, ultimately affecting the expression of many genes. Increased HBP flux in animal models induces insulin resistance, and increases adipocyte gene expression and circulating levels of many cytokines and acute phase reactants. These proteins, whose plasma levels are strongly correlated with insulin resistance in humans, likely contribute to the pathophysiology of many age-related diseases. Importantly, aging itself is associated with increased glycosylation of intracellular proteins, suggesting upregulation of the HBP and therefore increased susceptibility to the effects of nutrients. However, a causal link between the HBP, nutrient availability and aging-induced insulin resistance has not yet been established in humans. We will compare the effects of increased nutrient availability on whole-body insulin action, accumulation of HBP products, and adipocyte gene expression in 4 groups of subjects: young lean, young obese, lean elderly and obese elderly. The experimental design will therefore parallel that of Project 2 in aging ad libitum fed and caloric restricted rodents. We will thereby determine whether increased flux into the HBP mediates nutrient-induced metabolic changes in humans, and whether upregulation of the HBP with aging might exacerbate the metabolic impact of nutrient excess. Furthermore, we will examine subcutaneous and visceral adipose tissue to determine effects of aging and nutrients on depot-specific adipocyte gene expression. Together with Project 2, this project aims to define the biological characteristics ot the visceral fat depot that pose significant risk factors for the metabolic syndrome of aging. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: STRUCTURE BIOSYNTHESIS
AND
MECHANISM
OF
LPXC
IN
LIPID
A
Principal Investigator & Institution: Zhou, Pei; Biochemistry; Duke University Durham, Nc 27706 Timing: Fiscal Year 2003; Project Start 15-JUN-2003; Project End 30-NOV-2006 Summary: (provided by applicant): Lipid A, the hydrophobic anchor of lipopolysaccharide (LPS), is a glucosamine-based phospholipid that constitutes the outer monolayer of the outer membrane of most Gram-negative bacteria. Also known as endotoxin, lipid A is the active component of LPS that stimulates the immune system and causes lifethreatening Gram-negative septic shock, a severe condition characterized by disseminated intra-vascular coagulation and multiple organ failure. Lipid A biosynthesis is an essential pathway that is conserved in virtually all Gram-negative organisms. The committed step of lipid A biosynthesis is catalyzed by UDP-3-O- (acyl)N-acetylglucosamine deacetylase (LpxC). LpxC belongs to a novel family of zincdependent metalloamidases and shares no sequence homology with any known mammalian proteins. Hence, it is an excellent target for the design of novel antibiotics. Indeed, inhibition of LpxC causes rapid bacterial death and cures mice infected with a lethal intraperitoneal dose of Escherichia coil (E. coh). However, potent inhibitors against the LpxC from E. coli are relatively inactive against divergent LpxCs from other Gramnegative bacteria, particularly, those from Aquifex aeolicus and Pseudomonas aeruginosa. Although LpxCs have been the subject of extensive biochemical studies and pharmacological screenings, the unusual inhibitor specificity and the lack of structural information on LpxCs and their complexes, either with substrates or inhibitors, hinder
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further mechanistic studies on LpxCs and the optimization of their inhibitors. The overall goal of this proposal is to reveal the largely unknown molecular mechanism underlying LpxC catalysis in lipid A biosynthesis and to provide a structural basis to rationalize the specificity of LpxCs from different Gram-negative species. These studies should also facilitate the development of novel antibiotics targeting LpxC. In the proposed work, the specific aims are: 1) determining the solution structure of the LpxC from Aquifex aeolicus (AaLpxC); 2) determining the solution structure of the AaLpxC/TU-514 inhibitor complex and characterizing the interaction between AaLpxC and its substrate; 3) determining the solution structure of the LpxC from E. coil (EcLpxC); 4) characterizing the interactions between EcLpxC and various inhibitors using structural and biochemical approaches. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: STRUCTURE OF ANTIMITOGENIC MESANGIAL HEPARAN SULFATES Principal Investigator & Institution: Wang, Aimin; Cleveland Clinic Foundation 9500 Euclid Ave Cleveland, Oh 44195 Timing: Fiscal Year 2001; Project Start 01-JUN-2000; Project End 30-APR-2003 Summary: (adapted from the application) Heparan sulfates (HSs) and heparin, proposed as endogenous defending molecules in the "glomerular self-defense", are inhibitors of mesangial cell growth in human proliferative nephritides, in experimental renal disease models, and in cell culture, but the side activities of heparin, such as anti-coagulant activity, have limited its potential therapeutical applications. My previous studies have shown that HSs and heparin are inhibitors of rat mesangial cell (RMC) proliferation in culture, but that endogenous HS oligosaccharides synthesized by RMCs are much more potent than heparin on an equivalent mass basis. We hypothesize that a defined fine structure(s) in the HS oligosaccharides is required to bind to a specific receptor(s) on the mesangial cell surface, thereby inhibiting RMC proliferation. The overall purpose of this proposal is to adapt Fluorophore-Assisted Carbohydrate Electrophoresis (FACE) for the analysis of the fine structure of the RMC HS oligosaccharides and to deduce the essential structures required for their anti-mitogenic activity. We propose: 1) to adapt the FACE methods to separate, identify and quantitate fluorotagged derivatives prepared from digests of heparin/HS with the eliminase heparitinase enzymes; 2a) to use RMCs cultured with [3H]glucosamine and [35S]sulfate to label the intact HS proteoglycans and the HS oligosaccharides generated from them via intracellular endoglycosidases; and 2b) to prepare chemical amounts (>200 pg quantities) of the HS oligosaccharides and of the intact HS chains following proteinase K digestion of the parent proteoglycans; 3a) to determine the concentration dependence of the antimitogenic activity of the HS chains and of the HS oligosaccharides, and their binding constants to the RMCs; and 3b) to modify selectively the HS chains, the HS oligosaccharides and heparin by specific enzymes (heparitinase lyases) and by fluorotagging, and to test the products for anti-mitogenic and binding activities; 4a) to separate sub-fractions of bioactive and inactive HS oligosaccharides by affinity binding to RMCs at 4 degrees C; and 4b) to determine the fine structures of the active (bound) and inactive (unbound) HS oligosaccharides using FACE analyses and thereby identify key structures required for the antimitogenic activity. If successful, this project can provide a head start for defining the molecular basis of HSs in regulating mesangial cell growth and mechanism(s) underlying this function, and designing suitable compounds for clinical treatment of proliferative nephritides using HSs as model molecules. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen
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Project Title: THE HEXOSAMINE PATHWAY AND DIABETIC NEPHROPATHY Principal Investigator & Institution: James, Leighton R.; Pathology and Lab Medicine; University of North Carolina Chapel Hill Office of Sponsored Research Chapel Hill, Nc 27599 Timing: Fiscal Year 2003; Project Start 01-MAY-2003; Project End 30-APR-2006 Summary: (provided by applicant):In North America, diabetes mellitus (DM) is the leading cause of end stage kidney disease (ESRD). Prominent histologic features of diabetic nephropathy include podocyte loss, mesangial cell (MC) hypertrophy, mesangial matrix expansion, basement membrane thickening and tubulointerstitial fibrosis. Persistent albuminuria, believed to be the result of injury to podocytes, is a major clinical hallmark of diabetic nephropathy. Podocytes form part of the permselectivity barrier in the kidney and the podocytes-specific protein, nephrin, plays a cardinal role in the function of the permeability barrier. The MC-specific protein megsin, a serine protease inhibitor, may be important in matrix remodeling and maintenance. Although blood glucose control is critically related to albuminuria, the mechanisms by which DM causes kidney injury have not been fully elucidated. Studies have shown that maneuvers like overexpression of glutamine:fructose-6-phosphate amidotransferase (GFAT), or exposure of MC to glucosamine, upregulates the expression of genes that have been implicated in renal injury; [GFAT is the rate limiting enzyme for glucose entry in the hexosamine pathway; glucosamine is downstream of GFAT in this pathway]. My hypothesis is that increased flux through the hexosamine pathway is one mechanism whereby DM may cause kidney disease. The major objective of my study is to use gene-targeting technology to develop mice that will express the GFAT protein in podocytes and MC under the control of the promoters for nephrin and megsin respectively, and to determine how this may modulate susceptibility to kidney injury following induction of DM with streptozotocin. I will compare the renal physiology and morphology of diabetic and non-diabetic targeted and wildtype mice of the same strain to ascertain whether increased activity of the hexosamine pathway predisposes mice to kidney injury and glomerulosclerosis. If my hypothesis is correct, this in vivo overexpression of GFAT will lead to kidney damage in non-diabetic mice and to enhancement of that caused by DM. These studies should further our understanding of the role of the hexosamine pathway in diabetic nephropathy, and may also provide a new animal model, in which to study diabetic nephropathy and its associated vascular complications. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen
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Project Title: THE SIGNALING ROLE OF QSULF IN EMBRYONIC NEURAL TUBE Principal Investigator & Institution: Ai, Xingbin; Anatomy; University of Pennsylvania 3451 Walnut Street Philadelphia, Pa 19104 Timing: Fiscal Year 2002; Project Start 01-JUN-2002 Summary: (provided by applicant) The objective of this proposal is to characterize the signaling roles of two candidate heparan sulfate proteoglycan (HSPG) modifying enzymes, quail glucosamine 6-O-sulfatase 1 (QSulf1) and QSulf2 in developing neural tube. Cell surface HSPGs play important roles in modulating the distribution and/or activity of signaling molecules such as Wnts, Shh, FGFs and BMPs. QSulf1, the first known extracellular matrix G6-sulfatase, is required for somite MyoD activation through its enzymatic activity to regulate Wnt pathway. QSulf2 is the second member of the family with unknown function. QSulf1 and QSulf2 have overlapping and discrete expression domains in embryonic neural tube. The proposal will test the hypothesis that
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QSulf1 and QSulf2 have unique functions in extracellular signaling pathways and the functional distinction is controlled by their divergent hydrophilic domains. First, we will characterize the expression pattern of QSulf1 and QSulf2 during embryogenesis by whole mount in situ hybridization combined with immunohistochemistry. Results from this experiment will serve as the initial steps for the functional analysis of QSulfs in developing neural tube. Second, to define QSulf function in the neural tube, we will manipulate the expression of each gene both by electroporation-mediated overexpression and antisense inhibition in chick embryos at stage 12. Molecular markers for neural tube patterning and neural crest cells will be characterized by immunohistochemistry. Results from these experiments will provide information in signaling roles of QSulfs in embryonic neural tube. Third, co-immunoprecipitation and yeast two-hybrid screen will be conducted to identify the binding proteins for the divergent hydrophilic domains of QSulfs that are hypothesized to control the localized functions of QSuIf1 or QSulf2. This study will provide insights on the mechanisms for localized QSulf function in the embryo. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen •
Project Title: VIRULENCE AND IMMUNITY TO STAPHYLCOCCI Principal Investigator & Institution: Pier, Gerald B.; Professor; Brigham and Women's Hospital 75 Francis Street Boston, Ma 02115 Timing: Fiscal Year 2001; Project Start 01-FEB-2001; Project End 31-JAN-2006 Summary: (Verbatim from Applicant's Abstract): The long-term goal of this study is to understand the role in pathogenesis and immunity of an environmentally regulated surface polysaccharide of Staphylococcus aureus chemically characterized as poly-Nsuccinyl-B-1-6 glucosamine (PNSG). PNSG has previously been determined to be the protective capsular polysaccharide/adhesin (PS/A) antigen of Staphylococcus epidermidis, raising the possibility that PNSG could be used as a "pan-staphylococcal" vaccine. To define the role of PNSG in pathogenesis of S. aureus infection 5 different PNSG-deficient S. aureus strains representative of major lineages will be constructed by genetic means via interruption of the genes in the intracellular adhesin (ica) locus that encodes proteins needed for synthesis of PNSG. Isogenic parental, mutant and ica complemented strains will be evaluated in vitro to determine the role of PNSG in promoting S. aureus adherence to catheters and in providing resistance of bacterial cells to phagocytic killing by leukocytes and complement. The same strains will also be tested for infectious capability in several animal systems of S. aureus infection, including animals actively and passively immunized with ica-deleted S. aureus and normal human serum to reflect the immunologic status of humans, who have high levels of natural antibody to S. aureus surface antigens. Because PNSG isolated from some strains of staphylococci have up to 30 percent of the succinate substituents on the polyglucosamine backbone replaced by acetate, purified PNSG, with differing ratios of succinate and acetate substituents on the polyglucosamine backbone, will be produced for immunologic studies. Rabbits will be immunized with the variants and sera assessed for antibody titer and opsonic killing ability. The PNSG variant structures will be used to immunize mice to evaluate their ability to generate protective immunity in the same systems used for the study of the role of PNSG in S. aureus virulence. In addition, passive protection by the rabbit sera raised to the variant PNSG constructs will be evaluated in the animal systems. All the above mentioned studies will provide new and useful information regarding pathogenesis and immunity of staphylococcal infections, stressing the use of animal systems that reflect naturally acquired immunity in humans to S. aureus. By the end of these studies we expect to have a clear understanding of the
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role of PNSG in virulence, as determined in a variety of staphylococcal infection systems, the immunochemical properties of PNSG that can engender protective immunity, and the types of S. aureus infections wherein PNSG-specific immunotherapies show the most potential for success. Website: http://crisp.cit.nih.gov/crisp/Crisp_Query.Generate_Screen
E-Journals: PubMed Central3 PubMed Central (PMC) is a digital archive of life sciences journal literature developed and managed by the National Center for Biotechnology Information (NCBI) at the U.S. National Library of Medicine (NLM).4 Access to this growing archive of e-journals is free and unrestricted.5 To search, go to http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=Pmc, and type “glucosamine” (or synonyms) into the search box. This search gives you access to full-text articles. The following is a sample of items found for glucosamine in the PubMed Central database: •
A glycoprotein modified with terminal N-acetylglucosamine and localized at the nuclear rim shows sequence similarity to aldose-1-epimerases. by Heese-Peck A, Raikhel NV.; 1998 Apr; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&rendertype=abstr act&artid=144007
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A Review of Articular Cartilage Pathology and the Use of Glucosamine Sulfate. by James CB, Uhl TL.; 2001 Dec; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=155438
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Alveolar macrophage priming by intravenous administration of chitin particles, polymers of N-acetyl-D-glucosamine, in mice. by Shibata Y, Foster LA, Metzger WJ, Myrvik QN.; 1997 May; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&rendertype=abstr act&artid=175208
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An insecticidal N-acetylglucosamine-specific lectin gene from Griffonia simplicifolia (Leguminosae). by Zhu K, Huesing JE, Shade RE, Bressan RA, Hasegawa PM, Murdock LL.; 1996 Jan; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&rendertype=abstr act&artid=157709
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Attenuation of Virulence and Changes in Morphology in Candida albicans by Disruption of the N-Acetylglucosamine Catabolic Pathway. by Singh P, Ghosh S, Datta A.; 2001 Dec; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=98888
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Autophosphorylation of Phosphoglucosamine Mutase from Escherichia coli. by Jolly L, Pompeo F, van Heijenoort J, Fassy F, Mengin-Lecreulx D.; 2000 Mar 1; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=94413
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Adapted from the National Library of Medicine: http://www.pubmedcentral.nih.gov/about/intro.html.
With PubMed Central, NCBI is taking the lead in preservation and maintenance of open access to electronic literature, just as NLM has done for decades with printed biomedical literature. PubMed Central aims to become a world-class library of the digital age. 5 The value of PubMed Central, in addition to its role as an archive, lies in the availability of data from diverse sources stored in a common format in a single repository. Many journals already have online publishing operations, and there is a growing tendency to publish material online only, to the exclusion of print.
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Characterization of 20K fimbria, a new adhesin of septicemic and diarrhea-associated Escherichia coli strains, that belongs to a family of adhesins with N-acetyl-Dglucosamine recognition. by Bertin Y, Girardeau JP, Darfeuille-Michaud A, Contrepois M.; 1996 Jan; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&rendertype=abstr act&artid=173764
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Characterization of a Bacillus subtilis Thermosensitive Teichoic Acid-Deficient Mutant: Gene mnaA (yvyH) Encodes the UDP-N-Acetylglucosamine 2-Epimerase. by Soldo B, Lazarevic V, Pooley HM, Karamata D.; 2002 Aug; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=135192
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Convergent Pathways for Utilization of the Amino Sugars N-Acetylglucosamine, NAcetylmannosamine, and N-Acetylneuraminic Acid by Escherichia coli. by Plumbridge J, Vimr E.; 1999 Jan 1; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=103530
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Cytologic Assessment of Nuclear and Cytoplasmic O-Linked N- Acetylglucosamine Distribution by Using Anti-Streptococcal Monoclonal Antibodies. by Turner JR, Tartakoff AM, Greenspan NS.; 1990 Aug 1; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&rendertype=abstr act&artid=54376
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Direct Incorporation of Glucosamine and N-Acetylglucosamine into Exopolymers by Gluconacetobacter xylinus (=Acetobacter xylinum) ATCC 10245: Production of Chitosan-Cellulose and Chitin-Cellulose Exopolymers. by Lee JW, Deng F, Yeomans WG, Allen AL, Gross RA, Kaplan DL.; 2001 Sep; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=93117
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DNA binding sites for the Mlc and NagC proteins: regulation of nagE, encoding the N-acetylglucosamine-specific transporter in Escherichia coli. by Plumbridge J.; 2001 Jan 15; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=29661
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Glucosamine and chondroitin sulfate supplementation to treat symptomatic disc degeneration: Biochemical rationale and case report. by van Blitterswijk WJ, van de Nes JC, Wuisman PI.; 2003; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=165439
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Glucosamine: A potential disease-modifying agent in osteoarthritis? by Chen BH.; 2001 Jul 10; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=81264
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Glucose and Glucosamine Regulate Growth Factor Gene Expression in Vascular Smooth Muscle Cells. by McClain DA, Paterson AJ, Roos MD, Wei X, Kudlow JE.; 1992 Sep 1; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&rendertype=abstr act&artid=49874
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Heparin's anti-inflammatory effects require glucosamine 6-O-sulfation and are mediated by blockade of L- and P-selectins. by Wang L, Brown JR, Varki A, Esko JD.; 2002 Jul 1; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=151027
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Identification of a Dedicated Recycling Pathway for Anhydro-N-Acetylmuramic Acid and N-Acetylglucosamine Derived from Escherichia coli Cell Wall Murein. by Park JT.; 2001 Jul 1; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=95265
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Identification of the Pseudomonas aeruginosa glmM Gene, Encoding Phosphoglucosamine Mutase. by Tavares IM, Jolly L, Pompeo F, Leitao JH, Fialho AM, Sa-Correia I, Mengin-Lecreulx D.; 2000 Aug 15; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=94616
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Immunochemical Properties of the Staphylococcal Poly-N-Acetylglucosamine Surface Polysaccharide. by Maira-Litran T, Kropec A, Abeygunawardana C, Joyce J, Mark III G, Goldmann DA, Pier GB.; 2002 Aug; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=128161
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Inner core biosynthesis of lipooligosaccharide (LOS) in Neisseria meningitidis serogroup B: identification and role in LOS assembly of the alpha1,2 Nacetylglucosamine transferase (RfaK). by Kahler CM, Carlson RW, Rahman MM, Martin LE, Stephens DS.; 1996 Mar; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&rendertype=abstr act&artid=177798
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N-Acetylglucosamine and Glucosamine-Containing Arabinogalactan Proteins Control Somatic Embryogenesis. by van Hengel AJ, Tadesse Z, Immerzeel P, Schols H, van Kammen A, de Vries SC.; 2001 Apr 1; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=88843
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O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability. by Yang X, Su K, Roos MD, Chang Q, Paterson AJ, Kudlow JE.; 2001 Jun 5; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=34401
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Peptidoglycan N-Acetylglucosamine Deacetylase, a Putative Virulence Factor in Streptococcus pneumoniae. by Vollmer W, Tomasz A.; 2002 Dec; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=133073
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Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine. by Heese-Peck A, Cole RN, Borkhsenious ON, Hart GW, Raikhel NV.; 1995 Sep; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&rendertype=abstr act&artid=160971
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Probing the Role of Cysteine Residues in Glucosamine-1-Phosphate Acetyltransferase Activity of the Bifunctional GlmU Protein from Escherichia coli: Site-Directed Mutagenesis and Characterization of the Mutant Enzymes. by Pompeo F, van Heijenoort J, Mengin-Lecreulx D.; 1998 Sep 15; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=107502
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Specific Defect in N-Acetylglucosamine Incorporation in the Biosynthesis of the Glycosylphosphatidylinositol Anchor in Cloned Cell Lines from Patients with Paroxysmal Nocturnal Hemoglobinuria. by Hillmen P, Bessler M, Mason PJ, Watkins WM, Luzzatto L.; 1993 Jun 1; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&rendertype=abstr act&artid=46698
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T-Cell-Dependent Antibody Response to the Dominant Epitope of Streptococcal Polysaccharide, N-Acetyl-Glucosamine, Is Cross-Reactive with Cardiac Myosin. by Malkiel S, Liao L, Cunningham MW, Diamond B.; 2000 Oct; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=101540
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Th1 Adjuvant N-Acetyl-d-Glucosamine Polymer Up-Regulates Th1 Immunity but Down-Regulates Th2 Immunity against a Mycobacterial Protein (MPB-59) in Interleukin-10-Knockout and Wild-Type Mice. by Shibata Y, Honda I, Justice JP, Van Scott MR, Nakamura RM, Myrvik QN.; 2001 Oct; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=98742
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The Escherichia coli G-fimbrial lectin protein participates both in fimbrial biogenesis and in recognition of the receptor N-acetyl-D-glucosamine. by Saarela S, Taira S, Nurmiaho-Lassila EL, Makkonen A, Rhen M.; 1995 Mar; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&rendertype=abstr act&artid=176762
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The femR315 gene from Staphylococcus aureus, the interruption of which results in reduced methicillin resistance, encodes a phosphoglucosamine mutase. by Jolly L, Wu S, van Heijenoort J, de Lencastre H, Mengin-Lecreulx D, Tomasz A.; 1997 Sep; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&rendertype=abstr act&artid=179399
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The inducible N-acetylglucosamine catabolic pathway gene cluster in Candida albicans: Discrete N-acetylglucosamine-inducible factors interact at the promoter of NAG1. by Kumar MJ, Jamaluddin MS, Natarajan K, Kaur D, Datta A.; 2000 Dec 19; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=18898
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Transposon-Induced Mutations in Two Loci of Listeria monocytogenes Serotype 1/2a Result in Phage Resistance and Lack of N-Acetylglucosamine in the Teichoic Acid of the Cell Wall. by Tran HL, Fiedler F, Hodgson DA, Kathariou S.; 1999 Nov; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=91646
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Widespread N-Acetyl-d-Glucosamine Uptake among Pelagic Marine Bacteria and Its Ecological Implications. by Riemann L, Azam F.; 2002 Nov; http://www.pubmedcentral.gov/articlerender.fcgi?tool=pmcentrez&artid=129920
The National Library of Medicine: PubMed One of the quickest and most comprehensive ways to find academic studies in both English and other languages is to use PubMed, maintained by the National Library of Medicine.6 The advantage of PubMed over previously mentioned sources is that it covers a greater number of domestic and foreign references. It is also free to use. If the publisher has a Web site that offers full text of its journals, PubMed will provide links to that site, as well as to sites offering other related data. User registration, a subscription fee, or some other type of fee may be required to access the full text of articles in some journals. To generate your own bibliography of studies dealing with glucosamine, simply go to the PubMed Web site at http://www.ncbi.nlm.nih.gov/pubmed. Type “glucosamine” (or 6 PubMed was developed by the National Center for Biotechnology Information (NCBI) at the National Library of Medicine (NLM) at the National Institutes of Health (NIH). The PubMed database was developed in conjunction with publishers of biomedical literature as a search tool for accessing literature citations and linking to full-text journal articles at Web sites of participating publishers. Publishers that participate in PubMed supply NLM with their citations electronically prior to or at the time of publication.
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synonyms) into the search box, and click “Go.” The following is the type of output you can expect from PubMed for glucosamine (hyperlinks lead to article summaries): •
A case for glucosamine. Author(s): Hussain MA. Source: European Journal of Endocrinology / European Federation of Endocrine Societies. 1998 November; 139(5): 472-5. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9849808&dopt=Abstract
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A cDNA clone for human glucosamine-6-sulphatase reveals differences between arylsulphatases and non-arylsulphatases. Author(s): Robertson DA, Freeman C, Morris CP, Hopwood JJ. Source: The Biochemical Journal. 1992 December 1; 288 ( Pt 2): 539-44. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1463457&dopt=Abstract
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A detailed lectin analysis of IgG glycosylation, demonstrating disease specific changes in terminal galactose and N-acetylglucosamine. Author(s): Bond A, Alavi A, Axford JS, Bourke BE, Bruckner FE, Kerr MA, Maxwell JD, Tweed KJ, Weldon MJ, Youinou P, Hay FC. Source: Journal of Autoimmunity. 1997 February; 10(1): 77-85. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9080302&dopt=Abstract
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A family of human beta3-galactosyltransferases. Characterization of four members of a UDP-galactose:beta-N-acetyl-glucosamine/beta-nacetyl-galactosamine beta-1,3galactosyltransferase family. Author(s): Amado M, Almeida R, Carneiro F, Levery SB, Holmes EH, Nomoto M, Hollingsworth MA, Hassan H, Schwientek T, Nielsen PA, Bennett EP, Clausen H. Source: The Journal of Biological Chemistry. 1998 May 22; 273(21): 12770-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9582303&dopt=Abstract
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A new predictive test for in-vitro fertilization based on the induction of sperm acrosome reaction by N-acetylglucosamine-neoglycoprotein. Author(s): Brandelli A, Miranda PV, Anon-Vazquez MG, Marin-Briggiler CI, Sanjurjo C, Gonzalez-Echeverria F, Blaquier JA, Tezon JG. Source: Human Reproduction (Oxford, England). 1995 July; 10(7): 1751-6. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8582974&dopt=Abstract
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A novel assay for typing Rh antigens in blood-stains using a lectin specific to the bisecting N-acetyl-D-glucosamine side chain of glycoprotein. Author(s): Matsubara K, Tanabe K, Akane A, Nakamura H, Takahashi S, Kimura K. Source: Journal of Immunological Methods. 1994 August 1; 173(2): 175-80. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8046252&dopt=Abstract
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A novel carbohydrate binding activity of annexin V toward a bisecting Nacetylglucosamine. Author(s): Gao-Uozumi CX, Uozumi N, Miyoshi E, Nagai K, Ikeda Y, Teshima T, Noda K, Shiba T, Honke K, Taniguchi N. Source: Glycobiology. 2000 November; 10(11): 1209-16. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11087713&dopt=Abstract
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A pilot study evaluating the efficacy of a fully acetylated poly-N-acetyl glucosamine membrane formulation as a topical hemostatic agent. Author(s): Cole DJ, Connolly RJ, Chan MW, Schwaitzberg SD, Byrne TK, Adams DB, Baron PL, O'Brien PH, Metcalf JS, Demcheva M, Vournakis J. Source: Surgery. 1999 September; 126(3): 510-7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10486603&dopt=Abstract
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A pilot study of N-acetyl glucosamine, a nutritional substrate for glycosaminoglycan synthesis, in paediatric chronic inflammatory bowel disease. Author(s): Salvatore S, Heuschkel R, Tomlin S, Davies SE, Edwards S, Walker-Smith JA, French I, Murch SH. Source: Alimentary Pharmacology & Therapeutics. 2000 December; 14(12): 1567-79. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11121904&dopt=Abstract
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A randomized double-blind clinical trial of the effect of chondroitin sulfate and glucosamine hydrochloride on temporomandibular joint disorders: a pilot study. Author(s): Nguyen P, Mohamed SE, Gardiner D, Salinas T. Source: Cranio. 2001 April; 19(2): 130-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11842864&dopt=Abstract
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A randomized, double blind, placebo controlled trial of a topical cream containing glucosamine sulfate, chondroitin sulfate, and camphor for osteoarthritis of the knee. Author(s): Cohen M, Wolfe R, Mai T, Lewis D. Source: The Journal of Rheumatology. 2003 March; 30(3): 523-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12610812&dopt=Abstract
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A randomized, double-blind, placebo-controlled trial of glucosamine sulphate as an analgesic in osteoarthritis of the knee. Author(s): Hughes R, Carr A. Source: Rheumatology (Oxford, England). 2002 March; 41(3): 279-84. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11934964&dopt=Abstract
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A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance. Author(s): Wells L, Vosseller K, Hart GW. Source: Cellular and Molecular Life Sciences : Cmls. 2003 February; 60(2): 222-8. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12678487&dopt=Abstract
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A subpopulation of estrogen receptors are modified by O-linked Nacetylglucosamine. Author(s): Jiang MS, Hart GW. Source: The Journal of Biological Chemistry. 1997 January 24; 272(4): 2421-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8999954&dopt=Abstract
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A survey of self-medication practices and perceived effectiveness of glucosamine products among older adults. Author(s): Blakeley JA, Ribeiro V. Source: Complementary Therapies in Medicine. 2002 September; 10(3): 154-60. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12568144&dopt=Abstract
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Absorption, distribution, metabolism and excretion of glucosamine sulfate. A review. Author(s): Setnikar I, Rovati LC. Source: Arzneimittel-Forschung. 2001 September; 51(9): 699-725. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11642003&dopt=Abstract
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Active ingredient consistency of commercially available glucosamine sulfate products. Author(s): Russell AS, Aghazadeh-Habashi A, Jamali F. Source: The Journal of Rheumatology. 2002 November; 29(11): 2407-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12415601&dopt=Abstract
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Affected paroxysmal nocturnal hemoglobinuria T lymphocytes harbor a common defect in assembly of N-acetyl-D-glucosamine inositol phospholipid corresponding to that in class A Thy-1- murine lymphoma mutants. Author(s): Armstrong C, Schubert J, Ueda E, Knez JJ, Gelperin D, Hirose S, Silber R, Hollan S, Schmidt RE, Medof ME. Source: The Journal of Biological Chemistry. 1992 December 15; 267(35): 25347-51. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1460030&dopt=Abstract
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Affinity purification of N-acetylglucosamine specific lectins. Purification and partial charactersation of triticale lectin. Author(s): Nadimpalli SK, Kompella P. Source: Biochem Mol Biol Int. 1996 April; 38(5): 1059-66. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9132153&dopt=Abstract
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Ammonium ion and glucosamine dependent increases of oligosaccharide complexity in recombinant glycoproteins secreted from cultivated BHK-21 cells. Author(s): Gawlitzek M, Valley U, Wagner R. Source: Biotechnology and Bioengineering. 1998 March 5; 57(5): 518-28. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10099230&dopt=Abstract
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Antibodies from patients with psoriasis recognize N-acetylglucosamine terminals in glycoproteins from Pityrosporum ovale. Author(s): Mathov I, Plotkin L, Abatangelo C, Galimberti R, Squiquera L, Leoni J. Source: Clinical and Experimental Immunology. 1996 July; 105(1): 79-83. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8697640&dopt=Abstract
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Antibodies to N-acetylglucosamine and heparin in acute and remission phases of rheumatic fever. Author(s): Shastry P, Iyer SV, Jambotkar SM, Kandoth PW, Kinare SG. Source: J Clin Lab Immunol. 1991 June; 35(2): 65-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1668760&dopt=Abstract
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Are glucosamine and chondroitin effective in treating osteoarthritis? Author(s): Denham AC, Newton WP. Source: The Journal of Family Practice. 2000 June; 49(6): 571-2. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10923559&dopt=Abstract
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Asthma exacerbation associated with glucosamine-chondroitin supplement. Author(s): Tallia AF, Cardone DA. Source: The Journal of the American Board of Family Practice / American Board of Family Practice. 2002 November-December; 15(6): 481-4. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12463294&dopt=Abstract
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Biosynthesis of N-acetylneuraminic acid in cells lacking UDP-N-acetylglucosamine 2epimerase/N-acetylmannosamine kinase. Author(s): Hinderlich S, Berger M, Keppler OT, Pawlita M, Reutter W. Source: Biological Chemistry. 2001 February; 382(2): 291-7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11308027&dopt=Abstract
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Bisected N-acetylglucosamine residue of biantennary sugar chains and highmolecular-weight oligosaccharides of neuroblastoma cell membranes. Author(s): Motoyoshi F, Kondo N, Orii T. Source: Tumour Biology : the Journal of the International Society for Oncodevelopmental Biology and Medicine. 1993; 14(6): 334-7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8265979&dopt=Abstract
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Bisecting N-acetylglucosamine on K562 cells suppresses natural killer cytotoxicity and promotes spleen colonization. Author(s): Yoshimura M, Ihara Y, Ohnishi A, Ijuhin N, Nishiura T, Kanakura Y, Matsuzawa Y, Taniguchi N. Source: Cancer Research. 1996 January 15; 56(2): 412-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8542600&dopt=Abstract
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Campylobacter jejuni strains from patients with Guillain-Barre syndrome belong mostly to Penner serogroup 19 and contain beta-N-acetylglucosamine residues. Author(s): Kuroki S, Saida T, Nukina M, Haruta T, Yoshioka M, Kobayashi Y, Nakanishi H. Source: Annals of Neurology. 1993 March; 33(3): 243-7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8498807&dopt=Abstract
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Characterization of 20K fimbria, a new adhesin of septicemic and diarrhea-associated Escherichia coli strains, that belongs to a family of adhesins with N-acetyl-Dglucosamine recognition. Author(s): Bertin Y, Girardeau JP, Darfeuille-Michaud A, Contrepois M. Source: Infection and Immunity. 1996 January; 64(1): 332-42. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8557360&dopt=Abstract
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Characterization of a mouse monoclonal antibody specific for O-linked Nacetylglucosamine. Author(s): Comer FI, Vosseller K, Wells L, Accavitti MA, Hart GW. Source: Analytical Biochemistry. 2001 June 15; 293(2): 169-77. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11399029&dopt=Abstract
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Characterization of a sustained-release delivery system for combined cytokine/peptide vaccination using a poly-N-acetyl glucosamine-based polymer matrix. Author(s): Cole DJ, Gattoni-Celli S, McClay EF, Metcalf JS, Brown JM, Nabavi N, Newton DA 3rd, Woolhiser CB, Wilson MC, Vournakis JN. Source: Clinical Cancer Research : an Official Journal of the American Association for Cancer Research. 1997 June; 3(6): 867-73. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9815761&dopt=Abstract
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Characterization of an N-acetylglucosamine-6-O-sulfotransferase from human respiratory mucosa active on mucin carbohydrate chains. Author(s): Degroote S, Lo-Guidice JM, Strecker G, Ducourouble MP, Roussel P, Lamblin G. Source: The Journal of Biological Chemistry. 1997 November 21; 272(47): 29493-501. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9368010&dopt=Abstract
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Chondroprotective agents: glucosamine and chondroitin. Author(s): Hungerford MW, Valaik D. Source: Foot Ankle Clin. 2003 June; 8(2): 201-19. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12911236&dopt=Abstract
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Circulating malignant lymphocytes from Sezary syndrome express high level of glycoproteins carrying beta (1-6)N-acetylglucosamine-branched N-linked oligosaccharides. Author(s): Derappe C, Haentjens G, Lemaire S, Feugeas JP, Lebbe C, Pasqualetto V, Bussel A, Aubery M, Neel D. Source: Leukemia : Official Journal of the Leukemia Society of America, Leukemia Research Fund, U.K. 1996 January; 10(1): 138-41. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8558919&dopt=Abstract
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Cloning, sequencing, and expression analysis of mouse glucosamine-6-phosphate deaminase (GNPDA/oscillin). Author(s): Amireault P, Dube F. Source: Molecular Reproduction and Development. 2000 July; 56(3): 424-35. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10862010&dopt=Abstract
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Comment: glucosamine: selecting appropriate study exclusion criteria. Author(s): Barclay TS, Tsourounis C, McCart GM. Source: The Annals of Pharmacotherapy. 1998 December; 32(12): 1371-2. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9876825&dopt=Abstract
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Comparative metabolism of 3H-glucosamine by fibroblast populations exposed to cyclosporine. Author(s): Zebrowski EJ, Pylypas SP, Odlum O, Johnson RB. Source: J Periodontol. 1994 June; 65(6): 565-7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8083787&dopt=Abstract
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Complex-type N-linked oligosaccharides of gp120 from human immunodeficiency virus type 1 contain sulfated N-acetylglucosamine. Author(s): Shilatifard A, Merkle RK, Helland DE, Welles JL, Haseltine WA, Cummings RD. Source: Journal of Virology. 1993 February; 67(2): 943-52. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8419650&dopt=Abstract
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Conservative management of spinal osteoarthritis with glucosamine sulfate and chiropractic treatment. Author(s): Gottlieb MS. Source: Journal of Manipulative and Physiological Therapeutics. 1997 July-August; 20(6): 400-14. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9272473&dopt=Abstract
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Correlation between radiographic severity of knee osteoarthritis and future disease progression. Results from a 3-year prospective, placebo-controlled study evaluating the effect of glucosamine sulfate. Author(s): Bruyere O, Honore A, Ethgen O, Rovati LC, Giacovelli G, Henrotin YE, Seidel L, Reginster JY. Source: Osteoarthritis and Cartilage / Oars, Osteoarthritis Research Society. 2003 January; 11(1): 1-5. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12505481&dopt=Abstract
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Cytokeratin peptide SFGSGFGGGY mimics N-acetyl-beta-D-glucosamine in reaction with antibodies and lectins, and induces in vivo anti-carbohydrate antibody response. Author(s): Shikhman AR, Greenspan NS, Cunningham MW. Source: Journal of Immunology (Baltimore, Md. : 1950). 1994 December 15; 153(12): 5593606. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7527445&dopt=Abstract
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Decreased incorporation of D-glucosamine into glycosphingolipids of intact Familial Dysautonomia lymphoblasts. Author(s): Strasberg PM, Novak A, Warren IB. Source: Journal of Molecular Neuroscience : Mn. 1995; 6(2): 121-30. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8746450&dopt=Abstract
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Detection of glycosylation abnormality in rheumatoid IgG using Nacetylglucosamine-specific Psathyrella velutina lectin. Author(s): Tsuchiya N, Endo T, Matsuta K, Yoshinoya S, Takeuchi F, Nagano Y, Shiota M, Furukawa K, Kochibe N, Ito K, et al. Source: Journal of Immunology (Baltimore, Md. : 1950). 1993 July 15; 151(2): 1137-46. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8335895&dopt=Abstract
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Detection of O-linked N-acetylglucosamine (O-GlcNAc) on cytoplasmic and nuclear proteins. Author(s): Roquemore EP, Chou TY, Hart GW. Source: Methods Enzymol. 1994; 230: 443-60. No Abstract Available. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8139512&dopt=Abstract
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Determining the efficacy of glucosamine and chondroitin for osteoarthritis. Author(s): O'Rourke M. Source: The Nurse Practitioner. 2001 June; 26(6): 44-6, 49-52. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11416939&dopt=Abstract
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D-glucosamine propanedithioacetal, an efficient chiral auxiliary in beta-lactam chemistry. Author(s): Anaya J, Gero SD, Grande M, Hernando JI, Laso NM. Source: Bioorganic & Medicinal Chemistry. 1999 May; 7(5): 837-50. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10400337&dopt=Abstract
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Diagnosis and carrier detection of Tay-Sachs disease: direct determination of hexosaminidase A using 4-methylumbelliferyl derivatives of beta-Nacetylglucosamine-6-sulfate and beta-N-acetylgalactosamine-6-sulfate. Author(s): Ben-Yoseph Y, Reid JE, Shapiro B, Nadler HL. Source: American Journal of Human Genetics. 1985 July; 37(4): 733-40. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9556661&dopt=Abstract
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Differences in metabolism of 5-fluorouracil and 5-fluorouridine and regulation by glucosamine in human colon cancer multicell tumor spheroids. Author(s): Chen TB, Bajzer Z, Macura S, Vuk-Pavlovic S. Source: Nmr in Biomedicine. 1999 May; 12(3): 157-67. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10414950&dopt=Abstract
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D-mannose and N-acetylglucosamine moieties and their respective binding sites in salivary glands of Sjogren's syndrome. Author(s): Steinfeld S, Penaloza A, Ribai P, Decaestecker C, Danguy A, Gabius HJ, Salmon I, Appelboom T, Kiss R. Source: The Journal of Rheumatology. 1999 April; 26(4): 833-41. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10229404&dopt=Abstract
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Do glucosamine and chondroitin treat the symptoms of osteoarthritis? Author(s): Edelist DD, Evans MF. Source: Can Fam Physician. 2001 February; 47: 275-7. No Abstract Available. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11228027&dopt=Abstract
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Do glucosamine or chondroitin cause regeneration of cartilage in osteoarthritis? Author(s): Priebe D, McDiarmid T, Mackler L, Tudiver F. Source: The Journal of Family Practice. 2003 March; 52(3): 237-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12620182&dopt=Abstract
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Does glucosamine relieve arthritis joint pain? Author(s): Miller DC, Richardson J. Source: The Journal of Family Practice. 2003 August; 52(8): 645-7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12899824&dopt=Abstract
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Does glucosamine sulfate affect progression of symptoms and joint structure changes in osteoarthritis? Author(s): Carter IR. Source: The Journal of Family Practice. 2001 May; 50(5): 394. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11350698&dopt=Abstract
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Effect of glucosamine hydrochloride in the treatment of pain of osteoarthritis of the knee. Author(s): Houpt JB, McMillan R, Wein C, Paget-Dellio SD. Source: The Journal of Rheumatology. 1999 November; 26(11): 2423-30. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10555905&dopt=Abstract
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Effect of okadaic acid on O-linked N-acetylglucosamine levels in a neuroblastoma cell line. Author(s): Lefebvre T, Alonso C, Mahboub S, Dupire MJ, Zanetta JP, Caillet-Boudin ML, Michalski JC. Source: Biochimica Et Biophysica Acta. 1999 October 18; 1472(1-2): 71-81. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10572927&dopt=Abstract
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Effects of ammonia and glucosamine on the heterogeneity of erythropoietin glycoforms. Author(s): Yang M, Butler M. Source: Biotechnology Progress. 2002 January-February; 18(1): 129-38. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11822911&dopt=Abstract
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Effects of glucosamine infusion on insulin secretion and insulin action in humans. Author(s): Monauni T, Zenti MG, Cretti A, Daniels MC, Targher G, Caruso B, Caputo M, McClain D, Del Prato S, Giaccari A, Muggeo M, Bonora E, Bonadonna RC. Source: Diabetes. 2000 June; 49(6): 926-35. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10866044&dopt=Abstract
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Effects of nucleotides on N-acetyl-d-glucosamine 2-epimerases (renin-binding proteins): comparative biochemical studies. Author(s): Takahashi S, Hori K, Takahashi K, Ogasawara H, Tomatsu M, Saito K. Source: Journal of Biochemistry. 2001 December; 130(6): 815-21. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11726282&dopt=Abstract
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Effects of overexpression of glutamine:fructose-6-phosphate amidotransferase (GFAT) and glucosamine treatment on translocation of GLUT4 in rat adipose cells. Author(s): Chen H, Ing BL, Robinson KA, Feagin AC, Buse MG, Quon MJ. Source: Molecular and Cellular Endocrinology. 1997 November 30; 135(1): 67-77. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9453242&dopt=Abstract
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Efficacy and safety of glucosamine sulfate versus ibuprofen in patients with knee osteoarthritis. Author(s): Qiu GX, Gao SN, Giacovelli G, Rovati L, Setnikar I. Source: Arzneimittel-Forschung. 1998 May; 48(5): 469-74. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9638313&dopt=Abstract
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Efficacy and safety of intramuscular glucosamine sulfate in osteoarthritis of the knee. A randomised, placebo-controlled, double-blind study. Author(s): Reichelt A, Forster KK, Fischer M, Rovati LC, Setnikar I. Source: Arzneimittel-Forschung. 1994 January; 44(1): 75-80. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8135881&dopt=Abstract
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Efficacy of a combination of FCHG49 glucosamine hydrochloride, TRH122 low molecular weight sodium chondroitin sulfate and manganese ascorbate in the management of knee osteoarthritis. Author(s): Das A Jr, Hammad TA. Source: Osteoarthritis and Cartilage / Oars, Osteoarthritis Research Society. 2000 September; 8(5): 343-50. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10966840&dopt=Abstract
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Efficacy of glucosamine and chondroitin for treatment of osteoarthritis. Author(s): Donohoe M. Source: Jama : the Journal of the American Medical Association. 2000 September 13; 284(10): 1241; Author Reply 1242. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10979100&dopt=Abstract
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Efficacy of glucosamine and chondroitin for treatment of osteoarthritis. Author(s): Mautone G. Source: Jama : the Journal of the American Medical Association. 2000 September 13; 284(10): 1241; Author Reply 1242. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10979099&dopt=Abstract
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Elution of glomerular bound C3 by glucosamine in a case of acute glomerulonephritis. Author(s): Evans DJ. Source: Nephrology, Dialysis, Transplantation : Official Publication of the European Dialysis and Transplant Association - European Renal Association. 2000 July; 15(7): 1096-7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10862661&dopt=Abstract
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Endothelial heparan sulfate proteoglycans that bind to L-selectin have glucosamine residues with unsubstituted amino groups. Author(s): Norgard-Sumnicht K, Varki A. Source: The Journal of Biological Chemistry. 1995 May 19; 270(20): 12012-24. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7538130&dopt=Abstract
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Enhanced synovial production of hyaluronic acid may explain rapid clinical response to high-dose glucosamine in osteoarthritis. Author(s): McCarty MF. Source: Medical Hypotheses. 1998 June; 50(6): 507-10. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9710325&dopt=Abstract
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Enzyme-linked lectinsorbent assay measures N-acetyl-D-glucosamine in matrix of biofilm produced by Staphylococcus epidermidis. Author(s): Thomas VL, Sanford BA, Moreno R, Ramsay MA. Source: Current Microbiology. 1997 October; 35(4): 249-54. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9290068&dopt=Abstract
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Epitope mapping and tight-binding inhibition with monoclonal antibodies directed against Escherichia coli glucosamine 6-phosphate synthase. Author(s): Cochet O, Badet-Denisot MA, Teillaud JL, Badet B. Source: Archives of Biochemistry and Biophysics. 1995 December 20; 324(2): 391-400. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8554332&dopt=Abstract
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Evaluation of glucosamine sulfate compared to ibuprofen for the treatment of temporomandibular joint osteoarthritis: a randomized double blind controlled 3 month clinical trial. Author(s): Thie NM, Prasad NG, Major PW. Source: The Journal of Rheumatology. 2001 June; 28(6): 1347-55. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11409130&dopt=Abstract
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From Lobry de Bruyn to enzyme-catalyzed ammonia channelling: molecular studies of D-glucosamine-6P synthase. Author(s): Teplyakov A, Leriche C, Obmolova G, Badet B, Badet-Denisot MA. Source: Natural Product Reports. 2002 February; 19(1): 60-9. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11902440&dopt=Abstract
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From oranges and lemons to glucosamine and chondroitin sulfate: clinical observations stimulate basic research. Author(s): Buckwalter JA, Callaghan JJ, Rosier RN. Source: The Journal of Bone and Joint Surgery. American Volume. 2001 August; 83-A(8): 1266-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11507135&dopt=Abstract
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Functional expression and genomic structure of human N-acetylglucosamine-6-Osulfotransferase that transfers sulfate to beta-N-acetylglucosamine at the nonreducing end of an N-acetyllactosamine sequence. Author(s): Sakaguchi H, Kitagawa H, Sugahara K. Source: Biochimica Et Biophysica Acta. 2000 October 18; 1523(2-3): 269-76. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11042394&dopt=Abstract
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Functional interaction between the Ser/Thr kinase PKL12 and N-acetylglucosamine kinase, a prominent enzyme implicated in the salvage pathway for GlcNAc recycling. Author(s): Ligos JM, de Lera TL, Hinderlich S, Guinea B, Sanchez L, Roca R, Valencia A, Bernad A. Source: The Journal of Biological Chemistry. 2002 February 22; 277(8): 6333-43. Epub 2001 December 12. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11741987&dopt=Abstract
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Gene transfection-mediated overexpression of beta1,4-N-acetylglucosamine bisecting oligosaccharides in glioma cell line U373 MG inhibits epidermal growth factor receptor function. Author(s): Rebbaa A, Yamamoto H, Saito T, Meuillet E, Kim P, Kersey DS, Bremer EG, Taniguchi N, Moskal JR. Source: The Journal of Biological Chemistry. 1997 April 4; 272(14): 9275-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9083062&dopt=Abstract
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Generation of anti-factor Xa active, 3-O-sulfated glucosamine-rich sequences by controlled desulfation of oversulfated heparins. Author(s): Naggi A, De Cristofano B, Bisio A, Torri G, Casu B. Source: Carbohydrate Research. 2001 December 7; 336(4): 283-90. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11728396&dopt=Abstract
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Glucosamine 6-phosphate deaminase in normal human erythrocytes. Author(s): Weidanz JA, Campbell P, DeLucas LJ, Jin J, Moore D, Roden L, Yu H, Heilmann E, Vezza AC. Source: British Journal of Haematology. 1995 September; 91(1): 72-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7577655&dopt=Abstract
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Glucosamine and chondroitin for osteoarthritis. Author(s): Akama H, Saito S. Source: Arthritis and Rheumatism. 2001 February; 45(1): 107. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11308055&dopt=Abstract
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Glucosamine and chondroitin for osteoarthritis? Author(s): McAlindon T. Source: Bulletin on the Rheumatic Diseases. 2001 July; 50(7): 1-4. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11530541&dopt=Abstract
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Glucosamine and chondroitin for treating symptoms of osteoarthritis: evidence is widely touted but incomplete. Author(s): Towheed TE, Anastassiades TP. Source: Jama : the Journal of the American Medical Association. 2000 March 15; 283(11): 1483-4. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10732941&dopt=Abstract
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Glucosamine and chondroitin for treatment of osteoarthritis: a systematic quality assessment and meta-analysis. Author(s): McAlindon TE, LaValley MP, Gulin JP, Felson DT. Source: Jama : the Journal of the American Medical Association. 2000 March 15; 283(11): 1469-75. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10732937&dopt=Abstract
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Glucosamine and chondroitin may help in osteoarthritis. Author(s): Walker-Bone K, Javid K, Arden N, Cooper C. Source: Bmj (Clinical Research Ed.). 2001 March 17; 322(7287): 673. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11250841&dopt=Abstract
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Glucosamine and chondroitin sulfate are effective in the management of osteoarthritis. Author(s): Hungerford DS, Jones LC. Source: The Journal of Arthroplasty. 2003 April; 18(3 Suppl 1): 5-9. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12730919&dopt=Abstract
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Glucosamine and chondroitin sulfate for the treatment of osteoarthritis: comment on the article by Akama and Saito. Author(s): Leeb BF. Source: Arthritis and Rheumatism. 2001 December; 45(6): 537-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11762688&dopt=Abstract
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Glucosamine and chondroitin sulfates in the treatment of osteoarthritis: a survey. Author(s): de los Reyes GC, Koda RT, Lien EJ. Source: Prog Drug Res. 2000; 55: 81-103. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11127967&dopt=Abstract
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Glucosamine and chondroitin were found to improve outcomes in patients with osteoarthritis. Author(s): Kreder HJ. Source: The Journal of Bone and Joint Surgery. American Volume. 2000 September; 82(9): 1323. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11005524&dopt=Abstract
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Glucosamine and osteoarthritis. Author(s): Innis J. Source: The Nurse Practitioner. 2000 September; 25(9): 96-7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11016044&dopt=Abstract
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Glucosamine for arthritis. Author(s): Keller L. Source: Adv Nurse Pract. 2003 June; 11(6): 19-21, 100. Review. No Abstract Available. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12807050&dopt=Abstract
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Glucosamine for migraine prophylaxis? Author(s): Russell AL, McCarty MF. Source: Medical Hypotheses. 2000 September; 55(3): 195-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10985908&dopt=Abstract
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Glucosamine for osteoarthritis. Author(s): Blake G. Source: Adv Nurse Pract. 2002 August; 10(8): 26-7. Review. No Abstract Available. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12425186&dopt=Abstract
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Glucosamine for osteoarthritis. Patients' welfare should be primary concern. Author(s): Sonnino D. Source: Bmj (Clinical Research Ed.). 2001 October 27; 323(7319): 1003; Author Reply 1004. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11700629&dopt=Abstract
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Glucosamine for osteoarthritis. Sound science might have helped avoid confusion. Author(s): Setnikar I. Source: Bmj (Clinical Research Ed.). 2001 October 27; 323(7319): 1003-4. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11700628&dopt=Abstract
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Glucosamine for osteoarthritis: cure or conundrum? Author(s): Heyneman CA, Rhodes RS. Source: The Annals of Pharmacotherapy. 1998 May; 32(5): 602-3. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9606482&dopt=Abstract
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Glucosamine for osteoarthritis: magic, hype, or confusion? It's probably safe-but there's no good evidence that it works. Author(s): Chard J, Dieppe P. Source: Bmj (Clinical Research Ed.). 2001 June 16; 322(7300): 1439-40. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11408287&dopt=Abstract
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Glucosamine for psoriasis? Author(s): McCarty MF. Source: Medical Hypotheses. 1997 May; 48(5): 437-41. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9185133&dopt=Abstract
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Glucosamine for wound healing. Author(s): McCarty MF. Source: Medical Hypotheses. 1996 October; 47(4): 273-5. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8910875&dopt=Abstract
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Glucosamine HCl reduces equine articular cartilage degradation in explant culture. Author(s): Fenton JI, Chlebek-Brown KA, Peters TL, Caron JP, Orth MW. Source: Osteoarthritis and Cartilage / Oars, Osteoarthritis Research Society. 2000 July; 8(4): 258-65. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10903879&dopt=Abstract
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Glucosamine in osteoarthritis and gastrointestinal disorders: an exemplar of the need for a paradigm shift. Author(s): Russell AL. Source: Medical Hypotheses. 1998 October; 51(4): 347-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9824843&dopt=Abstract
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Glucosamine in osteoarthritis. Author(s): Russell AI, McCarty MF. Source: Lancet. 1999 November 6; 354(9190): 1641; Author Reply 1641-2. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10560695&dopt=Abstract
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Glucosamine in osteoarthritis. Author(s): Cumming A. Source: Lancet. 1999 November 6; 354(9190): 1640-1; Author Reply 1641-2. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10560694&dopt=Abstract
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Glucosamine in osteoarthritis. Author(s): Rovati LC, Annefeld M, Giacovelli G, Schmid K, Setnikar I. Source: Lancet. 1999 November 6; 354(9190): 1640; Author Reply 1641-2. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10560693&dopt=Abstract
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Glucosamine in serum of patients after myocardial infarction subjected to rehabilitation training. Author(s): Nowak A, Szczesniak L, Rychlewski T, Dylewicz P, Karolkiewicz J. Source: Journal of Physiology and Pharmacology : an Official Journal of the Polish Physiological Society. 1998 June; 49(2): 293-301. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9670112&dopt=Abstract
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Glucosamine in the treatment of osteoarthritis. Author(s): Delafuente JC. Source: Rheumatic Diseases Clinics of North America. 2000 February; 26(1): 1-11, Vii. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10680190&dopt=Abstract
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Glucosamine induces resistance to insulin-like growth factor I (IGF-I) and insulin in Hep G2 cell cultures: biological significance of IGF-I/insulin hybrid receptors. Author(s): Sakai K, Clemmons DR. Source: Endocrinology. 2003 June; 144(6): 2388-95. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12746299&dopt=Abstract
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Glucosamine inhibits glucokinase in vitro and produces a glucose-specific impairment of in vivo insulin secretion in rats. Author(s): Balkan B, Dunning BE. Source: Diabetes. 1994 October; 43(10): 1173-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7926284&dopt=Abstract
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Glucosamine inhibits IL-1beta-induced NFkappaB activation in human osteoarthritic chondrocytes. Author(s): Largo R, Alvarez-Soria MA, Diez-Ortego I, Calvo E, Sanchez-Pernaute O, Egido J, Herrero-Beaumont G. Source: Osteoarthritis and Cartilage / Oars, Osteoarthritis Research Society. 2003 April; 11(4): 290-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12681956&dopt=Abstract
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Glucosamine levels in people with ischaemic heart disease with and without type II diabetes. Author(s): Nowak A, Szczesniak L, Rychlewski T, Dylewicz P, Przywarska I. Source: Pol Arch Med Wewn. 1998 November; 100(5): 419-25. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10410575&dopt=Abstract
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Glucosamine may retard atherogenesis by promoting endothelial production of heparan sulfate proteoglycans. Author(s): McCarty MF. Source: Medical Hypotheses. 1997 March; 48(3): 245-51. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9140889&dopt=Abstract
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Glucosamine regulation of glucose metabolism in cultured human skeletal muscle cells: divergent effects on glucose transport/phosphorylation and glycogen synthase in non-diabetic and type 2 diabetic subjects. Author(s): Ciaraldi TP, Carter L, Nikoulina S, Mudaliar S, McClain DA, Henry RR. Source: Endocrinology. 1999 September; 140(9): 3971-80. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10465266&dopt=Abstract
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Glucosamine sulfate compared to ibuprofen in osteoarthritis of the knee. Author(s): Muller-Fassbender H, Bach GL, Haase W, Rovati LC, Setnikar I. Source: Osteoarthritis and Cartilage / Oars, Osteoarthritis Research Society. 1994 March; 2(1): 61-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11548225&dopt=Abstract
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Glucosamine sulfate does not crossreact with the antibodies of patients with heparininduced thrombocytopenia. Author(s): Weimann G, Lubenow N, Selleng K, Eichler P, Albrecht D, Greinacher A. Source: European Journal of Haematology. 2001 March; 66(3): 195-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11350488&dopt=Abstract
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Glucosamine sulfate for osteoarthritis. Author(s): da Camara CC, Dowless GV. Source: The Annals of Pharmacotherapy. 1998 May; 32(5): 580-7. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9606480&dopt=Abstract
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Glucosamine sulfate in osteoarthritis of the knee. Author(s): Noack W, Fischer M, Forster KK, Rovati LC, Setnikar I. Source: Osteoarthritis and Cartilage / Oars, Osteoarthritis Research Society. 1994 March; 2(1): 51-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11548224&dopt=Abstract
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Glucosamine sulfate modulates dysregulated activities of human osteoarthritic chondrocytes in vitro. Author(s): Piperno M, Reboul P, Hellio Le Graverand MP, Peschard MJ, Annefeld M, Richard M, Vignon E. Source: Osteoarthritis and Cartilage / Oars, Osteoarthritis Research Society. 2000 May; 8(3): 207-12. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10806048&dopt=Abstract
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Glucosamine sulfate modulates the levels of aggrecan and matrix metalloproteinase-3 synthesized by cultured human osteoarthritis articular chondrocytes. Author(s): Dodge GR, Jimenez SA. Source: Osteoarthritis and Cartilage / Oars, Osteoarthritis Research Society. 2003 June; 11(6): 424-32. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12801482&dopt=Abstract
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Glucosamine sulfate use and delay of progression of knee osteoarthritis: a 3-year, randomized, placebo-controlled, double-blind study. Author(s): Pavelka K, Gatterova J, Olejarova M, Machacek S, Giacovelli G, Rovati LC. Source: Archives of Internal Medicine. 2002 October 14; 162(18): 2113-23. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12374520&dopt=Abstract
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Glucosamine sulfate use in osteoarthritis. Author(s): Runkel DR, Cupp MJ. Source: American Journal of Health-System Pharmacy : Ajhp : Official Journal of the American Society of Health-System Pharmacists. 1999 February 1; 56(3): 267-9. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10030516&dopt=Abstract
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Glucosamine sulphate and osteoarthritis. Author(s): Payne RB. Source: Lancet. 2001 May 19; 357(9268): 1617; Author Reply 1618. Erratum In: Lancet 2001 September 22; 358(9286): 1018. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11386312&dopt=Abstract
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Glucosamine sulphate and osteoarthritis. Author(s): Swinburne LM. Source: Lancet. 2001 May 19; 357(9268): 1617; Author Reply 1618. Erratum In: Lancet 2001 September 22; 358(9286): 1018. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11386311&dopt=Abstract
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Glucosamine sulphate and osteoarthritis. Author(s): Halbekath J, Lehnert R, Wille H. Source: Lancet. 2001 May 19; 357(9268): 1617; Author Reply 1618. Erratum In: Lancet 2001 September 22; 358(9286): 1018. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11386310&dopt=Abstract
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Glucosamine sulphate and osteoarthritis. Author(s): Goldstein MR. Source: Lancet. 2001 May 19; 357(9268): 1617-8. Erratum In: Lancet 2001 September 22; 358(9286): 1018. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11386309&dopt=Abstract
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Glucosamine therapy compared to ibuprofen for joint pain. Author(s): Ruane R, Griffiths P. Source: British Journal of Community Nursing. 2002 March; 7(3): 148-52. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11904551&dopt=Abstract
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Glucosamine therapy for osteoarthritis. Author(s): Towheed TE, Anastassiades TP. Source: The Journal of Rheumatology. 1999 November; 26(11): 2294-7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10555879&dopt=Abstract
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Glucosamine therapy for treating osteoarthritis. Author(s): Towheed TE, Anastassiades TP, Shea B, Houpt J, Welch V, Hochberg MC. Source: Cochrane Database Syst Rev. 2001; (1): Cd002946. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11279782&dopt=Abstract
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Glucosamine therapy: does it work? Author(s): Bellamy N, Lybrand SG. Source: The Medical Journal of Australia. 2001 October 15; 175(8): 399-400. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11700830&dopt=Abstract
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Glucosamine, chondroitin, and manganese ascorbate for degenerative joint disease of the knee or low back: a randomized, double-blind, placebo-controlled pilot study. Author(s): Leffler CT, Philippi AF, Leffler SG, Mosure JC, Kim PD. Source: Military Medicine. 1999 February; 164(2): 85-91. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10050562&dopt=Abstract
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Glucosamine. Author(s): Barclay TS, Tsourounis C, McCart GM. Source: The Annals of Pharmacotherapy. 1998 May; 32(5): 574-9. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9606479&dopt=Abstract
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Glucosamine. A nutraceutical in osteoarthritis. Author(s): Phoon S, Manolios N. Source: Aust Fam Physician. 2002 June; 31(6): 539-41. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12154601&dopt=Abstract
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Glucosamine: con or cure? Author(s): Sutton L, Rapport L, Lockwood B. Source: Nutrition (Burbank, Los Angeles County, Calif.). 2002 June; 18(6): 534-6. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12044832&dopt=Abstract
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Glucosamine: con or cure? Part II. Author(s): Sutton L, Rapport L, Lockwood B. Source: Nutrition (Burbank, Los Angeles County, Calif.). 2002 July-August; 18(7-8): 693. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12093462&dopt=Abstract
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Glucosamine:fructose-6-phosphate aminotransferase: gene characterization, chitin biosynthesis and peritrophic matrix formation in Aedes aegypti. Author(s): Kato N, Dasgupta R, Smartt CT, Christensen BM. Source: Insect Molecular Biology. 2002 June; 11(3): 207-16. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12000639&dopt=Abstract
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Glucosamine-6-phosphate deaminase from beef kidney is an allosteric system of the V-type. Author(s): Lara-Lemus R, Calcagno ML. Source: Biochimica Et Biophysica Acta. 1998 October 14; 1388(1): 1-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9774701&dopt=Abstract
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Glucosamine-6-phosphate synthase--the multi-facets enzyme. Author(s): Milewski S. Source: Biochimica Et Biophysica Acta. 2002 June 3; 1597(2): 173-92. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12044898&dopt=Abstract
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Glucosamine-induced inhibition of liver glucokinase impairs the ability of hyperglycemia to suppress endogenous glucose production. Author(s): Barzilai N, Hawkins M, Angelov I, Hu M, Rossetti L. Source: Diabetes. 1996 October; 45(10): 1329-35. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8826967&dopt=Abstract
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GLUT2 is a high affinity glucosamine transporter. Author(s): Uldry M, Ibberson M, Hosokawa M, Thorens B. Source: Febs Letters. 2002 July 31; 524(1-3): 199-203. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12135767&dopt=Abstract
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Glycan-dependent signaling: O-linked N-acetylglucosamine. Author(s): Hanover JA. Source: The Faseb Journal : Official Publication of the Federation of American Societies for Experimental Biology. 2001 September; 15(11): 1865-76. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11532966&dopt=Abstract
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Glycoengineering of therapeutic glycoproteins: in vitro galactosylation and sialylation of glycoproteins with terminal N-acetylglucosamine and galactose residues. Author(s): Raju TS, Briggs JB, Chamow SM, Winkler ME, Jones AJ. Source: Biochemistry. 2001 July 31; 40(30): 8868-76. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11467948&dopt=Abstract
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Glycosylation of mammalian neurofilaments. Localization of multiple O-linked Nacetylglucosamine moieties on neurofilament polypeptides L and M. Author(s): Dong DL, Xu ZS, Chevrier MR, Cotter RJ, Cleveland DW, Hart GW. Source: The Journal of Biological Chemistry. 1993 August 5; 268(22): 16679-87. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8344946&dopt=Abstract
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Grappling with the “miracle” of glucosamine. Author(s): Di Fabio RP. Source: The Journal of Orthopaedic and Sports Physical Therapy. 1999 August; 29(8): 442-3. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10681146&dopt=Abstract
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Harvard symposium on the clinical efficacy and hemostatic mechanism of action of poly-N-acetyl glucosamine. Author(s): Hirsch JA. Source: J Invasive Cardiol. 2003 September; 15(9): 1-4. No Abstract Available. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=14526795&dopt=Abstract
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Heparin's anti-inflammatory effects require glucosamine 6-O-sulfation and are mediated by blockade of L- and P-selectins. Author(s): Wang L, Brown JR, Varki A, Esko JD. Source: The Journal of Clinical Investigation. 2002 July; 110(1): 127-36. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12093896&dopt=Abstract
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High expression of UDP-N-acetylglucosamine: beta-D mannoside beta-1,4-Nacetylglucosaminyltransferase III (GnT-III) in chronic myelogenous leukemia in blast crisis. Author(s): Yoshimura M, Nishikawa A, Ihara Y, Nishiura T, Nakao H, Kanayama Y, Matuzawa Y, Taniguchi N. Source: International Journal of Cancer. Journal International Du Cancer. 1995 February 8; 60(4): 443-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7829256&dopt=Abstract
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High molecular weight microtubule-associated proteins contain O-linked-Nacetylglucosamine. Author(s): Ding M, Vandre DD. Source: The Journal of Biological Chemistry. 1996 May 24; 271(21): 12555-61. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8647865&dopt=Abstract
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Histochemical reactivity of normal, metaplastic, and neoplastic tissues to alphalinked N-acetylglucosamine residue-specific monoclonal antibody HIK1083. Author(s): Nakamura N, Ota H, Katsuyama T, Akamatsu T, Ishihara K, Kurihara M, Hotta K. Source: The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society. 1998 July; 46(7): 793-801. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9632738&dopt=Abstract
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Human glucosamine-6-phosphate isomerase, a homologue of hamster oscillin, does not appear to be involved in Ca2+ release in mammalian oocytes. Author(s): Wolny YM, Fissore RA, Wu H, Reis MM, Colombero LT, Ergun B, Rosenwaks Z, Palermo GD. Source: Molecular Reproduction and Development. 1999 March; 52(3): 277-87. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10206659&dopt=Abstract
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Human glucosamine-6-sulphatase deficiency. Diagnostic enzymology towards heparin-derived trisaccharide substrates. Author(s): Freeman C, Hopwood JJ. Source: The Biochemical Journal. 1992 March 1; 282 ( Pt 2): 605-14. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1546976&dopt=Abstract
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Human renin-binding protein is the enzyme N-acetyl-D-glucosamine 2-epimerase. Author(s): Takahashi S, Takahashi K, Kaneko T, Ogasawara H, Shindo S, Kobayashi M. Source: Journal of Biochemistry. 1999 February; 125(2): 348-53. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9990133&dopt=Abstract
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Hype about glucosamine. Author(s): Adams ME. Source: Lancet. 1999 July 31; 354(9176): 353-4. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10437858&dopt=Abstract
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Identification and characterization of high glucose and glucosamine responsive element in the rat osteopontin promoter. Author(s): Asaumi S, Takemoto M, Yokote K, Ridall AL, Butler WT, Fujimoto M, Kobayashi K, Kawamura H, Take A, Saito Y, Mori S. Source: Journal of Diabetes and Its Complications. 2003 January-February; 17(1): 34-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12505755&dopt=Abstract
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Identification and characterization of N-acetylglucosamine-6-O-sulfate-specific beta1,4-galactosyltransferase in human colorectal mucosa. Author(s): Seko A, Hara-Kuge S, Yonezawa S, Nagata K, Yamashita K. Source: Febs Letters. 1998 December 4; 440(3): 307-10. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9872392&dopt=Abstract
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Identification of a domain conferring nucleotide binding to the N-acetyl-dglucosamine 2-epimerase (Renin binding protein). Author(s): Takahashi S, Ogasawara H, Takahashi K, Hori K, Saito K, Mori K. Source: Journal of Biochemistry. 2002 April; 131(4): 605-10. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11926999&dopt=Abstract
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Identification of cysteine-380 as the essential residue for the human N-acetyl-Dglucosamine 2-epimerase (renin binding protein). Author(s): Takahashi S, Takahashi K, Kaneko T, Ogasawara H, Shindo S, Saito K, Kobayashi M. Source: Journal of Biochemistry. 1999 October; 126(4): 639-42. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10502668&dopt=Abstract
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Identification of Ewing's sarcoma gene product as a glycoprotein using a monoclonal antibody that recognizes an immunodeterminant containing O-linked Nacetylglucosamine moiety. Author(s): Matsuoka Y, Matsuoka Y, Shibata S, Yasuhara N, Yoneda Y. Source: Hybridoma and Hybridomics. 2002 August; 21(4): 233-6. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12193275&dopt=Abstract
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Identification of functionally important cysteine residues of the human reninbinding protein as the enzyme N-acetyl-D-glucosamine 2-epimerase. Author(s): Takahashi S, Takahashi K, Kaneko T, Ogasawara H, Shindo S, Saito K, Kawamura Y. Source: Journal of Biochemistry. 2001 April; 129(4): 529-35. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11275551&dopt=Abstract
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Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier. Author(s): Zhang X, Bennett V. Source: The Journal of Biological Chemistry. 1996 December 6; 271(49): 31391-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8940148&dopt=Abstract
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Identification of two novel Dictyostelium discoideum cysteine proteinases that carry N-acetylglucosamine-1-P-modification. Author(s): Souza GM, Hirai J, Mehta DP, Freeze HH. Source: The Journal of Biological Chemistry. 1995 December 1; 270(48): 28938-45. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7499424&dopt=Abstract
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Identification of two nuclear N-acetylglucosamine-binding proteins. Author(s): Felin M, Doyennette-Moyne MA, Hadj-Sahraoui Y, Aubery M, Hubert J, Seve AP. Source: Journal of Cellular Biochemistry. 1994 December; 56(4): 527-35. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7890811&dopt=Abstract
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Immediate-hypersensitivity reaction to glucosamine sulfate. Author(s): Matheu V, Gracia Bara MT, Pelta R, Vivas E, Rubio M. Source: Allergy. 1999 June; 54(6): 643. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10435483&dopt=Abstract
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Immunological mimicry between N-acetyl-beta-D-glucosamine and cytokeratin peptides. Evidence for a microbially driven anti-keratin antibody response. Author(s): Shikhman AR, Cunningham MW. Source: Journal of Immunology (Baltimore, Md. : 1950). 1994 May 1; 152(9): 4375-87. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7512592&dopt=Abstract
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Immunosuppressive effects of glucosamine. Author(s): Ma L, Rudert WA, Harnaha J, Wright M, Machen J, Lakomy R, Qian S, Lu L, Robbins PD, Trucco M, Giannoukakis N. Source: The Journal of Biological Chemistry. 2002 October 18; 277(42): 39343-9. Epub 2002 August 09. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12176986&dopt=Abstract
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Incidental improvement of breast capsular contracture following treatment of arthritis with glucosamine and chondroitin. Author(s): Skillman JM, Ahmed OA, Rowsell AR. Source: British Journal of Plastic Surgery. 2002 July; 55(5): 454. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12372385&dopt=Abstract
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Increased N-acetyl-beta-glucosaminidase activity in primary breast carcinomas corresponds to a decrease in N-acetylglucosamine containing proteins. Author(s): Slawson C, Pidala J, Potter R. Source: Biochimica Et Biophysica Acta. 2001 September 28; 1537(2): 147-57. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11566258&dopt=Abstract
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Influence of L-fucose attached alpha 1-->6 to the asparagine-linked Nacetylglucosamine on the hydrolysis of the N-glycosidic linkage by human glycosylasparaginase. Author(s): Noronkoski T, Mononen I. Source: Glycobiology. 1997 March; 7(2): 217-20. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9134428&dopt=Abstract
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Inhibition of human HT-29 colon carcinoma cell adhesion by a 4-fluoro-glucosamine analogue. Author(s): Woynarowska B, Dimitroff CJ, Sharma M, Matta KL, Bernacki RJ. Source: Glycoconjugate Journal. 1996 August; 13(4): 663-74. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8872124&dopt=Abstract
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Inhibition of N-acetylglucosamine kinase and N-acetylmannosamine kinase by 3-Omethyl-N-acetyl-D-glucosamine in vitro. Author(s): Zeitler R, Giannis A, Danneschewski S, Henk E, Henk T, Bauer C, Reutter W, Sandhoff K. Source: European Journal of Biochemistry / Febs. 1992 March 15; 204(3): 1165-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1312935&dopt=Abstract
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Inhibition of superoxide anion release from human polymorphonuclear leukocytes by N-acetyl-galactosamine and N-acetyl-glucosamine. Author(s): Kamel M, Alnahdi M. Source: Clinical Rheumatology. 1992 June; 11(2): 254-60. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1319880&dopt=Abstract
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Inhibitory actions of glucosamine, a therapeutic agent for osteoarthritis, on the functions of neutrophils. Author(s): Hua J, Sakamoto K, Nagaoka I. Source: Journal of Leukocyte Biology. 2002 April; 71(4): 632-40. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11927650&dopt=Abstract
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Is glucosamine an effective treatment for osteoarthritic pain? Author(s): Hooper M. Source: Cleve Clin J Med. 2001 June; 68(6): 494-5. Review. No Abstract Available. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11405610&dopt=Abstract
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Isolation, characterization and inactivation of the mouse Mgat3 gene: the bisecting Nacetylglucosamine in asparagine-linked oligosaccharides appears dispensable for viability and reproduction. Author(s): Priatel JJ, Sarkar M, Schachter H, Marth JD. Source: Glycobiology. 1997 February; 7(1): 45-56. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9061364&dopt=Abstract
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Kinetic characterization of human glutamine-fructose-6-phosphate amidotransferase I: potent feedback inhibition by glucosamine 6-phosphate. Author(s): Broschat KO, Gorka C, Page JD, Martin-Berger CL, Davies MS, Huang Hc HC, Gulve EA, Salsgiver WJ, Kasten TP. Source: The Journal of Biological Chemistry. 2002 April 26; 277(17): 14764-70. Epub 2002 February 12. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11842094&dopt=Abstract
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Ligand interactions with E-selectin. Identification of a new binding site for recognition of N-acyl aromatic glucosamine substituents of sialyl Lewis X. Author(s): Ramphal JY, Hiroshige M, Lou B, Gaudino JJ, Hayashi M, Chen SM, Chiang LC, Gaeta FC, DeFrees SA. Source: Journal of Medicinal Chemistry. 1996 March 29; 39(7): 1357-60. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8691465&dopt=Abstract
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Location of N-unsubstituted glucosamine residues in heparan sulfate. Author(s): Westling C, Lindahl U. Source: The Journal of Biological Chemistry. 2002 December 20; 277(51): 49247-55. Epub 2002 October 08. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12374790&dopt=Abstract
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Long-term effects of glucosamine sulphate on osteoarthritis progression: a randomised, placebo-controlled clinical trial. Author(s): Reginster JY, Deroisy R, Rovati LC, Lee RL, Lejeune E, Bruyere O, Giacovelli G, Henrotin Y, Dacre JE, Gossett C. Source: Lancet. 2001 January 27; 357(9252): 251-6. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11214126&dopt=Abstract
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Measurement of activities of human serum sulfotransferases which transfer sulfate to the galactose residues of keratan sulfate and to the nonreducing end Nacetylglucosamine residues of N-acetyllactosamine trisaccharide: comparison between normal controls and patients with macular corneal dystrophy. Author(s): Hasegawa N, Torii T, Nagaoka I, Nakayasu K, Miyajima H, Habuchi O. Source: Journal of Biochemistry. 1999 February; 125(2): 245-52. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9990120&dopt=Abstract
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Metabolism of glycoprotein-derived sialic acid and N-acetylglucosamine by Streptococcus oralis. Author(s): Homer KA, Kelley S, Hawkes J, Beighton D, Grootveld MC. Source: Microbiology (Reading, England). 1996 May; 142 ( Pt 5): 1221-30. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8704962&dopt=Abstract
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M-ficolin is expressed on monocytes and is a lectin binding to N-acetyl-Dglucosamine and mediates monocyte adhesion and phagocytosis of Escherichia coli. Author(s): Teh C, Le Y, Lee SH, Lu J. Source: Immunology. 2000 October; 101(2): 225-32. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11012776&dopt=Abstract
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Mimics of the sialyl Lewis X tetrasaccharide. Replacement of the Nacetylglucosamine sugar with simple C2-symmetric 1,2-diols. Author(s): Prodger JC, Bamford MJ, Bird MI, Gore PM, Holmes DS, Priest R, Saez V. Source: Bioorganic & Medicinal Chemistry. 1996 June; 4(6): 793-801. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8818228&dopt=Abstract
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Mitotic arrest with nocodazole induces selective changes in the level of O-linked Nacetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells. Author(s): Haltiwanger RS, Philipsberg GA. Source: The Journal of Biological Chemistry. 1997 March 28; 272(13): 8752-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9079710&dopt=Abstract
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Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate. Author(s): Haltiwanger RS, Grove K, Philipsberg GA. Source: The Journal of Biological Chemistry. 1998 February 6; 273(6): 3611-7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9452489&dopt=Abstract
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Molecular analysis of polyreactive monoclonal antibodies from rheumatic carditis: human anti-N-acetylglucosamine/anti-myosin antibody V region genes. Author(s): Adderson EE, Shikhman AR, Ward KE, Cunningham MW. Source: Journal of Immunology (Baltimore, Md. : 1950). 1998 August 15; 161(4): 2020-31. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9712075&dopt=Abstract
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Molecular cloning, cDNA analysis, and localization of a monomer of the Nacetylglucosamine-specific receptor of the thyroid, NAGR1, to chromosome 19p13.313.2. Author(s): Blanck O, Perrin C, Mziaut H, Darbon H, Mattei MG, Miquelis R. Source: Genomics. 1994 May 1; 21(1): 18-26. Erratum In: http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8088785&dopt=Abstract
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Molecularly cloned mammalian glucosamine-6-phosphate deaminase localizes to transporting epithelium and lacks oscillin activity. Author(s): Wolosker H, Kline D, Bian Y, Blackshaw S, Cameron AM, Fralich TJ, Schnaar RL, Snyder SH. Source: The Faseb Journal : Official Publication of the Federation of American Societies for Experimental Biology. 1998 January; 12(1): 91-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9438414&dopt=Abstract
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Mucosal glucosamine synthetase activity in inflammatory bowel disease. Author(s): Winslet MC, Poxon V, Allan A, Keighley MR. Source: Digestive Diseases and Sciences. 1994 March; 39(3): 540-4. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8131690&dopt=Abstract
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N-acetyl-D-glucosamine medium improves recovery of Haemophilus influenzae from sputa of patients with cystic fibrosis. Author(s): Moller LV, van Alphen L, Grasselier H, Dankert J. Source: Journal of Clinical Microbiology. 1993 July; 31(7): 1952-4. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7688756&dopt=Abstract
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N-acetyl-D-glucosamine-specific lectin purified from Vibrio cholerae 01. Author(s): Sasmal D, Guhathakurta B, Ghosh AN, Pal CR, Datta A. Source: Fems Microbiology Letters. 1992 November 1; 77(1-3): 217-24. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1459412&dopt=Abstract
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N-acetylgalactosamine, N-acetylglucosamine and sialic acid expression in primary breast cancers. Author(s): Brooks SA, Carter TM. Source: Acta Histochemica. 2001 February; 103(1): 37-51. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11252626&dopt=Abstract
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N-acetylglucosamine kinase and N-acetylglucosamine 6-phosphate deacetylase in normal human erythrocytes and Plasmodium falciparum. Author(s): Weidanz JA, Campbell P, Moore D, DeLucas LJ, Roden L, Thompson JN, Vezza AC. Source: British Journal of Haematology. 1996 December; 95(4): 645-53. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8982040&dopt=Abstract
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N-acetylglucosamine prevents IL-1 beta-mediated activation of human chondrocytes. Author(s): Shikhman AR, Kuhn K, Alaaeddine N, Lotz M. Source: Journal of Immunology (Baltimore, Md. : 1950). 2001 April 15; 166(8): 5155-60. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11290798&dopt=Abstract
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N-acetylglucosamine: a new osmotic solute in peritoneal dialysis solutions. Author(s): Breborowicz A, Wieczorowska-Tobis K, Kuzlan M, Kupsz J, Korybalska K, Polubinska A, Krzysztof P, French I, Tam P, Wu G. Source: Perit Dial Int. 1997; 17 Suppl 2: S80-3. Review. No Abstract Available. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9163804&dopt=Abstract
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N-acetylglucosamine-dependent nuclear import of neoglycoproteins. Author(s): Duverger E, Roche AC, Monsigny M. Source: Glycobiology. 1996 June; 6(4): 381-6. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8842701&dopt=Abstract
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N-acetylglucosamine-phosphate mutase genotype and diabetic microvascular complications. Author(s): Pang H, Amano S, Inagaki Y, Okamoto T, Yamada K, Kimura H, Koda Y, Yamagishi SI. Source: Diabetic Medicine : a Journal of the British Diabetic Association. 2003 May; 20(5): 419-20. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12752494&dopt=Abstract
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New approaches to the treatment of osteoarthritis: oral glucosamine and chondroitin sulfate. Author(s): Schenck RC Jr. Source: Instr Course Lect. 2000; 49: 491-4. Review. No Abstract Available. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10829202&dopt=Abstract
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Nutraceuticals as therapeutic agents in osteoarthritis. The role of glucosamine, chondroitin sulfate, and collagen hydrolysate. Author(s): Deal CL, Moskowitz RW. Source: Rheumatic Diseases Clinics of North America. 1999 May; 25(2): 379-95. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10356424&dopt=Abstract
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O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability. Author(s): Yang X, Su K, Roos MD, Chang Q, Paterson AJ, Kudlow JE. Source: Proceedings of the National Academy of Sciences of the United States of America. 2001 June 5; 98(12): 6611-6. Epub 2001 May 22. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11371615&dopt=Abstract
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O-linked N-acetylglucosamine is upregulated in Alzheimer brains. Author(s): Griffith LS, Schmitz B. Source: Biochemical and Biophysical Research Communications. 1995 August 15; 213(2): 424-31. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7646495&dopt=Abstract
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O-linked N-acetylglucosamine: the “yin-yang” of Ser/Thr phosphorylation? Nuclear and cytoplasmic glycosylation. Author(s): Hart GW, Greis KD, Dong LY, Blomberg MA, Chou TY, Jiang MS, Roquemore EP, Snow DM, Kreppel LK, Cole RN, et al. Source: Advances in Experimental Medicine and Biology. 1995; 376: 115-23. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8597237&dopt=Abstract
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On call. I have arthritis of both knees. Prescription medicines didn't help and they irritated my stomach. I tried glucosamine, and it didn't do much good either. Finally my doctor sent me to a specialist, who washed out both knees with an arthroscope. My pain is nearly gone, but I read that doctors did a test that showed a fake operation was just as good as my surgery. It's an outrage. How can responsible doctors perform fake operations? Author(s): Simon HB. Source: Harvard Men's Health Watch. 2003 January; 7(6): 7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12543597&dopt=Abstract
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On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase. Author(s): Montero-Moran GM, Lara-Gonzalez S, Alvarez-Anorve LI, Plumbridge JA, Calcagno ML. Source: Biochemistry. 2001 August 28; 40(34): 10187-96. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11513596&dopt=Abstract
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Oral polymeric N-acetyl-D-glucosamine and osteoarthritis. Author(s): Rubin BR, Talent JM, Kongtawelert P, Pertusi RM, Forman MD, Gracy RW. Source: J Am Osteopath Assoc. 2001 June; 101(6): 339-44. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11432083&dopt=Abstract
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Partial purification and kinetic properties of three different D-glucosamine 6-P:Nacetyltransferase forms from human placenta. Author(s): Vessal M, Jaberi-Pour M. Source: Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 1998 December; 121(4): 379-84. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9972309&dopt=Abstract
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Peptidoglycan N-acetylglucosamine deacetylase, a putative virulence factor in Streptococcus pneumoniae. Author(s): Vollmer W, Tomasz A. Source: Infection and Immunity. 2002 December; 70(12): 7176-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12438406&dopt=Abstract
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Pharmacokinetics of glucosamine in man. Author(s): Setnikar I, Palumbo R, Canali S, Zanolo G. Source: Arzneimittel-Forschung. 1993 October; 43(10): 1109-13. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8267678&dopt=Abstract
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Pilot study of oral polymeric N-acetyl-D-glucosamine as a potential treatment for patients with osteoarthritis. Author(s): Talent JM, Gracy RW. Source: Clinical Therapeutics. 1996 November-December; 18(6): 1184-90. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9001835&dopt=Abstract
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Positions of conjugation of bile acids with glucose and N-acetylglucosamine in vitro. Author(s): Marschall HU, Griffiths WJ, Zhang J, Wietholtz H, Matern H, Matern S, Sjovall J. Source: Journal of Lipid Research. 1994 September; 35(9): 1599-610. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7806974&dopt=Abstract
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Possible association between glucosamine treatment and renal toxicity: comment on the letter by Danao-Camara. Author(s): Guillaume MP, Peretz A. Source: Arthritis and Rheumatism. 2001 December; 44(12): 2943-4. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11762963&dopt=Abstract
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Practical stereoselective synthesis of alpha-linked C-glucosamine propionic acid esters: conversion to GLA-60 derivatives. Author(s): Wakabayashi T, Shiozaki M, Kurakata S. Source: Carbohydrate Research. 2002 February 5; 337(2): 97-104. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11814441&dopt=Abstract
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Presence of glutamine:fructose-6-phosphate amidotransferase for glucosamine-6phosphate synthesis in endothelial cells: effects of hyperglycaemia and glutamine. Author(s): Wu G, Haynes TE, Yan W, Meininger CJ. Source: Diabetologia. 2001 February; 44(2): 196-202. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11270676&dopt=Abstract
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Presence of N-unsubstituted glucosamine units in native heparan sulfate revealed by a monoclonal antibody. Author(s): van den Born J, Gunnarsson K, Bakker MA, Kjellen L, Kusche-Gullberg M, Maccarana M, Berden JH, Lindahl U. Source: The Journal of Biological Chemistry. 1995 December 29; 270(52): 31303-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8537400&dopt=Abstract
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Primary biliary cirrhosis sera recognize not only gp210 but also proteins of the p62 complex bearing N-acetylglucosamine residues from rat liver nuclear envelope. Antip62 complex antibody in PBC. Author(s): Miyachi K, Shibata M, Onozuka Y, Kikuchi F, Imai N, Horigome T. Source: Molecular Biology Reports. 1996; 23(3-4): 227-34. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9112233&dopt=Abstract
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Primary open-angle glaucoma may be a hyaluronic acid deficiency disease: potential for glucosamine in prevention and therapy. Author(s): McCarty MF. Source: Medical Hypotheses. 1998 December; 51(6): 483-4. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10052867&dopt=Abstract
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Primary structure and expression analysis of human UDP-N-acetyl-glucosamine-2epimerase/N-acetylmannosamine kinase, the bifunctional enzyme in neuraminic acid biosynthesis. Author(s): Lucka L, Krause M, Danker K, Reutter W, Horstkorte R. Source: Febs Letters. 1999 July 9; 454(3): 341-4. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10431835&dopt=Abstract
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Purification and characterization of an N-acetylglucosamine-binding lectin from Koelreuteria paniculata seeds and its effect on the larval development of Callosobruchus maculatus (Coleoptera: Bruchidae) and Anagasta kuehniella (Lepidoptera: Pyralidae). Author(s): Macedo ML, Damico DC, Freire MG, Toyama MH, Marangoni S, Novello JC. Source: Journal of Agricultural and Food Chemistry. 2003 May 7; 51(10): 2980-6. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12720380&dopt=Abstract
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Purification and characterization of UDP-N-acetylglucosamine: alpha-6-D-mannoside beta 1-6N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase V) from a human lung cancer cell line. Author(s): Gu J, Nishikawa A, Tsuruoka N, Ohno M, Yamaguchi N, Kangawa K, Taniguchi N. Source: Journal of Biochemistry. 1993 May; 113(5): 614-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8393437&dopt=Abstract
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Randomized, controlled trial of glucosamine for treating osteoarthritis of the knee. Author(s): Rindone JP, Hiller D, Collacott E, Nordhaugen N, Arriola G. Source: The Western Journal of Medicine. 2000 February; 172(2): 91-4. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10693368&dopt=Abstract
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Reduction of O-linked N-acetylglucosamine-modified assembly protein-3 in Alzheimer's disease. Author(s): Yao PJ, Coleman PD. Source: The Journal of Neuroscience : the Official Journal of the Society for Neuroscience. 1998 April 1; 18(7): 2399-411. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9502801&dopt=Abstract
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Regulation of glycogen synthase by glucose, glucosamine, and glutamine:fructose-6phosphate amidotransferase. Author(s): Crook ED, Zhou J, Daniels M, Neidigh JL, McClain DA. Source: Diabetes. 1995 March; 44(3): 314-20. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7883119&dopt=Abstract
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Renin inhibits N-acetyl-D-glucosamine 2-epimerase (renin-binding protein). Author(s): Takahashi S, Kumagai M, Shindo S, Saito K, Kawamura Y. Source: Journal of Biochemistry. 2000 December; 128(6): 951-6. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11098137&dopt=Abstract
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Saccharomyces cerevisiae GNA1, an essential gene encoding a novel acetyltransferase involved in UDP-N-acetylglucosamine synthesis. Author(s): Mio T, Yamada-Okabe T, Arisawa M, Yamada-Okabe H. Source: The Journal of Biological Chemistry. 1999 January 1; 274(1): 424-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9867860&dopt=Abstract
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Sanfilippo D syndrome: correction of glucosamine-6-sulphatase deficiency following fibroblast culture in Chang's media. Author(s): Freeman C, Hopwood JJ. Source: Prenatal Diagnosis. 1991 September; 11(9): 711-7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1788178&dopt=Abstract
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Selective activation of N-acyl-D-glucosamine 2-epimerase expression in failing human heart ventricular myocytes. Author(s): Bohlmeyer T, Ferdensi A, Bristow MR, Takahashi S, Zisman LS. Source: Journal of Cardiac Failure. 2003 February; 9(1): 59-68. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12612874&dopt=Abstract
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Selective inhibition of N-acetylglucosamine and galactose-specific lectins including the 14-kDa vertebrate lectin by novel synthetic biantennary oligosaccharides. Author(s): Gupta D, Sabesan S, Brewer CF. Source: European Journal of Biochemistry / Febs. 1993 September 15; 216(3): 789-97. Erratum In: Eur J Biochem 1994 February 1; 219(3): 1087. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8404897&dopt=Abstract
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Sequence analysis of heparan sulphate indicates defined location of N-sulphated glucosamine and iduronate 2-sulphate residues proximal to the protein-linkage region. Author(s): Turnbull JE, Gallagher JT. Source: The Biochemical Journal. 1991 July 15; 277 ( Pt 2): 297-303. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1859357&dopt=Abstract
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Short-term glucosamine infusion does not affect insulin sensitivity in humans. Author(s): Pouwels MJ, Jacobs JR, Span PN, Lutterman JA, Smits P, Tack CJ. Source: The Journal of Clinical Endocrinology and Metabolism. 2001 May; 86(5): 2099103. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11344213&dopt=Abstract
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Specific defect in N-acetylglucosamine incorporation in the biosynthesis of the glycosylphosphatidylinositol anchor in cloned cell lines from patients with paroxysmal nocturnal hemoglobinuria. Author(s): Hillmen P, Bessler M, Mason PJ, Watkins WM, Luzzatto L. Source: Proceedings of the National Academy of Sciences of the United States of America. 1993 June 1; 90(11): 5272-6. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8389477&dopt=Abstract
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Staphylococcus hominis subsp. novobiosepticus subsp. nov., a novel trehalose- and N-acetyl-D-glucosamine-negative, novobiocin- and multiple-antibiotic-resistant subspecies isolated from human blood cultures. Author(s): Kloos WE, George CG, Olgiate JS, Van Pelt L, McKinnon ML, Zimmer BL, Muller E, Weinstein MP, Mirrett S. Source: International Journal of Systematic Bacteriology. 1998 July; 48 Pt 3: 799-812. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9734034&dopt=Abstract
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Stimulation of proteoglycan production by glucosamine sulfate in chondrocytes isolated from human osteoarthritic articular cartilage in vitro. Author(s): Bassleer C, Rovati L, Franchimont P. Source: Osteoarthritis and Cartilage / Oars, Osteoarthritis Research Society. 1998 November; 6(6): 427-34. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10343776&dopt=Abstract
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Structural and symptomatic efficacy of glucosamine and chondroitin in knee osteoarthritis: a comprehensive meta-analysis. Author(s): Richy F, Bruyere O, Ethgen O, Cucherat M, Henrotin Y, Reginster JY. Source: Archives of Internal Medicine. 2003 July 14; 163(13): 1514-22. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12860572&dopt=Abstract
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Structural diversity of N-sulfated heparan sulfate domains: distinct modes of glucuronyl C5 epimerization, iduronic acid 2-O-sulfation, and glucosamine 6-Osulfation. Author(s): Safaiyan F, Lindahl U, Salmivirta M. Source: Biochemistry. 2000 September 5; 39(35): 10823-30. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10978168&dopt=Abstract
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Structure and function of N-acetylglucosamine kinase. Identification of two active site cysteines. Author(s): Berger M, Chen H, Reutter W, Hinderlich S. Source: European Journal of Biochemistry / Febs. 2002 September; 269(17): 4212-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12199699&dopt=Abstract
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Sulfate could mediate the therapeutic effect of glucosamine sulfate. Author(s): Hoffer LJ, Kaplan LN, Hamadeh MJ, Grigoriu AC, Baron M. Source: Metabolism: Clinical and Experimental. 2001 July; 50(7): 767-70. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11436179&dopt=Abstract
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Sulfated glycosaminoglycans and glucosamine may synergize in promoting synovial hyaluronic acid synthesis. Author(s): McCarty MF, Russell AL, Seed MP. Source: Medical Hypotheses. 2000 May; 54(5): 798-802. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10859690&dopt=Abstract
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Sulfated polysaccharides (chondroitin sulfate and carrageenan) plus glucosamine sulfate are potent inhibitors of HIV. Author(s): Konlee M. Source: Posit Health News. 1998 Fall; (No 17): 4-7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11366556&dopt=Abstract
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Synthesis and characterization of a carbene-generating biotinylated Nacetylglucosamine for photoaffinity labeling of beta-(1-->4)-galactosyltransferase. Author(s): Hatanka Y, Hashimoto M, Nishihara S, Narimatsu H, Kanaoka Y. Source: Carbohydrate Research. 1996 November 20; 294: 95-108. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9011380&dopt=Abstract
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Synthesis and growth inhibitory properties of glucosamine-derived glycerolipids. Author(s): Yang G, Franck RW, Bittman R, Samadder P, Arthur G. Source: Organic Letters. 2001 January 25; 3(2): 197-200. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11430033&dopt=Abstract
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The absence of fucose but not the presence of galactose or bisecting Nacetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. Author(s): Shinkawa T, Nakamura K, Yamane N, Shoji-Hosaka E, Kanda Y, Sakurada M, Uchida K, Anazawa H, Satoh M, Yamasaki M, Hanai N, Shitara K. Source: The Journal of Biological Chemistry. 2003 January 31; 278(5): 3466-73. Epub 2002 November 08. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12427744&dopt=Abstract
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The effect of an oral supplement containing glucosamine, amino acids, minerals, and antioxidants on cutaneous aging: a preliminary study. Author(s): Murad H, Tabibian MP. Source: The Journal of Dermatological Treatment. 2001 March; 12(1): 47-51. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12171689&dopt=Abstract
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The effect of glucosamine supplementation on people experiencing regular knee pain. Author(s): Braham R, Dawson B, Goodman C. Source: British Journal of Sports Medicine. 2003 February; 37(1): 45-9; Discussion 49. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12547742&dopt=Abstract
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The effect of glucosamine-chondroitin supplementation on glycosylated hemoglobin levels in patients with type 2 diabetes mellitus: a placebo-controlled, double-blinded, randomized clinical trial. Author(s): Scroggie DA, Albright A, Harris MD. Source: Archives of Internal Medicine. 2003 July 14; 163(13): 1587-90. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12860582&dopt=Abstract
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The effect of N-acetylglucosamine as a substrate for in vitro synthesis of glycosaminoglycans by human peritoneal mesothelial cells and fibroblasts. Author(s): Breborowicz A, Kuzlan-Pawlaczyk M, Wieczorowska-Tobis K, Wisniewska J, Tam P, French I, Wu G. Source: Adv Perit Dial. 1998; 14: 31-5. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10649686&dopt=Abstract
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The effects of glucosamine and chondroitin sulfate on osteoarthritis of the TMJ: a preliminary report of 50 patients. Author(s): Shankland WE 2nd. Source: Cranio. 1998 October; 16(4): 230-5. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10029750&dopt=Abstract
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The enamel protein amelogenin binds to the N-acetyl-D-glucosamine-mimicking peptide motif of cytokeratins. Author(s): Ravindranath RM, Tam WY, Nguyen P, Fincham AG. Source: The Journal of Biological Chemistry. 2000 December 15; 275(50): 39654-61. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10980199&dopt=Abstract
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The human glucosamine-6-phosphate deaminase gene: cDNA cloning and expression, genomic organization and chromosomal localization. Author(s): Shevchenko V, Hogben M, Ekong R, Parrington J, Lai FA. Source: Gene. 1998 August 17; 216(1): 31-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9714720&dopt=Abstract
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The impact of fixatives on the binding of lectins to N-acetyl-glucosamine residues of human syncytiotrophoblast: a quantitative histochemical study. Author(s): Hoyer PE, Kirkeby S. Source: The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society. 1996 August; 44(8): 855-63. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8756758&dopt=Abstract
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The major metabolites of ursodeoxycholic acid in human urine are conjugated with N-acetylglucosamine. Author(s): Marschall HU, Griffiths WJ, Gotze U, Zhang J, Wietholtz H, Busch N, Sjovall J, Matern S. Source: Hepatology (Baltimore, Md.). 1994 October; 20(4 Pt 1): 845-53. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7927225&dopt=Abstract
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The major N-linked carbohydrate chains from human urokinase. The occurrence of 4O-sulfated, (alpha 2-6)-sialylated or (alpha 1-3)-fucosylated Nacetylgalactosamine(beta 1-4)-N-acetylglucosamine elements. Author(s): Bergwerff AA, Van Oostrum J, Kamerling JP, Vliegenthart JF. Source: European Journal of Biochemistry / Febs. 1995 March 15; 228(3): 1009-19. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7737145&dopt=Abstract
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The mannose-specific plant lectins from Cymbidium hybrid and Epipactis helleborine and the (N-acetylglucosamine)n-specific plant lectin from Urtica dioica are potent and selective inhibitors of human immunodeficiency virus and cytomegalovirus replication in vitro. Author(s): Balzarini J, Neyts J, Schols D, Hosoya M, Van Damme E, Peumans W, De Clercq E. Source: Antiviral Research. 1992 June; 18(2): 191-207. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1329650&dopt=Abstract
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The neglect of glucosamine as a treatment for osteoarthritis--a personal perspective. Author(s): McCarty MF. Source: Medical Hypotheses. 1994 May; 42(5): 323-7. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7935075&dopt=Abstract
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The reaction of hyaluronic acid and its monomers, glucuronic acid and Nacetylglucosamine, with reactive oxygen species. Author(s): Jahn M, Baynes JW, Spiteller G. Source: Carbohydrate Research. 1999 October 15; 321(3-4): 228-34. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10614067&dopt=Abstract
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The relationship between exposed galactose and N-acetylglucosamine residues on IgG in rheumatoid arthritis (RA), juvenile chronic arthritis (JCA) and Sjogren's syndrome (SS). Author(s): Bond A, Alavi A, Axford JS, Youinou P, Hay FC. Source: Clinical and Experimental Immunology. 1996 July; 105(1): 99-103. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8697643&dopt=Abstract
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The role of glucosamine sulfate and chondroitin sulfates in the treatment of degenerative joint disease. Author(s): Kelly GS. Source: Alternative Medicine Review : a Journal of Clinical Therapeutic. 1998 February; 3(1): 27-39. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9600024&dopt=Abstract
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The tumor association of a trisaccharide epitope: specificity of antiserum developed to galactose beta1->3 N-acetyl glucosamine beta1-->3 galactose. Author(s): Diakun KR, Vargas F, Tamburlin J. Source: Immunological Investigations. 1996 May; 25(3): 253-66. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8860696&dopt=Abstract
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The tumor suppressor EXT-like gene EXTL2 encodes an alpha1, 4-Nacetylhexosaminyltransferase that transfers N-acetylgalactosamine and Nacetylglucosamine to the common glycosaminoglycan-protein linkage region. The key enzyme for the chain initiation of heparan sulfate. Author(s): Kitagawa H, Shimakawa H, Sugahara K. Source: The Journal of Biological Chemistry. 1999 May 14; 274(20): 13933-7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10318803&dopt=Abstract
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Transglycosylation activity of Mucor hiemalis endo-beta-N-acetyl-glucosaminidase which transfers complex oligosaccharides to the N-acetylglucosamine moieties of peptides. Author(s): Yamamoto K, Kadowaki S, Watanabe J, Kumagai H. Source: Biochemical and Biophysical Research Communications. 1994 August 30; 203(1): 244-52. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8074662&dopt=Abstract
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Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study. Author(s): Arreola R, Valderrama B, Morante ML, Horjales E. Source: Febs Letters. 2003 September 11; 551(1-3): 63-70. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12965206&dopt=Abstract
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Tyrosyl motif in amelogenins binds N-acetyl-D-glucosamine. Author(s): Ravindranath RM, Moradian-Oldak J, Fincham AG. Source: The Journal of Biological Chemistry. 1999 January 22; 274(4): 2464-71. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9891017&dopt=Abstract
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UDP-N-Acetyl-alpha-D-glucosamine as acceptor substrate of beta-1,4galactosyltransferase. Enzymatic synthesis of UDP-N-acetyllactosamine. Author(s): Elling L, Zervosen A, Gallego RG, Nieder V, Malissard M, Berger EG, Vliegenthart JF, Kamerling JP. Source: Glycoconjugate Journal. 1999 July; 16(7): 327-36. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10619705&dopt=Abstract
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UDP-N-acetylhexosamine modulation by glucosamine and uridine in NCI N-417 variant small cell lung cancer cells: 31P nuclear magnetic resonance results. Author(s): Pederson NV, Knop RH, Miller WM. Source: Cancer Research. 1992 July 1; 52(13): 3782-6. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1319832&dopt=Abstract
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Use of glucosamine and chondroitin sulfate in the management of osteoarthritis. Author(s): Brief AA, Maurer SG, Di Cesare PE. Source: J Am Acad Orthop Surg. 2001 March-April; 9(2): 71-8. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11281631&dopt=Abstract
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Use of glucosamine and chondroitin sulfate in the management of osteoarthritis. Author(s): Arnold EL, Arnold WJ. Source: J Am Acad Orthop Surg. 2001 September-October; 9(5): 352-3. No Abstract Available. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11599524&dopt=Abstract
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Use of mannosamine for inducing the addition of outer arm N-acetylglucosamine onto N-linked oligosaccharides of recombinant proteins in insect cells. Author(s): Donaldson M, Wood HA, Kulakosky PC, Shuler ML. Source: Biotechnology Progress. 1999 March-April; 15(2): 168-73. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10194391&dopt=Abstract
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Vaccine potential of poly-1-6 beta-D-N-succinylglucosamine, an immunoprotective surface polysaccharide of Staphylococcus aureus and Staphylococcus epidermidis. Author(s): Mckenney D, Pouliot K, Wang Y, Murthy V, Ulrich M, Doring G, Lee JC, Goldmann DA, Pier GB. Source: Journal of Biotechnology. 2000 September 29; 83(1-2): 37-44. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11000458&dopt=Abstract
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Vascular heparan sulfates may limit the ability of leukocytes to penetrate the endothelial barrier--implications for use of glucosamine in inflammatory disorders. Author(s): McCarty MF. Source: Medical Hypotheses. 1998 July; 51(1): 11-5. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9881830&dopt=Abstract
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Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine. Author(s): Roquemore EP, Dell A, Morris HR, Panico M, Reason AJ, Savoy LA, Wistow GJ, Zigler JS Jr, Earles BJ, Hart GW. Source: The Journal of Biological Chemistry. 1992 January 5; 267(1): 555-63. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1730617&dopt=Abstract
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CHAPTER 2. NUTRITION AND GLUCOSAMINE Overview In this chapter, we will show you how to find studies dedicated specifically to nutrition and glucosamine.
Finding Nutrition Studies on Glucosamine The National Institutes of Health’s Office of Dietary Supplements (ODS) offers a searchable bibliographic database called the IBIDS (International Bibliographic Information on Dietary Supplements; National Institutes of Health, Building 31, Room 1B29, 31 Center Drive, MSC 2086, Bethesda, Maryland 20892-2086, Tel: 301-435-2920, Fax: 301-480-1845, E-mail:
[email protected]). The IBIDS contains over 460,000 scientific citations and summaries about dietary supplements and nutrition as well as references to published international, scientific literature on dietary supplements such as vitamins, minerals, and botanicals.7 The IBIDS includes references and citations to both human and animal research studies. As a service of the ODS, access to the IBIDS database is available free of charge at the following Web address: http://ods.od.nih.gov/databases/ibids.html. After entering the search area, you have three choices: (1) IBIDS Consumer Database, (2) Full IBIDS Database, or (3) Peer Reviewed Citations Only. Now that you have selected a database, click on the “Advanced” tab. An advanced search allows you to retrieve up to 100 fully explained references in a comprehensive format. Type “glucosamine” (or synonyms) into the search box, and click “Go.” To narrow the search, you can also select the “Title” field.
7 Adapted from http://ods.od.nih.gov. IBIDS is produced by the Office of Dietary Supplements (ODS) at the National Institutes of Health to assist the public, healthcare providers, educators, and researchers in locating credible, scientific information on dietary supplements. IBIDS was developed and will be maintained through an interagency partnership with the Food and Nutrition Information Center of the National Agricultural Library, U.S. Department of Agriculture.
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The following information is typical of that found when using the “Full IBIDS Database” to search for “glucosamine” (or a synonym): •
A carbon-centered radical as a reaction species in the DNA strand-breakage by Dglucosamine. Author(s): Department of Hygiene, Miyazaki Medical College, Japan. Source: Yamaguchi, T Kashige, N Matsumoto, S Satoh, K Yasuda, M Watanabe, K BiolPharm-Bull. 1998 March; 21(3): 205-9 0918-6158
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A friend recommended I take a dietary supplement for my arthritis that contains glucosamine and chondroitin. What are these made from? Do they help? Source: Anonymous Mayo-Clin-Health-Lett. 2003 January; 21(1): 8 0741-6245
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A friend recommends that I take something called glucosamine for my arthritis. What do you know about it? Source: Anonymous Mayo-Clin-Health-Lett. 1998 January; 16(1): 8 0741-6245
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A look at glucosamine and chondroitin for easing arthritis pain. Source: Tufts-Univ-health-nutr-lett. New York, NY : Tufts University Health & Nutrition Letter, c1997-. January 2000. volume 17 (11) page 4-5.
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A pilot study evaluating the efficacy of a fully acetylated poly-N-acetyl glucosamine membrane formulation as a topical hemostatic agent. Author(s): Department of Surgery, Medical University of South Carolina, Charleston 29425, USA. Source: Cole, D J Connolly, R J Chan, M W Schwaitzberg, S D Byrne, T K Adams, D B Baron, P L O'Brien, P H Metcalf, J S Demcheva, M Vournakis, J Surgery. 1999 September; 126(3): 510-7 0039-6060
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A randomized, double-blind, placebo-controlled trial of glucosamine sulphate as an analgesic in osteoarthritis of the knee. Author(s): St Peter's Hospital, Chertsey, Surrey, UK. Source: Hughes, R Carr, A Rheumatology-(Oxford). 2002 March; 41(3): 279-84 1462-0324
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A survey of self-medication practices and perceived effectiveness of glucosamine products among older adults. Author(s): School of Nursing, Memorial University of Newfoundland, St. John's, NF, Canada.
[email protected] Source: Blakeley, J A Ribeiro, V Complement-Ther-Med. 2002 September; 10(3): 154-60 0965-2299
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Alkylating agents from sugars: synthesis of chlorambucil derivatives carried by chiral glycosyl glycerols derived from D-glucosamine. Author(s): Departamento de Quimica Organica y Farmaceutica, Facultad de Farmacia, Universidad de Sevilla, Sevilla, Spain.
[email protected] Source: Iglesias Guerra, Fernando Candela, Jose I Blanco, Eugenia Alcudia, Felipe Vega Perez, Jose M Chirality. 2002 Feb-March; 14(2-3): 199-203 0899-0042
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Application to a cartilage targeting strategy: synthesis and in vivo biodistribution of (14)C-labeled quaternary ammonium-glucosamine conjugates. Author(s): INSERM Unite 484, Rue Montalembert, BP 184, 63005 Clermont-Ferrand Cedex, France. Source: Giraud, I Rapp, M Maurizis, J C Madelmont, J C Bioconjug-Chem. 2000 MarApril; 11(2): 212-8 1043-1802
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D-glucosamine propanedithioacetal, an efficient chiral auxiliary in beta-lactam chemistry. Author(s): Departamento de Quimica Organica, Universidad de Salamanca, Spain.
[email protected] Source: Anaya, J Gero, S D Grande, M Hernando, J I Laso, N M Bioorg-Med-Chem. 1999 May; 7(5): 837-50 0968-0896
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Differences in metabolism of 5-fluorouracil and 5-fluorouridine and regulation by glucosamine in human colon cancer multicell tumor spheroids. Author(s): Department of Oncology, Mayo Clinic and Mayo Foundation, Rochester, MN 55905, USA. Source: Chen, T B Bajzer, Z Macura, S Vuk Pavlovic, S NMR-Biomed. 1999 May; 12(3): 157-67 0952-3480
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Effect of glucosamine on interleukin-1-conditioned articular cartilage. Author(s): Department of Animal Science, Michigan State University, East Lansing 48824, USA. Source: Fenton, J I Chlebek Brown, K A Caron, J P Orth, M W Equine-Vet-J-Suppl. 2002 September; (34): 219-23
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Endoscopic injection of bleeding esophageal varices with a poly-N-acetyl glucosamine gel formulation in the canine portal hypertension model. Author(s): Digestive Disease Center, Department of Medicine, Medical University of South Carolina, Charleston, USA. Source: Kulling, D Vournakis, J N Woo, S Demcheva, M V Tagge, D U Rios, G Finkielsztein, S Hawes, R H Gastrointest-Endosc. 1999 June; 49(6): 764-71 0016-5107
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Enhanced synovial production of hyaluronic acid may explain rapid clinical response to high-dose glucosamine in osteoarthritis. Author(s): Nutrition 21, San Diego, CA 92109, USA. Source: McCarty, M F Med-Hypotheses. 1998 June; 50(6): 507-10 0306-9877
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Enhancement in the lysozyme activity of the hen egg white foam matrix by crosslinking in the presence of N-acetyl glucosamine. Author(s): Nuclear Agriculture and Biotechnology Division, Bhabha Atomic Research Centre, Trombay, Mumbai, India. Source: Marolia, K Z D'Souza, S F J-Biochem-Biophys-Methods. 1999 February 25; 39(12): 115-7 0165-022X
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Facilitated diffusion of glucosamine-6-phosphate synthase inhibitors enhances their antifungal activity. Author(s): Department of Pharmaceutical Technology and Biochemistry, Technical University of Gdansk, Poland. Source: Janiak, A Cybulska, B Szlinder Richert, J Borowski, E Milewski, S Acta-BiochimPol. 2002; 49(1): 77-86 0001-527X
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Folliculogenesis and ovarian expression of mRNA encoding aromatase in anoestrous sheep after 5 days of glucose or glucosamine infusion or supplementary lupin feeding. Author(s): Department of Veterinary Basic Sciences, Royal Veterinary College, University of London, Royal College Street, UK.
[email protected] Source: Munoz Gutierrez, M Blache, D Martin, G B Scaramuzzi, R J Reproduction. 2002 November; 124(5): 721-31 1470-1626
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Glucosamine & chondroitin: joint relief. Source: Schardt, D. Nutr-action-health-lett. [Washington, D.C. : Center for Science in the Public Interest,. October 2000. volume 27 (8) page 10. 0885-7792
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Glucosamine and chondroitin for osteoarthritis? Author(s): Arthritis Center, Boston University Medical Center, Boston, MA, USA. Source: McAlindon, T Bull-Rheum-Dis. 2001 July; 50(7): 1-4 0007-5248
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Glucosamine modulates IL-1-induced activation of rat chondrocytes at a receptor level, and by inhibiting the NF-kappa B pathway. Author(s): UMR 7561, CNRS-Universite Henri Poincare-Nancy I, Physiopathologie et Pharmacologie Articulaires, Faculte de Medecine, Vandoeuvre-les-Nancy, France. Source: Gouze, J N Bianchi, A Becuwe, P Dauca, M Netter, P Magdalou, J Terlain, B Bordji, K FEBS-Lett. 2002 January 16; 510(3): 166-70 0014-5793
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Glucosamine sulfate. Source: Anonymous Altern-Med-Revolume 1999 June; 4(3): 193-5 1089-5159
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Glucosamine therapy compared to ibuprofen for joint pain. Author(s): Primary Care and Community Pharmacy, King's College London. Source: Ruane, Rachael Griffiths, Peter Br-J-Community-Nurs. 2002 March; 7(3): 148-52 1462-4753
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Glucosamine. A nutraceutical in osteoarthritis. Author(s): Westmead Hospital, New South Wales. Source: Phoon, S Manolios, N Aust-Fam-Physician. 2002 June; 31(6): 539-41 0300-8495
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Inhibition of articular cartilage degradation by glucosamine-HCl and chondroitin sulphate. Author(s): Department of Animal Science, Michigan State University, East Lansing 48824-1225, USA. Source: Orth, M W Peters, T L Hawkins, J N Equine-Vet-J-Suppl. 2002 September; (34): 224-9
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Inhibitory actions of glucosamine, a therapeutic agent for osteoarthritis, on the functions of neutrophils. Author(s): Department of Biochemistry, Juntendo University, School of Medicine, Tokyo, Japan. Source: Hua, Jian Sakamoto, Koji Nagaoka, Isao J-Leukoc-Biol. 2002 April; 71(4): 632-40 0741-5400
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Is glucosamine worth taking for osteoarthritis? Source: Anonymous Drug-Ther-Bull. 2002 November; 40(11): 81-3 0012-6543
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Langerhans cell migration is modulated by N-sulfated glucosamine moieties in heparin. Author(s): Department of Medicine Dermatology, University of Sydney at Royal Prince Alfred Hospital, NSW, Australia.
[email protected] Source: O'Sullivan, G M Boswell, C M Halliday, G M Exp-Dermatol. 2000 February; 9(1): 25-33 0906-6705
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New approaches to the treatment of osteoarthritis: oral glucosamine and chondroitin sulfate. Author(s): Department of Orthopaedic Surgery, University of Texas Health Science Center, San Antonio, USA. Source: Schenck, R C Instr-Course-Lect. 2000; 49491-4 0065-6895
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Nutraceuticals, a call for quality control of delivery systems: a case study with chondroitin sulfate and glucosamine. Source: Adebowale, A.O. Liang, Z. Eddington, N.D. J-nutraceuticals-funct-med-foods. Binghamton, NY : Pharmaceutical Products Press, an imprint of the Haworth Press, Inc., c1997-. 1999. volume 2 (2) page 15-30. 1089-4179
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One-pot synthesis of glucosamine oligosaccharides. Author(s): Department of Chemistry and Institute of Catalysis Science and Technology, Technion-Israel Institute of Technology, Haifa 32000, Israel. Source: Fridman, Micha Solomon, Dmitry Yogev, Shay Baasov, Timor Org-Lett. 2002 January 24; 4(2): 281-3 1523-7060
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Poly-N-acetyl glucosamine: will it replace cyanoacrylate for treatment of gastric varices? A pilot study in a rabbit model. Author(s): Digestive Disease Center, Medical University of South Carolina, Charleston 29425, USA. Source: Kulling, D Woo, S Demcheva, M V Hawes, R H Vournakis, J N Endoscopy. 1998 March; 30(3): S41-2 0013-726X
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Single dose pharmacokinetics and bioavailability of glucosamine in the rat. Author(s): Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, Edmonton, Alberta, Canada. Source: Aghazadeh Habashi, A Sattari, S Pasutto, F Jamali, F J-Pharm-Pharm-Sci. 2002 May-August; 5(2): 181-4 1482-1826
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Sulfated glycosaminoglycans and glucosamine may synergize in promoting synovial hyaluronic acid synthesis. Author(s): NutriGuard Research, La Jolla, CA, USA. Source: McCarty, M F Russell, A L Seed, M P Med-Hypotheses. 2000 May; 54(5): 798-802 0306-9877
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The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution. Author(s): Instituto de Biotecnologia, Universidad Nacional Autonoma de Mexico (UNAM), Cuernavaca, Mor, Mexico.
[email protected] Source: Horjales, E Altamirano, M M Calcagno, M L Garratt, R C Oliva, G StructureFold-Des. 1999 May; 7(5): 527-37 0969-2126
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The bioavailability and pharmacokinetics of glucosamine hydrochloride and low molecular weight chondroitin sulfate after single and multiple doses to beagle dogs. Author(s): Center for Drug Evaluation and Research, Food and Drug Administration, Rockville, MD, USA. Source: Adebowale, A Du, J Liang, Z Leslie, J L Eddington, N D Biopharm-Drug-Dispos. 2002 September; 23(6): 217-25 0142-2782
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The effect of chitosan (poly-N-acetyl glucosamine) on lingual hemostasis in heparinized rabbits. Author(s): Section of Periodontics, UCLA School of Dentistry, Los Angeles, CA 900951668, USA. Source: Klokkevold, P R Fukayama, H Sung, E C Bertolami, C N J-Oral-Maxillofac-Surg. 1999 January; 57(1): 49-52 0278-2391
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The role of glucosamine sulfate and chondroitin sulfates in the treatment of degenerative joint disease. Source: Kelly, G S Altern-Med-Revolume 1998 February; 3(1): 27-39 1089-5159
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Federal Resources on Nutrition In addition to the IBIDS, the United States Department of Health and Human Services (HHS) and the United States Department of Agriculture (USDA) provide many sources of information on general nutrition and health. Recommended resources include: •
healthfinder®, HHS’s gateway to health information, including diet and nutrition: http://www.healthfinder.gov/scripts/SearchContext.asp?topic=238&page=0
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The United States Department of Agriculture’s Web site dedicated to nutrition information: www.nutrition.gov
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The Food and Drug Administration’s Web site for federal food safety information: www.foodsafety.gov
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The National Action Plan on Overweight and Obesity sponsored by the United States Surgeon General: http://www.surgeongeneral.gov/topics/obesity/
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The Center for Food Safety and Applied Nutrition has an Internet site sponsored by the Food and Drug Administration and the Department of Health and Human Services: http://vm.cfsan.fda.gov/
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Center for Nutrition Policy and Promotion sponsored by the United States Department of Agriculture: http://www.usda.gov/cnpp/
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Food and Nutrition Information Center, National Agricultural Library sponsored by the United States Department of Agriculture: http://www.nal.usda.gov/fnic/
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Food and Nutrition Service sponsored by the United States Department of Agriculture: http://www.fns.usda.gov/fns/
Additional Web Resources A number of additional Web sites offer encyclopedic information covering food and nutrition. The following is a representative sample: •
AOL: http://search.aol.com/cat.adp?id=174&layer=&from=subcats
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Family Village: http://www.familyvillage.wisc.edu/med_nutrition.html
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Google: http://directory.google.com/Top/Health/Nutrition/
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Healthnotes: http://www.healthnotes.com/
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Open Directory Project: http://dmoz.org/Health/Nutrition/
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Yahoo.com: http://dir.yahoo.com/Health/Nutrition/
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WebMD®Health: http://my.webmd.com/nutrition
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WholeHealthMD.com: http://www.wholehealthmd.com/reflib/0,1529,00.html
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The following is a specific Web list relating to glucosamine; please note that any particular subject below may indicate either a therapeutic use, or a contraindication (potential danger), and does not reflect an official recommendation: •
Minerals Boron Source: Prima Communications, Inc.www.personalhealthzone.com Chondroitin Source: Integrative Medicine Communications; www.drkoop.com Chondroitin Source: Prima Communications, Inc.www.personalhealthzone.com Chondroitin Source: WholeHealthMD.com, LLC.; www.wholehealthmd.com Hyperlink: http://www.wholehealthmd.com/refshelf/substances_view/0,1525,10017,00.html Glucosamine/chondroitin Source: Healthnotes, Inc.; www.healthnotes.com Stinging Nettle Alternative names: Urtica dioica, Urtica urens, Nettle Source: Integrative Medicine Communications; www.drkoop.com
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Food and Diet Cartilage Source: Prima Communications, Inc.www.personalhealthzone.com Chondroitin Sulfate Source: Healthnotes, Inc.; www.healthnotes.com Sprains and Strains Source: Healthnotes, Inc.; www.healthnotes.com
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CHAPTER 3. ALTERNATIVE MEDICINE AND GLUCOSAMINE Overview In this chapter, we will begin by introducing you to official information sources on complementary and alternative medicine (CAM) relating to glucosamine. At the conclusion of this chapter, we will provide additional sources.
The Combined Health Information Database The Combined Health Information Database (CHID) is a bibliographic database produced by health-related agencies of the U.S. federal government (mostly from the National Institutes of Health) that can offer concise information for a targeted search. The CHID database is updated four times a year at the end of January, April, July, and October. Check the titles, summaries, and availability of CAM-related information by using the “Simple Search” option at the following Web site: http://chid.nih.gov/simple/simple.html. In the drop box at the top, select “Complementary and Alternative Medicine.” Then type “glucosamine” (or synonyms) in the second search box. We recommend that you select 100 “documents per page” and to check the “whole records” options. The following was extracted using this technique: •
Complementary and Alternative Therapies for Rheumatic Disease Source: Hospital Practice. 36(4): 31-36. April 15, 2001. Summary: This journal article discusses some of the complementary and alternative therapies used for rheumatic disease. First, it briefly reviews patterns of complementary and alternative therapy use among rheumatology patients. Then, it highlights findings from clinical investigations of selected therapies, including glucosamine and chondroitin, dietary interventions, vitamin supplements, herbal preparations (willow bark, devil's claw, feverfew, and Chinese thunder god vine), and acupuncture. Finally, it discusses management concerns for physicians whose patients may be using complementary and alternative therapies. It includes a list of suggested questions to ask and information to give patients about nontraditional therapies. The article has 2 figures, 3 tables, and a suggested reading list.
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National Center for Complementary and Alternative Medicine The National Center for Complementary and Alternative Medicine (NCCAM) of the National Institutes of Health (http://nccam.nih.gov/) has created a link to the National Library of Medicine’s databases to facilitate research for articles that specifically relate to glucosamine and complementary medicine. To search the database, go to the following Web site: http://www.nlm.nih.gov/nccam/camonpubmed.html. Select “CAM on PubMed.” Enter “glucosamine” (or synonyms) into the search box. Click “Go.” The following references provide information on particular aspects of complementary and alternative medicine that are related to glucosamine: •
A pilot study of N-acetyl glucosamine, a nutritional substrate for glycosaminoglycan synthesis, in paediatric chronic inflammatory bowel disease. Author(s): Salvatore S, Heuschkel R, Tomlin S, Davies SE, Edwards S, Walker-Smith JA, French I, Murch SH. Source: Alimentary Pharmacology & Therapeutics. 2000 December; 14(12): 1567-79. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11121904&dopt=Abstract
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A randomized, double blind, placebo controlled trial of a topical cream containing glucosamine sulfate, chondroitin sulfate, and camphor for osteoarthritis of the knee. Author(s): Cohen M, Wolfe R, Mai T, Lewis D. Source: The Journal of Rheumatology. 2003 March; 30(3): 523-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12610812&dopt=Abstract
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A randomized, double-blind, placebo-controlled trial of glucosamine sulphate as an analgesic in osteoarthritis of the knee. Author(s): Hughes R, Carr A. Source: Rheumatology (Oxford, England). 2002 March; 41(3): 279-84. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11934964&dopt=Abstract
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A survey of self-medication practices and perceived effectiveness of glucosamine products among older adults. Author(s): Blakeley JA, Ribeiro V. Source: Complementary Therapies in Medicine. 2002 September; 10(3): 154-60. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12568144&dopt=Abstract
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Active ingredient consistency of commercially available glucosamine sulfate products. Author(s): Russell AS, Aghazadeh-Habashi A, Jamali F. Source: The Journal of Rheumatology. 2002 November; 29(11): 2407-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12415601&dopt=Abstract
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An insecticidal N-acetylglucosamine-specific lectin gene from Griffonia simplicifolia (Leguminosae). Author(s): Zhu K, Huesing JE, Shade RE, Bressan RA, Hasegawa PM, Murdock LL.
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Source: Plant Physiology. 1996 January; 110(1): 195-202. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8587982&dopt=Abstract •
Antinutritive effects of wheat-germ agglutinin and other N-acetylglucosaminespecific lectins. Author(s): Pusztai A, Ewen SW, Grant G, Brown DS, Stewart JC, Peumans WJ, Van Damme EJ, Bardocz S. Source: The British Journal of Nutrition. 1993 July; 70(1): 313-21. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8399111&dopt=Abstract
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Asthma exacerbation associated with glucosamine-chondroitin supplement. Author(s): Tallia AF, Cardone DA. Source: The Journal of the American Board of Family Practice / American Board of Family Practice. 2002 November-December; 15(6): 481-4. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12463294&dopt=Abstract
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Autophosphorylation of phosphoglucosamine mutase from Escherichia coli. Author(s): Jolly L, Pompeo F, van Heijenoort J, Fassy F, Mengin-Lecreulx D. Source: Journal of Bacteriology. 2000 March; 182(5): 1280-5. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10671448&dopt=Abstract
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Bioactivity of nickel(II) complex containing N-glycosides derived from Dglucosamine and ethylenediamine against pathogenic yeast, Candida albicans. Author(s): Yano S, Inoue S, Nouchi R, Kato M, Suzuki T. Source: Biological & Pharmaceutical Bulletin. 1995 June; 18(6): 923-5. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7550136&dopt=Abstract
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Comment: glucosamine: selecting appropriate study exclusion criteria. Author(s): Barclay TS, Tsourounis C, McCart GM. Source: The Annals of Pharmacotherapy. 1998 December; 32(12): 1371-2. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9876825&dopt=Abstract
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Conservative management of spinal osteoarthritis with glucosamine sulfate and chiropractic treatment. Author(s): Gottlieb MS. Source: Journal of Manipulative and Physiological Therapeutics. 1997 July-August; 20(6): 400-14. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9272473&dopt=Abstract
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Datura stramonium agglutinin released histamine from rat peritoneal mast cells that was inhibited by pertussis toxin, haptenic sugar and N-acetylglucosamine-specific lectins: involvement of glycoproteins with N-acetylglucosamine residues. Author(s): Matsuda K, Aoki J, Uchida MK, Suzuki-Nishimura T.
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Source: Japanese Journal of Pharmacology. 1994 October; 66(2): 195-204. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7532733&dopt=Abstract •
Detection of terminal N-linked N-acetylglucosamine residues in the Golgi apparatus using galactosyltransferase and endoglucosaminidase F/peptide N-glycosidase F: adaptation of a biochemical approach to electron microscopy. Author(s): Lucocq JM, Berger EG, Roth J. Source: The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society. 1987 January; 35(1): 67-74. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=2432113&dopt=Abstract
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Determining the efficacy of glucosamine and chondroitin for osteoarthritis. Author(s): O'Rourke M. Source: The Nurse Practitioner. 2001 June; 26(6): 44-6, 49-52. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11416939&dopt=Abstract
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Effect of Brand's glucosamine with essence of chicken on collagen-induced arthritis in rats. Author(s): Tsi D, Khow A, Iino T, Kiso Y, Ono H. Source: Life Sciences. 2003 October 24; 73(23): 2953-62. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=14519444&dopt=Abstract
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Effect of longeing and glucosamine supplementation on serum markers of bone and joint metabolism in yearling quarter horses. Author(s): Fenton JI, Orth MW, Chlebek-Brown KA, Nielsen BD, Corn CD, Waite KS, Caron JP. Source: Can J Vet Res. 1999 October; 63(4): 288-91. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10534010&dopt=Abstract
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Effect of pre-loading oral glucosamine HCl/chondroitin sulfate/manganese ascorbate combination on experimental arthritis in rats. Author(s): Beren J, Hill SL, Diener-West M, Rose NR. Source: Experimental Biology and Medicine (Maywood, N.J.). 2001 February; 226(2): 144-51. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11446439&dopt=Abstract
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Effects of eicosapentaenoic acid and its 15-hydroperoxy and 15-hydroxy derivatives on glucosamine synthetase activity in rabbit gastric mucosa. Author(s): Fujita T, Sakuma S, Yamamoto N, Fujimoto Y. Source: Biochem Mol Biol Int. 1998 September; 46(1): 157-63. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9784850&dopt=Abstract
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Effects of environmental complexity on glucosamine incorporation into rat cerebral cortex and hippocampus in vivo. Author(s): Ramirez G, Karlsson B, Perrin CL. Source: Brain Research. 1974 October 18; 79(2): 296-300. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=4418683&dopt=Abstract
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Endothelin-stimulated glucose uptake: effects of intracellular Ca(2+), cAMP and glucosamine. Author(s): Wu-Wong JR, Berg CE, Dayton BD. Source: Clinical Science (London, England : 1979). 2002 August; 103 Suppl 48: 418S-423S. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12193136&dopt=Abstract
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Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide beta-Nacetylglucosaminyltransferase. Author(s): Haltiwanger RS, Holt GD, Hart GW. Source: The Journal of Biological Chemistry. 1990 February 15; 265(5): 2563-8. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=2137449&dopt=Abstract
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Enzymic degradation of uridine diphosphoacetylglucosamine. Author(s): PATTABIRAMAN TN, VARMA TN, BACHHAWAT BK. Source: Biochimica Et Biophysica Acta. 1964 March 2; 83: 74-83. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=14152201&dopt=Abstract
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Glucosamine 6-phosphate deaminase in normal human erythrocytes. Author(s): Weidanz JA, Campbell P, DeLucas LJ, Jin J, Moore D, Roden L, Yu H, Heilmann E, Vezza AC. Source: British Journal of Haematology. 1995 September; 91(1): 72-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=7577655&dopt=Abstract
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Glucosamine and chondroitin for osteoarthritis? Author(s): McAlindon T. Source: Bulletin on the Rheumatic Diseases. 2001 July; 50(7): 1-4. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11530541&dopt=Abstract
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Glucosamine and chondroitin for treating symptoms of osteoarthritis: evidence is widely touted but incomplete. Author(s): Towheed TE, Anastassiades TP. Source: Jama : the Journal of the American Medical Association. 2000 March 15; 283(11): 1483-4. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10732941&dopt=Abstract
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Glucosamine and chondroitin for treatment of osteoarthritis: a systematic quality assessment and meta-analysis. Author(s): McAlindon TE, LaValley MP, Gulin JP, Felson DT. Source: Jama : the Journal of the American Medical Association. 2000 March 15; 283(11): 1469-75. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10732937&dopt=Abstract
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Glucosamine and chondroitin sulfate are effective in the management of osteoarthritis. Author(s): Hungerford DS, Jones LC. Source: The Journal of Arthroplasty. 2003 April; 18(3 Suppl 1): 5-9. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12730919&dopt=Abstract
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Glucosamine and chondroitin sulfate supplementation to treat symptomatic disc degeneration: biochemical rationale and case report. Author(s): van Blitterswijk WJ, van de Nes JC, Wuisman PI. Source: Bmc Complementary and Alternative Medicine [electronic Resource]. 2003 June 10; 3(1): 2. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12797867&dopt=Abstract
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Glucosamine and experimental atherosclerosis. Increased wet weight and changed composition of cholesterol fatty acids in aorta of rabbits fed a cholesterol-enriched diet with added glucosamine. Author(s): Stender S, Astrup P. Source: Atherosclerosis. 1977 February; 26(2): 205-13. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=836356&dopt=Abstract
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Glucosamine for arthritis. Author(s): Keller L. Source: Adv Nurse Pract. 2003 June; 11(6): 19-21, 100. Review. No Abstract Available. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12807050&dopt=Abstract
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Glucosamine in the treatment of osteoarthritis. Author(s): Delafuente JC. Source: Rheumatic Diseases Clinics of North America. 2000 February; 26(1): 1-11, Vii. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10680190&dopt=Abstract
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Glucosamine sulfate use and delay of progression of knee osteoarthritis: a 3-year, randomized, placebo-controlled, double-blind study. Author(s): Pavelka K, Gatterova J, Olejarova M, Machacek S, Giacovelli G, Rovati LC.
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Source: Archives of Internal Medicine. 2002 October 14; 162(18): 2113-23. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12374520&dopt=Abstract •
Glucosamine therapy: does it work? Author(s): Bellamy N, Lybrand SG. Source: The Medical Journal of Australia. 2001 October 15; 175(8): 399-400. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11700830&dopt=Abstract
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In vivo chondroprotection and metabolic synergy of glucosamine and chondroitin sulfate. Author(s): Lippiello L, Woodward J, Karpman R, Hammad TA. Source: Clinical Orthopaedics and Related Research. 2000 December; (381): 229-40. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11127660&dopt=Abstract
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Labelling of the gangliosidic fraction from brains of chickens exposed to different levels of stimulation after injection of (6-3H)glucosamine. Author(s): Maccioni AH, Gimenez MS, Caputto BL, Caputto R. Source: Brain Research. 1974 June 28; 73(3): 503-11. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=4835371&dopt=Abstract
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Long-term effects of glucosamine sulphate on osteoarthritis progression: a randomised, placebo-controlled clinical trial. Author(s): Reginster JY, Deroisy R, Rovati LC, Lee RL, Lejeune E, Bruyere O, Giacovelli G, Henrotin Y, Dacre JE, Gossett C. Source: Lancet. 2001 January 27; 357(9252): 251-6. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11214126&dopt=Abstract
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N-acetyl-D-glucosamine-asparagine structure in ribosome-inactivating proteins from the seeds of Luffa cylindrica and Phytolacca americana. Author(s): Islam MR, Kung SS, Kimura Y, Funatsu G. Source: Agric Biol Chem. 1991 May; 55(5): 1375-81. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1368685&dopt=Abstract
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N-acetylglucosamine binding activity in extracts of adult newt skin. Author(s): Atnip KD, Hade EP, Donaldson DJ. Source: Comp Biochem Physiol A. 1988; 90(3): 475-9. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=2901319&dopt=Abstract
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N-acetylglucosamine changes permeability of peritoneum during chronic peritoneal dialysis in rats. Author(s): Wu G, Wieczorowska-Tobis K, Polubinska A, Korybalska K, Filas V, Tam P, French I, Breborowicz A.
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Source: Perit Dial Int. 1998 March-April; 18(2): 217-24. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9576372&dopt=Abstract •
N-acetylglucosamine prevents IL-1 beta-mediated activation of human chondrocytes. Author(s): Shikhman AR, Kuhn K, Alaaeddine N, Lotz M. Source: Journal of Immunology (Baltimore, Md. : 1950). 2001 April 15; 166(8): 5155-60. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11290798&dopt=Abstract
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Nutraceuticals as therapeutic agents in osteoarthritis. The role of glucosamine, chondroitin sulfate, and collagen hydrolysate. Author(s): Deal CL, Moskowitz RW. Source: Rheumatic Diseases Clinics of North America. 1999 May; 25(2): 379-95. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=10356424&dopt=Abstract
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Preferential incorporation of tunicamycin, an antiviral antibiotic containing glucosamine, into the cell membranes. Author(s): Takatsuki A, Tamura G. Source: J Antibiot (Tokyo). 1972 June; 25(6): 362-4. No Abstract Available. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=4630978&dopt=Abstract
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Preformulation studies and characterization of proposed chondroprotective agents: glucosamine HCl and chondroitin sulfate. Author(s): Ebube NK, Mark W, Hahm H. Source: Pharmaceutical Development and Technology. 2002 November; 7(4): 457-69. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12503527&dopt=Abstract
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Proteins of the kidney microvillar membrane. Effects of monensin, vinblastine, swainsonine and glucosamine on the processing and assembly of endopeptidase24.11 and dipeptidyl peptidase IV in pig kidney slices. Author(s): Stewart JR, Kenny AJ. Source: The Biochemical Journal. 1984 December 1; 224(2): 559-68. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=6440534&dopt=Abstract
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Purification and characterization of N-acetylglucosamine 6-phosphate deacetylase with activity against N-acetylglucosamine from Vibrio cholerae non-O1. Author(s): Yamano N, Matsushita Y, Kamada Y, Fujishima S, Arita M. Source: Bioscience, Biotechnology, and Biochemistry. 1996 August; 60(8): 1320-3. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8987551&dopt=Abstract
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Structural and symptomatic efficacy of glucosamine and chondroitin in knee osteoarthritis: a comprehensive meta-analysis. Author(s): Richy F, Bruyere O, Ethgen O, Cucherat M, Henrotin Y, Reginster JY.
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Source: Archives of Internal Medicine. 2003 July 14; 163(13): 1514-22. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12860572&dopt=Abstract •
Sulfated polysaccharides (chondroitin sulfate and carrageenan) plus glucosamine sulfate are potent inhibitors of HIV. Author(s): Konlee M. Source: Posit Health News. 1998 Fall; (No 17): 4-7. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11366556&dopt=Abstract
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Symbiotic host specificity between leguminous plants and rhizobia is determined by substituted and acylated glucosamine oligosaccharide signals. Author(s): Lerouge P. Source: Glycobiology. 1994 April; 4(2): 127-34. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=8054712&dopt=Abstract
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Th1 adjuvant N-acetyl-D-glucosamine polymer up-regulates Th1 immunity but down-regulates Th2 immunity against a mycobacterial protein (MPB-59) in interleukin-10-knockout and wild-type mice. Author(s): Shibata Y, Honda I, Justice JP, Van Scott MR, Nakamura RM, Myrvik QN. Source: Infection and Immunity. 2001 October; 69(10): 6123-30. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=11553551&dopt=Abstract
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The effect of an oral supplement containing glucosamine, amino acids, minerals, and antioxidants on cutaneous aging: a preliminary study. Author(s): Murad H, Tabibian MP. Source: The Journal of Dermatological Treatment. 2001 March; 12(1): 47-51. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12171689&dopt=Abstract
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The effect of glucosamine supplementation on people experiencing regular knee pain. Author(s): Braham R, Dawson B, Goodman C. Source: British Journal of Sports Medicine. 2003 February; 37(1): 45-9; Discussion 49. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12547742&dopt=Abstract
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The effect of glucosamine-chondroitin supplementation on glycosylated hemoglobin levels in patients with type 2 diabetes mellitus: a placebo-controlled, double-blinded, randomized clinical trial. Author(s): Scroggie DA, Albright A, Harris MD. Source: Archives of Internal Medicine. 2003 July 14; 163(13): 1587-90. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=12860582&dopt=Abstract
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The mannose-specific plant lectins from Cymbidium hybrid and Epipactis helleborine and the (N-acetylglucosamine)n-specific plant lectin from Urtica dioica
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are potent and selective inhibitors of human immunodeficiency virus and cytomegalovirus replication in vitro. Author(s): Balzarini J, Neyts J, Schols D, Hosoya M, Van Damme E, Peumans W, De Clercq E. Source: Antiviral Research. 1992 June; 18(2): 191-207. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1329650&dopt=Abstract •
The role of glucosamine sulfate and chondroitin sulfates in the treatment of degenerative joint disease. Author(s): Kelly GS. Source: Alternative Medicine Review : a Journal of Clinical Therapeutic. 1998 February; 3(1): 27-39. Review. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9600024&dopt=Abstract
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The role of lipid peroxidation in the possible involvement of membrane-bound monoamine oxidases in gamma-aminobutyric acid and glucosamine deamination in rat brain. Focus on chemical pathogenesis of experimental audiogenic epilepsy. Author(s): Medvedev AE, Rajgorodskaya DI, Gorkin VZ, Fedotova IB, Semiokhina AF. Source: Mol Chem Neuropathol. 1992 February-April; 16(1-2): 187-201. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=1520403&dopt=Abstract
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The sialic acids. v. n-acyl-d-glucosamine 2-epimerase. Author(s): GHOSH S, ROSEMAN S. Source: The Journal of Biological Chemistry. 1965 April; 240: 1531-6. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=14285488&dopt=Abstract
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Thermodynamic parameters of the interaction of Urtica dioica agglutinin with Nacetylglucosamine and its oligomers. Author(s): Lee RT, Gabius HJ, Lee YC. Source: Glycoconjugate Journal. 1998 July; 15(7): 649-55. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=9881770&dopt=Abstract
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Zinc binding and its trapping by allosteric transition in glucosamine-6-phosphate deaminase from Escherichia coli. Author(s): Altamirano MM, Calcagno M. Source: Biochimica Et Biophysica Acta. 1990 May 8; 1038(3): 291-4. http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_ uids=2111170&dopt=Abstract
Additional Web Resources A number of additional Web sites offer encyclopedic information covering CAM and related topics. The following is a representative sample: •
Alternative Medicine Foundation, Inc.: http://www.herbmed.org/
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AOL: http://search.aol.com/cat.adp?id=169&layer=&from=subcats
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Chinese Medicine: http://www.newcenturynutrition.com/
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drkoop.com®: http://www.drkoop.com/InteractiveMedicine/IndexC.html
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Family Village: http://www.familyvillage.wisc.edu/med_altn.htm
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Google: http://directory.google.com/Top/Health/Alternative/
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Healthnotes: http://www.healthnotes.com/
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MedWebPlus: http://medwebplus.com/subject/Alternative_and_Complementary_Medicine
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Open Directory Project: http://dmoz.org/Health/Alternative/
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HealthGate: http://www.tnp.com/
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WebMD®Health: http://my.webmd.com/drugs_and_herbs
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WholeHealthMD.com: http://www.wholehealthmd.com/reflib/0,1529,00.html
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Yahoo.com: http://dir.yahoo.com/Health/Alternative_Medicine/
The following is a specific Web list relating to glucosamine; please note that any particular subject below may indicate either a therapeutic use, or a contraindication (potential danger), and does not reflect an official recommendation: •
General Overview Arthritis Source: Integrative Medicine Communications; www.drkoop.com Bursitis Source: Integrative Medicine Communications; www.drkoop.com Diabetes Source: Prima Communications, Inc.www.personalhealthzone.com Inflammatory Bowel Disease Source: Integrative Medicine Communications; www.drkoop.com Osteoarthritis Source: Healthnotes, Inc.; www.healthnotes.com Osteoarthritis Source: Integrative Medicine Communications; www.drkoop.com Osteoarthritis Source: Prima Communications, Inc.www.personalhealthzone.com Reiter's Syndrome Source: Integrative Medicine Communications; www.drkoop.com
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Ulcerative Colitis Source: Integrative Medicine Communications; www.drkoop.com Wound Healing Source: Healthnotes, Inc.; www.healthnotes.com •
Alternative Therapy Chiropractic Source: Integrative Medicine Communications; www.drkoop.com
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Herbs and Supplements Astragalus Mem Alternative names: Huang-Qi; Astragalus membranaceus Source: Alternative Medicine Foundation, Inc.; www.amfoundation.org Glucosamine Source: Healthnotes, Inc.; www.healthnotes.com Glucosamine Source: Integrative Medicine Communications; www.drkoop.com Glucosamine Source: Prima Communications, Inc.www.personalhealthzone.com Glucosamine Source: WholeHealthMD.com, LLC.; www.wholehealthmd.com Hyperlink: http://www.wholehealthmd.com/refshelf/substances_view/0,1525,790,00.html Msm Source: WholeHealthMD.com, LLC.; www.wholehealthmd.com Hyperlink: http://www.wholehealthmd.com/refshelf/substances_view/0,1525,807,00.html N-acetyl-glucosamine Source: Healthnotes, Inc.; www.healthnotes.com Nettle Source: Integrative Medicine Communications; www.drkoop.com Phytolacca Alternative names: Poke root, Endod; Phytolacca dodecandra L. Source: Alternative Medicine Foundation, Inc.; www.amfoundation.org Plantago Psyllium Alternative names: Psyllium, Ispaghula; Plantago psyllium/ovata Source: Alternative Medicine Foundation, Inc.; www.amfoundation.org
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Same (s-adenosylmethionine) Source: Prima Communications, Inc.www.personalhealthzone.com Urtica Dioica Source: Integrative Medicine Communications; www.drkoop.com Urtica Urens Source: Integrative Medicine Communications; www.drkoop.com Withania Ashwagandha Alternative names: Ashwagandha; Withania somnifera L. Source: Alternative Medicine Foundation, Inc.; www.amfoundation.org
General References A good place to find general background information on CAM is the National Library of Medicine. It has prepared within the MEDLINEplus system an information topic page dedicated to complementary and alternative medicine. To access this page, go to the MEDLINEplus site at http://www.nlm.nih.gov/medlineplus/alternativemedicine.html. This Web site provides a general overview of various topics and can lead to a number of general sources.
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CHAPTER 4. DISSERTATIONS ON GLUCOSAMINE Overview In this chapter, we will give you a bibliography on recent dissertations relating to glucosamine. We will also provide you with information on how to use the Internet to stay current on dissertations. IMPORTANT NOTE: When following the search strategy described below, you may discover non-medical dissertations that use the generic term “glucosamine” (or a synonym) in their titles. To accurately reflect the results that you might find while conducting research on glucosamine, we have not necessarily excluded nonmedical dissertations in this bibliography.
Dissertations on Glucosamine ProQuest Digital Dissertations, the largest archive of academic dissertations available, is located at the following Web address: http://wwwlib.umi.com/dissertations. From this archive, we have compiled the following list covering dissertations devoted to glucosamine. You will see that the information provided includes the dissertation’s title, its author, and the institution with which the author is associated. The following covers recent dissertations found when using this search procedure: •
Influence of Glucosamine on Matrix Metalloproteinase Expression and Activity in Lps-stimulated Equine Chondrocytes by Byron, Christopher Robert; MS from Michigan State University, 2002, 74 pages http://wwwlib.umi.com/dissertations/fullcit/1411915
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Purification and Properties of Uridine Diphospho-n-acetylenolpyruvyl-glucosamine Reductase by Taku, Akio; PhD from University of Toronto (Canada), 1973 http://wwwlib.umi.com/dissertations/fullcit/NK22369
Keeping Current Ask the medical librarian at your library if it has full and unlimited access to the ProQuest Digital Dissertations database. From the library, you should be able to do more complete searches via http://wwwlib.umi.com/dissertations.
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CHAPTER 5. CLINICAL TRIALS AND GLUCOSAMINE Overview In this chapter, we will show you how to keep informed of the latest clinical trials concerning glucosamine.
Recent Trials on Glucosamine The following is a list of recent trials dedicated to glucosamine.8 Further information on a trial is available at the Web site indicated. •
Effects of Oral Glucosamine on Insulin and Blood Vessel Activity in Normal and Obese People Condition(s): Obesity; Insulin Resistance Study Status: This study is currently recruiting patients. Sponsor(s): National Center for Complementary and Alternative Medicine (NCCAM) Purpose - Excerpt: This study will examine whether glucosamine affects the way the body responds to insulin. Insulin is a hormone that causes the body to use glucose (sugar). Insulin does not work as well in overweight people, causing a condition called insulin resistance. Insulin also increases the flow of blood into muscle by opening inactive blood vessels. This study will test whether glucosamine, a nutritional supplement that many people take to treat arthritis, can cause or worsen insulin resistance or change how blood vessels react to insulin in normal weight and overweight people. Healthy normal weight and overweight volunteers between 21 and 65 years of age may be eligible for this study. Candidates will be screened with a brief physical examination, medical history, and blood and urine tests. After screening, participants will have three additional outpatient clinic visits for the following procedures: Visit 1 - Glucose clamp test to measure the body's response to insulin: For this procedure, a needle is placed in a vein of each arm, one for drawing blood samples, and one for infusing glucose and a potassium solution. The glucose is infused continuously during this 4-hour test and blood is drawn frequently to monitor glucose and insulin levels. After the test, blood glucose levels are monitored for another 2 hours
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These are listed at www.ClinicalTrials.gov.
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to make sure they remain at an adequate level to prevent hypoglycemia (low blood sugar). - Blood flow measurement: Blood flow in the brachial artery of the arm is measured to assess how many capillaries (very small blood vessels) are being used to supply nutrients and oxygen to the muscle in the forearm. This test is done at the same time as the glucose clamp test. Blood flow is measured using a technique called contrast ultrasound. A small amount of contrast agent consisting of gas-filled bubbles the size of red blood cells is infused over 10 minutes through one of the catheters placed in the vein for the glucose clamp test. The contrast agent is infused twice, once at the beginning of the glucose clamp test and once at the end of the test. The contrast material creates a signal in response to ultrasound that provides information about the distribution of capillaries in the forearm. - Assignment to medication group: Participants are randomly assigned to take either glucosamine or placebo three times a day by mouth for 6 weeks. At the end of the 6 weeks, no study drug is taken for 1 week, and then participants "cross-over" medications, those who took glucosamine for the first 6 weeks take placebo for the next 6 weeks and vice versa. Visits 2 and 3 For these visits, the glucose clamp test and blood flow measurements are repeated. Visit 2 is scheduled at the end of the first 6week treatment period, and Visit 3 is scheduled at the end of the second 6-week treatment period. Phase(s): Phase I Study Type: Interventional Contact(s): see Web site below Web Site: http://clinicaltrials.gov/ct/show/NCT00065377 •
Glucosamine/Chondroitin Arthritis Intervention Trial (GAIT) Condition(s): Osteoarthritis Study Status: This study is currently recruiting patients. Sponsor(s): Department of Veterans Affairs; Department of Veterans Affairs Cooperative Studies Program; National Institutes of Health (NIH); National Center for Complementary and Alternative Medicine (NCCAM) Purpose - Excerpt: This study will determine whether glucosamine, chondroitin sulfate and/or the combination of glucosamine and chondroitin sulfate are more effective than placebo and whether the combination is more effective than glucosamine or chondroitin sulfate alone in the treatment of knee pain associated with osteoarthritis (OA) of the knee. These substances, marketed in the United States as nutritional supplements, have been widely touted by the lay press and by anecdotal personal experience as effective in treating OA. To date, however, only a few small studies have been published in the worldwide literature. The study proposed herein has been carefully constructed to definitively determine the efficacy of these agents. Phase(s): Phase III Study Type: Interventional Contact(s): see Web site below Web Site: http://clinicaltrials.gov/ct/show/NCT00032890
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Keeping Current on Clinical Trials The U.S. National Institutes of Health, through the National Library of Medicine, has developed ClinicalTrials.gov to provide current information about clinical research across the broadest number of diseases and conditions. The site was launched in February 2000 and currently contains approximately 5,700 clinical studies in over 59,000 locations worldwide, with most studies being conducted in the United States. ClinicalTrials.gov receives about 2 million hits per month and hosts approximately 5,400 visitors daily. To access this database, simply go to the Web site at http://www.clinicaltrials.gov/ and search by “glucosamine” (or synonyms). While ClinicalTrials.gov is the most comprehensive listing of NIH-supported clinical trials available, not all trials are in the database. The database is updated regularly, so clinical trials are continually being added. The following is a list of specialty databases affiliated with the National Institutes of Health that offer additional information on trials: •
For clinical studies at the Warren Grant Magnuson Clinical Center located in Bethesda, Maryland, visit their Web site: http://clinicalstudies.info.nih.gov/
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For clinical studies conducted at the Bayview Campus in Baltimore, Maryland, visit their Web site: http://www.jhbmc.jhu.edu/studies/index.html
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For cancer trials, visit the National Cancer Institute: http://cancertrials.nci.nih.gov/
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For eye-related trials, visit and search the Web page of the National Eye Institute: http://www.nei.nih.gov/neitrials/index.htm
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For heart, lung and blood trials, visit the Web page of the National Heart, Lung and Blood Institute: http://www.nhlbi.nih.gov/studies/index.htm
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For trials on aging, visit and search the Web site of the National Institute on Aging: http://www.grc.nia.nih.gov/studies/index.htm
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For rare diseases, visit and search the Web site sponsored by the Office of Rare Diseases: http://ord.aspensys.com/asp/resources/rsch_trials.asp
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For alcoholism, visit the National Institute on Alcohol Abuse and Alcoholism: http://www.niaaa.nih.gov/intramural/Web_dicbr_hp/particip.htm
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For trials on infectious, immune, and allergic diseases, visit the site of the National Institute of Allergy and Infectious Diseases: http://www.niaid.nih.gov/clintrials/
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For trials on arthritis, musculoskeletal and skin diseases, visit newly revised site of the National Institute of Arthritis and Musculoskeletal and Skin Diseases of the National Institutes of Health: http://www.niams.nih.gov/hi/studies/index.htm
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For hearing-related trials, visit the National Institute on Deafness and Other Communication Disorders: http://www.nidcd.nih.gov/health/clinical/index.htm
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For trials on diseases of the digestive system and kidneys, and diabetes, visit the National Institute of Diabetes and Digestive and Kidney Diseases: http://www.niddk.nih.gov/patient/patient.htm
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For drug abuse trials, visit and search the Web site sponsored by the National Institute on Drug Abuse: http://www.nida.nih.gov/CTN/Index.htm
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For trials on mental disorders, visit and search the Web site of the National Institute of Mental Health: http://www.nimh.nih.gov/studies/index.cfm
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For trials on neurological disorders and stroke, visit and search the Web site sponsored by the National Institute of Neurological Disorders and Stroke of the NIH: http://www.ninds.nih.gov/funding/funding_opportunities.htm#Clinical_Trials
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CHAPTER 6. PATENTS ON GLUCOSAMINE Overview Patents can be physical innovations (e.g. chemicals, pharmaceuticals, medical equipment) or processes (e.g. treatments or diagnostic procedures). The United States Patent and Trademark Office defines a patent as a grant of a property right to the inventor, issued by the Patent and Trademark Office.9 Patents, therefore, are intellectual property. For the United States, the term of a new patent is 20 years from the date when the patent application was filed. If the inventor wishes to receive economic benefits, it is likely that the invention will become commercially available within 20 years of the initial filing. It is important to understand, therefore, that an inventor’s patent does not indicate that a product or service is or will be commercially available. The patent implies only that the inventor has “the right to exclude others from making, using, offering for sale, or selling” the invention in the United States. While this relates to U.S. patents, similar rules govern foreign patents. In this chapter, we show you how to locate information on patents and their inventors. If you find a patent that is particularly interesting to you, contact the inventor or the assignee for further information. IMPORTANT NOTE: When following the search strategy described below, you may discover non-medical patents that use the generic term “glucosamine” (or a synonym) in their titles. To accurately reflect the results that you might find while conducting research on glucosamine, we have not necessarily excluded nonmedical patents in this bibliography.
Patents on Glucosamine By performing a patent search focusing on glucosamine, you can obtain information such as the title of the invention, the names of the inventor(s), the assignee(s) or the company that owns or controls the patent, a short abstract that summarizes the patent, and a few excerpts from the description of the patent. The abstract of a patent tends to be more technical in nature, while the description is often written for the public. Full patent descriptions contain much more information than is presented here (e.g. claims, references, figures, diagrams, etc.). We will tell you how to obtain this information later in the chapter. The following is an 9Adapted
from the United States Patent and Trademark Office: http://www.uspto.gov/web/offices/pac/doc/general/whatis.htm.
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example of the type of information that you can expect to obtain from a patent search on glucosamine: •
Aminoalkyl glucosamine phosphate compounds and their use as adjuvants and immunoeffectors Inventor(s): Johnson; David A. (Hamilton, MT), Sowell; C. Gregory (Hamilton, MT) Assignee(s): Corixa Corporation (Seattle, WA) Patent Number: 6,355,257 Date filed: May 7, 1998 Abstract: Aminoalkyl glucosamine phosphate compounds that are adjuvants and immunoeffectors are described and claimed. The compounds have a 2-deoxy-2-amino glucose in glycosidic linkage with an aminoalkyl (aglycon) group. Compounds are phosphorylated at the 4 or 6 carbon on the glucosamine ring and comprise three 3alkanoyloxyalkanoyl residues. The compounds augment antibody production in immunized animals as well as stimulate cytokine production and activate macrophages. Methods for using the compounds as adjuvants and immunoeffectors are also disclosed. Excerpt(s): Humoral immunity and cell-mediated immunity are the two major branches of the mammalian immune response. Humoral immunity involves the generation of antibodies to foreign antigens. Antibodies are produced by B-lymphocytes. Cellmediated immunity involves the activation of T-lymphocytes which either act upon infected cells bearing foreign antigens or stimulate other cells to act upon infected cells. Both branches of the mammalian immune system are important in fighting disease. Humoral immunity is the major line of defense against bacterial pathogens. In the case of viral disease, the induction of cytotoxic T lymphocytes (CTLs) appears to be crucial for protective immunity. An effective vaccine stimulates both branches of the immune system to protect against disease. Vaccines present foreign antigens from disease causing agents to a host so that the host can mount a protective immune response. Often vaccine antigens are killed or attenuated forms of the microbes which cause the disease. The presence of non-essential components and antigens in these killed or attenuated vaccines has encouraged considerable efforts to refine vaccine components including developing well-defined synthetic antigens using chemical and recombinant techniques. The refinement and simplification of microbial vaccines, however, has led to a concomitant loss in potency. Low-molecular weight synthetic antigens, though devoid of potentially harmful contaminants, are themselves not very immunogenic. These observations have led investigators to add adjuvants to vaccine compositions to potentiate the activity of the refined vaccine components. Presently, the only adjuvant licensed for human use in the United States is alum, a group of aluminum salts (e.g., aluminum hydroxide, aluminum phosphate) in which vaccine antigens are formulated. Particulate carriers like alum serve to promote the uptake, processing and presentation of soluble antigens by macrophage. Alum, however, is not without side-effects and enhances humoral (antibody) immunity only. Web site: http://www.delphion.com/details?pn=US06355257__
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Cartilage enhancing food supplements and methods of preparing the same Inventor(s): Stone; Kevin R. (Mill Valley, CA) Assignee(s): Joint Juice, Inc. (San Francisco, CA) Patent Number: 6,432,929 Date filed: June 21, 2000 Abstract: A food supplement, either in the form of a snack bar or a beverage, which contains one or more cartilage enhancing supplements is provided. The cartilage supplements include chondroitin, glucosamine, and hyaluronic acid. The food supplement may additionally be fortified with cetyl myristoleate. The beverage is a mixture of a juice drink base which may include a water-based fruit flavored juice prepared using a pasteurization process at a relatively high temperature and a cartilage supplement solution which includes a cartilage supplement prepared at a relatively low temperature. The beverage may be carbonated, non-carbonated or concentrated. The preferred cartilage supplement is glucosamine, preferably associated with a counter ion, more preferably as glucosamine HCl. Excerpt(s): The present invention relates to food supplements, such for example, snack bars and beverages which are fortified with one or more cartilage supplements. Nutritional bars and energy drinks are convenient nutritional supplements, particularly for those persons too busy to eat regular meals and for hikers, cyclists, runners or other athletes who need prepackaged, ready-to-eat, high-energy snacks while they are exercising. Such bars and drinks are also convenient nutritional supplements for the elderly who need prepackaged, ready-to-eat snacks. Additionally, such food supplements can supply consumers with the necessary vitamins and minerals specified in the recommended daily allowances provided by the U.S. government. By way of example, U.S. Pat. No. 4,543,262 discloses a high protein, low or no lactose, vitamin and mineral fortified, nutritionally-balanced snack bar. Additionally, U.S. Pat. No. 3,814,819 teaches a protein-fortified food bar composed of several baked crisp wafers layered on top of the other with a creamy filling between them. The creamy filling contains added vitamins, providing twenty-five percent (25%) of the recommended daily allowance of vitamins and minerals. U.S. Pat. No. 4,152,462 teaches a highly nutritious protein and vitamin enriched food bar, having a marshmallow base. Lastly, U.S. Pat. No. 3,901,799 discloses a high protein chocolate bar. Caseinate and peanut butter are added to a mixture of chocolate and cocoa butter. Vitamins compatible with the ingredients, it is disclosed, can be added to the snack bar. Web site: http://www.delphion.com/details?pn=US06432929__
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Chemical composition for aiding the absorption, binding and elimination of undigested fat Inventor(s): Diaz; Jose A. (2950 Jackson Ave., Coconut Grove, FL 33133), Naranjo; Eduardo M. (5009 SW. 71st Pl., Miami, FL 33155) Assignee(s): none reported Patent Number: 6,447,812 Date filed: March 13, 2001 Abstract: A composition and method for reducing cholesterol, facilitating weight loss and aiding in the maintenance of a stable weight in humans, wherein the composition
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includes at least one preferred embodiment comprising a mixture of oat bran generally in an amount of about 83% to 85% by weight, glucosamine HCL generally in an amount about 6% to 8% by weight, glucomannan generally in an amount of 5% to 6% by weight, an amount of apple pectin or other fruit or vegetable pectin generally in an amount of about 2% by weight. Stearic acid may also be included in the composition in an amount of generally about 1% to 2% by weight of the composition. Excerpt(s): The present invention relates to a chemical composition and a method for reducing cholesterol as well accomplishing weight loss in humans, whereby a human ingests the chemical composition in recommended dosages prior to eating a meal, and thereby facilitates the binding of undigested fat to a fibrous agent for rapid elimination from the human body. In this day and age, many people's lifestyles have become less physically active. A natural result of a sedentary lifestyle is the tendency to gain weight. Indeed, it is commonly thought that many people are now over-weight with obesity being a growing problem. Due to this trend, countless efforts have been made to help people control their weight. As a few examples, many have proclaimed to have won the "battle of the bulge" with a specific diet program or a particular exercise program. Others have explored hypnosis and other mechanisms for controlling the appetite of an individual. Still others in the scientific arena have formulated sugar substitutes and are pursuing fat substitutes as methods to reduce the caloric intake of an individual hopefully, without sacrificing the taste of otherwise highly fattening foods. While these efforts are generally capable of aiding many in their fight to lose weight or to maintain a desired weight, many are in general, ineffective or simply not practical. For example, some good meaning souls have tried in earnest to follow a particular diet plan but eventually, fall off the plan lacking will-power to continue for weeks and months at a time. This is equally true of those who try hypnosis and similar weight-loss gimmicks. Finally, some view sugar substitutes as being tasteless or worse, as carrying an intolerable health risk, given that some studies have linked them to carcinogens and/or the formation of brain tumors. It has been appreciated in recent years that the fat content of foods eaten are a major culprit behind human weight gain. For example, regardless of the type of fat present in a food product, fat has the highest caloric value per gram-about 9 calories per gram--of any food group. It is understood that the body tends to store fat for future use, rather than to utilize it immediately, and this factor helps lead to weight-gain. However, in recent years it has been recognized, that there is a connection between the amount of fat stored in the body and the level of cholesterol in the body. A diet high in fat is more likely to result in the development of higher cholesterol levels. As cholesterol has been indicated as a factor in arteriosclerosis or hardening of the arteries, the risk for heart disease and/or a heart attack is elevated when a diet high in fat is followed. Unfortunately, fat also makes many food items more tasty--whether butter on bread, dressings on salads, sour cream on potatoes, or frosting on cake--and are therefore, difficult to eliminate entirely from one's diet. Thus, fat usually finds its way into the body. Once it does so, a healthy body automatically secretes lipase, an enzyme that accelerates synthesis of fats, i.e., breaking down the fat molecule. The majority of all fats in foods are present in "triglyceride form", which the body seeks to break down by removing the glycerol molecule from the triglyceride and thereby, release the free fatty acids. Once this occurs, the body is well on its way to absorbing the fat and likely, storing same instead of utilizing it for energy. Web site: http://www.delphion.com/details?pn=US06447812__
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Composition for the treatment of osteoarthritis Inventor(s): Graus; Ivo Maria Franciscus (Wg Ede, NL), Smit; Hobbe Friso (As Utrecht, NL) Assignee(s): N.V. Nutricia (Zoetermeer, NL) Patent Number: 6,492,429 Date filed: September 14, 2000 Abstract: Osteoarthritis is treated by a composition containing both apocynin and an inhibitor of inducible nitric oxide synthase such as curcumin. Further components such as boswellic acids, glucosamine, acetylcysteine and boron further enhance the beneficial effect of apocynin and curcumin. Excerpt(s): The invention is concerned with compositions for the treatment of osteoarthritis and related diseases and with methods for treating osteoarthritis. Osteoarthritis (OA) is a degenerative joint disease, which develops by wear and tear of the joints during aging. OA mostly affects the weight-bearing joints such as spine, knees and hips, but thumb and finger joints may also be affected. Repetitive mechanical injury of the cartilage eventually results in loss of cartilage and damage to joint surfaces and adjacent bone. As a result of the tissue destruction, inflammatory cells invade the joint and the synovial membrane which is manifested by pain, swelling and stiffness of the affected joints. The repetitive mechanical injury leads to pathological changes that result in loss of proteoglycans and collagen from the cartilage matrix, which in turn leads to surface erosion and decreased loading capacity, In OA, chondro-cytes show a reduced potential to synthesize matrix constituents (proteoglycans and collagen fibers) and the expression of proteolytic enzymes (called matrix metallo-proteases, MNMP's) contributes to cartilage destruction and release of proteoglycan fragments in the synovial fluid. The inflammatory responses to the mechanical insults further contribute to cartilage destruction. The inflammatory mediator interleukin I (IL-1) is considered as the principal mediator of cartilage destruction. It induces a number of changes in chondrocytes, including the concurrent generation of significant amounts of NO (nitrogen oxide) and superoxide radicals by inducible NO synthase (iNOS) and NADPH oxidase, respectively. NO reacts with superoxide to form peroxynitrite, which is largely responsible for the decrease in proteoglycan synthesis induced by IL-1. The role of superoxide was further demonstrated by the ability of superoxide dismutase to reverse the decrease in proteoglycan synthesis. The prevention of peroxynitrite formation via selective inhibition of iNOS and thus NO formation in vivo resulted in a marked decrease of MMP's. In addition, intra-articular treatment of OA patients with superoxide dismutase reduces symptoms of OA for prolonged periods. These studies demonstrate that induction of catabolic enzymes (MMP's) and cartilage destruction is mediated via the formation of NO and O.sub.2.sup.- radicals by chondrocytes or inflammatory cells. While the primary cause of OA is mechanical damage, rheumatoid arthritis (RA) is mainly the result of an autoimmune response that leads to chronic inflammation in the joint. Contrary to OA, typical manifestations of RA are an increase of parameters that are associated with inflammation, such as haematocrite and white blood cell count and pannus formation or hyperplasia of the joint capsule that leads to deformed joints. This in turn leads to morning stiffness. Although the (primary) aetiology of RA and OA are different, the pathological processes at a later stage result in some manifestations that are similar such as joint pain, cartilage degradation and general joint disability. Lafeber et al. (Rheumatology, 1999 (38) 1088-1093) describe in vitro studies on the utility of apocynin (4-hydroxy-3-methoxy-acetophenone, acetovanillone) for the treatment of rheumatoid arthritis.
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Web site: http://www.delphion.com/details?pn=US06492429__ •
Compositions useful in the treatment of diseases of connective tissues Inventor(s): Ekanayake; V. G. Sunetra (Halifax, CA) Assignee(s): Ocean Nutrition Canada Limited (Nova Scotia, CA) Patent Number: 6,632,804 Date filed: April 25, 2001 Abstract: Compositions comprising ferrous ion and an ascorbate have a synergistic effect on cartilage development. Therapeutic compositions comprising ferrous ion and an ascorbate are therefore useful in the treatment of osteoarthritis. The addition of a glucosamine, such as glucosamine hydrochloride, to the composition has a further enhanced effect on cartilage production. Therapeutic compositions comprising ferrous ion, an ascorbate and a glucosamine derivative are even more useful in the treatment of osteoarthritis. Excerpt(s): This invention relates to therapeutic compositions for use in treating diseases of connective tissues in animals, more particularly, for use in treating osteoarthritis in mammals, such as humans, dogs, cats, pigs, horses, cows, goats and sheep. Arthritic diseases, characterized by the pain, inflammation and stiffness of the joints leading to reduced range of mobility, are due to the degradation of connective tissue (mainly cartilage) in joints. Such diseases particularly affect weight-bearing joints such as the hips, knees, spine, ankles and feet and those joints with frequent movement such as hands, arms and neck. Osteoarthritis (OA) in particular is a degenerative disease of the joint cartilage resulting in narrowing of the joint space and changes in the underlying bone (Barclay, et al., The Annals of Pharmacotherapy, (May, 1998) 32: 574-79). OA is the most common form of arthritis among people and it affects approximately one in ten people in North America. People of all ages can get OA, but it more often affects older people and women. For example, 85% of the age group 70 years or older is affected by OA (The Arthritis Society website, (http://www.arthritis.ca), Feb. 4, 2000, published by The Arthritis Society). OA is not limited to humans, but occurs in other mammals such as horses, dogs, cats, mice and guinea pigs as well, making OA one of the most common sources of chronic pain seen by veterinarians. Web site: http://www.delphion.com/details?pn=US06632804__
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Effervescent vitaceutical compositions and related methods Inventor(s): Pandya; Mahendra (8018 Daytona St. NW., Massillon, OH 44646-2336) Assignee(s): none reported Patent Number: 6,589,555 Date filed: December 27, 2000 Abstract: The invention relates to a dry effervescent composition containing inulin, and optionally containing at least one vitaceutical and other active agents. The effervescent products optionally contain lubricants and essential oils and can generate magnesium malate, a therapeutic effector. The invention also relates to a dry effervescent composition containing glucosamine. The invention also encompasses methods of preparing the effervescent compositions of the invention.
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Excerpt(s): The invention relates to a dry effervescent composition containing at least one vitaceutical, and optionally containing inulin and other active agents. The effervescent products optionally contain lubricants and essential oils and can generate magnesium malate, a therapeutic effector. The invention also encompasses methods of preparing the effervescent compositions of the invention. Many types of formulations are available for administering medicaments to a subject. Solid dosage forms which are swallowed, such as tablets and capsules are useful because they provide quick and easy administration routes as well as accurate dosages. Many medicinal compositions, including vitamins, nutritional supplements and medicines have unpleasant tastes. These compositions can be administered in the form of a tablet or capsule to avoid unpleasant taste. Solid dosage forms, however, must disintegrate in the gastrointestinal tract and the medicament must dissolve before it is absorbed. As a result, absorption tends to be slower than from a liquid suspension and may be incomplete. Additionally, some subjects have difficulty swallowing tablets and capsules. Another draw-back of solid dosage forms is that tablets and capsules can only have a maximal size which can easily be swallowed and thus the dosage cannot be increased above that size. If more medicament is required, multiple tablets or capsules must be administered. Medicinals can also be administered as liquids, chewables or formulations which dissolve in the mouth. In these instances, it is desirable to add a component which masks the taste of the bitter medicinals. Fruit flavoring mixed with sugars are often used. Web site: http://www.delphion.com/details?pn=US06589555__ •
Fractions of Chlorella extract containing polysaccharide having immunomodulating properties Inventor(s): Kralovec; Jaroslav A. (Halifax, CA) Assignee(s): Ocean Nutrition Canada Limited (Halifax, CA) Patent Number: 6,551,596 Date filed: August 10, 2001 Abstract: Chlorella fractionated extracts containing high molecular weight Chlorella polysaccharide and polysaccharide complexes show immune modulatory, specifically immune stimulatory activity. The fractionated extracts are obtained by size fractionation of an extract of Chlorella and selecting fractions containing high molecular weight polysaccharides and polysaccharide complexes of about 1.times.10.sup.4 Da to about 1.times.10.sup.7 Da. A fraction of about 4.times.10.sup.6 Da to about 1.times.10.sup.7 Da is preferably obtained by size fractionation. The polysaccharide and polysaccharide complexes contain glucose and any combination of: galactose, rhamnose, mannose and arabinose, as well as N-acetyl glucosamine and N-acetyl galactosamine. The extracts may be treated with pronase, DNAse, RNAse and proteases to remove unassociated nucleic acids, ribonucleic acids and proteins. The extracts may also undergo treatment to effect cleavage of specific glycosidic linkages, the linkages being defined by their susceptibility to cleavage by amylase, amyloglucosidase, cellulase or neuraminidase. Chlorella extracts may be administered to a mammal to increase proliferation of splenocytes and increase production of cytokines such as IL-6, IL-10, INF-.gamma. and TNF-.alpha. They may be used as a supplement to a vaccination regimen. Excerpt(s): The present invention relates to Chlorella extracts for use as immunomodulators. Chlorella is a unicellular green algae that has been called a sunpowered supernutrient. Attested beneficial properties of this edible microalgae include wound healing, detoxification, constipation relief and growth stimulation. A number of
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studies have also indicated that Chlorella has beneficial effects on the immune system, both in vitro and in vivo. Chlorella occurs in both fresh water and marine water. Species of the Chlorella genus exhibit striking diversity of physiological and biochemical properties (Kessler, E. "Phycotalk" 1989, 1:141-153; V. Rastogi Publ., New Delhi, India). Chlorella produces little cellulose and other indigestible cell wall material, and hence has been extensively investigated as a possible new source of food, especially as feedstock (Lee, Robert E. "Phycology" 2.sup.nd edition; 1989, page 281; Cambridge University Press). Web site: http://www.delphion.com/details?pn=US06551596__ •
Glucosamine sulfate calcium chloride composition and processes for the preparation of glucosamine sulfate metal chlorides Inventor(s): Burger; Christopher M. (Highstown, NJ), Chopdekar; Vilas M. (Edison, NJ), Schleck; James R. (Somerset, NJ) Assignee(s): Jame Fine Chemicals, Inc. (Bound Brook, NJ) Patent Number: 6,472,380 Date filed: November 8, 2000 Abstract: Glucosamine compositions comprising the compounds glucosamine sulfate metal chloride, wherein the metal, i.e., the cation is potassium, sodium, magnesium, lithium, calcium, zinc or manganese. The compounds have purity levels of at least about 97%, with water present in a maximum amount of about 10 wt. %, based on the weight of the composition. The compounds are prepared by contacting glucosamine hydrochloride with a hydroxide of the metal in the presence of water to form a first aqueous solution of the free glucosamine base and a chloride of the metal, acidifying the first aqueous solution with sulfuric acid to form a second aqueous solution of glucosamine sulfate and the chloride of the metal, and thereafter freeze-drying the second aqueous solution at a temperature and at a reduced pressure for such period of time that at least about 90 wt. % of the water is removed and decomposition of the compound glucosamine sulfate metal chloride is limited to a maximum of about 3%. Excerpt(s): The invention relates to a glucosamine sulfate calcium chloride composition and to processes for preparing glucosamine sulfate metal chloride compositions. The glucosamine sulfate metal chloride compositions of the invention are true compounds having a purity level of at least about 97%. Glucosamine is a well known and widely used substance for the treatment of rheumatic fever, arthritic and arthosic complaints, in the acute as well as chronic forms, as well as in the treatment of pathological conditions originating from metabolic disorders of the osteo-articular tissue. Although products in the marketplace are labeled as, or referred to as, "glucosamine sulfate" or "stabilized glucosamine sulfate," they are misnomers, since such products are not true compounds, but rather are unreacted mixtures of glucosamine hydrochloride and a salt such as potassium or sodium sulfate. Mixed salts of glucosamine hydrochloride and alkaline or earth alkaline metal sulfates such as potassium sulfate, and sodium sulfate are well known. Such mixed salts are used rather than glucosamine sulfate alone since the latter is unstable in view of its highly hygroscopic nature and the facility with which its amino group oxidizes if not completely saltified, see, e.g., U.S. Pat. No. 4,642,340 and U.S. Pat. No. 3,683,076 which discloses a mixture of glucosamine sulfate and glucosamine hydroiodide. Web site: http://www.delphion.com/details?pn=US06472380__
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Glycosaminoglycan and drug compositions containing the same Inventor(s): Hara; Saburo (Takatsuki, JP), Hori; Yusuke (Tokyo, JP), Kamei; Kaeko (Kyoto, JP), Kariya; Yutaka (Yokohama, JP), Onaya; Junichi (Higashimurayama, JP), Takano; Ryo (Kyoto, JP) Assignee(s): Seikagaku Corporation (Tokyo, JP) Patent Number: 6,492,503 Date filed: May 22, 2000 Abstract: There is provided a glycosaminoglycan having a backbone structure comprising a repetitive disaccharide bearing a uronic acid residue and a glucosamine residue, and having sulfate groups, wherein substantially no sulfate group bound to the hydroxyl group at the 6-position of the glucosamine residue in the backbone structure is detected as determined by a chemical disaccharide analysis method in which the glycosaminoglycan is decomposed with nitrous acid, reacted with paranitrophenylhydrazine and analyzed by high performance liquid chromatography, and the molar % of a uronic acid residue having a sulfate group at the 2-position is not less than 45% relative to total uronic acid residues, which is calculated from a disaccharide composition obtained by an enzymatic disaccharide analysis method in which the glycosaminoglycan is digested with glycosaminoglycan-degrading enzymes and analyzed by high performance liquid chromatography. The glycosaminoglycan can be used as an active ingredient of pharmaceuticals. Excerpt(s): The present invention relates to a glycosaminoglycan having sulfate groups, in which substantially all the sulfate groups bound to the 6-positions of the glucosamine residues constituting the glycosaminoglycan are removed and the removal of other sulfate groups is minimized, and to pharmaceuticals comprising the glycosaminoglycan as an active ingredient, in addition to a method for producing the glycosaminoglycan. Heparin is one of glycosaminoglycans having as a backbone structure being composed of a repetitive structure of a disaccharide unit composed of a uronic acid (iduronic acid (IdoA) or glucuronic acid (GlcA)) residue and a glucosamine (GlcN) residue. Heparin is one of glycosaminoglycans in which the hydroxyl group at the 2-position of the uronic acid residue and the hydroxyl group at the 6-position and the amino group at the 2position of the glucosamine residue each undergo a certain degree of sulfation. Because heparin has an antithorombin III (hereinafter also referred to as "ATIII") binding site (FEBS Lett. (1980) 117, 203-206), and binds with ATIII to inhibit the action of the thorombin, thereby giving rise to anticoagulative action, heparin has long been extensively used as a pharmaceutical agent such as anticoagulants for improving the results of dialysis treatment and the like. More recently, it has been found that heparin interacts with various physiological active factors. For example, heparin interacts with lipoprotein lipase (J. Biol. Chem. (1981) 256, 12893-12898) and has an affinity for basic fibroblast growth factor (J. Cell Biol. (1990) 111, 1651-1659). Under such a situation, attention has been focusing on the domain structures within heparin that take part in the binding between heparin and specific cell growth factors or cytokines. Moreover, considerable research is being conducted relating to chemical modifications represented by desulfation of heparin aiming at reducing the anticoagulative action due to the presence of the ATIII binding site to thereby increase the interaction with physiological active factors (J. Carbohydr. Chem. (1993) 12, 507-521; Carbohydr. Res. (1989) 193, 165172; Carbohydr. Res. (1976) 46, 87-95; WO 95/30424, etc.). Web site: http://www.delphion.com/details?pn=US06492503__
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Herbal composition and method for combating inflammation Inventor(s): Blackner; Lori (Chattanooga, TN), Charters; Alec (Salt Lake City, UT), Morris; Shayne (Ogden, UT), Selander; James (Park City, UT), Thompson; Robert Charles (Peterson, UT) Assignee(s): Nutraceutical Corporation (Park City, UT) Patent Number: 6,541,045 Date filed: January 4, 2002 Abstract: An herbal composition for combating inflammation, comprising therapeutically effective amounts of Japanese knotweed, Devil's claw, grapeskin, and syzygium is provided. Also provided is an herbal composition for treating a cough and/or common cold, comprising therapeutically effective amounts of Japanese knotweed, lobelia, echinacea, slippery elm, Devil's claw, adhatoda, vitamin C, grapeskin, and syzygium. An herbal composition for alleviating menstrual discomfort, comprising therapeutically effective amounts of Japanese knotweed, chaste tree berry, Mexican wild yam, dandelion, Devil's claw, grapeskin, and syzygium is provided. Also provided is an herbal composition for soothing muscles and joints, comprising therapeutically effective amounts of Japanese knotweed, N-acetyl D-glucosamine, chondroitin sulfate, D-glucosamine hydrochloride, methylsulfonylmethane, grapeskin, syzygium, and Devil's claw. Methods of using the herbal compositions are also provided. Excerpt(s): The present invention relates generally to herbal compositions and methods for combating inflammation. Arthritic disorders, including rheumatism, osteoarthritis, dysplasia, lupus, bursitis, and gout, are all characterized by inflammation and pain in bones, joints, muscles, and related connective tissues. Most of the forms are progressive. Those who suffer from inflammation experience pain and discomfort and may, in advanced cases, lose the effective use of inflamed joints. Thus, the goal of therapeutic methods for treating bone or joint inflammation is the relief of pain and discomfort and the restoration of use of inflamed joints. Certain enzymes play a role in causing inflammation. One of the features of inflammation is increased oxygenation of arachidonic acid, which is metabolized by two enzymic pathways--the cyclooxygenase (CO) and the 5-lipoxygenase (5-LO) pathways--leading to the production of prostaglandins and leukotrienes, respectively. Prostaglandins and leukotrienes are mediators of inflammation. Therapies designed to inhibit cyclooxygenase and/or lipoxygenase activity are therefore of great interest. Web site: http://www.delphion.com/details?pn=US06541045__
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LPS with reduced toxicity from genetically modified gram negative bacteria Inventor(s): Hamstra; Hendrik Jan (Wijk Bij Duurstede, NL), Steeghs; Liana Juliana Josephine Margriet (Utrecht, NL), Van Der Ley; Peter Andre (Utrecht, NL) Assignee(s): De Staat Der Nederlanden, vertegenwoordigd door de minister van welzijn, (Rijswijk, NL) Patent Number: 6,482,807 Date filed: July 2, 2001 Abstract: The subject invention lies in the field of vaccines. Specifically new compounds that can be used as adjuvants are provided. Recombinant LPS having a reduced number
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of secondary acyl chains per molecule of LPS vis a vis the corresponding non modified LPS molecule, said secondary acyl chains being bound to primary acyl chains, said primary acyl chains being bound to the glucosamine of said recombinant LPS molecule, said recombinant LPS being homogenous in acylation pattern is an example of such a compound. Also recombinant LPS having a phosphate group attached to the glucosamine at the non reducing end of the LPS molecule and a phosphate group attached to the glucosamine at the reducing end of the molecule per recombinant LPS molecule provides a further example. Excerpt(s): This application is a 371 of PCT/NL98/00633 Nov. 3, 1998. The subject invention lies in the field of vaccines and more specifically provides novel compounds that can be used as adjuvants in vaccines. Many adjuvants have been described e.g. Freund type mineral oil emulsions, aluminium salts, saponins, muramyl dipeptide and derivatives MPL, MF59 etc. However only a few have actually been licensed for use in humans. This is generally due to an unfavorable ratio between immunostimmulatory action versus toxicity. A general reference concerning adjuvants can be found in The Theory and Practical Application of Adjuvants (D.E.S. Stewart-Tull ed. John Wiley & Sons 1995) and the information therein is incorporated by reference. The prior art also teaches for a number of organisms that enzymatic treatment of LPS can lead to reduced toxicity. The LPS illustrated as having undergone such treatment are: Salmonella typhimurium and Salmonella minnesota. The following are also suggested to exhibit such: all Gram negative bacteria and specifically Salmonella, Escherichia, Haemophilus, Moraxella, Campylobacter and Neisseria. Nowhere however are details provided concerning proof of adjuvant activity. Looking at this prior art in detail shows that Munford et al (in U.S. Pat. No. 4,929,604 issued in 1990) show S typhimurium LPS in which 95% of secondary acyl groups have been removed through enzymatic treatment. The Munford treatment cannot specifically remove secondary acyl chains ensuring only partial deacylation. The Munford method cannot provide uniform product at best nearly all secondary acyl groups will be removed. Web site: http://www.delphion.com/details?pn=US06482807__ •
Method for producing low acid beverage Inventor(s): Hino; Yoshiko (Osaka, JP), Matsumoto; Nobuya (Osaka, JP), Matsumoto; Shigemi (Osaka, JP), Yokoo; Yoshiaki (Osaka, JP) Assignee(s): Suntory Limited (Osaka, JP) Patent Number: 6,482,456 Date filed: June 16, 2000 Abstract: A method for producing a low acid beverage in which a deterioration in quality associated with a pH decrease during heat sterilization or long-term storage in a heated condition is eliminated or minimized, and which is characterized by adding at least one of chitosan, chitosan oligosaccharide and glucosamine. Excerpt(s): This invention relates to a method for producing a low acid beverage in which deterioration in quality associated with a pH decrease during heat sterilization or during long-term storage in a heated condition is minimized or eliminated. Noncarbonated canned beverages can be generally classified into two types depending on the hydrogen ion concentration exponent (hereinafter referred to as "pH") of the contents: acid beverages having a pH of less than 4.6, which include fruit drinks, sport drinks, tomato juice, and so on; and low acid beverages having a pH of 4.6 or above,
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which include black coffee, white coffee, milk tea, milk, green tea, soup, and so on (Beverage Japan No. 80, August 1988, "Production of Canned Beverages"). Under the Japanese Food Sanitation Law (Standards for the Foods and Additives, D, each Article), beverages that have a pH of 4.6 or above, and water activity in excess of 0.94 are required to be sterilized by a method such as is effective in destroying microorganisms introduced into beverages from raw material sources, etc. and which have the ability to survive and proliferate in such beverages. Low acid beverages generally require heat sterilization at 100.degree. C. or above. However, heat sterilization causes a decrease in the pH of low acid beverages. Furthermore, long-term storage in a heated condition (55 to 60.degree. C.) such as is employed in vending machines also causes a decrease in pH. In addition, environmental factors may cause a rise in temperature of beverages during storage or distribution, thus similarly affecting the pH thereof. Web site: http://www.delphion.com/details?pn=US06482456__ •
Method for supplementing the diet Inventor(s): Deffner; Kathleen (Taylorsville, UT), Rosenberg; Thomas D. (Salt Lake City, UT) Assignee(s): Nutriex, L.L.C. (Salt Lake City, UT) Patent Number: 6,579,544 Date filed: May 31, 2000 Abstract: A dietary supplement blend composition is disclosed, the basic formulation of the composition containing vitamins, minerals, and carotenoids. The composition can also contain bioflavonoids, cartilage protectors such as glucosamine or chondroitin,.alpha.-lipoic acid, coenzyme Q10, and a source of omega-3 fatty acids such as flax seed oil. The composition is beneficial for improving health and preventing disease, particularly for degenerative conditions. A method for supplementing the diet is also disclosed, wherein the quantity of daily rations of the dietary supplement blend composition is determined based on the person's age, body weight, and quality of diet. Excerpt(s): Not Applicable. This invention relates to dietary supplements. More particularly, the invention relates to compositions and methods for supplementing the diet for improving health and preventing disease. Web site: http://www.delphion.com/details?pn=US06579544__
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Method of plant selection using glucosamine-6-phosphate deaminase Inventor(s): Bojsen; Kirsten (Allerod, DK), Donaldson; Iain A. (Tinglev, DK), Jorgensen; Kirsten (Guldborg, DK), Jorsboe; Morten (Nykobing Falster, DK) Assignee(s): Danisco A/S (Copenhagen, DK) Patent Number: 6,444,878 Date filed: December 23, 1999 Abstract: A selection method for selecting from a population of plant cells one or more genetically transformed plant cells is described. In the method, the population of plant cells includes selectable genetically transformed plant cells and possible nontransformed plant cells. Each of the selectable genetically transformed plant cells comprises a first expressible nucleotide sequence and optionally a second expressible
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nucleotide sequence. In the method, a component or a metabolic derivative thereof when present in a low concentration in a medium is a nutrient for both the selectable genetically transformed plant cells and the non-transformed plant cells. In the method, the component or the metabolic derivative thereof when present in a high concentration in a medium is toxic to the non-transformed plant cells. The first nucleotide sequence codes for a gene product having glucosamine-6-phosphate deaminase activity which is capable of converting the component or the metabolic derivative thereof when present in a high concentration in a medium to a nutrient for the selectable genetically transformed plant cells. The method includes the step of introducing the population of plant cells to a medium, wherein the medium includes a high concentration of the component or the metabolic derivative thereof. In the method, the component or the metabolic derivative thereof is a source of both carbohydrate and nitrogen for the selectable genetically transformed plant cells. Excerpt(s): The present invention relates to a selection method. The present invention also relates to an enzyme and a nucleotide sequence coding for same that are useful in a selection method. In particular, the present invention relates to a method for the selection (e.g. identification and/or separation) of genetically transformed cells and compounds and genetic material for use in the method. Web site: http://www.delphion.com/details?pn=US06444878__ •
Method of producing derivatives of lactosamine Inventor(s): Nilsson; Kurt (Lund, SE) Assignee(s): Procur AB (Lund, SE) Patent Number: 6,653,109 Date filed: June 28, 1996 Abstract: Disclosed is a method of producing a compound with.beta.1-4 linkage which contains the lactosamine structure involving reacting at least one donor substance Gal.beta.OR where R is an organic group, and at least one acceptor substance which is a glucopyranosamino derivative having the formula GlcNR"--R'", wherein NR" is an azido, 2-N-acetyl-, 2-N-phtalimido, or an organic group bound to the 2-N-group of glucosamine, wherein R'" is a glycosidically bound fluoro or is an O-, C-, N- or Sglycosidically bound aliphatic or aromatic compound, with the proviso that if NR" is NHAc then R'" is not OH and if NR" is not NHAc then R'" may be OH, in the presence of Bullera singularis or an E.C. group 3.2 glycosidase of essentially the same structure as an E.C. Group 3.2 glycosidase obtained from Bullera singularis to form the lactosamine derivative; and optionally isolating the compound with.beta.1-4 linkage which contains the lactosamine structure. Excerpt(s): The present invention describes a new method for the production of certain carbohydrate containing compounds related to glycoconjugates; namely, lactosamine derivatives and substances derived therefrom. In a further aspect the present invention relates to products produced by the above method as well as uses of the resulting products. Glycoconjugates contain saccharide chains with from one up to twenty monosaccharide units and in which certain sequences have been shown to have biological activity, for example in the binding of different cells, pathogens, toxins, as well as antibodies or other proteins to cell surfaces, in cancer metastasis, in inflammatory processes, for instance selectin-carbohydrate interactions in the binding of white blood cells to the blood vessel wall, as a modifier of the biological activity and
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stability of glycoproteins, as immunogenic substances, which have potential in the vaccination against different diseases (See for instance Annual Review of Biochemistry, vol. 58 (1989), pages 309-350, and Current Opinion in Structural Biology, for example review articles in vol. 3 (1993) and references therein). Structures containing the sequence Gal.beta.1-4GlcNAc, called N-acetyl-lactosamine below, are especially of importance and are found for instance in glycoconjugate oligosaccharides of the lactosamine type. The structure is found in blood group structures, for instance Lewis-x (e.g. Gal.beta.1-4(Fuc.alpha.1-3)GlcNAc), sialylated Lewis-x and 3'-sulfated Lewis-x, and is of importance in e.g. selectin-carbohydrate interactions (as reviewed by J. B. Lowe, in Molecular Glycobiology, pages 163-205, Fukuda and Hindsgaul, Eds., IRL Press at Oxford University Press, Oxford, 1994; see also Curr. Opin. Struct. Biol. vol. 3 (1993)). Web site: http://www.delphion.com/details?pn=US06653109__ •
Oral and injectable nutritional composition Inventor(s): Petito; Anita M. (1890 Bucknell Dr., Bethlehem, PA 18015), Petito; George D. (1890 Bucknell Dr., Bethlehem, PA 18015) Assignee(s): none reported Patent Number: 6,476,005 Date filed: July 26, 1999 Abstract: An oral and injectable composition for mammals comprising a salt of glucosamine, such as glucosamine hydrochloride, sulfate, nitrate, or iodide, a chondroitin sulfate, hydrolyzed or native collagen, a sodium hyaluronate, chelated manganese ascorbate, and L-malic acid in powder form for oral ingestion or in a solution of sterilized water for injection. The composition acts as a chondroprotective agent which provides foundational support for the creation of new body tissue and cartilage growth in humans and animals. Other beneficial physiological properties include the enhancement of chondrocyte synthesis, the healing of chronic or acute wounds, the maintenance of healthy muscle and tissue, increasing the desirable concentration of hyaluronic acid, and anti-inflammatory activity. Excerpt(s): The present invention relates to an oral and injectable nutritional composition in powder or aqueous form for mammalian use comprising glucosamine or a glucosamine salt, chondroitin sulfate, hydrolyzed collagen, sodium hyaluronate, a manganese salt, and, optionally, L-malic acid. Phosphate salts are excluded from this nutritional composition. The related art of interest describes various oral and topical products for improving various physiological functions of the human body. The related art will be discussed in the order of perceived relevance to the present invention. U.S. Pat. No. 5,141,928 issued on Aug. 25, 1992, to Lawrence Goldman describes ophthalmic medications containing glycosaminoglycan polysulfates (GAGPS) or mucopolysaccharides having a molecular weight in the range of 5,000 to 20,000 Daltons combined with antibiotics for treating eye infections and antimicrobial agents such as pilocarpine or epinephrine for glaucoma. GAGPS include chondroitin sulfate and hyaluronic acid that contain hexosamines. The medicament composition is thus distinguishable from the present invention prohibiting sulfates for its reliance on glycosaminoglycan polysulfates, antibiotics, and antimicrobial agents, which composition is limited to human use. Web site: http://www.delphion.com/details?pn=US06476005__
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Preparation of fiber, L-glutamine and a soy derivative for the purpose of enhancement of isoflavone bioavailability Inventor(s): Hsu; Charles C. (Long Beach, CA), Hu; Qing-Fu (Laguna Niguel, CA), Paul; Stephen M. (Rancho Santa Margarita, CA), See; Melissa (Long Beach, CA), Shu; Daniel (Laguna Niguel, CA) Assignee(s): Sun Ten Laboratories, Inc. (Irvine, CA) Patent Number: 6,488,968 Date filed: February 22, 2002 Abstract: A method of enhancing phytoestrogen bioavailability and a method for supplementing the dietary needs of warm blooded animals comprising orally administering an effective amount of a dietary supplement composition comprising a phytoestrogen, a fiber and L-glutamine, and optionally N-acetyl-D-glucosamine, in admixture with a biologically acceptable inert carrier. Excerpt(s): This invention relates to nutritional supplements. More particularly, the invention relates to a nutritional supplement composition, and methods of use thereof, to enhance the bioavailability of isoflavone. Nearly 70 years ago, it was reported that certain plants could induce estrus in animals. Subsequently, over 300 plants have been found to possess estrogenic activity (see e.g., Bradbury and White, Vitamin Horm. 12:207 (1954), and Farnsworth et al., J. Pharm. Sci. 64:717(1954)). These compounds have been given the general name of "phytoestrogens" and represent several chemical classes of diphenolic plant compounds that are somewhat related structurally to the mammalian sex hormone 17-beta-estradiol. See Setchell, K. D. R., et al Am. J. Clin. Nutr., 40:569 to 578 (1984). Similarities in the molecular structure of phytoestrogens facilitate binding to the estrogen receptor. An important class of the phytoestrogens is the isoflavone class. Two chemical classes of phytoestrogens are abundant in soybeans, total soy products, and soy protein isolates. Those two classes are coumestrol and isoflavones. The latter class includes daidzein, genistein, glycitein, as well as their glycoside and acetylated forms. Phytoestrogens and their metabolites interact with specific cell receptors and compete with endogenous hormone molecules [see Folman, Y. et al, J. Endocr., 44:213 to 218 (1969)], but the biological estrogen-like effect of these compounds is relatively weak. See Kaziro, R. et al, J. Endocr., 103:395 to 399 (1984) and Tang, B. Y. et al, J. Endocr. 85:291 to 297 (1980). Phytoestrogens can induce two different effects in an organism. When the level of endogenous sex hormones is relatively high, the antiestrogenic effect prevails. There are several mechanisms of antiestrogenic activity of the phytoestrogens, including feedback inhibition at the hypothalamus and pituitary gland, and competition and blockade of cell receptors. It has been observed that a phytoestrogen and lignan-rich diet is associated with a reduction in free plasma estradiol, and in reduction of the risk of breast cancer. See Adlercreutz, H. et al, J. Steroid. Biochem., 27:1135 to 1144 (1987) and Mousavi, Y. et al, Steroids, 58:301 to 304 (1993). On the other hand, in postmenopausal women, phytoestrogens can provoke an estrogenic response. See Adlercruetz, H. et al, Lancet, 339:1233 (1992). This dual effect of weak estrogens is demonstrated, and well known "partial" antigens such as Tamoxifen have these properties. Web site: http://www.delphion.com/details?pn=US06488968__
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Probiotic formulation Inventor(s): Watson; Brenda F. (Tarpon Springs, FL), Watson; Tommy Stanley (Tarpon Springs, FL) Assignee(s): Renew Life, Inc. (Clearwater, FL) Patent Number: 6,468,525 Date filed: August 10, 1999 Abstract: A probiotic formulation, useful as a food supplement and a material for reestablishing beneficial bacteria to the body's intestinal tract, comprises a mixture of beneficial probiotic microflora comprising lactobacillus acidophilus, bifidobacterium bifidum, lactobacillus salivarius, bifidobacterium infantis, and bifidobacterium longum, fructooligosaccharides, L-glutamine, and N-acetyl glucosamine. Excerpt(s): The present invention relates generally to a probiotic formulation. More particularly, the invention is directed to a food supplement formulation comprising five specific microflora and additional ingredients which work together to support the body's ability to replace mucosal linings such as those found in the digestive tract. Probiotic formulations have been used as dietary supplements for many years. Hundreds of different strains of probiotics exist, but only a select few (about 50) of these strains have been tested for efficacy. Beneficial probiotics are categorized as either resident or transient. Resident probiotic bacterial strains live and reproduce in each person's digestive tract. Transient probiotic bacterial strains typically are introduced into the body through ingested food or by means of dietary supplements; however, they do not reproduce nor stay within the digestive system. Probiotic bacteria which normally inhabit the digestive tract reduce the levels of harmful bacteria which may be introduced to the body. For example, naturally occurring probiotic bacteria reduce levels of E. Coli and Salmonella by producing metabolic acid products, e.g., hydrogen peroxide, lactic acid, and acetic acid, that inhibit or antagonize these harmful bacteria. Probiotics also inhibit the levels of harmful microbial pathogens, by lowering the pH in the intestines. This production of organic acids effectively lowers intestinal pH to a level that is favorable for beneficial bacteria and destructive to pathogens. Probiotic bacteria also prevent the establishment of harmful fungus and parasites, such as Candida albicans and Giardia lamblia, which became attached to the walls of the colon. Probiotic bacteria can reduce the levels of toxic byproducts such as indole, skatole, and methane produced by the metabolic reaction of harmful bacteria to certain foods. Probiotics also assist the body's digestion of lactose and dietary carbohydrates. Finally, probiotic bacteria can aid the synthesis of B vitamins such as folic acid, niacin, pantothenic acid, and biotin. Web site: http://www.delphion.com/details?pn=US06468525__
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Process and materials for production of glucosamine Inventor(s): Berry; Alan (Manitowoc, WI), Burlingame; Richard P. (Manitowoc, WI), Millis; James R. (Kohler, WI) Assignee(s): Arkion Life Sciences LLC (Wilmington, DE) Patent Number: 6,372,457 Date filed: July 15, 1998
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Abstract: The present invention relates to a method and materials for producing glucosamine by fermentation of a genetically modified microorganism. Included in the present invention are genetically modified microorganisms useful in the present method for producing glucsamine, as well as recombinant nucleic acid molecules and the proteins produces by such recombinant nucleic acid molecules. Excerpt(s): The present invention relates to a method for producing glucosamine by fermentation. The present invention also relates to genetically modified strains of microorganisms useful for producing glucosamine. Amino sugars are usually found as monomer residues in complex oligosaccharides and polysaccharides. Glucosamine is an amino derivative of the simple sugar, glucose. Glucosamine and other amino sugars are important constituents of many natural polysaccharides. For example, polysaccharides containing amino sugars can form structural materials for cells, analogous to structural proteins. Glucosamine is manufactured as a nutraceutical product with applications in the treatment of osteoarthritic conditions in animals and humans. The market for glucosamine is experiencing tremendous growth. Furthermore, significant erosion of the world market price for glucosamine is not expected. Web site: http://www.delphion.com/details?pn=US06372457__ •
Product and method for treating joint disorders in vertebrates Inventor(s): Chrisope; Gerald L. (Boulder, CO), Rose; Rebecca (Longmont, CO) Assignee(s): In Clover, Inc. (Boulder, CO) Patent Number: 6,344,220 Date filed: June 28, 1999 Abstract: A compound and method of using such compound is disclosed that, when administered to an animal, is capable of arresting the inflammatory response in affected tissues and facilitates the repair and maintenance of damaged tissues in the joints of vertebrates. The combination of natural physiological metabolites and herbal phytochemicals is used to treat connective tissue diseases, the composition preferably orally administered. One embodiment of the composition includes chondroitin sulfate and glucosamine that, when ingested by a vertebrate, suppresses the degradation of connective tissue by an autoimmune response. A preferred composition of the present invention includes a palatability agent, an herbal phytochemical, and a metabolic precursor that synergistically acts to increase blood circulation, thereby enhancing transport of the phytochemical and metabolic precursors to an affected site whereby deleterious inflammatory byproducts are removed. Excerpt(s): The present invention is directed to compounds, and methods using such compounds, that when administered to an animal, arrest the inflammatory response in affected tissues and facilitate repair and maintenance of damaged tissues in the joints of vertebrates. In healthy conditions, articular cartilage forms a smooth surface between articulating bone ends to reduce the friction caused by movement. This friction is further reduced by the synovial fluid. Articular cartilage consists of chondrocytes and two major macro-molecules; i.e., collagen and proteoglycans, which are synthesized by and deposited around the chondrocytes. The chondrocytes also synthesize the synovial fluid which bathes the articular cartilage. Web site: http://www.delphion.com/details?pn=US06344220__
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Protection of pancreatic.beta.-cells during islet isolation and assessment of islet viability and candidate diabetes drugs after islet isolation Inventor(s): Konrad; Robert (Hoover, AL), Kudlow; Jeffrey (Birmingham, AL) Assignee(s): NAB Research Foundation (Birmingham, AL) Patent Number: 6,361,995 Date filed: July 26, 2000 Abstract: Standard pancreatic islet isolation results in.beta.-cell toxicity due to nitric oxide and/or streptozotocin-like molecules that are generated during the isolation process. This toxicity can be limited by the addition of compounds that work through the glucosamine pathway in islets and/or by the addition of nitric oxide inhibitors. Unless prevented, this toxicity results in.beta.-cells being unable to properly respond to high glucose, glucosamine, N-acetylglucosamine, or streptozotocin by increasing their relative amount of O-glycosylated protein. Likewise, in order to assess islet viability or the effect of diabetes drugs on.beta.-cell function, islets that have been adequately protected during their isolation can be stimulated with low glucose, high glucose, glucosamine, N-acetylglucosamine, or streptozotocin with or without the drug(s) of interest present. By analyzing the pattern of islet protein O-glycosylation that occurs, one can determine whether the islets are viable and whether or not the candidate drug(s) might be useful in the treatment of diabetes. Excerpt(s): The present invention relates generally to the fields of pancreatic islet isolation and medical therapy for diabetes. More specifically, the present invention relates to improved procedures for isolating pancreatic islets that better protect the islets during the isolation process. In order to screen for new drugs to treat type 2 diabetes, or to prepare islets for transplantation for type 1 diabetes, isolated islets must be protected from toxic molecules that form during the isolation process. Early in the course of type 2 diabetes, pancreatic.beta.-cell function is sufficient such that in many patients, oral hypoglycemic agents are adequate to compensate for increased insulin resistance (1). As type 2 diabetes progresses, however,.beta.-cells lose their capacity to produce sufficient amounts of insulin to control the blood glucose level and patients become increasingly hyperglycemic (2). It has been suggested that the hyperglycemia itself may cause damage to.beta.-cells (3-5). The exact mechanism by which a n increased concentration of glucose may affect.beta.-cells, however, is not completely elucidated. One metabolite of glucose that has been proposed to mediate adverse effects of hyperglycemia is glucosamine (2-amino-2-deoxyglucose) (6,7). Glucosamine is a product of glucose metabolism and is synthesized from fructose-6-phosphate by the apparently unique and rate limiting enzyme, glutamine:fructose-6-phosphate amidotransferase (GFAT) (8-10). This metabolic step provides the substrate UDP-N-acetylglucosamine (UDP-GlcNAc) for glycoprotein synthesis. Quantitatively, most glycosylation occurs on proteins destined for export from the cell or for the plasma membrane of the cell. In eukaryotic cells, however, there is a cytoplasmic form of glycosylation that involves O-linkage of the monosaccharide, N-acetylglucosamine (GlcNAc), to proteins at serine or threonine residues (11-19). An enzyme responsible for this form of protein modification, O-linked N-acetylglucosamine transferase (OGT), has recently been characterized, and its cDNA has been cloned (20). Studies on the tissue distribution of O-GlcNAc transferase have indicated that O-linked N-acetylglucosamine transferase mRNA, although ubiquitous, is particularly abundant in the pancreatic.beta.-cell (21, 22). Web site: http://www.delphion.com/details?pn=US06361995__
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Proteoglycan compositions for treatment of cardiovascular inflammatory diseases Inventor(s): Theoharides; Theoharis C. (14 Parkman St., Brookline, MA 02446) Assignee(s): none reported Patent Number: 6,624,148 Date filed: December 27, 2002 Abstract: Compositions with synergistic anti-inflammatory effects in inflammatory diseases resulting from activation and consequent degranulation of mast cells and followed by secretion of inflammatory biomolecules from the activated mast cells, composed of a heavily sulfated, non-bovine proteoglycan such as shark cartilage chondroitin sulfate C, and one or more of a hexosamine sulfate such as D-glucosamine sulfate, a flavone such as quercetin, an unrefined olive kernel extract that increases absorption of these compositions in various routes of administration, Sadenosylmethionine, a histamine-1 receptor antagonist, a histamine-3 receptor agonist, an antagonist of the actions of CRH, caffeine, and a polyamine. Excerpt(s): The invention is generally related to the treatment of inflammatory conditions. More specifically, the invention is related to compositions containing inhibitors of mast cell activation and secretion such as a proteoglycan that are designed to be used as dietary supplements or adjuvants to conventional approved medications for the relief of inflammatory conditions. There have been a number of mostly anecdotal reports that the proteoglycan chondroitin sulfate, as well as glucosamine sulfate, a product of the intestinal breakdown of proteoglycans, may be helpful in relieving the pain of osteoarthritis:--Shute N. Aching for an arthritis cure. US News and World Report, Feb. 10, 1997.--Cowley G. The arthritis cure? Newsweek, Feb. 17, 1997; Foreman J., People, and their pets, tout arthritis remedy. The Boston Globe, Apr. 7, 1997; Tye L. Treatment gains scientific attention. The Boston Globe, Sep. 25, 2000. A recent metaanalysis showed potential therapeutic benefit of chondroitin sulfate and/or glucosamine in osteoarthritis [McAlindon et al. J Am Med Assn. 283:1469 (2000)], while a double-blind clinical trial with glucosamine showed definite benefits in osteoarthritis with respect to both pain and radiographic joint appearance [Reginster et al., Lancet 337:252 (2001)]. However, less than 5% of the chondroitin sulfate in commercially available preparations is absorbed orally, because the size of the molecule and the degree of sulfation impede its absorption from the gastrointestinal tract. Furthermore, such commercial preparations use chondroitin sulfate obtained from cow trachea, with the possible danger of contracting spongiform encephalopathy or "mad cow disease". In fact, the European Union has banned even cosmetics that contain bovine-derived products. Web site: http://www.delphion.com/details?pn=US06624148__
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Sterilization-protecting agent and sterilization method Inventor(s): Onodera; Hirokazu (Oita, JP), Suemitsu; Junsuke (Oita, JP) Assignee(s): Asahi Medical Co., Ltd. (Tokyo, JP) Patent Number: 6,572,820 Date filed: August 4, 1998 Abstract: A material comprising a biologically active substance (or ligand) to be sterilized, including proteins (e.g., antibodies and enzymes), peptides, DNA, RNA, and
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glycoproteins, with or without a carrier, and sterilization-protecting agent comprising a trisaccharide or higher saccharide ("polysaccharide") having a positive charge, is provided. The skeletal background of the polysaccharide confers stability to the ligand and its positive charge traps destructive radicals produced during the sterilization process. The molecular weight ratio of sterilization-protecting agent to the ligand should be at least 1/500 but less than 1/2 to protect the ligand effectively without obstructing the ligand's activity. In particular, polysaccharides, such as chitosan (a polymer of Dglucosamine) and chitin which is partially converted into chitosan, are preferable as a sterilization-protecting agent. The biologically active substance in such a material is stabilized against various sterilization methods, including irradiation, wet heat, and chemical sterilization, either in a wet state or a dry state. Further, a method for sterilizing a biologically active substance in the presence of the above-described sterilization-protecting agent is provided. Excerpt(s): The present invention relates to a material comprising a material to be sterilized and a sterilization-protecting agent comprising a trisaccharide or higher saccharide having a positive charge(s); a sterilization method using said sterilizationprotecting agent; and said sterilization-protecting agent. In recent years, attempts have been made on selective separation, division, removal, etc. of a substance interacting with a biologically active substance (hereinafter referred to simply as an active substance or a ligand), using said active substance; and research has been done on active materials obtained by immobilizing, as a biologically active substance, a ligand such as a peptide, protein, synthetic substance or the like onto a carrier. Investigations have been made particularly on techniques for specifically removing blood cells using an active material obtained by immobilizing a protein such as an enzyme, antibody or the like onto a carrier, or for using said active material as a bioreactor. These active materials, however, are very unstable to sterilization; particularly in the case of an active material having a ligand immobilized thereon, the interactivity of the ligand with a substance to be affected is reduced by sterilization in many cases and it has been difficult to conduct sufficient sterilization of the active material without impairing the activity of the ligand. In U.S. Pat. No. 5,283,034, a sterilization method is disclosed which comprises conducting sterilization in the presence of a substance (e.g. human serum albumin) used as a surface stabilizer, and a mono- or di-saccharide (e.g. glucose, sucrose, lactose, trehalose or amylose) or a glycoprotein (e.g. immunoglobulin) used as an oxygen radical-capturing agent. In this sterilization method, however, sterilization is possible only in a dry state of less than 1% of water content; consequently, the sterilized material has an inferior priming property and has been difficult to handle. Web site: http://www.delphion.com/details?pn=US06572820__ •
Synergistic agents for enhancing tissue repair Inventor(s): Jaffe; Russell (10430 Hunter View, Vienna, VA 22181) Assignee(s): none reported Patent Number: 6,620,798 Date filed: June 6, 2000 Abstract: Methods for the repair, reconstruction and protection of tissue using compositions containing flavonoids and/or flavonols, including simultaneous administration of agents in order to obtain synergistic effects from the combinations taught and claimed herein. The administration of the flavonols and /or flavonoids in conjuction with compositions containing vitamin C and/or salts and esters of vitamin C
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provides advantageous sparing of autocoids (internal steroids). The simultaneous administration of flavonols and /or flavonoids to compositions containing glucosamine and or glucosamine sulfate and chondroitin stimulates rapid improvement in joint function. The addition to the flavonoids and/or flavonols to previously administered compositions is a most convenient method of achieving enhanced benefits. The use of combinations of flavonoids and flavonols for use in relieving pain is also a part of the invention. Excerpt(s): This invention is related to the repair, reconstruction and protection of tissue using compositions containing flavonoids and/or flavonols. It has been known that phenolic compounds, including flavonoids and flavonols, have anti-inflammatory properties. It has been known that several flavonones, flavonols, isoflavonones and catechins, can inhibit the proliferation of inflammatory (granulation) tissue. These agents can decrease capillary permeability and strengthen the blood vessel wall, thus preventing vascular fragility. The agents have been shown to have affinity for and enhance synthesis of connective tissue. Some flavonoids have been found to stimulate collagen and elastin cross-linking. It is believed that proline hydroxylation and modulation of polysaccharide production and function may be among the mechanisms by which benefit occurs. However, bioaction of these compounds, when given alone, is inadequate to provide desired clinical results. It is necessary to find more effective means of delivering clinical benefits that can arise from exposure to flavonoids. Web site: http://www.delphion.com/details?pn=US06620798__ •
Therapeutic compositions containing glucosamine, collagen and a bioflavanol for repair and maintenance of connective tissue Inventor(s): Bath; Teresa K. (6325 Newland St., Arvada, CO 80003), Lynch; Neal (6325 Newland St., Arvada, CO 80003) Assignee(s): none reported Patent Number: 6,333,304 Date filed: April 20, 1999 Abstract: A composition for treating arthroses in animals includes exogenous glucosamine, hydrolyzed collagen and a bioflavanol. Preferred glucosamines are glucosamine hydrochloride (HCI) and glucosamine sulfate. Preferred bioflavanols are those extracted from grape seeds, pine bark or turmeric root. Proanthocyanidin (also referred to as leucocyanidin or pcynogenol) is the most preferred bioflavanol. With horses and larger animals, a preferred treated method involves application of the composition of the present invention as a top dressing twice a day to the animal's feed. A preferred treatment for humans, dogs and cats involves the ingestion of 1 to 4 tablets or capsules per day of the composition of the present invention. Excerpt(s): The present invention relates to the use of exogenous therapeutic compositions containing glucosamine, hydrolyzed collagen and a bioflavanol for the repair of animal connective tissue, and to therapeutic techniques employing exogenous glucosamine, hydrolyzed collagen and a bioflavanol. Cartilage is the connective tissue which cushions moveable joints. Joint cartilage damage is commonly referred to by a number of terms which are used interchangeably here, including arthritis, arthroses and osteoarthritis. Osteoarthritis is a syndrome characterized by pathologic change of synovial joints accompanied by clinical signs of pain and disability. Unfortunately, most animals have sustained damage to joint cartilage by middle age. Although the causes of
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degenerative processes are generally unknown, as a general matter, cartilage damage can be classified as one of two forms of osteoarthritis. Primary osteoarthritis occurs when normal forces act on abnormal cartilage causing degeneration. An example is the aging process, where daily physical activity and cellular metabolism create wear and tear on the articular cartilage leading to an arthritic condition. Secondary osteoarthritis occurs when abnormal forces act on normal cartilage causing degeneration. An example is traumatic injury such as tearing the anterior cruciate ligament which may cause enough damage to the joint capsule to lead to arthritis. The result of primary and secondary osteoarthritis is the same--a painful condition in which the animal typically is caught up in a cycle in which the body cannot efficiently repair itself at a rate faster than the rate of degeneration. Many factors affect or exacerbate the extent of cartilage deterioration. For example, some animals are predisposed genetically to joint disease and degeneration of joint tissue at an early age. In addition, an animal's genetic makeup can influence the thickness and durability of cartilage which will affect an animal's predisposition to arthritis. Other animals experience abnormal wear and tear on joints as a result of poor conformation and/or excess mechanical stress on musculoskeletal systems. Also, aggressive exercise schedules during youth (as may occur with race horses or athletes) may accelerate the manifestation of joint deterioration problems in later years. Web site: http://www.delphion.com/details?pn=US06333304__ •
Topically applied creatine containing composition Inventor(s): Stoll; David M. (9735 Wilshire Blvd. Suite 418, Beverly Hills, CA 90212) Assignee(s): none reported Patent Number: 6,413,552 Date filed: August 28, 2001 Abstract: The present invention is a stable topical creatine application suitable for absorption directly through the skin into the underlying muscle without traveling through the blood system for the purpose of increasing muscle energy. It is created by combining creatine with phosphoric acid in a cosmetically elegant vehicle suitable for topical use. Chondroitin sulfate and glucosamine can also be added. Topical creatine avoids the side effects of oral creatine supplements. Excerpt(s): The present invention relates to the field of muscle stimulation and more particularly to enhancing the production of the energy used to cause contractions and expansions in the muscles of mammals. Creatine is an important source of providing energy to muscles through its role in adenosine triphosphate (ATP) formation. ATP is the fuel source for muscle contraction. It is formed when adenosine diphosphate (ADP), adds another phosphate group to form ATP. Creatine provides the source for replacing the phosphate group to convert ADP to ATP. As such, it is an integral part of the muscle contraction and expansion process. The more creatine available to muscles, the more ADP can be converted to ATP for use by those muscles. Therefore, for persons involved in strenuous physical activities, such as athletes, a constant source of creatine is vital in order to maintain muscle energy levels. Creatine is a popular nutritional supplement useful as an energy source for muscles. Chemically, creatine is N-methyl-Nguanylglycine. Creatine is biosynthesized through the transamidination and transmethylation of the amino acids glycine, arginine and methionine. Web site: http://www.delphion.com/details?pn=US06413552__
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UDP-galactose:.beta.-N-acetyl-glucosamine.beta.-1,4-galactosyl-transferase,.beta.4GalT2 Inventor(s): Bennett; Eric Paul (Lyngby, DK), Clausen; Henrik (Holte, DK) Assignee(s): Glycozm APS (Holte, DK) Patent Number: 6,558,934 Date filed: July 17, 1998 Abstract: A novel gene defining a novel enzyme in the UDP-D-galactose:.beta.-N-acetylglucosamine.beta.-1,4-galactosyltransferase family, termed.beta.4Gal-T2, with unique enzymatic properties is disclosed. The enzymatic activity of.beta.4Gal-T2 is shown to be distinct from that of previously identified enzymes of this gene family. The invention discloses isolated DNA molecules and DNA constructs encoding.beta.4Gal-T2 and derivatives thereof by way of amino acid deletion, substitution or insertion exhibiting.beta.4Gal-T2 activity, as well as cloning and expression vectors including such DNA, cells transfected with the vectors, and recombinant methods for providing.beta.4Gal-T2. The enzyme.beta.4Gal-T2 and.beta.4Gal-T2-active derivatives thereof are disclosed, in particular soluble derivatives comprising the catalytically active domain of.beta.4Gal-T2. Further, the invention discloses methods of obtaining.beta.-1,4galactosyl glycosylated saccharides, glycopeptides or glycoproteins by use of an enzymically active.beta.4Gal-T2 protein or fusion protein thereof or by using cells stably transfected with a vector including DNA encoding an enzymatically active.beta.4Gal-T2 protein as an expression system for recombinant production of such glycopeptides or glycoproteins. Also a method for the identification of DNA sequence variations in the.beta.4Gal-T2 gene by isolating DNA from a patient, amplifying.beta.4Gal-T2-coding exons by PCR, and detecting the presence of DNA sequence variation, are disclosed. Excerpt(s): The present invention relates generally to the biosynthesis of glycans found as free oligosaccharides or covalently bound to proteins and glycosphingolipids. This invention is more particularly related to a family of nucleic acids encoding UDP-Dgalactose:.beta.-N-acetylglucosamine.beta.-1,4-galactosyltransferases (.beta.4Galtransferases), which add galactose to the hydroxy group at carbon 4 of 2-acetamido-2deoxy-D-glucose (GlcNAc). This invention is more particularly related to a gene encoding the second member of the family of.beta.4Gal-transferases, termed.beta.4GalT2, probes to the DNA encoding.beta.4Gal-T2, DNA constructs comprising DNA encoding.beta.4Gal-T2, recombinant plasmids and recombinant methods for producing.beta.4Gal-T2, recombinant methods for stably transfecting cells for expression of.beta.4Gal-T2, and methods for identification of DNA polymorphism in patients. The UDP-galactose:.beta.-N-acetyl-glucosamine.beta.-1,4-galactosyltransferase (.beta.4Gal-T1) was the first animal glycosyltransferase to be isolated and cloned (Narimatsu et al., 1986; Shaper et al., 1986; Nakazawa et al, 1988; Shaper et al., 1988; D'Agostaro et al., 1989), and early searches for homologous genes by low stringency Southern hybridisation suggested that this gene was unique. Characterisation of.beta.4Gal-transferase activities from different sources, however, indicate that distinct activities exist (Sheares and Carlson, 1984; Furukawa et al., 1990). Emerging evidence now reveal that several.beta.4galactosyltransferase genes may exist. Shaper and colleagues (Shaper et al., 1995) have identified two different chick cDNA sequences, which have 65% and 48% sequence similarity to human.beta.4Gal-T1. Both chick cDNAs were shown to encode catalytically active p4Gal-transferases (Shaper et al., 1997). Two independent groups have analysed.beta.4Gal-transferase activities in mice homozygously deficient for.beta.4Gal-T1 (Asano et al., 1997; Lu et al., 1997). Both studies showed residual.beta.4Gal-transferase activity, providing clear evidence for the
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existence of additional.beta.4Gal-transferases. Thus, the.beta.4Gal-T1 gene is likely to be part of a homologous gene family with recognisable sequence motifs, and this is supported by a large number of human ESTs with sequence similarities to.beta.4Gal-T1 in EST databases (National Center for Biotechnology Information).beta.-1,4Galactosyltransferase activities add galactose to different acceptor substrates including free oligosaccharides, N- and O-linked glycoproteins, and glycosphingolipids (Kobata, 1992). In addition,.beta.4Gal-T1 is modulated by.alpha.-lactalbumin to function as lactose synthase and hence has a major role in lactation (Brew et al., 1968). Given the diverse functions of.beta.-1,4-galactosyltransferase activities and the evidence that multiple.beta.4Gal-transferases exist, it is likely that these enzymes may have different kinetic properties. Furukawa et al (Furukawa et al., 1990) showed that liver.beta.4Galtransferase activity was near 20-fold higher with asialo-agalacto-transferrin compared to asialo-agalacto-IgG, whereas the activity found in T and B cells only showed a 4 to 5fold difference with the two substrates. The.beta.4Gal-transferase activity in B cells of rheumatoid arthritis patients appear to be similar to B cells from healthy controls with several substrates including asialo-agalacto-transferrin (Furukawa et al., 1990) and.beta.GlcNAc-pITC-BSA (Keusch et al., 1995), but different with asialo-agalacto-IgG (Furukawa et al., 1990). Furthermore, the Km for UDP-Gal of.beta.4Gal-transferase activity from B cells of rheumatoid arthritis patients were 2-fold higher (35.6 mM) than normal B cells (17.6 mM) (Furukawa et al., 1990). Finally, the activity in B cells for asialoagalacto-transferrin was more sensitive to.alpha.-lactalbumin inhibition than the activity with asialo-agalacto-IgG. A number of studies have concluded that there was no change in.beta.4Gal-transferase activity in B cells of rheumatoid arthritis patients (Wilson et al., 1993; Axford et al., 1994). However, if multiple.beta.4Gal-transferases exist, it is possible that the contradictory findings of Furukawa et al. (Furukawa et al., 1990) can be explained by a model with two.beta.4Gal-transferases with different kinetic parameters expressed in normal B cells, and a selective down regulation of one in B cells of rheumatoid arthritis patients. Web site: http://www.delphion.com/details?pn=US06558934__ •
Use of glucosamine and glucosamine derivatives for quick alleviation of itching or localized pain Inventor(s): Vanden Berghe; Dirk Andre Richard (Laarne, BE) Assignee(s): New Key Foods N. V. (Knokke, BE) Patent Number: 6,495,531 Date filed: October 1, 1999 Abstract: The present invention relates to the new use of glucosamine and/or its derivatives for the preparation of a therapeutical composition for treating and quick relief of itching and/or local pain which results from a variety of causes. The invention further relates to therapeutical compositions for use in this treatment. Excerpt(s): The invention relates to the preparation of a topical medication for very quick alleviation and relief of itching and/or localized pain caused by a wide range of medical indications. Itching (pruritus) has a lot of underlying causes and can lead to a lot of complications by scratching. Itching may be associated with local pain. Pain can also occur independently. Both local pain and itching comprise the sensation associated with a lot of causes: inflammation, dry skin, infection by micro-organisms such as bacteria, fungi and viruses, corns, wounds, ulcers, stings, insect bites, allergic reactions, hyper proliferation of the epithelial layer, different types of treatment with chemicals,
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affecting the skin, eczema, etc. But there is also local pain associated with other affections, such as tendinitis, rheumatism and rheumatic affections, such as reumatalgia, reumatide reumatismus articulorum acutus, reumatismus articulorum chronicus, reumatismus musculorum, reumatismus nervosum, reumatismus nodosum, rheumatoid affections, different kinds of arthritis such as arthritis urica, arthritis acuta, arthritis sicca, arthritis hyperthrophica, arthritis infectiosa, arthritis rheumatica, different forms of arthrosis, skin burning by sun, other irradiations, chemicals or heat sources. In all these and other cases pain and/or itching may very often be difficult to treat. Moreover, oral pain killers may have undesired side effects due to their systemic mode of action, especially when taken over a prolonged period of time. Itching in itself can be very inconvenient and scratching can deteriorate the condition. Web site: http://www.delphion.com/details?pn=US06495531__ •
Vaccine compositions including chitosan for intranasal administration and use thereof Inventor(s): Chatfield; Steven Neville (Berkshire, GB), Illum; Lisbeth (Nottingham, GB) Assignee(s): West Pharmaceutical Services Drug Delivery & Clinical Research Centre (Nottingham, GB) Patent Number: 6,391,318 Date filed: June 1, 1998 Abstract: A variety of different types of nasal vaccine systems have been described including cholera toxin, microspheres, nanoparticles, liposomes, attenuated virus, and outer membrane proteins (proteosomes). The present invention is directed toward a novel nasal vaccine composition that utilizes the cationic polysaccharide, chitosan, as a delivery system. Chitosan is a polysaccharide comprising copolymers of glucosamine and N-acetylglucosamine. The term chitosan encompasses a series of chitosan polymers with different molecular weights (50 kDa-2,000 kDa) and degree of acetylation (40%98%). Several vaccine animal studies were carried out employing influenza or pertussis antigens in combination with chitosan. Nasal administration of chitosan-antigen nasal vaccines induced significant serum IgG responses and secretory IgA levels. Animals vaccinated via the nasal route with various chitosan-antigen vaccines were also found to be protected against the appropriate challenge. Excerpt(s): The invention is generally in the field of vaccine compositions, and specifically those for intranasal administration. Vaccines are preparations of antigenic materials, administered to recipients with a view to enhancing resistance to infection by inducing active immunity to specific microorganisms, for example bacteria or viruses. Vaccines, which may be as single or mixed component vaccines, are presented in a variety of forms. For example, current influenza vaccines consist of either inactivated whole virus, disrupted virus (split vaccines) or purified preparations of antigenic proteins. Web site: http://www.delphion.com/details?pn=US06391318__
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Patent Applications on Glucosamine As of December 2000, U.S. patent applications are open to public viewing.10 Applications are patent requests which have yet to be granted. (The process to achieve a patent can take several years.) The following patent applications have been filed since December 2000 relating to glucosamine: •
Aminosugar, glycosaminoglycan, and S-Adenosylmethionine composition for the treatment and repair of connective tissue Inventor(s): Hammad, Tarek; (Baltimore, MD), Henderson, Robert W.; (Baldwin, MD) Correspondence: Covington & Burling; Attn: Patent Docketing; 1201 Pennsylvania Avenue, N.W.; Washington; DC; 20004-2401; US Patent Application Number: 20030216348 Date filed: April 8, 2003 Abstract: A composition for the protection, treatment and repair and for reducing the inflammation of connective tissue in mammals and a method for the treatment of connective tissue in mammals by the administration of the composition. The composition includes S-Adenosylmethionine (SAM), and a component selected from an aminosugar or salts thereof (e.g., glucosamine) or glycosaminoglycans (e.g., chondroitin salts) or mixtures or fragments thereof. The composition optionally includes manganese which promotes the production of connective tissue matrix. The composition also optionally includes methyl donors or methyl donor cofactors, such as vitamin B12, vitamin B6, folic acid, dimethylglycine or trimethylglycine. Excerpt(s): The present application is a continuation-in-part of co-pending U.S. patent application Ser. No. 08/779,996, filed Dec. 23, 1996, the disclosure of which is incorporated by reference herein in its entirety. The present invention relates to compositions for the repair and reduction of inflammation of connective tissue in humans and animals and, in particular, to compositions capable of promoting antiinflammation, chondroprotection, chondromodulation, chondrostabilization, chondrometabolization and the repair and replacement of human and animal connective tissue. The connective tissues of humans and animals are constantly subjected to stresses and strains from mechanical forces and from diseases that can result in afflictions, such as arthritis, joint inflammation and stiffness. Indeed, connective tissue afflictions are quite common, presently affecting millions of Americans. Further, such afflictions can be not only painful but, in their extreme, debilitating. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Aqueous electrolyzed solution of ascorbyl glucosamine and preparation process therefor Inventor(s): Hanaoka, Kokichi; (Nagano, JP) Correspondence: Bruce Londa; Norris, Mclaughlin & Marcus, P.A.; 220 East 42nd Street, 30th Floor; New York; NY; 10017; US Patent Application Number: 20020179455 Date filed: April 2, 2002
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This has been a common practice outside the United States prior to December 2000.
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Abstract: This invention discloses an aqueous cathodic electrolyzed solution of ascorbyl glucosamine exhibiting a lower oxidation-reduction potential than that in an aqueous solution of ascorbyl glucosamine in which a concentration of water-soluble inorganic salts is less than 0.1 M prepared by electrolyzing the starting ascorbyl glucosamine solution as well as a preparation process therefor. A concentration of ascorbyl glucosamine is 0.1 to 3 wt %. A current density in electrolysis is preferably 0.003 to 0.03 A/cm.sup.2. Excerpt(s): This invention relates to an aqueous electrolyzed solution prepared by electrolysis of a starting aqueous solution of ascorbyl glucosamine, which has a lower oxidation-reduction potential than the starting aqueous solution of ascorbyl glucosamine, as well as a preparation process therefor. It is a well-known technique that a dilute starting aqueous solution of an electrolyte (e.g., an alkali-metal chloride) as an electrolysis aid is electrolyzed in an electrolytic cell while removing an aqueous anodic electrolyzed solution with a lower pH generated around the anode (acidic water), which is then utilized for sterilization or disinfection (JP-A 6-246272). The electrolytic cell internally comprises inactive electrodes made of, e.g., platinum or a platinum alloy separated by a septum. The septum used is a charged membrane which is an ionexchange resin film or a non-charged membrane having a microporous structure. The aqueous anodic electrolyzed solution formed around the anode contains hypochlorous acid. Potent oxidizing and chlorinating action of hypochlorous acid has been widely utilized for sterilization or disinfection in medical institutions. In addition, since a small amount of ozone and/or dissolved oxygen in the acidic water can promote granulation, the acidic water has been studied for its use as an aid in surgical treatment. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Cartilage enhancing food supplements with sucralose and methods of preparing the same Inventor(s): Stone, Kevin R.; (Mill Valley, CA) Correspondence: Mcdermott, Will & Emery; 28 State Street; Boston; MA; 02109; US Patent Application Number: 20030124200 Date filed: July 1, 2002 Abstract: A food supplement, either in the form of a snack bar or a beverage, which contains one or more cartilage enhancing supplements and sucralose is provided. The cartilage supplements include chondroitin, glucosamine, and hyaluronic acid. The food supplement may additionally be fortified with cetyl myristoleate. The beverage is a mixture of a juice drink base which may include a water-based fruit flavored juice prepared using a pasteurization process at a relatively high temperature and a cartilage supplement solution which includes a cartilage supplement prepared at a relatively low temperature. The beverage may be carbonated, non-carbonated or concentrated. The preferred cartilage supplement is glucosamine, preferably associated with a counter ion, more preferably as glucosamine hydrochloride. Excerpt(s): This application is a continuation-in-part of U.S. patent application Ser. No. 09/598,634, filed Jun. 21, 2000, which is a continuation-in-part of U.S. patent application Ser. No. 09/338,021, filed Jun. 22, 1999, the disclosures of which are incorporated herein by references. The present invention relates to food supplements, such for example, snack bars and beverages that are fortified with one or more cartilage supplements. Nutritional bars and energy drinks are convenient nutritional supplements, particularly
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for those persons too busy to eat regular meals and for hikers, cyclists, runners or other athletes who need prepackaged, ready-to-eat, high-energy snacks while they are exercising. Such bars and drinks are also convenient nutritional supplements for the elderly who need prepackaged, ready-to-eat snacks. Additionally, such food supplements can supply consumers with the necessary vitamins and minerals specified in the recommended daily allowances provided by the U.S. government. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Cholesterol sulfate and amino sugar compositions for enhancement of stratum corneum function Inventor(s): Maes, Daniel H.; (Huntington, NY), Zecchino, Jules; (Closter, NJ) Correspondence: Karen A. Lowney, ESQ.; Estee Lauder Companies; 125 Pinelawn Road; Melville; NY; 11747; US Patent Application Number: 20020142013 Date filed: January 31, 2001 Abstract: The present invention provides compositions containing a mixture of cholesterol sulfate and an exfoliant. The exfoliant can be N-acetyl-D-glucosamine, Nacetylgalactosamine, or a combination thereof. The combination of the cholesterol sulfate with the exfoliant surprisingly enhances the skin barrier even though the activity of each of the components is opposite the other. In addition, because of the ability to enhance or repair the skin barrier function, methods of improving or maintaining a healthy skin barrier are included in the present invention by applying to the skin an effective amount of the mixture of cholesterol sulfate with the exfoliant. The mixture can also be useful in treating or preventing damage to the skin, where the damage is caused by a compromised skin barrier function. As a result of improving the skin barrier function with the combination of cholesterol sulfate and the exfoliant, the appearance of lines and wrinkles is generally reduced; rough and dry skin conditions are also improved. Excerpt(s): The present invention relates to cosmetic compositions. More specifically, the invention relates to topical compositions containing a combination of cholesterol sulfate and an amino sugar for the treatment of skin. The stratum corneum represents the major chemical and physical barrier between the body and the environment. It is formed by a process in the epidermis which involves the transformation of germinative cells into terminally differentiated cells; the process of transformation takes approximately one month, by which time the terminally differentiated cells are shed from the skin surface. The cells at the outermost layer of the skin, which regularly slough off, are replaced by cells that generate originally at the basal layer of the epidermis and rise up to the outer surface as other newer cells are generated at the basal layer. As these cells migrate from the basal layers up to the outer levels of the skin, these cells produce and accumulate keratin, to the point at which there is virtually no cytoplasm remaining; at this point, the cell dies and sheds off of the skin. The shed layer of dead skin reveals a fresh layer of healthy skin, another phalanx of migrating epidermal cells. The thickness of the stratum corneum and epidermis, in general, varies in different regions of the body, and plays a role in the rate of shedding dead skin layers. The cornified barrier performs a number of functions. As mentioned, a particularly important aspect of its presence is as a physical barrier, between the deeper layers of the skin as well as the internal organs and the environment. Prevention or attenuation of penetration of UV radiation, as well as other harmful stimuli such as free radicals, to the deeper skin layers are examples of the
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critical aspect of this skin layer. The skin acts as a permeability barrier and therefore, the skin functions to prevent the loss of body water to the external environment. Unfortunately, as with many other skin functions, the capacity of the stratum corneum to cyclically generate new layers of the skin progressively diminishes with age. The stratum corneum is a densely packed structure of intracellular fibrous elements that are hydrophilic and able to trap water. The intercellular space is filled with lipids that provide a diffusion pathway to channel substances with low solubility in water. Thus, the skin barrier of the stratum corneum resembles a brick wall, the corneocytes are the bricks and the intercellular matrix is the mortar. The turnover rate of the stratum corneum is considerably decreased in older individuals, however, and the cornified layer gradually becomes thinner, thereby reducing the efficacy of this physical barrier and making it easier for harmful stimuli such as UV rays to penetrate the skin barrier. This in turn leads to UV-damage to the dermal layers of the skin, degradation of collagen and elastin, and finally, wrinkling and skin atrophy. These are examples of a skin barrier that is compromised and unhealthy. Moreover, the thinning of the stratum corneum can enhance the visibility of wrinkling and atrophy, the cause of which is rooted in the dermis. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Composition and method for growing, protecting, and healing tissues and cells Inventor(s): Petito, Anita M.; (Bethlehem, PA), Petito, George D.; (Bethlehem, PA) Correspondence: Richard C. Litman; Litman Law Offices, LTD.; P.O. Box 15035; Arlington; VA; 22215; US Patent Application Number: 20030212005 Date filed: June 10, 2003 Abstract: A method and medicinal compositions for facilitating the growth, protection and healing of tissues and cells in animals and humans. The compositions are formulated as a either a powder, gel, paste, film, fluid injectable, rehydratable freezedried paste or sponge, sprayable solution, topically applied patch with adhesive and reservoir system, an intermediate for coatables such as films and bandages, a matrix for membranes, or as a matrix of flexible polymer(s), or delivered as either an orally ingestible liquid, tablet or capsule. The main ingredient of the formulated compositions is hydrolyzed collagen, which can be combined with polysulfated glycosaminoglycans, hyaluronic acid or salts thereof, or a glucosamine salt, and mixtures thereof Excerpt(s): This application is a continuation of application Ser. No. 09/983,274 filed Oct. 23, 2001, which is a continuation-in-part of application Ser. No. 09/360,169 filed Jul. 26, 1999, now U.S. Pat. No. 6,476,005, which is a continuation-in-part of application Ser. No. 09/046,710 filed Mar. 24, 1998, now abandoned. The present invention relates to a method and composition for growing, protecting, and healing tissues and cells of animals or humans. The invention particularly pertains to a method for repairing connective and other tissues, and, in particular, wound healing and scar reduction by administering a composition comprising a hydrolyzed collagen as the basic ingredient, preferably in combination with at least one therapeutic agent selected from the group consisting of a polysulfated glycosaminoglycan, hyaluronic acid and salts thereof, and a glucosamine salt. Just as nature has provided the skin as a barrier for protection, it has also provided mechanisms for skin repair. Depending upon the nature of the injury, this repair process may take hours, days, months, or even years. Many factors determine the length of times it takes for an injured skin to heal. Pathogenic contaminants may enter
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the body through the wound until the skin's integrity is restored. For this reason, it desirable to heal open wounds as quickly as possible. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Composition for promoting healthy bone structure Inventor(s): Johnson, Holly A.; (San Clemente, CA), Krumhar, Kim C.; (Carlsbad, CA) Correspondence: Knobbe Martens Olson & Bear Llp; 2040 Main Street; Fourteenth Floor; Irvine; CA; 92614; US Patent Application Number: 20030059481 Date filed: September 9, 2002 Abstract: A dietary supplement for benefitting human bone health includes a calcium source, a source of vitamin D activity, and an osteoblast stimulant. A preferred calcium source is microcrystalline hydroxyapatite, which also contains protein (mostly collagen), phosphorus, fat, and other minerals. A preferred source of vitamin D activity is cholecalciferol, and a preferred osteoblast stimulant is ipriflavone. In addition to these basic ingredients, the composition can further include various other minerals known to occur in bone, vitamin C, and glucosamine sulfate, all of which exert beneficial effects on growth and maintenance of healthy bone. A method for benefitting human bone health involves administering a daily regimen of the dietary supplement. Excerpt(s): This application is a continuation of application Ser. No. 09/568,903, filed May 11, 2000, which claims the benefit of U.S. Provisional Application No. 60/133,603, filed May 11, 1999, which is hereby incorporated herein by reference. This invention relates to dietary supplements. More particularly, this invention relates to compositions and methods for promoting healthy bone structure. Osteoporosis is a common metabolic bone disease that leads to the gradual loss of mineralized bone from the skeletal mass. This is due in part to an imbalance in the rates of cell-mediated bone deposition and resorption due to the actions of osteoblasts and osteoclasts in the bone matrix. Bone mineral is in a constant state of destruction and repair referred to as "remodeling," and maintenance of bone density over time is believed to require a precise balance after menopause or during the course of certain disease states. Bone resorption, when exceeding bone formation, can lead to bone fractures resulting from minimal trauma. Unfortunately, there are no symptoms preceding fractures. A common cause of osteoporosis is the decrease in estrogen production following menopause that leads to an increase in bone resorption. Conventional methods to counter bone resorption in women include estrogen therapy and calcium supplementation. Long-term treatment with estrogen has been the only method correlated to significant protection from bone loss in postmenopausal women. See Agnusdei D, Bufalino L. Efficacy of ipriflavone in established osteoporosis and long-term safety. Calcified Tissue International 1997;61:S23-S27. The isoflavone, ipriflavone, is now successfully used in many countries to treat and prevent osteoporosis. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Composition for the relief of joint pain and myofascial pain and method of preparing same Inventor(s): Knigge, Jan Donald; (St. Petersburg, FL) Correspondence: N. Whitney Wilson; Bryan Cave Llp; 245 Park Avenue; New York; NY; 10167-0034; US Patent Application Number: 20030045503 Date filed: September 30, 2002 Abstract: A stable, formulation comprising glucosamine and chondroitin compounds in a base which can be used for topical application to relieve joint pain and myofascial pain. A method of preparing the composition by adding the glucosamine and chondroitin after the rest of the components of the formulation have been mixed and heated is also disclosed. Excerpt(s): This invention relates to a topically applied composition for the treatment of joint pain and myofascial pain, a process for preparing the composition, and a method of treating joint pain and, myofascial pain using the composition. Joint pain and myofascial pain can be caused by arthritis, cartilage injury or disease, and other sources. Patients can find such pain to be debilitating, and have used a variety of treatments for relief of pain, including formulations administered orally, parenterally, and topically. A popular form of treatment for joint pain and myofascial pain is the topical application of pain relieving ointments which contain menthol. Formulations for topical application can either be water-based or substantially anhydrous. For many applications, anhydrous (i.e. oil-based) formulations are preferable because anhydrous formulations will not evaporate like those containing water or alcohol. Anhydrous formulations, therefore, are easier to use in massaging applications. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Compositions and methods directed towards sore muscles and joints Inventor(s): Reynolds, Peter L.; (Marietta, GA) Correspondence: Thomas, Kayden, Horstemeyer & Risley, Llp; 100 Galleria Parkway, NW; Ste 1750; Atlanta; GA; 30339-5948; US Patent Application Number: 20030185904 Date filed: March 26, 2002 Abstract: Chemical formulations and methods for reducing muscle and joint soreness are disclosed. A representative chemical formulation includes compounds such as a selenium-compound, chondroitin sulfate, glucosamine, and/or methylsulfonylmethane. A representative method for reducing muscle and joint soreness includes administering the chemical formulation to a host. Excerpt(s): The present invention is generally related to chemical formulations and methods for administration of the chemical formulation to mammals and, more particularly, is related to chemical formulations directed towards reducing muscle and joint soreness and methods of administration thereof. Often muscle soreness and joint pain occur concurrently as a result of physical exertion or old age. In addition, joint pain may occur as a result of arthritis or other degenerative joint diseases, which may also indirectly cause muscle soreness. Muscle and joint soreness occur in most mammals and, in particular, occur in humans, horses, dogs, and cats. The soreness creates many
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problems, such as making normal mammalian actions difficult and painful. These actions include walking, squatting, running, grasping, etc. To alleviate this discomfort, multiple pain relievers need to be taken, e.g., one pain reliever to address the muscle soreness and another pain reliever to address joint soreness. Multiple pain relievers, e.g. pills or tablets, can be difficult to administer in same mammals, such as horses, dogs, and cats. Further, there are significant costs associated with purchasing multiple pain relievers. Selenium compounds, both organic and inorganic, and methylsulfonylmethane have been used for years as mineral supplements to maintain good health and relieve muscle soreness, but not joint pain or soreness. Glucosamine has been shown to be effective for reducing arthritis and soreness of the joints, but not muscle soreness. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Effervescent glucosamine, chondroitin and MSM formula Inventor(s): Phillips, Cleve Alan; (Hayward, CA) Correspondence: Williams Mullen; 1 Old Oyster Point Road; Suite 210; Newport News; VA; 23602; US Patent Application Number: 20030180389 Date filed: March 20, 2003 Abstract: A composition which acts to protect, maintain and repair connective tissue in mammals. The composition includes glucosamine, chondroitin sulfate and sulfur in an effervescent base as its major elements. The effervescent base includes one or more acids and one or more bases and may also include a starch, a flavoring agent and a coloring agent. The composition can be formed into a tablet or can be granular. The tablet or granular mixture is dissolved in a neutral pH liquid such as water for consumption purposes. Excerpt(s): The present application claims priority from U.S. Provisional Application Ser. No. 60/150,552, filed Aug. 25, 1999. The present invention pertains to the field of nutritional formulas. Specifically, the present invention pertains to an improved formula for delivering glucosamine, chondroitin and MSM to the body. It is well known that products containing glucosamine, chondroitin and MSM can aid in the protection, maintenance and repair of connective tissue in mammals. Such tissues are regularly exposed to stresses and strains from forces which cause problems such as arthritis, joint inflammation and stiffness. These problems can affect all joints in both humans and animals and can be both painful and debilitating to the sufferer. While the optimal treatment is relief from the force causing the joint problems, this is not always possible. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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External compositions for skin comprising sphingoglycolipid Inventor(s): Asai, Michiki; (Tokyo, JP), Hara, Hisako; (Tokyo, JP), Murata, Katsumi; (Tokyo, JP), Nozawa, Takashi; (Tokyo, JP), Wakayama, Sachio; (Tokyo, JP) Correspondence: Browdy And Neimark P.L.L.C.; Suite 300; 624 9th Street, N.W.; Washington; DC; 20001-5303; US Patent Application Number: 20020164351 Date filed: December 12, 2001 Abstract: A white fungus of genus Sphingomonas, when washed with acetone and then extracted with alcohol or alcohol-water mixture yields a shingoglycolipid represented by the following formula: 1where, R.sub.1 represents a sugar portion of a single uronic acid or one to four hexoses of uronic acid, glucosamine, galactose and/or mannose; R.sub.2 represents an alkyl group which may have a cycloalkyl group, an alkenyl group or an alkynyl group; and R.sub.3 represents on alkyl group. Excerpt(s): This is a division of copending parent application Ser. No. 09/084,394, filed May 27, 1998. This invention relates to external compositions for skin comprising sphingoglycolipid available as cosmetic and medicine. The external compositions for skin of the present invention have a potent moisturizing effect and preventive effect against skin roughness. Skin roughness is caused by losing moisture from the skin surface during dry weather or cleansing. Miscellaneous chemical substances present in modern society can contact skin to inhibit skin functions, which may also result in skin roughness due to depression of lipid secretion ability. It is thus expected to provide external compositions for skin having an excellent moisturizing effect and capable of preventing skin roughness before it occurs. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Food product supplemented with proteoglycan precursors Inventor(s): Bahoshy, Robert; (Long Beach, CA) Correspondence: Peng Chen; Morrison & Foerster Llp; Suite 500; 3811 Valley Centre Drive; San Diego; CA; 92130-2332; US Patent Application Number: 20030134825 Date filed: January 3, 2003 Abstract: A food product for supplementing the proteoglycan precursor intake of humans suffering from joint related ailments and a method of making and administering such a food product is disclosed. More specifically, a settable food product, supplemented with glucosamine and chondroitin, which comes in a suitable form, e.g., a pudding or pie filling, is disclosed, along with a method of making and administering the product to persons in need thereof. Excerpt(s): This application claims the benefit of Provisional Patent Application No. 60/344,053 filed on Jan. 3, 2002, and Provisional Patent Application No. 60/353,051 filed on Jan. 29, 2002 under 35 U.S.C.sctn.119(e). The contents of the above-referenced applications are incorporated herein in their entireties. Throughout this application, various references are referred to. Disclosures of these publications in their entireties are hereby incorporated by reference into this application to more fully describe the state of the art to which this invention pertains. The present invention generally relates to food compositions for the treatment of joint related ailments, and methods for making and
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administering these compositions. In particular, the present invention relates to the preparation of compositions including proteoglycan precursors and method for administering these precursors in a beneficial and appetizing manner to persons in need thereof. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Glucosamine and method of making glucosamine from microbial blomass Inventor(s): Bohlman, John A.; (Ottumwa, IA), Fan, Weiyu; (Minnetonka, MN), Henning, Joseph P.; (Eddyville, IA), Hwang, Ki-Oh; (Oskaloosa, IA), Steinke, James Donald; (Oskaloosa, IA), Trinkle, James R.; (Bussey, IA) Correspondence: Merchant & Gould PC; P.O. Box 2903; Minneapolis; MN; 55402-0903; US Patent Application Number: 20020115639 Date filed: February 16, 2001 Abstract: Glucosamine suitable for human or animal consumption is disclosed. The glucosamine is derived from microbial biomass containing chitin. Suitable starting materials include substantially uniform microbial fungal sources, such as fungal sources derived from Aspergillus sp., Penicillium sp., Mucor sp. and combinations thereof. Methods of producing glucosamine by acid hydrolysis of fermented fungal biomass are also disclosed. Excerpt(s): The present invention is directed to glucosamine compositions and to methods of making glucosamine compositions. Glucosamine is a nutraceutical supplement that has been shown to provide significant therapeutic relief for arthritis and joint pain. Although the mechanism is not entirely known, it is believed that glucosamine functions to aid in restoration of the cartilage to relieve inflammation in the joints, thereby providing significant benefit to patients. Presently, glucosamine is primarily derived from harvested natural sources, such as shellfish and other aquatic organisms. Components of the shell or exoskeleton of these organisms are converted into glucosamine using various production techniques. These natural sources are acceptable for producing glucosamine for some applications, but they have limitations. These limitations include the fact that wild shellfish can have significant variations in their composition because they grow naturally under uncontrolled circumstances. The shellfish can vary in such aspects as their size and composition depending upon the growing conditions as well as their species. Also, without control over the growing conditions, the shellfish can be exposed to environmental contaminants, including heavy metals, that can be retained in glucosamine or other products produced from the shellfish. Shellfish harvests are often seasonal, and thus the supply and price of shellfish shows significant variation over time. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Hard surface cleaners containing chitosan and furanone Inventor(s): Avery, Richard W.; (Radnage, GB), Robb, Ian; (Duncan, OK), Wick, Roberta A.; (Racine, WI) Correspondence: S.C. Johnson & Son, INC.; 1525 Howe Street; Racine; WI; 53403-2236; US Patent Application Number: 20030083224 Date filed: October 26, 2001 Abstract: Disclosed herein are acidic aqueous hard surface cleaners and methods for using them. The cleaners include a poly D-glucosamine such as chitosan and also a furanone. The cleaners provide residual benefits on the hard surface such as soil resistance and resistance to bacteria, molds and biofilms. Excerpt(s): The present invention relates to cleaning compositions for hard surfaces. They appear to be especially well suited for use in cleaning toilets, baths, shower surrounds and other plumbing fixtures, bathroom and kitchen hard surfaces, drains and floor surfaces. The art has developed a variety of hard surface cleaning compositions, including some which are acidic. For example, U.S. Pat. No. 5,008,030 discloses cleaning compositions that contain nonionic surfactants, a monocarboxylic acid, water, and other additives. The disclosure of this patent and of all other patents described herein are incorporated by reference as if fully set forth herein. Also, U.S. Pat. No. 5,061,393 teaches a hard surface cleaner that is a mixture of a zwitterionic surfactant, nonionic surfactant, citric acid, and various other components, and U.S. Pat. No. 5,851,980 teaches aqueous acidic liquid hard surface cleaners having nonionic surfactants, glycolic and lactic acids, N-alkyldimethyl benzyl ammonium chloride, and fragrance. Ether solvents are also taught in the last of these patents. U.S. Pat. No. 5,061,397 also teaches hard surface cleaners with butyl cellosolve, citric acid, and colorants. Other publications describe the use of sulfamic acid, amine oxides and cellulosic thickeners and hard surface cleaners. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Hemostasis pad and method Inventor(s): Levinson, Melvin; (Pinecrest, FL) Correspondence: Mark G. Lappin, P.C.; Mcdermott, Will & Emery; 28 State Street; Boston; MA; 02109; US Patent Application Number: 20030093115 Date filed: November 1, 2002 Abstract: The present invention relates generally to medical devices for applying hemostatic composition to a puncture or wound site with indwelling tubular element, such as catheter, introducer or tube therein, particularly a hemostatic pad with an opening therethrough in order to allow egress of the indwelling tubular element through the hemostatic pad as the hemostatic pad provide hemostasis at the hemorrhaging site. The device may be applied to, or removed from, the wound site while the tubular element is in place. A method for effecting hemostasis at a puncture wound, includes applying pressure proximal to the puncture wound, and directing a cationic biopolymer of glucosamine application surface of a closure pad against the puncture wound with force sufficient to prevent fluid from exiting the puncture wound. Then the pressure proximal to the puncture wound is removed and the force on the
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closure pad is maintained for at least a first predetermined time period. The force on the closure pad is removed if hemostasis is verified. The puncture wound may then be dressed over the closure pad, and the dressing and the closure pad removed after a second predetermined time period. Excerpt(s): This application is a continuation in part of U.S. patent application Ser. No. 10/008,052, filed Nov. 13, 2001, the disclosure of which is incorporated herein by reference. The present invention relates to medical devices for hemostasis, and methods of using the medical devices for hemostasis. More particularly, the present invention relates to medical devices for effecting hemostasis at a puncture wound with an indwelling tubular element extending therethrough. Puncture of blood vessels is a necessary stage in many of the minimally invasive approaches to diagnosis and treatment, including interventional radiology and cardiology. Therefore, a need to create hemostasis as rapidly as possible following the procedure becomes an important priority. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Low molecular weight chondroitin sulphate compound having cosmetic activity Inventor(s): Delannoy, Charles; (Wimereux, FR), Durand, Patrick; (Reze, FR), Landrein, Annie; (Nantes, FR), Roy, Philippe; (Nantes, FR) Correspondence: Jacobson Holman; Professional Limited Liabilty Company; 400 Seventh Street, N.W.; Washington; DC; 20004; US Patent Application Number: 20030032620 Date filed: July 25, 2001 Abstract: The invention relates to a low molecular weight chondroitin sulphate compound having cosmetic activity, characterised more particularly by efficient incorporation in vitro of thymidine, glucosamine and leucine in fibroblast macromolecules of the human cutis. Local application of this compound stimulates fibroblast metabolism. The invention also relates to a method of preparing the said compound. Excerpt(s): The constituents of the extracellular matrix of the skin are divided among various categories mainly comprising laminin, the various kinds of collagens, elastin, fibronectin and various proteoglycanes, the main ones being heparan sulphate and chondroitin sulphates. These proteoglycanes (J. T. Gallagher, 1989. Current Biol., 1, 1201) comprise a protein part on to which glycosylated chains with repeating units called glycosaminoglycans (GAG) are grafted. Depending on the type of skin (phanerogenic or glabrous) their distribution may be heterogeneous or homogeneous. They also occur as constituents of the plasmic membrane and some are directly associated with the collagen fibrils. Owing to their negative charges, they produce an environment round them capable of trapping ions, water and various metabolites. GAG chains also perform an essential function owing to their affinity for circulating growth factors. Chondroitin sulphates (CS) are usually obtained from animal cartilage or skins and are characterised by the presence of a sulphate group on the disaccharide unit. Industrially, CS are obtained mainly from avian, ovine, bovine, porcine and shark cartilages. In view of the risk of bovine spongiform encephalopathy, bovine and ovine cartilages are no longer used to a significant extent. It is also likely that in the near future a larger number of shark species will be classed as protected species. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Means for regulating hematopoietic differentiation Inventor(s): Charrad, Rachida-Sihem; (Villejuif, FR), Chomienne, Christine; (Paris, FR), Delpech, Bertrand; (Saint Aubin Les Elbeuf, FR), Jasmin, Claude; (Charenton, FR), Smadja-Joffe, Florence; (Fontenay aux Roses, FR) Correspondence: Nixon & Vanderhye P.C.; 8th Floor; 1100 North Glebe Road; Arlington; VA; 22201-4714; US Patent Application Number: 20030032621 Date filed: August 13, 2001 Abstract: The invention concerns the use of a polymer comprising an efficient amount of disaccharide units each consisting of a molecule with N-acetyl-D-glucosamine structure bound by the O-glucoside.beta.1,4 linkage to a molecule with glucuronic acid structure for producing a medicine designed to induce or stimulate the differentiation of hematopoietic cells, and leukemic cells in particular. Excerpt(s): The present invention, as a general rule, relates to means used to regulate the differentiation of haematopoietic cells. Remarkably, the regulation means according to the invention apply to the differentiation of cells wherein the differentiation no longer corresponds to a normal profile and particularly to cells wherein differentiation is inhibited (leukaemic cells, in particular acute myeloblastic leukaemia blasts). According to another remarkable aspect, the regulation means according to the invention also apply to the differentiation of haematopoietic cells. Indeed, the regulation means according to the invention make it possible to induce or stimulate the differentiation of leukaemic cells and AML blasts in particular, and that of strain cells according to the granulocytic process and the monocytic process. In spite of spectacular therapeutic progress in recent years, AML remains a severe disease since the first remission, although it can be induced in 70% of cases, frequently does not last for more than one year, and 60% of patients relapse within 5 years. AML relapse treatments, which generally require bone marrow grafts, are experiencing significant limitations due to the rarity of related donors and an age limit of 45 years. Recently, the induction of the differentiation of leukaemic blasts in mature granulocytes by administering retinoic acid (RA, or all-transretinoic acid ATRA) has improved the clinical progression of patients suffering from M3 AML spectacularly, wherein the remission rate is currently 70% after 5 years. However, this differentiation treatment is not applicable to patients suffering from M3 sub-type AML, a rare sub-type which only represents approximately 10% of AML cases, and poses in vivo resistance problems. In addition, this treatment remains ineffective for other types of AML. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Method and compositions for the treatment and prevention of pain and inflammation with a cyclooxygenase-2 selective inhibitor and chondroitin sulfate Inventor(s): Kundel, Susan; (Basel, CH), Pulaski, Steven P.; (Branchburg, NJ) Correspondence: Charles E. Dunlap; Keenan Building, Third Floor; 1330 Lady Street; Columbia; SC; 29201; US Patent Application Number: 20030114416 Date filed: August 9, 2002
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Abstract: A method of treating, preventing, or inhibiting pain, inflammation or inflammation-associated disorder in a subject in need of such treatment or prevention provides for treating the subject with chondroitin sulfate and a cyclooxygenase-2 selective inhibitor, or a prodrug thereof, wherein the amount of chondroitin sulfate and the amount of a cyclooxygenase-2 selective inhibitor or a pharmaceutically acceptable salt or prodrug thereof together constitute a pain or inflammation suppressing treatment or prevention effective amount. Glucosamine can optionally be present. Compositions that contain the combination of chondroitin sulfate and cyclooxygenase-2 selective inhibitor and, optionally, the glucosamine, are disclosed, as are pharmaceutical compositions. Excerpt(s): The present application claims the benefit of U.S. Provisional Application Serial No. 60/312,211 filed Aug. 14, 2001, which is incorporated herein by reference thereto. The present invention relates to methods for the treatment and prevention of pain and inflammation and compositions for such treatment, and more particularly to methods for the treatment and prevention of pain and inflammation in subjects needing such treatment and prevention and to compositions comprising a cyclooxygenase-2 selective inhibitor that are useful in such methods. Inflammation is a manifestation of the body's response to tissue damage and infection. Although the complex mechanisms of inflammation are not fully elucidated, inflammation is known to have a close relationship with the immune response and to be associated with pain and fever in the subject. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Method for effecting hemostasis Inventor(s): Diaz, Raymond; (Weston, FL), Golik, George; (Miami, FL), Levinson, Melvin; (Pinecrest, FL), Manzano, Ernest; (Miami, FL) Correspondence: Mcdermott, Will & Emery; 28 State Street; Boston; MA; 02109; US Patent Application Number: 20030093114 Date filed: November 13, 2001 Abstract: A method for effecting hemostasis at a puncture wound, includes applying pressure proximal to the puncture wound, and directing a cationic biopolymer of glucosamine application surface of a closure pad against the puncture wound with force sufficient to prevent fluid from exiting the puncture wound. Then the pressure proximal to the puncture wound is removed and the force on the closure pad is maintained for at least a first predetermined time period. The force on the closure pad is removed if hemostasis is verified. The puncture wound may then be dressed over the closure pad, and the dressing and the closure pad removed after a second predetermined time period. Excerpt(s): The present invention relates to a method for local management of bleeding wounds and, more particularly, a method for rapidly controlling bleeding even in patients receiving hemodialysis and anticoagulation treatments. During catheterization procedures, the nurse or physician will create an opening into an artery or other vessel with a conventional catheter introducer or dilator. Additionally, the catheter is often twisted or otherwise manipulated as it is advanced to the treatment site, thereby causing a further enlargement of the incision or puncture in the body of the patient. When the medical procedure is completed and the catheter is removed from the artery or other blood vessel, conventional practice has been to apply external pressure to the entry site
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until hemostasis occurs. Because many of the patients undergoing these procedures have been medicated with an anticoagulant such as heparin, the nurse may be required to apply external pressure to the incision site for an extended period of time period. The time period required to stop bleeding at the incision is not an efficient use of the nurses time period and a painful hematoma or unsightly bruise may still occur at the incision site because the artery will continue to bleed internally until clotting blocks the opening in the artery. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Methods for inhibiting angiogenesis Inventor(s): Banerjee, Dipak K.; (Guaynabo, PR), Martinez, Juan A.; (Rio Piedras, PR) Correspondence: Greenblum & Bernstein, P.L.C.; 1941 Roland Clarke Place; Reston; VA; 20191; US Patent Application Number: 20020160979 Date filed: February 9, 2001 Abstract: A method for inhibiting angiogenesis, including: administering a nucleoside, such as tunicamycin, in an amount effective to inhibit angiogenesis, to a patient in need of such treatment. A method for inhibiting angiogenesis, including: administering a nucleoside, which comprises glucosamine, in an amount effective to inhibit angiogenesis, to a patient in need of such treatment; wherein the nucleoside is administered for a period of time, subsequently the administration of the nucleoside is suspended for a period of time of at least about 1 week, and subsequently the administration of the nucleoside is resumed. Excerpt(s): The present application claims the priority under 35 U.S.C.sctn.119(e) of U.S. Provisional Application No. 60/181,312, filed Feb. 9, 2000, the disclosure of which is expressly incorporated by reference herein in its entirety. The present invention relates to methods for inhibiting angiogenesis. Thus, the present invention relates to methods of inhibiting the growth of capillary endothelial cells which form new blood microvessels. Accordingly, the present invention is directed to treating disease states, e.g., tumors such as malignant and benign tumors, characterized by an abnormally high amount of angiogenesis. Endothelial cell proliferation and differentiation into blood capillaries (i.e., angiogenesis) are essential for growth and development, wound healing, osteogenesis, etc. Endothelial cells in adult tissues are quiescent but rapid proliferation occurs for a limited period of time during menstruation, ovulation, reproduction, implantation, mammary gland changes during lactation, and wound healing, as discussed in COCKREILL et al., "Angiogenesis: Model and Modulators", Int Rev Cytol, 159: 113-159 (1995); and FOLKMAN et al., "Angiogenesis", J Biol Chem, 267:10931-10934 (1992), the disclosures of which are herein incorporated by reference in their entireties. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Methods for making and using a Chlorella extract having immunomodulating properties Inventor(s): Kralovec, Jaroslav A.; (Halifax, CA) Correspondence: Smart & Biggar; P.O. Box 2999, Station D; 55 Metcalfe Street, Suite 900; Ottawa; ON; K1p5y6; CA Patent Application Number: 20030152587 Date filed: February 19, 2003 Abstract: Chlorella extracts containing high molecular weight Chlorella polysaccharide and polysaccharide complexes show immune modulatory, specifically immune stimulatory, activity. The polysaccharide and polysaccharide complexes contain glucose and any combination of: galactose, rhamnose, mannose and arabinose, as well as Nacetyl glucosamine and N-acetyl galactosamine. The extracts may be treated with pronase, DNAse, RNAse and proteases to remove unassociated nucleic acids, ribonucleic acids and proteins. The extracts may also undergo treatment to effect cleavage of specific glycosidic linkages, the linkages being defined by their susceptibility to cleavage by amylase, amyloglucosidase, cellulase or neuraminidase. Chlorella extracts may be administered to a mammal to increase proliferation of splenocytes and increase production of cytokines such as IL-6, IL-10, INF-.gamma. and TNF-.alpha. They may be used as a supplement to a vaccination regimen. Excerpt(s): This application claims the benefit of U.S. Provisional Application No. 60/224,014, filed Aug. 10, 2000, the content of which is herein incorporated by reference. The present invention relates to Chlorella extracts for use as immunomodulators. Chlorella is a unicellular green algae that has been called a sun-powered supernutrient. Attested beneficial properties of this edible microalgae include wound healing, detoxification, constipation relief and growth stimulation. A number of studies have also indicated that Chlorella has beneficial effects on the immune system, both in vitro and in vivo. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Methods for the identification of fungal glucose utilization inhibitors and antifungal agents Inventor(s): Nakata, Mitsunori; (Denver, CO), Selitrennikoff, Claude P.; (Evergreen, CO) Correspondence: Medlen & Carroll, Llp; 101 Howard Street; Suite 350; San Francisco; CA; 94105; US Patent Application Number: 20030194758 Date filed: August 10, 2001 Excerpt(s): The present invention provides methods for simultaneously assessing microbial phosphoglucose isomerase, ketol-isomerase and glucosamine-6-phosphate acetyltransferase activities, by measuring the production of Coenzyme A (CoA). The present invention finds use in the isolation of new classes of antifungal drugs, wherein the compounds have the ability to inhibit fungal glucose utilization. During the last three decades there has been a dramatic increase in the frequency of fungal infections, especially disseminated systemic mycoses in immunocompromised patients (Cox and Perfect, Curr. Opin. Infect. Dis. 6:422-426 [1993]; and Fox, ASM News 59:515-518 [1993]). Human pathogenic fungi of particular importance include: Candida sp. (C. albicans, C.
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glabrata, C. krusei and C. parapsilosis), Aspergillus fumigatus, and Cryptococcus neoformans. C. albicans and A. fumigatus cause most opportunistic mycoses. At present, treatments for fungal infections are limited to few options. Amphotericin B (a polyene) is fungicidal, but is toxic to humans. Azoles (fluconazole, itraconazole, and others) are safer than amphotericin B, but are only fungistatic. In addition, resistance to azoles has become a major clinical concern. Some azoles (Sheehan, Clin. Microbiol. Rev. 12:40-79 [1999]) and a new class of (1,3).beta.-glucan synthase inhibitors, echinocandins (Denning, J. Antimicrob. Chemother. 40:611-614 [1997]), are now in clinical and preclinical trials. Recently, the FDA approved caspofungin, a (1,3).beta.-glucan synthase inhibitor, as a "salvage treatment" for aspergillosis. In spite of the new azoles and the (1,3).beta.-glucan synthase inhibitors, new classes of antifungal drugs are needed for therapy of infections caused by drug-resistant mutants (and species) or for preventing the emergence of drug-resistant mutants. Fungal organisms have become increasingly significant pathogens in immunocompromised patients, especially those who because of cancer, organ transplantation, chemotherapy, pregnancy, age, diabetes, complications following extensive surgery, and various immune system dysfunctions, are at risk of experiencing life-threatening diseases caused by microorganisms which do not ordinarily pose a threat to normal, immunocompetent people. Other risk factors for deeply invasive fungal infections include protracted treatment using broad spectrum antimicrobials, corticosteroids, and vascular catheters. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Methods for treating joint inflammation, pain, and loss of mobility Inventor(s): Cherukuri, Reddy Sastry V.; (Folsom, CA), Cheruvanky, Rukmini; (Folsom, CA), Mazhar, Mohammed; (El Dorado Hills, CA), McPeak, Patricia; (El Dorado Hills, CA) Correspondence: Townsend And Townsend And Crew, Llp; Two Embarcadero Center; Eighth Floor; San Francisco; CA; 94111-3834; US Patent Application Number: 20030118672 Date filed: November 6, 2001 Abstract: This invention provides methods and formulations for treating an inflammatory disease or reducing an inflammatory reaction comprising administering a fortified formulation comprising stabilized rice bran derivative and a fortification agent. Preferred rice bran derivatives are rice bran oil and the solubilized fraction of rice bran. Preferred fortification agents are glucosamine derivative, methylsulfonylmethane, yucca concentrate, and grape seed extract. Excerpt(s): This application claims priority to U.S. Application Serial No. 60/307,588, filed Jul. 23, 2001, the disclosure of which is incorporated herein by reference in its entirety for all purposes. This invention relates to fortified formulations and methods for using such formulations for treating joint inflammation, pain, and loss of mobility. Joint disorders and injuries are widespread, can cause considerable discomfort, and cost billions of dollars in lost days of work. Symptoms of these diseases and injuries include inflammation, lameness, loss of mobility, and pain. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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N-acetyl-D-glucosamine and process for producing N-acetyl-D-glucosamine Inventor(s): Anderson, Todd Bryan; (Oskaloosa, IA), Bohlmann, John Andrew; (Ottumwa, IA), Henning, Joseph P.; (Eddyville, IA), Hwang, Ki-Oh; (Oskaloosa, IA), Schisler, David O.; (Oskaloosa, IA), Steinke, James Donald; (Oskaloosa, IA), Trinkle, James R.; (Bussey, IA), Vanderhoff, Andrea; (Pella, IA) Correspondence: Merchant & Gould PC; P.O. Box 2903; Minneapolis; MN; 55402-0903; US Patent Application Number: 20030073666 Date filed: August 8, 2001 Abstract: The present invention is directed to N-acetyl-D-glucosamine obtained from microbial biomass, and to methods of obtaining N-acetyl-D-glucosamine from microbial biomass. In particular, the present invention is directed to the use of fungal biomass to create N-acetyl-D-glucosamine. The N-acetyl-D-glucosamine is efficiently obtained at high purity by degrading chitin in the fungal biomass to create N-acetyl-D-glucosamine. Excerpt(s): The present invention is directed to N-Acetyl-D-Glucosamine and methods of making N-Acetyl-D-Glucosamine. Chitin is typically an amorphous solid that is largely insoluble in water, dilute acids, and alkali. Although chitin has many uses, it can also be degraded to form other useful materials, such as carbohydrates, one of which is the amino sugar N-acetyl-D-glucosamine (NAG). N-acetyl-D-glucosamine typically includes a single glucosamine unit, but can also include small amounts of short oligomers, such as chitobiose or chitotriose, that have two and three glucosamine units, respectively. N-acetyl-D-glucosamine can be used for various applications, including as a food additive and in pharmaceutical compositions. The most common source of chitin for use in making N-acetyl-D-glucosamine is shellfish (such as shrimp) biomass. Unfortunately, limitations exist with the recovery of N-acetyl-D-glucosamine from shellfish biomass. One problem with recovering N-acetyl-D-glucosamine from shellfish is that it is very difficult to obtain uniform shellfish biomass. The uniformity problems occur in part because shellfish often vary by size, age, and species; are grown under varied environmental conditions; and are gathered from diverse locations. This lack of uniformity makes it difficult to precisely process shellfish biomass. In addition, some quality control issues can arise due to the fact that N-acetyl-D-glucosamine obtained from crustacea can have a high ash content and can contain heavy metals that are concentrated in the crustacea from their aquatic environment. A further problem with N-acetyl-D-glucosamine derived from harvested crustacea is that it has the potential to include undesired proteins and allergens. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Neutrophil function inhibitors Inventor(s): Nagaoka, Isao; (Yokohama-shi, JP), Sakamoto, Koji; (Fujioka-shi, JP) Correspondence: Oblon Spivak Mcclelland Maier & Neustadt PC; Fourth Floor; 1755 Jefferson Davis Highway; Arlington; VA; 22202; US Patent Application Number: 20020128230 Date filed: July 18, 2001 Abstract: Glucosamine salts are effective for the inhibition of neutrophil functions, and hence, are useful for the prevention and/or treatment of diseases, caused as a result of
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an excessive extracellular release of active oxygen and antibiotic proteins by neutrophils, such as respiratory disease syndrome and adult respiratory disease syndrome. Use of glucosamine salts can, therefore, provide neutrophil function inhibitors, preventives and/or remedies for diseases caused as a result of an excessive extracellular release of active oxygen and antibiotic proteins by neutrophils, and also methods for the prevention and/or treatment of such diseases. Excerpt(s): This invention relates to inhibitors of neutrophil functions (hereinafter called "neutrophil function inhibitors"), each of which comprises a glucosamine salt as an active ingredient. These neutrophil function inhibitors are useful as drugs, drinks, foods or the like for the prevention or treatment of troubles caused by exaltation of neutrophil functions, for example, respiratory disease syndrome (RDS), adult respiratory disease syndrome (ARDS) and other neutrophil-associated inflammations. A neutrophil is principal one of granules in a leukocyte. When an exogenous substance such as bacteria invades a living body, neutrophils emigrate to the invaded site, ingest the exogenous substance, have active oxygen generated and at the same time, antibiotic proteins (granules) such as lysozyme and defensins released, and play an important role to expel the exogenous substance under the action of the antibiotic proteins and also under the action of various acid hydrolases. However, an excessive extracellular release of these active oxygen and antibiotic proteins causes destruction of a tissue, and in some instances, further aggravates an acute inflammation occurred by the invasion of the exogenous substance. In the case of certain specific diseases such as respiratory distress syndrome, adult respiratory distress syndrome and other neutrophil-associated inflammations, this action of neutrophils is known to give adverse effects on these diseases. Glucosamine salts, especially the sulfate or the hydrochloride have been produced, for example, by the process disclosed in JP1-28757 B or U.S. Pat. No. 3,683,076. U.S. Pat. No. 3,683,076 also discloses that glucosamine salts in the form of capsules or tablets are used as arthritis remedies and the like. However, absolutely nothing is known about effects of glucosamine salts on leukocytes. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Nucleotide-sugar-synthesizing enzymes from nonparasitic protists Inventor(s): Elling, Lothar; (Aachen, DE), Kiy, Thomas; (Frankfurt, DE), Kula, Maria Regina; (Niederzier-Hambach, DE) Correspondence: Frommer Lawrence & Haug; 745 Fifth Avenue- 10th FL.; New York; NY; 10151; US Patent Application Number: 20030207433 Date filed: May 12, 2003 Abstract: The present invention relates to nucleotide-sugar-synthesizing enzymes (enzymes with nucleotidyltransferase or pyrophosphorylase activity) from nonparasitic protists, to a process for the preparation thereof and to the use thereof for preparing nucleotide-sugars. The enzymes according to the invention make possible or greatly simplify the enzymatic preparation of various nucleotide-sugars on the industrial scale from low-cost precursors. It is possible with the aid of the discovered enzymes to prepare, for example, GDP-fucose, GDP-mannose, UDP-glucose, UDP-glucosamine, UDP-galactose, UDP-galactosamine, UDP-N-acetylglucosamine and UDP-Nacetylgalactosamine in economic quantities.
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Excerpt(s): The present invention relates to nucleotide-sugar-synthesizing enzymes, i.e. enzymes with nucleotidyltransferase or pyrophosphorylase activity, from nonparasitic protists, to a process for the preparation thereof and to the use thereof for preparing nucleotide-sugars. Oligo- and polysaccharides play an important part in nature. They are of essential importance as components of glycoproteins and glycolipids in cellular communication processes and as binding sites for, for example, antibodies, lectins and hormones. They also crucially determine the physical properties of proteins such as solubility, stability and 3D structure. They furthermore act as receptors for pathological states mediated by viruses, bacteria and protists. The recognition of the versatile functions of the carbohydrate residues in glycoconjugates is also associated with an increasing interest in synthesizing such compounds. However, because of their great complexity and the specific requirements for chemoselectivity, regioselectivity and stereoselectivity, the synthesis even of lower oligosaccharides by chemical means is extremely difficult. As the complexity of the saccharides increases there is also an increase in the difficulty of reproducing them by chemical synthesis. For this reason it is obvious to copy the biological synthetic routes and to have recourse to enzymes, which usually catalyze substrate-, regio- and stereospecific reactions, for synthesizing complex saccharides. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Nutraceutical solutions comprising dimethyl sulfoxide Inventor(s): Kretschmer, Louis Frank; (Olympia, WA) Correspondence: Louis Frank Kretschmer M.D.; 405a Black Hills LN S.W.; Olympia; WA; 98502; US Patent Application Number: 20030109495 Date filed: August 23, 2002 Abstract: A unique topical treatment for diseases of joints and soft tissues with a proven scientific basis. The carrying agent is DMSO or (dimethyl sulfoxide) in purified form. This has ability to carry molecules of molecular weight 1000 Daltons or less through the skin. DMSO is also a proven anti-inflammatory for the treatment of joint and soft tissue diseases. By adjusting the acidity one can prepare a unique stable topical gel containing 5% glucosamine (molecular weight 200 Daltons) for the treatment of joint and ligament diseases. By adding 5% MSM we include a powerful anti-oxidant of sufficient low molecular weight to also be delivered through the skin. No other topical application presently available for the treatment of joint and soft tissue disorders can make such claims with scientific fact. No other topical can claim glucosamine, MSM, an antiinflammatory and anti-oxidant in sufficient concentrations through the skin to have a beneficial affect on joints and soft tissues. Excerpt(s): This invention involves the topical application of nutraceuticals with dimethyl sulfoxide (DMSO) as a carrying agent. DMSO was founded by my close friend Dr. Stanley Jacob at the University of Oregon Medical School which I attended. Its unique agent for low molecular weight compounds is unparalleled. Now we have medical grade DMSO that does not posses the unpleasant garlic taste and smell of previous impure preparations. U.S. Pat. No. 3,549,720 as well as personal communication with Dr. Jacob confirms nutraceuticals (not pharmaceuticals) effectively treat tissue damage, arthritis pain, muscle pain. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Nutritional composition for the treatment of connective tissue Inventor(s): Petito, Anita M.; (Bethlehem, PA), Petito, George D.; (Bethlehem, PA) Correspondence: Richard C. Litman; Crystal City Station; P.O. Box 15035; Arlington; VA; 22215-0035; US Patent Application Number: 20030069171 Date filed: November 5, 2002 Abstract: A nutritional composition for the treatment of connective tissue in mammals which includes a glucosamine salt, chondroitin sulfate, collagen and sodium hyaluronate which synergistically act as a chondroprotective agent. The composition can further include a detoxifying agent, an anti-inflammatory agent or an analgesic to demonstrate additional therapeutic and physiologic properties. The nutritional composition acts as a chondro-protective agent which provides foundational support for the creation of new body tissue and cartilage growth in humans and animals. Excerpt(s): This application is a continuation-in-part of application Ser. No. 09/360,169 filed Jul. 26, 1999, which is a continuation-in-part of application Ser. No. 09/046,710 filed Mar. 24, 1998, and now abandoned. The present invention relates to therapeutic compositions which provide for the treatment of connective tissue in mammals and, more particularly to nutritional compositions capable of acting as chondroprotective agents, as well as exhibiting added pharmacological properties. The related art of interest discloses numerous pharmaceutical compositions and methods for the treatment of connective tissue in humans and animals. For example, U.S. Pat. No. 4,837,024 issued on Jun. 6, 1989, to Dov Michaeli describes topical compositions for improving wound healing comprising a suspension of particles of collagen and a glycosaminoglycan. The composition is taught to be useful for treating surface wounds by applying the composition to a gauze, bandage or the like. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Patch for the delivery of topical agents Inventor(s): Hayes, Harry; (Hampden, MA), Young, Tyler F.; (Hampden, MA) Correspondence: Kevin H. Vanderleeden; Mccormick, Paulding & Huber Llp; 185 Asylum Street, Cityplace II; Hartford; CT; 06103; US Patent Application Number: 20030180347 Date filed: March 13, 2003 Abstract: The adhesive patch for the delivery of topical agents to the skin including a polymer matrix, generally a hydrogel matrix having adhesive properties, a skin conditioner and a penetration enhancer. The hydrogel matrix including purified water, glycerin, polyacylate, sorbitol, kaolin, CMC (carboxymethyl cellulose), alcohol, castor oil, TWEEN 80 (polyoxyethylene sorbitan monooleate), fragrance and citric acid. Skin conditioners and penetration enhancers including methyl sulfonyl methane, glucosamine and chondroitin. The matrix may also include a topically effective drug. The adhesive patch includes a support backing of non-woven material or a nonocclusive film and a protective film covering the polymer matrix. Excerpt(s): This application claims the benefit of U.S. Provisional Application Serial No. 60/365,193, filed on Mar. 19, 2002. The present invention relates to a patch for the delivery of topical agents to the skin. In particular, the present invention involves a
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patch that utilizes a polymer matrix containing an adhesive, a skin conditioner, a penetration enhancer, and, optionally, a topically effective drug. The polymer matrix facilitates the slow diffusion of the topical agents' active ingredients over a period of time. Additionally, the polymer matrix provides adhesion such that the topical agents are kept in contact with the skin for a period of time sufficient for the agents to be effective. The delivery of topical agents to the skin may be desirable to improve the health and appearance of skin and alleviate conditions such as psoriasis, dry skin, blemishes, abrasions, cuts, or rashes. If such skin conditions are not treated, further damage may occur leading to infections and other maladies. Additionally, the treatment of chronic or acute pain often involves the topical application of an anesthetic such as lidocaine or benzocaine. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
PROCESS FOR PRODUCTION OF N-GLUCOSAMINE Inventor(s): BERRY, ALAN; (BLOOMFIELD, NJ), BURLINGAME, RICHARD P.; (MANITOWOC, WI), MILLIS, JAMES R.; (KOHLER, WI) Correspondence: Sheridan Ross PC; 1560 Broadway; Suite 1200; Denver; CO; 80202 Patent Application Number: 20020160459 Date filed: September 15, 1999 Abstract: The present invention relates to a method for producing N-glucosamine by fermentation of a genetically modified microorganism. Excerpt(s): The present invention relates to a method for producing N-glucosamine by fermentation. The present invention also relates to genetically modified strains of microorganisms useful for producing N-glucosamine. Amino sugars are usually found as monomer residues in complex oligosaccharides and polysaccharides. N-glucosamine is an amino derivative of the simple sugar, glucose. N-glucosamine and other amino sugars are important constituents of many natural polysaccharides. For example, polysaccharides containing amino sugars can form structural materials for cells, analogous to structural proteins. N-glucosamine is manufactured as a nutraceutical product with applications in the treatment of osteoarthritic conditions in animals and humans. The market for N-glucosamine is experiencing tremendous growth. Furthermore, significant erosion of the world market price for N-glucosamine is not expected. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Self-assembled thin film coating to enhance biocompatibility of materials Inventor(s): Claus, Richard O; (Blacksburg, VA), Spillman, William B JR.; (Floyd, VA), Wang, You-Xiong; (Blacksburg, VA) Correspondence: Dewitt Ross & Stevens; Intellectual Property Department; Suite 401; 8000 Excelsior Drive; Madison; WI; 53717-1914; US Patent Application Number: 20030211129 Date filed: October 14, 2002 Abstract: We make a substrate biocompatible by contacting it with a starting material and initiating alternating charge layer electrostatic self assembly to form a thin film.
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Starting materials may be poly(vinylpyrrolidone), poly{bis(carboxylatophenoxy)phosphazene}, poly(methacrylic acid), poly(l)-lysine, poly(ethylene glycol), poly(D-glucosamine), poly(l-glutamic acid), poly(diallyldimethylamine), poly(ethylenimine), hydroxy fullerene, long-sidechain fullerene, or other polymers that participate in electrostatic self-assembly. The thin film fabrication advantageously may be at room temperature. A biocompatible thin film that is uniform and homogeneous can be provided. Optionally, ZrO.sub.2, Al.sub.2O.sub.3 or TiO.sub.2 nanoclusters also may be used in the film assembly. The film may be used in a drug delivery device or a medical device. The film may be used for tissue engineering. We also provide a biocompatible composition in which are present a plurality of layers electrostatically self-assembled from at least a polymer or fullerene asmentioned. The substrate is not particulary limited, and may be quartz, glass, plastic, metal or ceramic, a material for a bone implant, bioactive glass, polyester or other polymers, plastic or rubber tubing, bandaging material, composite material, insulator material, semi-conductor material, an artificial hip, a pacemaker, a catheter, a stent or other substrates. Excerpt(s): This application claims priority based on U.S. application 60/197,776 filed Apr. 14, 2000. The invention generally relates to biocompatible materials, and more particularly, to making a substrate biocompatible and constructing biocompatible thin films by electrostatic self-assembly. Medical and pharmaceutical technologies have developed over the years to the point that many medical conditions are treated by implanting or otherwise putting into the body a foreign object that is not naturally occurring in the body. For example, medical devices and objects made of plastic, rubber, metal, composite materials, insulator materials, semi-conductor materials or other materials are implanted to perform a particular function. Tubing used in dialysis, tubing used in heart lung machines, stents, bandaging material, artificial hips and other joints, pacemakers and catheters are examples of such internally-implanted foreign objects. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Synergistic proteoglycan compositions for treatment of inflammatory diseases Inventor(s): Theoharides, Theoharis C.; (Brookline, MA) Correspondence: Melvin Blecher, PH.D. J.D.; Attorney AT Law; 4329 Van Ness Street, N.W.; Washington; DC; 20016-5625; US Patent Application Number: 20020176902 Date filed: January 30, 2001 Abstract: Compositions with synergistic anti-inflammatory effect in inflammatory diseases resulting from activation and consequent degranulation of mast cell and followed by secretion of inflammatory biomolecules from the activated mast cells, composed of a heavily sulfated, non-bovine proteoglycan such as chondroitin sulfate C and one or more of a hexosamine sulfate such as D-glucosamine sulfate, a flavone such as quercetin, a special organic extra virgin kernel seed olive oil, S-adenosylmethionine and diphenhydramine. Excerpt(s): The invention is generally related to the treatment of inflammatory conditions. More specifically, the invention is related to compositions containing inhibitors of mast cell activation and secretion designed to be used as dietary supplement in the treatment of inflammatory conditions. There have been a number of mostly anecdotal reports that the proteoglycan chondroitin sulfate, as well as
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glucosamine sulfate, a product of the intestinal breakdown of proteoglycans may be helpful in relieving the pain of osteoarthritis:--Shute N. Aching for an arthritis cure. US News and World Report, Feb. 10, 1997.--Cowley G. The arthritis cure? Newsweek, Feb. 17, 1997.--Foreman J. People, and their pets, tout arthritis remedy. The Boston Globe, Apr. 7, 1997; Tye L. Treatment gains scientific attention. The Boston Globe, Sep. 25, 2000. A recent meta-analysis showed potential therapeutic benefit of chondroitin sulfate in osteoarthritis [McAlindon et al. J Am Med Assn. 283:1469 (2000), and NIH-funded clinical trial OD-98-003 dated Oct. 10, 1997]. However, less than 5% of the chondroitin sulfate in available preparations is absorbed orally. Furthermore, such commercial preparations use chondroitin sulfate obtained from cow trachea, with the possible danger of contracting "mad cow disease" [McAlindon et al. above]. In fact, the European Union has banned even cosmetics that contain bovine-derived products. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Topical agent for dermatological use Inventor(s): Kuriki, Takashi; (Osaka, JP), Nakae, Takashi; (Hyogo, JP), Nakayama, Hiroki; (Tokyo, JP), Nishimura, Takahisa; (Nara, JP) Correspondence: Pennie And Edmonds; 1155 Avenue OF The Americas; New York; NY; 100362711 Patent Application Number: 20030198610 Date filed: June 4, 2003 Abstract: The objetive of the present invention was to enhance the skin whitening effects and blackening prevention effects and supply safe and stable topical agents for dermatological use. For that purpose 4-Hydroxyphenyl-.alpha.-D-glucopyranoside was combined with auxiliary agents such as ascorbic acid and its derivatives, crude drugs and its extracts, hydroxycarboxylic acid and its salts, oil soluble glycyrrhiza extract, gentian extract, phenol derivatives and their salts, placenta extract, kojic acid and its derivative, glucosamine and its derivatives, azelaic acid and its derivatives, retinol and its derivatives, pyridoxin and its derivatives, tocopherol and its derivatives, chitosan and its decomposition products, caffeic acid derivatives, hydroxycinnamate and its derivatives, Umbelliferae plant extracts, mycelial cultures and their extracts, plant leaves and their extracts. Excerpt(s): The present invention is related to topical agents for dermatological use which whiten the skin color or prevent its blackening and prevent or relieve liver spots, freckles, etc. and which show generally desirable formulation properties in terms of the safety and stability. Various melanin formation preventing agents have been used to whiten the skin color or prevent its blackening and prevent or relieve skin troubles such as liver spots and freckles caused due to excessive exposure to UV rays. These agents include 1,4-dihydroxybenzene,.beta.-arbutin, vitamin C and its derivatives, and kojic acid. However, vitamin C, 1,4-dihydroxybenzene and kojic acid are extremely unstable with respect to heat and oxidation in water. When added to topical agents for dermatological use, therefore, these compounds decompose over time and cause coloration. Their derivatives, such as phosphate-ascorbyl magnesium and.beta.-arbutin, which is obtained as a result of the.beta.-binding of glucose to one of the hydroxy groups of 1,4-dihydroxybenzene, are not necessa-rily satisfactory in terms of efficacy although they are more stable than their parent compounds with respect to heat and oxidation.
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Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Topical composition for the treatment of psoriasis and related skin disorders Inventor(s): Meisner, Lorraine Faxon; (Madison, WI) Correspondence: Gardere Wynne Sewell Llp; Thanksgiving Tower; Suite 3000; 1601 Elm Street; Dallas; TX; 75201; US Patent Application Number: 20020164386 Date filed: June 28, 2002 Abstract: Compositions and methods of use thereof for the treatment of psoriasis and related skin ailments are disclosed. The compositions include topical skin formulations of glucosamine in an emollient base such as moisturizing cream. In addition to glucosamine, the formulations may include keratolytic substances such as coal tar extract or salicylic acid. The formulations may also include glucosamine and antioxidant anti-inflammatory herbal extracts such as oleuropein and berberine in an emollient base. Excerpt(s): The present invention relates in general to the field of the treatment of psoriasis and related skin disorders, and more particularly to a non-toxic topical formulation that includes antioxidants and a pharmaceutically effective amount of an herbal extract for the treatment of psoriasis and related skin ailments. Without limiting the scope of the invention, its background is described in connection with disorders of the skin and, more particularly, to the general field of diseases that cause psoriasis, as an example. Psoriasis is a common skin disease characterized by hyperplasia of keratinocytes resulting in thickening of the epidermis and the presence of red scaly plaques. The lesions in this chronic disease typically are subject to remissions and exacerbations. There are several patterns, of which plaque psoriasis is the most common. Guttate psoriasis, with raindrop shaped lesions scattered on the trunk and limbs, is the most frequent form in children, while pustular psoriasis is usually localized to the palms and soles. The classical inflammatory lesions vary from discrete erythematous papules and plaques covered with silvery scales, to scaly itching patches that bleed when the scales are removed. Despite a voluminous scientific literature and numerous treatment strategies, there is still no effective treatment for psoriasis that is completely without side effects. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
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Transdermal formulation for repair and maintenance of connective tissue Inventor(s): Kucharchuk, Andrew; (Baton Rouge, LA) Correspondence: Thomas S. Keaty; Keaty Professional Law CORP.; 2140 World Trade Center; NO. 2 Canal Street; New Orleans; LA; 70130; US Patent Application Number: 20030125303 Date filed: December 28, 2001 Abstract: The invention describes composition and method for treatment of arthritis. The composition uses glucosamine or its salts admixed with ascorbic acid, menthol, and niacin in a cream base to form a topical agent. The method of treatment of arthritis
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provides for topical application of the mixed compound to the skin of the user adjacent to the inflamed or injured joint. Excerpt(s): This invention relates to the use of therapeutic compositions containing glucosamine for the repair of human connective tissue, and to the transdermal formulation for treatment of the connective tissue. Inflammatory conditions of a joint afflict and disable millions of people worldwide. A person afflicted with such chronic disease suffers from degeneration of the cartilage, the connective tissue, which cushions moveable joints. Damage to the joint cartilage is oftentimes referred as arthritis or osteoarthritis. Osteoarthritis is diagnosed when synovial joints suffer pathological changes. The cartilage and bone are slowly eroded away by reactive proliferation of bone and cartilage around the joint. Osteoarthritis is a cell-mediated active process that may result from an inappropriate response of chondrocytes to catabolic and anabolic penalytes. The clinical manifestations include pain, tenderness, swelling and loss of function of affected joints, morning stiffness, and loss of cartilage, erosion of bone matter and subluxation of joints if the conditions are left untreated. These conditions may immobilize the patient or at least severely restrict the patient's movement. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Treating arthritis in animals with dietary supplements Inventor(s): Myers, Andrew; (Boise, ID) Correspondence: Pedersen & Company, Pllc; P.O. Box 2666; Boise; ID; 83701; US Patent Application Number: 20030147971 Date filed: November 18, 2002 Abstract: The invention is a dietary supplement for animals, especially dogs, for treating arthritis and joint discomfort. A biscuit form of the supplement may be in the form of a conventional carrier composition of, for example, typical dog biscuit materials including cereal grains, vegetables or animal meat, fat and by-products. Typically, the biscuit contains about 89-97 weight percent (wt. %) of the conventional carrier composition. Optional vitamins and minerals may also be added to the carrier material, typically in about the 1-5 wt. % range. Importantly, the biscuit of the present invention contains about 3-7 wt. % of an arthritis-treating combination, namely, glucosamine sulfate, vitamin C and an array of intracellular ions namely potassium, sodium and iodine. The glucosamine component is present by weight at approximately the same level as the vitamin C, and at approximately 10 (ten) times the level of the sum of the above-named intracellular ions. The biscuit is formulated so that its composition is approximately:Glucosamine component, 5 mg to 5,000 mg;Vitamin C component, 5 mg to 3,000 mg;Potassium component, 50 mcg to 150 mg;Sodium component, 50 mcg to 150 mg; andIodine component, 25 mcg to 100 mg.The biscuit is dosed at approximately 10 mg glucosamine component per pound of body weight of the animal per day. Excerpt(s): This application is a continuation application of, and claims priority from, U.S. patent application Ser. No. 09/642,112, filed on Aug. 18, 2000, entitled "Treating Arthritis in Animals with Dietary Supplements", which application claims priority from Provisional Patent Application No. 60/149,779, filed Aug. 18, 1999, and which applications are hereby, incorporated by reference. This invention relates generally to animals and animal nutrition. More specifically, this invention relates to treating arthritis and joint discomfort in dogs by use of dietary supplements. Degenerative joint diseases or arthroses are conditions where degenerative changes in cartilage lead to a
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breakdown in the integrity of the structural matrix of cartilage or tendinous tissues. Conventionally referred to as arthritis, the complaints associated with the degenerative changes occur most frequently in aged individuals. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
UDP-galactose: beta-N-acetyl-glucosamine beta-1,4-galactosyltransferase, beta4GalT2 Inventor(s): Bennett, Eric Paul; (Lyngby, DK), Clausen, Henrik; (Holte, DK) Correspondence: Darby & Darby P.C.; Post Office Box 5257; New York; NY; 10150-5257; US Patent Application Number: 20030013173 Date filed: April 24, 2002 Abstract: A novel gene defining a novel enzyme in the UDP-D-galactose: b-N-acetylglucosamine.beta.-1,4-galactosyltransferase family, termed.beta.4Gal-T2, with unique enzymatic properties is disclosed. The enzymatic activity of.beta.4Gal-T2 is shown to be distinct from that of previously identified enzymes of this gene family. The invention discloses isolated DNA molecules and DNA constructs encoding.beta.4Gal-T2 and derivatives thereof by way of amino acid deletion, substitution or insertion exhibiting.beta.4Gal-T2 activity, as well as cloning and expression vectors including such DNA, cells transfected with the vectors, and recombinant methods for providing.beta.4Gal-T2. The enzyme.beta.4Gal-T2 and.beta.4Gal-T2-active derivatives thereof are disclosed, in particular soluble derivatives comprising the catalytically active domain of.beta.4Gal-T2. Further, the invention discloses methods of obtaining.beta.-1,4galactosyl glycosylated saccharides, glycopeptides or glycoproteins by use of an enzymically active.beta.4Gal-T2 protein or fusion protein thereof or by using cells stably transfected with a vector including DNA encoding an enzymatically active.beta.4Gal-T2 protein as an expression system for recombinant production of such glycopeptides or glycoproteins. Also a method for the identification of DNA sequence variations in the.beta.4Gal-T2 gene by isolating DNA from a patient, amplifying.beta.4Gal-T2-coding exons by PCR, and detecting the presence of DNA sequence variation, are disclosed. Excerpt(s): The present invention relates generally to the biosynthesis of glycans found as free oligosaccharides or covalently bound to proteins and glycosphingolipids. This invention is more particularly related to a family of nucleic acids encoding UDP-Dgalactose:.beta.-N-acetylglucosamine.beta.-1,4-galactosyltransferases (.beta.4Galtransferases), which add galactose to the hydroxy group at carbon 4 of 2-acetamido-2deoxy-D-gluco- se (GlcNAc). This invention is more particularly related to a gene encoding the second member of the family of.beta.4Gal-transferases, termed.beta.4GalT2, probes to the DNA encoding.beta.4Gal-T2, DNA constructs comprising DNA encoding.beta.4Gal-T2, recombinant plasmids and recombinant methods for producing.beta.4Gal-T2, recombinant methods for stably transfecting cells for expression of.beta.4Gal-T2, and methods for identification of DNA polymorphism in patients. The UDP-galactose:.beta.-N-acetyl-glucosamine.beta.-1,4-galactosyltransferase (.beta.4Gal-T1) was the first animal glycosyltransferase to be isolated and cloned (Narimatsu et al., 1986; Shaper et al., 1986; Nakazawa et al., 1988; Shaper et al., 1988; D'Agostaro et al., 1989), and early searches for homologous genes by low stringency Southern hybridisation suggested that this gene was unique. Characterisation of.beta.4Gal-transferase activities from different sources, however, indicate that distinct activities exist (Sheares and Carlson, 1984; Furukawa et al., 1990). Emerging evidence
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now reveal that several b4galactosyltransferase genes may exist. Shaper and colleagues (Shaper et al., 1995) have identified two different chick cDNA sequences, which have 65% and 48% sequence similarity to human.beta.4Gal-T1. Both chick cDNAs were shown to encode catalytically active b4Gal-transferases (Shaper et al., 1997). Two independent groups have analysed.beta.4Gal-transferase activities in mice homozygously deficient for.beta.4Gal-T1 (Asano et al., 1997; Lu et al., 1997). Both studies showed residual.beta.4Gal-transferase activity, providing clear evidence for the existence of additional.beta.4Gal-transferases. Thus, the.beta.4Gal-T1 gene is likely to be part of a homologous gene family with recognisable sequence motifs, and this is supported by a large number of human ESTs with sequence similarities to.beta.4Gal-T1 in EST databases (National Center for Biotechnology Information).beta.-1,4Galactosyltransferase activities add galactose to different acceptor substrates including free oligosaccharides, N- and O-linked glycoproteins, and glycosphingolipids (Kobata, 1992). In addition,.beta.4Gal-T1 is modulated by a-lactalbumin to function as lactose synthase and hence has a major role in lactation (Brew et al., 1968). Given the diverse functions of.beta.-1,4-galactosyltransferase activities and the evidence that multiple b4Gal-transferases exist, it is likely that these enzymes may have different kinetic properties. Furukawa et al. (Furukawa et al., 1990) showed that liver.beta.4Galtransferase activity was near 20-fold higher with asialo-agalacto-transferrin compared to asialo-agalacto-IgG, whereas the activity found in T and B cells only showed a 4 to 5fold difference with the two substrates. The.beta.4Gal-transferase activity in B cells of rheumatoid arthritis patients appear to be similar to B cells from healthy controls with several substrates including asialo-agalacto-transferrin (Furukawa et al., 1990) and.beta.GlcNAc-pITC-BSA (Keusch et al., 1995), but different with asialo-agalacto-IgG (Furukawa et al., 1990). Furthermore, the Km for UDP-Gal of.beta.4Gal-transferase activity from B cells of rheumatoid arthritis patients were 2-fold higher (35.6 mM) than normal B cells (17.6 mM) (Furukawa et al., 1990). Finally, the activity in B cells for asialoagalacto-transferrin was more sensitive to a-lactalbumin inhibition than the activity with asialo-agalacto-IgG. A number of studies have concluded that there was no change in.beta.4Gal-transferase activity in B cells of rheumatoid arthritis patients (Wilson et al., 1993; Axford et al., 1994). However, if multiple.beta.4Gal-transferases exist, it is possible that the contradictory findings of Furukawa et al. (Furukawa et al., 1990) can be explained by a model with two.beta.4Gal-transferases with different kinetic parameters expressed in normal B cells, and a selective down regulation of one in B cells of rheumatoid arthritis patients. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html •
Use of vegetable butter-based cetyl myristoleate for treating osteoarthritis and other musculoskeletal disease conditions and injuries Inventor(s): Leonard, Edward C.; (Memphis, TN), Simonton, Dori; (Broken Bow, NE) Correspondence: H. Roy Berkenstock; Garvey, Smith, Nehrbass & Doody, L.L.C.; 3838 N. Causeway BLVD., STE. 3290; Metairie; LA; 70002; US Patent Application Number: 20030181521 Date filed: March 21, 2002 Abstract: A vegetable butter based dietary supplement of cetyl myristoleate for use in the treatment of osteoarthritis and other joint inflammatory diseases of the musculoskeletal system in animals, especially equines. In its preferred form, the cetyl myristoleate is a vegetable butter-based and is administered in doses of about 4000 to
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about 4500 mg. The dosage may also include 3000 mg methylsulfonylmethane, 3000 mg glucosamine HCL and 1000 mg of Vitamin C. Excerpt(s): The present invention relates to the dietary supplement, cetyl myristoleate. More particularly, the present invention relates to the use of cetyl myristoleate derived exclusively from vegetable sources as a treatment for osteoarthritis and other inflammatory diseases of the musculoskeletal system in animals, specifically equines. In addition, the present invention also relates to the treatment of injuries and stress-related trauma that adversely affect the orthopedic and muscular systems of horses. Nearly 50% of the Western world population over 65 has chronic, painful, disabling arthritis in one form or another of the disease. New prescription drugs, most notably Vioxx.RTM. and Celebrex.RTM. offered for arthritis relief have efficacy for large numbers of patients. Each of these drugs has achieved U.S. sales of billions of dollars in a relatively short time. Unfortunately, these chemically and biologically very powerful drugs have resulted in adverse reactions in a small minority of patients, some of which have been fatal. There are a number of dietary supplements on the market that purport to offer relief for arthritis; glucosamine and chondroitin are examples. Dietary supplements need no prescription. Glucosamine has been on the market for two decades and has achieved annual U.S. sales of more than one hundred million dollars. Web site: http://appft1.uspto.gov/netahtml/PTO/search-bool.html
Keeping Current In order to stay informed about patents and patent applications dealing with glucosamine, you can access the U.S. Patent Office archive via the Internet at the following Web address: http://www.uspto.gov/patft/index.html. You will see two broad options: (1) Issued Patent, and (2) Published Applications. To see a list of issued patents, perform the following steps: Under “Issued Patents,” click “Quick Search.” Then, type “glucosamine” (or synonyms) into the “Term 1” box. After clicking on the search button, scroll down to see the various patents which have been granted to date on glucosamine. You can also use this procedure to view pending patent applications concerning glucosamine. Simply go back to http://www.uspto.gov/patft/index.html. Select “Quick Search” under “Published Applications.” Then proceed with the steps listed above.
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CHAPTER 7. BOOKS ON GLUCOSAMINE Overview This chapter provides bibliographic book references relating to glucosamine. In addition to online booksellers such as www.amazon.com and www.bn.com, excellent sources for book titles on glucosamine include the Combined Health Information Database and the National Library of Medicine. Your local medical library also may have these titles available for loan.
Book Summaries: Federal Agencies The Combined Health Information Database collects various book abstracts from a variety of healthcare institutions and federal agencies. To access these summaries, go directly to the following hyperlink: http://chid.nih.gov/detail/detail.html. You will need to use the “Detailed Search” option. To find book summaries, use the drop boxes at the bottom of the search page where “You may refine your search by.” Select the dates and language you prefer. For the format option, select “Monograph/Book.” Now type “glucosamine” (or synonyms) into the “For these words:” box. You should check back periodically with this database which is updated every three months. The following is a typical result when searching for books on glucosamine: •
Diagnosis and Nonsurgical Management of Osteoarthritis, Second Edition Source: Caddo, OK: Professional Communications, Inc. 2000. 304 p. Contact: Available from Professional Communications, Inc. P.O. Box 10, Caddo, OK 74729. (800) 337-9838. Fax (580) 367-9989. PRICE: $24.95 plus shipping and handling. ISBN 1884735576. Summary: This monograph provides health professionals with information on the diagnosis and nonsurgical management of osteoarthritis (OA). Part 1 presents general information about OA, including its definition, epidemiology (prevalence and risk factors), pathology, and pathogenesis. Part 2 deals with diagnosis, focusing on the clinical features of OA; the origins of joint pain; the pitfalls in diagnosing OA such as misinterpreting pain, the deformity, the radiographs, and the laboratory results; synovial fluid analysis; and the radiographic features of OA. Part 3 examines nonmedicinal therapy for OA pain, including aerobic exercise, range of motion and
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strengthening exercises, joint protection, weight loss, thermal modalities, patellar taping, tidal irrigation of the knee, use of wedged insoles, and patient education. Part 4 discusses the efficacy and adverse effects of systemic pharmacologic therapy, focusing on acetaminophen and nonspecific nonsteroidal antiinflammatory drugs (NSAIDs), NSAIDs that are specific inhibitors of cyclooxygenase-2, and opioids. Part 5 explores local therapies, including rubefacients and capsaicin cream, intraarticular injection of corticosteroids, and intraarticular injection of hyaluronic acid. Part 6 presents a rational strategy for treating OA pain. Part 7 highlights other therapies, including disease modifying drugs such as NSAIDs, heparinoids, tetracyclines, diacerhein, and glucosamine sulfate, as well as surgical intervention. 34 figures, 39 tables, 23 color plates, and numerous references.
Book Summaries: Online Booksellers Commercial Internet-based booksellers, such as Amazon.com and Barnes&Noble.com, offer summaries which have been supplied by each title’s publisher. Some summaries also include customer reviews. Your local bookseller may have access to in-house and commercial databases that index all published books (e.g. Books in Print®). IMPORTANT NOTE: Online booksellers typically produce search results for medical and non-medical books. When searching for “glucosamine” at online booksellers’ Web sites, you may discover non-medical books that use the generic term “glucosamine” (or a synonym) in their titles. The following is indicative of the results you might find when searching for “glucosamine” (sorted alphabetically by title; follow the hyperlink to view more details at Amazon.com): •
All About Glucosamine and Chondroitin by Jack Challem (Editor), Ray Sahelian; ISBN: 0895298945; http://www.amazon.com/exec/obidos/ASIN/0895298945/icongroupinterna
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Glucosamine Sulfate and Chondroitin Sulfate by Rita Elkins (1997); ISBN: 1885670486; http://www.amazon.com/exec/obidos/ASIN/1885670486/icongroupinterna
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Glucosamine Sulfate and Chondroitin Sulfate by Dallas Clouatre; ISBN: 0879838744; http://www.amazon.com/exec/obidos/ASIN/0879838744/icongroupinterna
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Glucosamine: Nature's Arthritis Remedy by Ray Sahelian; ISBN: 0963975528; http://www.amazon.com/exec/obidos/ASIN/0963975528/icongroupinterna
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User's Guide to Glucosamine and Chondroitin: Don't Be a Dummy: Become an Expert on What Glucosamine & Choneroitin Can Do by Victoria Dolby Toews, Victoria Dolby Toews; ISBN: 1591200059; http://www.amazon.com/exec/obidos/ASIN/1591200059/icongroupinterna
Chapters on Glucosamine In order to find chapters that specifically relate to glucosamine, an excellent source of abstracts is the Combined Health Information Database. You will need to limit your search to book chapters and glucosamine using the “Detailed Search” option. Go to the following hyperlink: http://chid.nih.gov/detail/detail.html. To find book chapters, use the drop boxes at the bottom of the search page where “You may refine your search by.” Select the dates and language you prefer, and the format option “Book Chapter.” Type “glucosamine” (or
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synonyms) into the “For these words:” box. The following is a typical result when searching for book chapters on glucosamine: •
Oral Medications Source: in Moldwin, R.M. Interstitial Cystitis Survival Guide: Your Guide to the Latest Treatment Options and Coping Strategies. Oakland, CA: New Harbinger Publications, Inc. 2000. p. 81-112. Contact: Available from Interstitial Cystitis Association. 51 Monroe Street, Suite 1402, Rockville, MD 20850. (800) HELP-ICA or (301) 610-5300. Fax (301) 610-5308. E-mail:
[email protected]. Website: www.ichelp.org. PRICE: $12.00 plus shipping and handling. ISBN: 1572242108. Summary: More than 700,000 Americans have interstitial cystitis (IC), a condition that includes symptoms of recurring bladder pain and discomfort on urination. This chapter on oral medications used to treat IC is from a self care book designed to empower readers by simplifying the diagnostic and treatment process for IC. The primary object of the book is to build a framework for delivering proper care to the IC patient. Oral medications, used alone or in combination with other medications, will improve symptoms in most patients with IC. Patients may still have some symptoms while on oral medications, but they may be improved to the point where they wish to wait before undergoing more invasive therapy. Most of the medications used cause few significant side effects. The author notes that most of the medications discussed in this chapter have been used for many years but for other purposes. Medications and dosages may need to be changed due to side effects or poor responses. The author first discusses medications thought to coat the bladder's surface, including pentosan polysulfate sodium (Elmiron), chondroitin sulfate, and glucosamine. The author then discusses the use of antidepressants (primarily to reduce pain), including amitriptyline (Elavil); selective serotonin reuptake inhibitors (SSRIs); antihistamines, including hydroxyzine (Atarax, Vistaril); cromolyn sodium (Gastrocrom); cimetidine (Tagamet); antiseizure medications, including gabapentin (Neurontin), and carbamazepine (Tegretol); nonsteroidal antiinflammatory drugs (NSAIDs); immunosuppressants, including steroids; muscle relaxants, notably diazepam (Valium); narcotic therapy; urinary anesthetics, including phenazopyridine hydrochloride (Pyridium), atropine sulfate, benzoic acid, hyoscyamine, methenamine, methylene blue, and phenyl salicylate (Urised); anticholinergic therapy; L arginine; calcium channel blockers, including nifedipine (Procardia); and alpha blockers. The author reviews the use of each of these drugs, along with the hypothesis about why they may be of use in IC.
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CHAPTER 8. PERIODICALS AND NEWS ON GLUCOSAMINE Overview In this chapter, we suggest a number of news sources and present various periodicals that cover glucosamine.
News Services and Press Releases One of the simplest ways of tracking press releases on glucosamine is to search the news wires. In the following sample of sources, we will briefly describe how to access each service. These services only post recent news intended for public viewing. PR Newswire To access the PR Newswire archive, simply go to http://www.prnewswire.com/. Select your country. Type “glucosamine” (or synonyms) into the search box. You will automatically receive information on relevant news releases posted within the last 30 days. The search results are shown by order of relevance. Reuters Health The Reuters’ Medical News and Health eLine databases can be very useful in exploring news archives relating to glucosamine. While some of the listed articles are free to view, others are available for purchase for a nominal fee. To access this archive, go to http://www.reutershealth.com/en/index.html and search by “glucosamine” (or synonyms). The following was recently listed in this archive for glucosamine: •
Glucosamine supplements OK for diabetics Source: Reuters Health eLine Date: July 21, 2003
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Glucosamine supplementation does not impair glucose control in type 2 diabetes Source: Reuters Industry Breifing Date: July 21, 2003
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Topical glucosamine/chondroitin cream relieves osteoarthritis knee pain Source: Reuters Industry Breifing Date: April 08, 2003
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Glucosamine supplement may ease knee pain Source: Reuters Health eLine Date: January 28, 2003
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Glucosamine content of OTC products varies widely from label statement Source: Reuters Medical News Date: December 13, 2002
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Glucosamine sulfate treats osteoarthritis in postmenopausal wome Source: Reuters Industry Breifing Date: October 09, 2001
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Glucosamine tops ibuprofen in treatment of TMJ osteoarthritis Source: Reuters Industry Breifing Date: June 20, 2001
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Long-term glucosamine sulfate use appears to modify osteoarthritis Source: Reuters Industry Breifing Date: January 25, 2001
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Glucosamine supplements may promote insulin resistance Source: Reuters Medical News Date: April 19, 2000
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Glucosamine supplements may raise diabetes risk Source: Reuters Health eLine Date: April 18, 2000
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Glucosamine, chondroitin probably efficacious in treating osteoarthritis Source: Reuters Medical News Date: March 15, 2000
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Glucosamine, chondroitin may help arthritis Source: Reuters Health eLine Date: March 14, 2000
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Glucosamine no more effective than placebo for osteoarthritis of the knee Source: Reuters Medical News Date: February 21, 2000
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Glucosamine sulfate reduces osteoarthritis of the knee disease progression Source: Reuters Medical News Date: November 17, 1999
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Glucosamine reduces knee osteoarthritis Source: Reuters Health eLine Date: November 15, 1999
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Glucosamine effective alternative to NSAIDs in treatment of osteoarthritis Source: Reuters Medical News Date: February 12, 1999
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Glucosamine accepted as alternative treatment for osteoarthritis Source: Reuters Medical News Date: February 10, 1999
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The NIH Within MEDLINEplus, the NIH has made an agreement with the New York Times Syndicate, the AP News Service, and Reuters to deliver news that can be browsed by the public. Search news releases at http://www.nlm.nih.gov/medlineplus/alphanews_a.html. MEDLINEplus allows you to browse across an alphabetical index. Or you can search by date at the following Web page: http://www.nlm.nih.gov/medlineplus/newsbydate.html. Often, news items are indexed by MEDLINEplus within its search engine. Business Wire Business Wire is similar to PR Newswire. To access this archive, simply go to http://www.businesswire.com/. You can scan the news by industry category or company name. Market Wire Market Wire is more focused on technology than the other wires. To browse the latest press releases by topic, such as alternative medicine, biotechnology, fitness, healthcare, legal, nutrition, and pharmaceuticals, access Market Wire’s Medical/Health channel at http://www.marketwire.com/mw/release_index?channel=MedicalHealth. Or simply go to Market Wire’s home page at http://www.marketwire.com/mw/home, type “glucosamine” (or synonyms) into the search box, and click on “Search News.” As this service is technology oriented, you may wish to use it when searching for press releases covering diagnostic procedures or tests. Search Engines Medical news is also available in the news sections of commercial Internet search engines. See the health news page at Yahoo (http://dir.yahoo.com/Health/News_and_Media/), or you can use this Web site’s general news search page at http://news.yahoo.com/. Type in “glucosamine” (or synonyms). If you know the name of a company that is relevant to glucosamine, you can go to any stock trading Web site (such as http://www.etrade.com/) and search for the company name there. News items across various news sources are reported on indicated hyperlinks. Google offers a similar service at http://news.google.com/. BBC Covering news from a more European perspective, the British Broadcasting Corporation (BBC) allows the public free access to their news archive located at http://www.bbc.co.uk/. Search by “glucosamine” (or synonyms).
Newsletters on Glucosamine Find newsletters on glucosamine using the Combined Health Information Database (CHID). You will need to use the “Detailed Search” option. To access CHID, go to the following
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hyperlink: http://chid.nih.gov/detail/detail.html. Limit your search to “Newsletter” and “glucosamine.” Go to the bottom of the search page where “You may refine your search by.” Select the dates and language that you prefer. For the format option, select “Newsletter.” Type “glucosamine” (or synonyms) into the “For these words:” box. The following list was generated using the options described above: •
Glucosamine and Chondroitin for Osteoarthritis? Source: Bulletin on the Rheumatic Diseases. 50(7): 1-4. 2001. Contact: Available from Arthritis Foundation. 1330 West Peachtree Street, Atlanta, GA 30309. (800) 268-6942 or (404) 872-7100. Fax (404) 872-9559. Website: www.arthritis.org. Summary: This newsletter provides health professionals and people who have osteoarthritis (OA) with information on the therapeutic effects of glucosamine and chondroitin. The article reviews laboratory studies, placebo controlled clinical trials, comparator trials, and human disease modification studies of glucosamine and chondroitin. Evidence currently supports a modest efficacy for glucosamine and chondroitin in the treatment of OA. The products are safe and could have a role in the management of this disorder. However, further independent studies are needed to confirm findings on efficacy and to determine the clinical applicability of these compounds. In addition, preliminary findings support the idea that glucosamine and chondroitin might have disease modifying effects in OA. Research is needed to confirm these findings and to evaluate the impact of glucosamine and chondroitin on all aspects of OA progression. 1 table and 16 references.
Newsletter Articles Use the Combined Health Information Database, and limit your search criteria to “newsletter articles.” Again, you will need to use the “Detailed Search” option. Go directly to the following hyperlink: http://chid.nih.gov/detail/detail.html. Go to the bottom of the search page where “You may refine your search by.” Select the dates and language that you prefer. For the format option, select “Newsletter Article.” Type “glucosamine” (or synonyms) into the “For these words:” box. You should check back periodically with this database as it is updated every three months. The following is a typical result when searching for newsletter articles on glucosamine: •
Study Finds Glucosamine Doesn't Work Source: Harvard Health Letter. 25(8): 3. June 2000. Contact: Available from Harvard Health Publications, P.O. Box 421073, Palm Coast, FL 32142-1073. (800) 829-9045 or (617) 432-1485. Email:
[email protected]. Summary: This newsletter article provides people who have arthritis with information on a study that assessed the effectiveness of glucosamine in treating osteoarthritis (OA). The study, which was conducted by researchers at the Veterans Affairs Medical Center in Prescott, AZ, involved 98 patients aged 34 to 81 who suffered from OA of the knee for an average of 13 years. The group was randomly split between treatment with a 500 milligram pill of glucosamine sulfate three times a day for 2 months or treatment with a placebo. The participants scored their pain on a visual analog scale. Assessments were conducted at the beginning, middle, and end of the trial. Although both groups showed some improvement in their pain scores, there was little difference between the two. The
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article concludes that the effectiveness of glucosamine may depend on a person's age and degree of arthritis. 1 figure. •
Supplements: Glucosamine for Osteoarthritis Source: Harvard Women's Health Watch. 7(9): 5. May 2000. Contact: Available from Harvard Women's Health Watch. Department SR, P.O. Box 380, Boston, MA 02117. (800) 829-5921. E-mail:
[email protected]. Summary: This newsletter article provides women who have arthritis with information on the supplement glucosamine. This popular nutritional supplement, which is derived from the shells of lobster, shrimp, and crabs, is being promoted for treating osteoarthritis (OA) naturally. Glucosamine occurs naturally in the body and encourages cartilage cells to produce glycosaminoglycans and proteoglycans. Mild and moderate OA cases have generally been treated with nonsteroidal antiinflammatory drugs, but long term use of these medications can cause serious gastrointestinal side effects. Thus, people who have OA are looking for gentler, less expensive ways to treat their pain. Numerous studies conducted in Europe and Asia suggest that glucosamine has promise as a pain reliever. The National Institutes of Health awarded the University of Utah School of Medicine a $6.6 million grant to coordinate the first multicenter, randomized, double blind clinical trial of glucosamine and chondroitin, a companion supplement, in patients with OA of the knee. The 1,000 patients participating in the study will take either glucosamine, chondroitin, a combination of both, or a placebo for 16 weeks and be evaluated monthly for improvement of pain. The article offers suggestions on taking glucosamine safely.
Academic Periodicals covering Glucosamine Numerous periodicals are currently indexed within the National Library of Medicine’s PubMed database that are known to publish articles relating to glucosamine. In addition to these sources, you can search for articles covering glucosamine that have been published by any of the periodicals listed in previous chapters. To find the latest studies published, go to http://www.ncbi.nlm.nih.gov/pubmed, type the name of the periodical into the search box, and click “Go.” If you want complete details about the historical contents of a journal, you can also visit the following Web site: http://www.ncbi.nlm.nih.gov/entrez/jrbrowser.cgi. Here, type in the name of the journal or its abbreviation, and you will receive an index of published articles. At http://locatorplus.gov/, you can retrieve more indexing information on medical periodicals (e.g. the name of the publisher). Select the button “Search LOCATORplus.” Then type in the name of the journal and select the advanced search option “Journal Title Search.”
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APPENDICES
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APPENDIX A. PHYSICIAN RESOURCES Overview In this chapter, we focus on databases and Internet-based guidelines and information resources created or written for a professional audience.
NIH Guidelines Commonly referred to as “clinical” or “professional” guidelines, the National Institutes of Health publish physician guidelines for the most common diseases. Publications are available at the following by relevant Institute11: •
Office of the Director (OD); guidelines consolidated across agencies available at http://www.nih.gov/health/consumer/conkey.htm
•
National Institute of General Medical Sciences (NIGMS); fact sheets available at http://www.nigms.nih.gov/news/facts/
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National Library of Medicine (NLM); extensive encyclopedia (A.D.A.M., Inc.) with guidelines: http://www.nlm.nih.gov/medlineplus/healthtopics.html
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National Cancer Institute (NCI); guidelines available at http://www.cancer.gov/cancerinfo/list.aspx?viewid=5f35036e-5497-4d86-8c2c714a9f7c8d25
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National Eye Institute (NEI); guidelines available at http://www.nei.nih.gov/order/index.htm
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National Heart, Lung, and Blood Institute (NHLBI); guidelines available at http://www.nhlbi.nih.gov/guidelines/index.htm
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National Human Genome Research Institute (NHGRI); research available at http://www.genome.gov/page.cfm?pageID=10000375
•
National Institute on Aging (NIA); guidelines available at http://www.nia.nih.gov/health/
11
These publications are typically written by one or more of the various NIH Institutes.
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•
National Institute on Alcohol Abuse and Alcoholism (NIAAA); guidelines available at http://www.niaaa.nih.gov/publications/publications.htm
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National Institute of Allergy and Infectious Diseases (NIAID); guidelines available at http://www.niaid.nih.gov/publications/
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National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS); fact sheets and guidelines available at http://www.niams.nih.gov/hi/index.htm
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National Institute of Child Health and Human Development (NICHD); guidelines available at http://www.nichd.nih.gov/publications/pubskey.cfm
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National Institute on Deafness and Other Communication Disorders (NIDCD); fact sheets and guidelines at http://www.nidcd.nih.gov/health/
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National Institute of Dental and Craniofacial Research (NIDCR); guidelines available at http://www.nidr.nih.gov/health/
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National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK); guidelines available at http://www.niddk.nih.gov/health/health.htm
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National Institute on Drug Abuse (NIDA); guidelines available at http://www.nida.nih.gov/DrugAbuse.html
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National Institute of Environmental Health Sciences (NIEHS); environmental health information available at http://www.niehs.nih.gov/external/facts.htm
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National Institute of Mental Health (NIMH); guidelines available at http://www.nimh.nih.gov/practitioners/index.cfm
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National Institute of Neurological Disorders and Stroke (NINDS); neurological disorder information pages available at http://www.ninds.nih.gov/health_and_medical/disorder_index.htm
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National Institute of Nursing Research (NINR); publications on selected illnesses at http://www.nih.gov/ninr/news-info/publications.html
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National Institute of Biomedical Imaging and Bioengineering; general information at http://grants.nih.gov/grants/becon/becon_info.htm
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Center for Information Technology (CIT); referrals to other agencies based on keyword searches available at http://kb.nih.gov/www_query_main.asp
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National Center for Complementary and Alternative Medicine (NCCAM); health information available at http://nccam.nih.gov/health/
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National Center for Research Resources (NCRR); various information directories available at http://www.ncrr.nih.gov/publications.asp
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Office of Rare Diseases; various fact sheets available at http://rarediseases.info.nih.gov/html/resources/rep_pubs.html
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Centers for Disease Control and Prevention; various fact sheets on infectious diseases available at http://www.cdc.gov/publications.htm
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NIH Databases In addition to the various Institutes of Health that publish professional guidelines, the NIH has designed a number of databases for professionals.12 Physician-oriented resources provide a wide variety of information related to the biomedical and health sciences, both past and present. The format of these resources varies. Searchable databases, bibliographic citations, full-text articles (when available), archival collections, and images are all available. The following are referenced by the National Library of Medicine:13 •
Bioethics: Access to published literature on the ethical, legal, and public policy issues surrounding healthcare and biomedical research. This information is provided in conjunction with the Kennedy Institute of Ethics located at Georgetown University, Washington, D.C.: http://www.nlm.nih.gov/databases/databases_bioethics.html
•
HIV/AIDS Resources: Describes various links and databases dedicated to HIV/AIDS research: http://www.nlm.nih.gov/pubs/factsheets/aidsinfs.html
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NLM Online Exhibitions: Describes “Exhibitions in the History of Medicine”: http://www.nlm.nih.gov/exhibition/exhibition.html. Additional resources for historical scholarship in medicine: http://www.nlm.nih.gov/hmd/hmd.html
•
Biotechnology Information: Access to public databases. The National Center for Biotechnology Information conducts research in computational biology, develops software tools for analyzing genome data, and disseminates biomedical information for the better understanding of molecular processes affecting human health and disease: http://www.ncbi.nlm.nih.gov/
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Population Information: The National Library of Medicine provides access to worldwide coverage of population, family planning, and related health issues, including family planning technology and programs, fertility, and population law and policy: http://www.nlm.nih.gov/databases/databases_population.html
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Cancer Information: Access to cancer-oriented databases: http://www.nlm.nih.gov/databases/databases_cancer.html
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Profiles in Science: Offering the archival collections of prominent twentieth-century biomedical scientists to the public through modern digital technology: http://www.profiles.nlm.nih.gov/
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Chemical Information: Provides links to various chemical databases and references: http://sis.nlm.nih.gov/Chem/ChemMain.html
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Clinical Alerts: Reports the release of findings from the NIH-funded clinical trials where such release could significantly affect morbidity and mortality: http://www.nlm.nih.gov/databases/alerts/clinical_alerts.html
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Space Life Sciences: Provides links and information to space-based research (including NASA): http://www.nlm.nih.gov/databases/databases_space.html
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MEDLINE: Bibliographic database covering the fields of medicine, nursing, dentistry, veterinary medicine, the healthcare system, and the pre-clinical sciences: http://www.nlm.nih.gov/databases/databases_medline.html
12
Remember, for the general public, the National Library of Medicine recommends the databases referenced in MEDLINEplus (http://medlineplus.gov/ or http://www.nlm.nih.gov/medlineplus/databases.html). 13 See http://www.nlm.nih.gov/databases/databases.html.
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•
Toxicology and Environmental Health Information (TOXNET): Databases covering toxicology and environmental health: http://sis.nlm.nih.gov/Tox/ToxMain.html
•
Visible Human Interface: Anatomically detailed, three-dimensional representations of normal male and female human bodies: http://www.nlm.nih.gov/research/visible/visible_human.html The Combined Health Information Database
A comprehensive source of information on clinical guidelines written for professionals is the Combined Health Information Database. You will need to limit your search to one of the following: Brochure/Pamphlet, Fact Sheet, or Information Package, and “glucosamine” using the “Detailed Search” option. Go directly to the following hyperlink: http://chid.nih.gov/detail/detail.html. To find associations, use the drop boxes at the bottom of the search page where “You may refine your search by.” For the publication date, select “All Years.” Select your preferred language and the format option “Fact Sheet.” Type “glucosamine” (or synonyms) into the “For these words:” box. The following is a sample result: •
Osteoarthritis: New Insights: Part 2: Treatment Approaches Source: Annals of Internal Medicine. 133(9): 726-737. November 7, 2000. Summary: This journal article, the second of a two part summary of a National Institutes of Health conference on osteoarthritis (OA), provides health professionals with information on treatment approaches. The conference brought together experts on OA from diverse backgrounds and provided a multidisciplinary and comprehensive summary of recent advances in the prevention of OA onset, progression, and disability. The article reviews evidence for the efficacy of commonly used oral therapies, including nonopioid analgesics, nonsteroidal antiinflammatory drugs, opioid analgesics, and glucosamine and chondroitin. This is followed by a discussion of biomechanical interventions, such as exercise and bracing, and behavioral interventions, such as individualized telephone based interventions and group programs directed toward enhancing self management. The article then reports on the use of acupuncture in the treatment of OA. In addition, the article describes current surgical approaches. Four categories of nonbiological procedures are considered surgical management: osteotomy, arthroscopy, arthrodesis, and arthroplasty. The article concludes with suggestions on probable future biotechnology oriented approaches to treatment, including cartilage transplantation and tissue engineering of biologically active cells, signal molecules, and a biomatrix to assemble functional tissues and organs. 2 figures, 1 table, and 135 references. (AA-M).
•
Osteoarthritis of the Knee: A Special Report Source: Physician and Sportsmedicine. Special Report. May 2000. Contact: Available from McGraw-Hill Healthcare Information. 4530 West 77th Street, Floor 3, Minneapolis, MN 55435. (800) 525-5003 or (609) 426-7070 (for subscriptions) or (952) 835-3222 (for back issues). Summary: This special report presents a series of articles that provide health professionals with information on osteoarthritis (OA) of the knee. The first article reviews the pathophysiological characteristics of OA and discusses its etiology, diagnosis, and evaluation. OA is caused by multiple factors, including genetic,
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metabolic, biochemical, enzymatic, biomechanical, and environmental factors. The history, physical examination, and radiographic examination help establish the diagnosis. The second article offers an overview of the nonoperative management of OA of the knee. Nonoperative techniques can be effective in relieving pain and improving functional ability. Nonpharmacologic treatment options include decreasing physical activity, exercising, losing weight, using supports and braces, and undergoing physiotherapy. Topical treatments include nonsteroidal anti-inflammatory drugs (NSAIDs) and capsaicin. Systemic therapies include nonnarcotic and narcotic analgesics, antidepressants, NSAIDs, chondroitin, and glucosamine. Intra-articular therapies include corticosteroids and viscosupplementation. The third article discusses operative treatment for the arthritic knee, focusing on the role of arthroscopy, the indications for joint replacement, and the new area of articular cartilage restoration and resurfacing. The choice of procedure is based on the patient's age, the extent of disease, and the desired level of physical activity. The fourth article presents case reports of active patients with arthritis who underwent viscosupplementation. The fifth article uses a question and answer format to provide health professionals with information on traditional and innovative treatments for OA of the knee. The final article is a continuing medical education activity. 5 tables and 95 references.
The NLM Gateway14 The NLM (National Library of Medicine) Gateway is a Web-based system that lets users search simultaneously in multiple retrieval systems at the U.S. National Library of Medicine (NLM). It allows users of NLM services to initiate searches from one Web interface, providing one-stop searching for many of NLM’s information resources or databases.15 To use the NLM Gateway, simply go to the search site at http://gateway.nlm.nih.gov/gw/Cmd. Type “glucosamine” (or synonyms) into the search box and click “Search.” The results will be presented in a tabular form, indicating the number of references in each database category. Results Summary Category Journal Articles Books / Periodicals / Audio Visual Consumer Health Meeting Abstracts Other Collections Total
Items Found 14717 34 11 9 0 14771
HSTAT16 HSTAT is a free, Web-based resource that provides access to full-text documents used in healthcare decision-making.17 These documents include clinical practice guidelines, quick14
Adapted from NLM: http://gateway.nlm.nih.gov/gw/Cmd?Overview.x.
15
The NLM Gateway is currently being developed by the Lister Hill National Center for Biomedical Communications (LHNCBC) at the National Library of Medicine (NLM) of the National Institutes of Health (NIH). 16 Adapted from HSTAT: http://www.nlm.nih.gov/pubs/factsheets/hstat.html. 17
The HSTAT URL is http://hstat.nlm.nih.gov/.
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reference guides for clinicians, consumer health brochures, evidence reports and technology assessments from the Agency for Healthcare Research and Quality (AHRQ), as well as AHRQ’s Put Prevention Into Practice.18 Simply search by “glucosamine” (or synonyms) at the following Web site: http://text.nlm.nih.gov.
Coffee Break: Tutorials for Biologists19 Coffee Break is a general healthcare site that takes a scientific view of the news and covers recent breakthroughs in biology that may one day assist physicians in developing treatments. Here you will find a collection of short reports on recent biological discoveries. Each report incorporates interactive tutorials that demonstrate how bioinformatics tools are used as a part of the research process. Currently, all Coffee Breaks are written by NCBI staff.20 Each report is about 400 words and is usually based on a discovery reported in one or more articles from recently published, peer-reviewed literature.21 This site has new articles every few weeks, so it can be considered an online magazine of sorts. It is intended for general background information. You can access the Coffee Break Web site at the following hyperlink: http://www.ncbi.nlm.nih.gov/Coffeebreak/.
Other Commercial Databases In addition to resources maintained by official agencies, other databases exist that are commercial ventures addressing medical professionals. Here are some examples that may interest you: •
CliniWeb International: Index and table of contents to selected clinical information on the Internet; see http://www.ohsu.edu/cliniweb/.
•
Medical World Search: Searches full text from thousands of selected medical sites on the Internet; see http://www.mwsearch.com/.
The Genome Project and Glucosamine In the following section, we will discuss databases and references which relate to the Genome Project and glucosamine.
18 Other important documents in HSTAT include: the National Institutes of Health (NIH) Consensus Conference Reports and Technology Assessment Reports; the HIV/AIDS Treatment Information Service (ATIS) resource documents; the Substance Abuse and Mental Health Services Administration's Center for Substance Abuse Treatment (SAMHSA/CSAT) Treatment Improvement Protocols (TIP) and Center for Substance Abuse Prevention (SAMHSA/CSAP) Prevention Enhancement Protocols System (PEPS); the Public Health Service (PHS) Preventive Services Task Force's Guide to Clinical Preventive Services; the independent, nonfederal Task Force on Community Services’ Guide to Community Preventive Services; and the Health Technology Advisory Committee (HTAC) of the Minnesota Health Care Commission (MHCC) health technology evaluations. 19 Adapted from http://www.ncbi.nlm.nih.gov/Coffeebreak/Archive/FAQ.html. 20 The figure that accompanies each article is frequently supplied by an expert external to NCBI, in which case the source of the figure is cited. The result is an interactive tutorial that tells a biological story. 21 After a brief introduction that sets the work described into a broader context, the report focuses on how a molecular understanding can provide explanations of observed biology and lead to therapies for diseases. Each vignette is accompanied by a figure and hypertext links that lead to a series of pages that interactively show how NCBI tools and resources are used in the research process.
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Online Mendelian Inheritance in Man (OMIM) The Online Mendelian Inheritance in Man (OMIM) database is a catalog of human genes and genetic disorders authored and edited by Dr. Victor A. McKusick and his colleagues at Johns Hopkins and elsewhere. OMIM was developed for the World Wide Web by the National Center for Biotechnology Information (NCBI).22 The database contains textual information, pictures, and reference information. It also contains copious links to NCBI’s Entrez database of MEDLINE articles and sequence information. To search the database, go to http://www.ncbi.nlm.nih.gov/Omim/searchomim.html. Type “glucosamine” (or synonyms) into the search box, and click “Submit Search.” If too many results appear, you can narrow the search by adding the word “clinical.” Each report will have additional links to related research and databases. In particular, the option “Database Links” will search across technical databases that offer an abundance of information. The following is an example of the results you can obtain from the OMIM for glucosamine: •
Glucosamine 6-phosphate Deaminase Web site: http://www.ncbi.nlm.nih.gov/htbin-post/Omim/dispmim?601798
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N-acetylglucosamine-6-sulfatase Web site: http://www.ncbi.nlm.nih.gov/htbin-post/Omim/dispmim?607664
•
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine Kinase Web site: http://www.ncbi.nlm.nih.gov/htbin-post/Omim/dispmim?603824 Genes and Disease (NCBI - Map)
The Genes and Disease database is produced by the National Center for Biotechnology Information of the National Library of Medicine at the National Institutes of Health. This Web site categorizes each disorder by system of the body. Go to http://www.ncbi.nlm.nih.gov/disease/, and browse the system pages to have a full view of important conditions linked to human genes. Since this site is regularly updated, you may wish to revisit it from time to time. The following systems and associated disorders are addressed: •
Cancer: Uncontrolled cell division. Examples: Breast and ovarian cancer, Burkitt lymphoma, chronic myeloid leukemia, colon cancer, lung cancer, malignant melanoma, multiple endocrine neoplasia, neurofibromatosis, p53 tumor suppressor, pancreatic cancer, prostate cancer, Ras oncogene, RB: retinoblastoma, von Hippel-Lindau syndrome. Web site: http://www.ncbi.nlm.nih.gov/disease/Cancer.html
•
Immune System: Fights invaders. Examples: Asthma, autoimmune polyglandular syndrome, Crohn’s disease, DiGeorge syndrome, familial Mediterranean fever, immunodeficiency with Hyper-IgM, severe combined immunodeficiency. Web site: http://www.ncbi.nlm.nih.gov/disease/Immune.html
22 Adapted from http://www.ncbi.nlm.nih.gov/. Established in 1988 as a national resource for molecular biology information, NCBI creates public databases, conducts research in computational biology, develops software tools for analyzing genome data, and disseminates biomedical information--all for the better understanding of molecular processes affecting human health and disease.
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Metabolism: Food and energy. Examples: Adreno-leukodystrophy, atherosclerosis, Best disease, Gaucher disease, glucose galactose malabsorption, gyrate atrophy, juvenile-onset diabetes, obesity, paroxysmal nocturnal hemoglobinuria, phenylketonuria, Refsum disease, Tangier disease, Tay-Sachs disease. Web site: http://www.ncbi.nlm.nih.gov/disease/Metabolism.html
•
Muscle and Bone: Movement and growth. Examples: Duchenne muscular dystrophy, Ellis-van Creveld syndrome, Marfan syndrome, myotonic dystrophy, spinal muscular atrophy. Web site: http://www.ncbi.nlm.nih.gov/disease/Muscle.html
•
Nervous System: Mind and body. Examples: Alzheimer disease, amyotrophic lateral sclerosis, Angelman syndrome, Charcot-Marie-Tooth disease, epilepsy, essential tremor, fragile X syndrome, Friedreich’s ataxia, Huntington disease, Niemann-Pick disease, Parkinson disease, Prader-Willi syndrome, Rett syndrome, spinocerebellar atrophy, Williams syndrome. Web site: http://www.ncbi.nlm.nih.gov/disease/Brain.html
•
Signals: Cellular messages. Examples: Ataxia telangiectasia, Cockayne syndrome, glaucoma, male-patterned baldness, SRY: sex determination, tuberous sclerosis, Waardenburg syndrome, Werner syndrome. Web site: http://www.ncbi.nlm.nih.gov/disease/Signals.html
•
Transporters: Pumps and channels. Examples: Cystic fibrosis, deafness, diastrophic dysplasia, Hemophilia A, long-QT syndrome, Menkes syndrome, Pendred syndrome, polycystic kidney disease, sickle cell anemia, Wilson’s disease, Zellweger syndrome. Web site: http://www.ncbi.nlm.nih.gov/disease/Transporters.html Entrez
Entrez is a search and retrieval system that integrates several linked databases at the National Center for Biotechnology Information (NCBI). These databases include nucleotide sequences, protein sequences, macromolecular structures, whole genomes, and MEDLINE through PubMed. Entrez provides access to the following databases: •
3D Domains: Domains from Entrez Structure, Web site: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=geo
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Books: Online books, Web site: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=books
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Genome: Complete genome assemblies, Web site: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=Genome
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NCBI’s Protein Sequence Information Survey Results: Web site: http://www.ncbi.nlm.nih.gov/About/proteinsurvey/
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Nucleotide Sequence Database (Genbank): Web site: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=Nucleotide
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OMIM: Online Mendelian Inheritance in Man, Web site: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=OMIM
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PopSet: Population study data sets, Web site: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=Popset
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ProbeSet: Gene Expression Omnibus (GEO), Web site: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=geo
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Protein Sequence Database: Web site: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=Protein
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PubMed: Biomedical literature (PubMed), Web site: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
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Structure: Three-dimensional macromolecular structures, Web site: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=Structure
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Taxonomy: Organisms in GenBank, Web site: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=Taxonomy
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To access the Entrez system at the National Center for Biotechnology Information, go to http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?CMD=search&DB=genome, and then select the database that you would like to search. The databases available are listed in the drop box next to “Search.” Enter “glucosamine” (or synonyms) into the search box and click “Go.” Jablonski’s Multiple Congenital Anomaly/Mental Retardation (MCA/MR) Syndromes Database23 This online resource has been developed to facilitate the identification and differentiation of syndromic entities. Special attention is given to the type of information that is usually limited or completely omitted in existing reference sources due to space limitations of the printed form. At http://www.nlm.nih.gov/mesh/jablonski/syndrome_toc/toc_a.html, you can search across syndromes using an alphabetical index. Search by keywords at http://www.nlm.nih.gov/mesh/jablonski/syndrome_db.html. The Genome Database24 Established at Johns Hopkins University in Baltimore, Maryland in 1990, the Genome Database (GDB) is the official central repository for genomic mapping data resulting from the Human Genome Initiative. In the spring of 1999, the Bioinformatics Supercomputing Centre (BiSC) at the Hospital for Sick Children in Toronto, Ontario assumed the management of GDB. The Human Genome Initiative is a worldwide research effort focusing on structural analysis of human DNA to determine the location and sequence of the estimated 100,000 human genes. In support of this project, GDB stores and curates data generated by researchers worldwide who are engaged in the mapping effort of the Human Genome Project (HGP). GDB’s mission is to provide scientists with an encyclopedia of the human genome which is continually revised and updated to reflect the current state of 23
Adapted from the National Library of Medicine: http://www.nlm.nih.gov/mesh/jablonski/about_syndrome.html. 24 Adapted from the Genome Database: http://gdbwww.gdb.org/gdb/aboutGDB.html - mission.
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scientific knowledge. Although GDB has historically focused on gene mapping, its focus will broaden as the Genome Project moves from mapping to sequence, and finally, to functional analysis. To access the GDB, simply go to the following hyperlink: http://www.gdb.org/. Search “All Biological Data” by “Keyword.” Type “glucosamine” (or synonyms) into the search box, and review the results. If more than one word is used in the search box, then separate each one with the word “and” or “or” (using “or” might be useful when using synonyms).
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APPENDIX B. PATIENT RESOURCES Overview Official agencies, as well as federally funded institutions supported by national grants, frequently publish a variety of guidelines written with the patient in mind. These are typically called “Fact Sheets” or “Guidelines.” They can take the form of a brochure, information kit, pamphlet, or flyer. Often they are only a few pages in length. Since new guidelines on glucosamine can appear at any moment and be published by a number of sources, the best approach to finding guidelines is to systematically scan the Internet-based services that post them.
Patient Guideline Sources The remainder of this chapter directs you to sources which either publish or can help you find additional guidelines on topics related to glucosamine. Due to space limitations, these sources are listed in a concise manner. Do not hesitate to consult the following sources by either using the Internet hyperlink provided, or, in cases where the contact information is provided, contacting the publisher or author directly. The National Institutes of Health The NIH gateway to patients is located at http://health.nih.gov/. From this site, you can search across various sources and institutes, a number of which are summarized below. Topic Pages: MEDLINEplus The National Library of Medicine has created a vast and patient-oriented healthcare information portal called MEDLINEplus. Within this Internet-based system are “health topic pages” which list links to available materials relevant to glucosamine. To access this system, log on to http://www.nlm.nih.gov/medlineplus/healthtopics.html. From there you can either search using the alphabetical index or browse by broad topic areas. Recently, MEDLINEplus listed the following when searched for “glucosamine”:
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•
Other guides Arthritis http://www.nlm.nih.gov/medlineplus/arthritis.html Cartilage Disorders http://www.nlm.nih.gov/medlineplus/cartilagedisorders.html Knee Injuries and Disorders http://www.nlm.nih.gov/medlineplus/kneeinjuriesanddisorders.html Osteoarthritis http://www.nlm.nih.gov/medlineplus/osteoarthritis.html Rheumatoid Arthritis http://www.nlm.nih.gov/medlineplus/rheumatoidarthritis.html
You may also choose to use the search utility provided by MEDLINEplus at the following Web address: http://www.nlm.nih.gov/medlineplus/. Simply type a keyword into the search box and click “Search.” This utility is similar to the NIH search utility, with the exception that it only includes materials that are linked within the MEDLINEplus system (mostly patient-oriented information). It also has the disadvantage of generating unstructured results. We recommend, therefore, that you use this method only if you have a very targeted search. The Combined Health Information Database (CHID) CHID Online is a reference tool that maintains a database directory of thousands of journal articles and patient education guidelines on glucosamine. CHID offers summaries that describe the guidelines available, including contact information and pricing. CHID’s general Web site is http://chid.nih.gov/. To search this database, go to http://chid.nih.gov/detail/detail.html. In particular, you can use the advanced search options to look up pamphlets, reports, brochures, and information kits. The following was recently posted in this archive: •
Questions & Answers: NIH Glucosamine/Chondroitin Arthritis Intervention Trial (GAIT) Source: Gaithersburg, MD: National Center for Complementary and Alternative Medicine. 2002. 5 p. Contact: Available from National Center for Complementary and Alternative Medicine Clearinghouse. P.O. Box 7923, Gaithersburg, MD 20898. (888) 644-6226; INTERNATIONAL PHONE: (301) 519-3153; TTY: (866) 464-3615; FAX: (866) 464-3616; EMAIL:
[email protected]. PRICE: Free. Publication Number: D147. Summary: This National Institutes of Health fact sheet provides information about the Glucosamine/Chondroitin Arthritis Intervention Trial in a question and answer format. It discusses the overall purpose of the trial as well as the circumstances that prompted the NIH to study glucosamine and chondroitin for osteoarthritis. It describes the basic design of the study and includes information about the number of patients included, who is eligible to take part, and how people can sign up to participate in the study. The fact sheet provides general facts about osteoarthritis and the dietary supplements glucosamine and chondroitin, which are being tested to treat the condition.
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Glucosamine and Chondroitin Sulfate Source: Atlanta, GA: Arthritis Foundation. 1999. 8 p. Contact: Available from Arthritis Foundation. P.O. Box 1616, Alpharetta, GA 300091616. (800) 207-8633. Fax (credit card orders only) (770) 442-9742. Website: www.arthritis.org. PRICE: Single copy free from local Arthritis Foundation chapter (call (800) 283-7800 for closest local chapter); bulk orders may be purchased from address above. Summary: This pamphlet uses a question and answer format to provide people who have arthritis with information on glucosamine and chondroitin sulfate. These substances, which are found naturally in the body, are sold as dietary or nutritional supplements. They have been used in Europe to treat osteoarthritis since the 1980s. Studies conducted primarily in Europe have shown that some people with mild to moderate osteoarthritis who took either substance experienced pain relief at a level similar to that of nonsteroidal anti-inflammatory drugs. Glucosamine and chondroitin are unregulated, so the quality and content may vary widely. A person choosing to take these supplements should consult his or her physician to make sure that osteoarthritis is the cause of pain and should choose products sold by large, well established companies. Recommended dosages are 1,500 milligrams (mg) per day for glucosamine and 1,200 mg per day for chondroitin. Common side effects are increased intestinal gas and softened stools. There are some people who need to be especially careful when considering the use of these supplements. Healthfinder™
Healthfinder™ is sponsored by the U.S. Department of Health and Human Services and offers links to hundreds of other sites that contain healthcare information. This Web site is located at http://www.healthfinder.gov. Again, keyword searches can be used to find guidelines. The following was recently found in this database: •
Glucosamine and Chondroitin Sulfate Summary: Facts about the dietary (nutritional) supplements glucosamine and chondroitin sulfate and their use as treatment options for arthritis. Source: Arthritis Foundation http://www.healthfinder.gov/scripts/recordpass.asp?RecordType=0&RecordID=6007 The NIH Search Utility
The NIH search utility allows you to search for documents on over 100 selected Web sites that comprise the NIH-WEB-SPACE. Each of these servers is “crawled” and indexed on an ongoing basis. Your search will produce a list of various documents, all of which will relate in some way to glucosamine. The drawbacks of this approach are that the information is not organized by theme and that the references are often a mix of information for professionals and patients. Nevertheless, a large number of the listed Web sites provide useful background information. We can only recommend this route, therefore, for relatively rare or specific disorders, or when using highly targeted searches. To use the NIH search utility, visit the following Web page: http://search.nih.gov/index.html.
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Additional Web Sources A number of Web sites are available to the public that often link to government sites. These can also point you in the direction of essential information. The following is a representative sample: •
AOL: http://search.aol.com/cat.adp?id=168&layer=&from=subcats
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Family Village: http://www.familyvillage.wisc.edu/specific.htm
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Google: http://directory.google.com/Top/Health/Conditions_and_Diseases/
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Med Help International: http://www.medhelp.org/HealthTopics/A.html
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Open Directory Project: http://dmoz.org/Health/Conditions_and_Diseases/
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Yahoo.com: http://dir.yahoo.com/Health/Diseases_and_Conditions/
•
WebMD®Health: http://my.webmd.com/health_topics
Finding Associations There are several Internet directories that provide lists of medical associations with information on or resources relating to glucosamine. By consulting all of associations listed in this chapter, you will have nearly exhausted all sources for patient associations concerned with glucosamine. The National Health Information Center (NHIC) The National Health Information Center (NHIC) offers a free referral service to help people find organizations that provide information about glucosamine. For more information, see the NHIC’s Web site at http://www.health.gov/NHIC/ or contact an information specialist by calling 1-800-336-4797. Directory of Health Organizations The Directory of Health Organizations, provided by the National Library of Medicine Specialized Information Services, is a comprehensive source of information on associations. The Directory of Health Organizations database can be accessed via the Internet at http://www.sis.nlm.nih.gov/Dir/DirMain.html. It is composed of two parts: DIRLINE and Health Hotlines. The DIRLINE database comprises some 10,000 records of organizations, research centers, and government institutes and associations that primarily focus on health and biomedicine. To access DIRLINE directly, go to the following Web site: http://dirline.nlm.nih.gov/. Simply type in “glucosamine” (or a synonym), and you will receive information on all relevant organizations listed in the database. Health Hotlines directs you to toll-free numbers to over 300 organizations. You can access this database directly at http://www.sis.nlm.nih.gov/hotlines/. On this page, you are given the option to search by keyword or by browsing the subject list. When you have received
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your search results, click on the name of the organization for its description and contact information. The Combined Health Information Database Another comprehensive source of information on healthcare associations is the Combined Health Information Database. Using the “Detailed Search” option, you will need to limit your search to “Organizations” and “glucosamine”. Type the following hyperlink into your Web browser: http://chid.nih.gov/detail/detail.html. To find associations, use the drop boxes at the bottom of the search page where “You may refine your search by.” For publication date, select “All Years.” Then, select your preferred language and the format option “Organization Resource Sheet.” Type “glucosamine” (or synonyms) into the “For these words:” box. You should check back periodically with this database since it is updated every three months. The National Organization for Rare Disorders, Inc. The National Organization for Rare Disorders, Inc. has prepared a Web site that provides, at no charge, lists of associations organized by health topic. You can access this database at the following Web site: http://www.rarediseases.org/search/orgsearch.html. Type “glucosamine” (or a synonym) into the search box, and click “Submit Query.”
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APPENDIX C. FINDING MEDICAL LIBRARIES Overview In this Appendix, we show you how to quickly find a medical library in your area.
Preparation Your local public library and medical libraries have interlibrary loan programs with the National Library of Medicine (NLM), one of the largest medical collections in the world. According to the NLM, most of the literature in the general and historical collections of the National Library of Medicine is available on interlibrary loan to any library. If you would like to access NLM medical literature, then visit a library in your area that can request the publications for you.25
Finding a Local Medical Library The quickest method to locate medical libraries is to use the Internet-based directory published by the National Network of Libraries of Medicine (NN/LM). This network includes 4626 members and affiliates that provide many services to librarians, health professionals, and the public. To find a library in your area, simply visit http://nnlm.gov/members/adv.html or call 1-800-338-7657.
Medical Libraries in the U.S. and Canada In addition to the NN/LM, the National Library of Medicine (NLM) lists a number of libraries with reference facilities that are open to the public. The following is the NLM’s list and includes hyperlinks to each library’s Web site. These Web pages can provide information on hours of operation and other restrictions. The list below is a small sample of
25
Adapted from the NLM: http://www.nlm.nih.gov/psd/cas/interlibrary.html.
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libraries recommended by the National Library of Medicine (sorted alphabetically by name of the U.S. state or Canadian province where the library is located)26: •
Alabama: Health InfoNet of Jefferson County (Jefferson County Library Cooperative, Lister Hill Library of the Health Sciences), http://www.uab.edu/infonet/
•
Alabama: Richard M. Scrushy Library (American Sports Medicine Institute)
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Arizona: Samaritan Regional Medical Center: The Learning Center (Samaritan Health System, Phoenix, Arizona), http://www.samaritan.edu/library/bannerlibs.htm
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California: Kris Kelly Health Information Center (St. Joseph Health System, Humboldt), http://www.humboldt1.com/~kkhic/index.html
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California: Community Health Library of Los Gatos, http://www.healthlib.org/orgresources.html
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California: Consumer Health Program and Services (CHIPS) (County of Los Angeles Public Library, Los Angeles County Harbor-UCLA Medical Center Library) - Carson, CA, http://www.colapublib.org/services/chips.html
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California: Gateway Health Library (Sutter Gould Medical Foundation)
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California: Health Library (Stanford University Medical Center), http://wwwmed.stanford.edu/healthlibrary/
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California: Patient Education Resource Center - Health Information and Resources (University of California, San Francisco), http://sfghdean.ucsf.edu/barnett/PERC/default.asp
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California: Redwood Health Library (Petaluma Health Care District), http://www.phcd.org/rdwdlib.html
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California: Los Gatos PlaneTree Health Library, http://planetreesanjose.org/
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California: Sutter Resource Library (Sutter Hospitals Foundation, Sacramento), http://suttermedicalcenter.org/library/
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California: Health Sciences Libraries (University of California, Davis), http://www.lib.ucdavis.edu/healthsci/
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California: ValleyCare Health Library & Ryan Comer Cancer Resource Center (ValleyCare Health System, Pleasanton), http://gaelnet.stmarysca.edu/other.libs/gbal/east/vchl.html
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California: Washington Community Health Resource Library (Fremont), http://www.healthlibrary.org/
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Colorado: William V. Gervasini Memorial Library (Exempla Healthcare), http://www.saintjosephdenver.org/yourhealth/libraries/
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Connecticut: Hartford Hospital Health Science Libraries (Hartford Hospital), http://www.harthosp.org/library/
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Connecticut: Healthnet: Connecticut Consumer Health Information Center (University of Connecticut Health Center, Lyman Maynard Stowe Library), http://library.uchc.edu/departm/hnet/
26
Abstracted from http://www.nlm.nih.gov/medlineplus/libraries.html.
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•
Connecticut: Waterbury Hospital Health Center Library (Waterbury Hospital, Waterbury), http://www.waterburyhospital.com/library/consumer.shtml
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Delaware: Consumer Health Library (Christiana Care Health System, Eugene du Pont Preventive Medicine & Rehabilitation Institute, Wilmington), http://www.christianacare.org/health_guide/health_guide_pmri_health_info.cfm
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Delaware: Lewis B. Flinn Library (Delaware Academy of Medicine, Wilmington), http://www.delamed.org/chls.html
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Georgia: Family Resource Library (Medical College of Georgia, Augusta), http://cmc.mcg.edu/kids_families/fam_resources/fam_res_lib/frl.htm
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Georgia: Health Resource Center (Medical Center of Central Georgia, Macon), http://www.mccg.org/hrc/hrchome.asp
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Hawaii: Hawaii Medical Library: Consumer Health Information Service (Hawaii Medical Library, Honolulu), http://hml.org/CHIS/
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Idaho: DeArmond Consumer Health Library (Kootenai Medical Center, Coeur d’Alene), http://www.nicon.org/DeArmond/index.htm
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Illinois: Health Learning Center of Northwestern Memorial Hospital (Chicago), http://www.nmh.org/health_info/hlc.html
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Illinois: Medical Library (OSF Saint Francis Medical Center, Peoria), http://www.osfsaintfrancis.org/general/library/
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Kentucky: Medical Library - Services for Patients, Families, Students & the Public (Central Baptist Hospital, Lexington), http://www.centralbap.com/education/community/library.cfm
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Kentucky: University of Kentucky - Health Information Library (Chandler Medical Center, Lexington), http://www.mc.uky.edu/PatientEd/
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Louisiana: Alton Ochsner Medical Foundation Library (Alton Ochsner Medical Foundation, New Orleans), http://www.ochsner.org/library/
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Louisiana: Louisiana State University Health Sciences Center Medical LibraryShreveport, http://lib-sh.lsuhsc.edu/
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Maine: Franklin Memorial Hospital Medical Library (Franklin Memorial Hospital, Farmington), http://www.fchn.org/fmh/lib.htm
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Maine: Gerrish-True Health Sciences Library (Central Maine Medical Center, Lewiston), http://www.cmmc.org/library/library.html
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Maine: Hadley Parrot Health Science Library (Eastern Maine Healthcare, Bangor), http://www.emh.org/hll/hpl/guide.htm
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Maine: Maine Medical Center Library (Maine Medical Center, Portland), http://www.mmc.org/library/
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Maine: Parkview Hospital (Brunswick), http://www.parkviewhospital.org/
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Maine: Southern Maine Medical Center Health Sciences Library (Southern Maine Medical Center, Biddeford), http://www.smmc.org/services/service.php3?choice=10
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Maine: Stephens Memorial Hospital’s Health Information Library (Western Maine Health, Norway), http://www.wmhcc.org/Library/
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Manitoba, Canada: Consumer & Patient Health Information Service (University of Manitoba Libraries), http://www.umanitoba.ca/libraries/units/health/reference/chis.html
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Manitoba, Canada: J.W. Crane Memorial Library (Deer Lodge Centre, Winnipeg), http://www.deerlodge.mb.ca/crane_library/about.asp
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Maryland: Health Information Center at the Wheaton Regional Library (Montgomery County, Dept. of Public Libraries, Wheaton Regional Library), http://www.mont.lib.md.us/healthinfo/hic.asp
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Massachusetts: Baystate Medical Center Library (Baystate Health System), http://www.baystatehealth.com/1024/
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Massachusetts: Boston University Medical Center Alumni Medical Library (Boston University Medical Center), http://med-libwww.bu.edu/library/lib.html
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Massachusetts: Lowell General Hospital Health Sciences Library (Lowell General Hospital, Lowell), http://www.lowellgeneral.org/library/HomePageLinks/WWW.htm
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Massachusetts: Paul E. Woodard Health Sciences Library (New England Baptist Hospital, Boston), http://www.nebh.org/health_lib.asp
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Massachusetts: St. Luke’s Hospital Health Sciences Library (St. Luke’s Hospital, Southcoast Health System, New Bedford), http://www.southcoast.org/library/
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Massachusetts: Treadwell Library Consumer Health Reference Center (Massachusetts General Hospital), http://www.mgh.harvard.edu/library/chrcindex.html
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Massachusetts: UMass HealthNet (University of Massachusetts Medical School, Worchester), http://healthnet.umassmed.edu/
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Michigan: Botsford General Hospital Library - Consumer Health (Botsford General Hospital, Library & Internet Services), http://www.botsfordlibrary.org/consumer.htm
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Michigan: Helen DeRoy Medical Library (Providence Hospital and Medical Centers), http://www.providence-hospital.org/library/
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Michigan: Marquette General Hospital - Consumer Health Library (Marquette General Hospital, Health Information Center), http://www.mgh.org/center.html
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Michigan: Patient Education Resouce Center - University of Michigan Cancer Center (University of Michigan Comprehensive Cancer Center, Ann Arbor), http://www.cancer.med.umich.edu/learn/leares.htm
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Michigan: Sladen Library & Center for Health Information Resources - Consumer Health Information (Detroit), http://www.henryford.com/body.cfm?id=39330
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Montana: Center for Health Information (St. Patrick Hospital and Health Sciences Center, Missoula)
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National: Consumer Health Library Directory (Medical Library Association, Consumer and Patient Health Information Section), http://caphis.mlanet.org/directory/index.html
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National: National Network of Libraries of Medicine (National Library of Medicine) provides library services for health professionals in the United States who do not have access to a medical library, http://nnlm.gov/
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National: NN/LM List of Libraries Serving the Public (National Network of Libraries of Medicine), http://nnlm.gov/members/
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Nevada: Health Science Library, West Charleston Library (Las Vegas-Clark County Library District, Las Vegas), http://www.lvccld.org/special_collections/medical/index.htm
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New Hampshire: Dartmouth Biomedical Libraries (Dartmouth College Library, Hanover), http://www.dartmouth.edu/~biomed/resources.htmld/conshealth.htmld/
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New Jersey: Consumer Health Library (Rahway Hospital, Rahway), http://www.rahwayhospital.com/library.htm
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New Jersey: Dr. Walter Phillips Health Sciences Library (Englewood Hospital and Medical Center, Englewood), http://www.englewoodhospital.com/links/index.htm
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New Jersey: Meland Foundation (Englewood Hospital and Medical Center, Englewood), http://www.geocities.com/ResearchTriangle/9360/
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New York: Choices in Health Information (New York Public Library) - NLM Consumer Pilot Project participant, http://www.nypl.org/branch/health/links.html
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New York: Health Information Center (Upstate Medical University, State University of New York, Syracuse), http://www.upstate.edu/library/hic/
•
New York: Health Sciences Library (Long Island Jewish Medical Center, New Hyde Park), http://www.lij.edu/library/library.html
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New York: ViaHealth Medical Library (Rochester General Hospital), http://www.nyam.org/library/
•
Ohio: Consumer Health Library (Akron General Medical Center, Medical & Consumer Health Library), http://www.akrongeneral.org/hwlibrary.htm
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Oklahoma: The Health Information Center at Saint Francis Hospital (Saint Francis Health System, Tulsa), http://www.sfh-tulsa.com/services/healthinfo.asp
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Oregon: Planetree Health Resource Center (Mid-Columbia Medical Center, The Dalles), http://www.mcmc.net/phrc/
•
Pennsylvania: Community Health Information Library (Milton S. Hershey Medical Center, Hershey), http://www.hmc.psu.edu/commhealth/
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Pennsylvania: Community Health Resource Library (Geisinger Medical Center, Danville), http://www.geisinger.edu/education/commlib.shtml
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Pennsylvania: HealthInfo Library (Moses Taylor Hospital, Scranton), http://www.mth.org/healthwellness.html
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Pennsylvania: Hopwood Library (University of Pittsburgh, Health Sciences Library System, Pittsburgh), http://www.hsls.pitt.edu/guides/chi/hopwood/index_html
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Pennsylvania: Koop Community Health Information Center (College of Physicians of Philadelphia), http://www.collphyphil.org/kooppg1.shtml
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Pennsylvania: Learning Resources Center - Medical Library (Susquehanna Health System, Williamsport), http://www.shscares.org/services/lrc/index.asp
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Pennsylvania: Medical Library (UPMC Health System, Pittsburgh), http://www.upmc.edu/passavant/library.htm
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Quebec, Canada: Medical Library (Montreal General Hospital), http://www.mghlib.mcgill.ca/
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South Dakota: Rapid City Regional Hospital Medical Library (Rapid City Regional Hospital), http://www.rcrh.org/Services/Library/Default.asp
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Texas: Houston HealthWays (Houston Academy of Medicine-Texas Medical Center Library), http://hhw.library.tmc.edu/
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Washington: Community Health Library (Kittitas Valley Community Hospital), http://www.kvch.com/
•
Washington: Southwest Washington Medical Center Library (Southwest Washington Medical Center, Vancouver), http://www.swmedicalcenter.com/body.cfm?id=72
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ONLINE GLOSSARIES The Internet provides access to a number of free-to-use medical dictionaries. The National Library of Medicine has compiled the following list of online dictionaries: •
ADAM Medical Encyclopedia (A.D.A.M., Inc.), comprehensive medical reference: http://www.nlm.nih.gov/medlineplus/encyclopedia.html
•
MedicineNet.com Medical Dictionary (MedicineNet, Inc.): http://www.medterms.com/Script/Main/hp.asp
•
Merriam-Webster Medical Dictionary (Inteli-Health, Inc.): http://www.intelihealth.com/IH/
•
Multilingual Glossary of Technical and Popular Medical Terms in Eight European Languages (European Commission) - Danish, Dutch, English, French, German, Italian, Portuguese, and Spanish: http://allserv.rug.ac.be/~rvdstich/eugloss/welcome.html
•
On-line Medical Dictionary (CancerWEB): http://cancerweb.ncl.ac.uk/omd/
•
Rare Diseases Terms (Office of Rare Diseases): http://ord.aspensys.com/asp/diseases/diseases.asp
•
Technology Glossary (National Library of Medicine) - Health Care Technology: http://www.nlm.nih.gov/nichsr/ta101/ta10108.htm
Beyond these, MEDLINEplus contains a very patient-friendly encyclopedia covering every aspect of medicine (licensed from A.D.A.M., Inc.). The ADAM Medical Encyclopedia can be accessed at http://www.nlm.nih.gov/medlineplus/encyclopedia.html. ADAM is also available on commercial Web sites such as drkoop.com (http://www.drkoop.com/) and Web MD (http://my.webmd.com/adam/asset/adam_disease_articles/a_to_z/a).
Online Dictionary Directories The following are additional online directories compiled by the National Library of Medicine, including a number of specialized medical dictionaries: •
Medical Dictionaries: Medical & Biological (World Health Organization): http://www.who.int/hlt/virtuallibrary/English/diction.htm#Medical
•
MEL-Michigan Electronic Library List of Online Health and Medical Dictionaries (Michigan Electronic Library): http://mel.lib.mi.us/health/health-dictionaries.html
•
Patient Education: Glossaries (DMOZ Open Directory Project): http://dmoz.org/Health/Education/Patient_Education/Glossaries/
•
Web of Online Dictionaries (Bucknell University): http://www.yourdictionary.com/diction5.html#medicine
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GLUCOSAMINE DICTIONARY The definitions below are derived from official public sources, including the National Institutes of Health [NIH] and the European Union [EU]. Abdominal: Having to do with the abdomen, which is the part of the body between the chest and the hips that contains the pancreas, stomach, intestines, liver, gallbladder, and other organs. [NIH] Abdominal fat: Fat (adipose tissue) that is centrally distributed between the thorax and pelvis and that induces greater health risk. [NIH] Abrasion: 1. The wearing away of a substance or structure (such as the skin or the teeth) through some unusual or abnormal mechanical process. 2. An area of body surface denuded of skin or mucous membrane by some unusual or abnormal mechanical process. [EU] Acceptor: A substance which, while normally not oxidized by oxygen or reduced by hydrogen, can be oxidized or reduced in presence of a substance which is itself undergoing oxidation or reduction. [NIH] Acetaminophen: Analgesic antipyretic derivative of acetanilide. It has weak antiinflammatory properties and is used as a common analgesic, but may cause liver, blood cell, and kidney damage. [NIH] Acetone: A colorless liquid used as a solvent and an antiseptic. It is one of the ketone bodies produced during ketoacidosis. [NIH] Acetylcholine: A neurotransmitter. Acetylcholine in vertebrates is the major transmitter at neuromuscular junctions, autonomic ganglia, parasympathetic effector junctions, a subset of sympathetic effector junctions, and at many sites in the central nervous system. It is generally not used as an administered drug because it is broken down very rapidly by cholinesterases, but it is useful in some ophthalmological applications. [NIH] Acetylcysteine: The N-acetyl derivative of cysteine. It is used as a mucolytic agent to reduce the viscosity of mucous secretions. It has also been shown to have antiviral effects in patients with HIV due to inhibition of viral stimulation by reactive oxygen intermediates. [NIH] Acetylgalactosamine: The N-acetyl derivative of galactosamine. [NIH] Acetylglucosamine: The N-acetyl derivative of glucosamine. [NIH] Acetylglucosaminidase: 2-Acetamido-2-deoxy-beta-D-glucoside acetamidodeoxyglucohydrolase. Catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-betaglucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as mucolipidosis and various inflammatory disorders of muscle and connective tissue. [NIH] Acrosome: Cap-like structure covering the nucleus and anterior part of the sperm head. [NIH]
Acrosome Reaction: Changes that occur to liberate the enzymes of the acrosome of spermatozoa that allow the entry of a spermatozoon into the ovum. [NIH] Acrylonitrile: A highly poisonous compound used widely in the manufacture of plastics, adhesives and synthetic rubber. [NIH] Actin: Essential component of the cell skeleton. [NIH] Acyl: Chemical signal used by bacteria to communicate. [NIH]
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Acyl Carrier Protein: Consists of a polypeptide chain and 4'-phosphopantetheine linked to a serine residue by a phosphodiester bond. Acyl groups are bound as thiol esters to the pantothenyl group. Acyl carrier protein is involved in every step of fatty acid synthesis by the cytoplasmic system. [NIH] Acylation: The addition of an organic acid radical into a molecule. [NIH] Adaptation: 1. The adjustment of an organism to its environment, or the process by which it enhances such fitness. 2. The normal ability of the eye to adjust itself to variations in the intensity of light; the adjustment to such variations. 3. The decline in the frequency of firing of a neuron, particularly of a receptor, under conditions of constant stimulation. 4. In dentistry, (a) the proper fitting of a denture, (b) the degree of proximity and interlocking of restorative material to a tooth preparation, (c) the exact adjustment of bands to teeth. 5. In microbiology, the adjustment of bacterial physiology to a new environment. [EU] Adenine: A purine base and a fundamental unit of adenine nucleotides. [NIH] Adenosine: A nucleoside that is composed of adenine and d-ribose. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. Adenosine itself is a neurotransmitter. [NIH] Adenosine Diphosphate: Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position. [NIH] Adenosine Triphosphate: Adenosine 5'-(tetrahydrogen triphosphate). An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter. [NIH] Adenylate Cyclase: An enzyme of the lyase class that catalyzes the formation of cyclic AMP and pyrophosphate from ATP. EC 4.6.1.1. [NIH] Adipocytes: Fat-storing cells found mostly in the abdominal cavity and subcutaneous tissue. Fat is usually stored in the form of tryglycerides. [NIH] Adipose Tissue: Connective tissue composed of fat cells lodged in the meshes of areolar tissue. [NIH] Adjustment: The dynamic process wherein the thoughts, feelings, behavior, and biophysiological mechanisms of the individual continually change to adjust to the environment. [NIH] Adjuvant: A substance which aids another, such as an auxiliary remedy; in immunology, nonspecific stimulator (e.g., BCG vaccine) of the immune response. [EU] Adoptive Transfer: Form of passive immunization where previously sensitized immunologic agents (cells or serum) are transferred to non-immune recipients. When transfer of cells is used as a therapy for the treatment of neoplasms, it is called adoptive immunotherapy (immunotherapy, adoptive). [NIH] Adrenal Medulla: The inner part of the adrenal gland; it synthesizes, stores and releases catecholamines. [NIH] Adrenergic: Activated by, characteristic of, or secreting epinephrine or substances with similar activity; the term is applied to those nerve fibres that liberate norepinephrine at a synapse when a nerve impulse passes, i.e., the sympathetic fibres. [EU] Adverse Effect: An unwanted side effect of treatment. [NIH] Aerobic: In biochemistry, reactions that need oxygen to happen or happen when oxygen is present. [NIH] Aerobic Exercise: A type of physical activity that includes walking, jogging, running, and dancing. Aerobic training improves the efficiency of the aerobic energy-producing systems
Dictionary 193
that can improve cardiorespiratory endurance. [NIH] Aetiology: Study of the causes of disease. [EU] Affinity: 1. Inherent likeness or relationship. 2. A special attraction for a specific element, organ, or structure. 3. Chemical affinity; the force that binds atoms in molecules; the tendency of substances to combine by chemical reaction. 4. The strength of noncovalent chemical binding between two substances as measured by the dissociation constant of the complex. 5. In immunology, a thermodynamic expression of the strength of interaction between a single antigen-binding site and a single antigenic determinant (and thus of the stereochemical compatibility between them), most accurately applied to interactions among simple, uniform antigenic determinants such as haptens. Expressed as the association constant (K litres mole -1), which, owing to the heterogeneity of affinities in a population of antibody molecules of a given specificity, actually represents an average value (mean intrinsic association constant). 6. The reciprocal of the dissociation constant. [EU] Agar: A complex sulfated polymer of galactose units, extracted from Gelidium cartilagineum, Gracilaria confervoides, and related red algae. It is used as a gel in the preparation of solid culture media for microorganisms, as a bulk laxative, in making emulsions, and as a supporting medium for immunodiffusion and immunoelectrophoresis. [NIH]
Age of Onset: The age or period of life at which a disease or the initial symptoms or manifestations of a disease appear in an individual. [NIH] Agonist: In anatomy, a prime mover. In pharmacology, a drug that has affinity for and stimulates physiologic activity at cell receptors normally stimulated by naturally occurring substances. [EU] Albumin: 1. Any protein that is soluble in water and moderately concentrated salt solutions and is coagulable by heat. 2. Serum albumin; the major plasma protein (approximately 60 per cent of the total), which is responsible for much of the plasma colloidal osmotic pressure and serves as a transport protein carrying large organic anions, such as fatty acids, bilirubin, and many drugs, and also carrying certain hormones, such as cortisol and thyroxine, when their specific binding globulins are saturated. Albumin is synthesized in the liver. Low serum levels occur in protein malnutrition, active inflammation and serious hepatic and renal disease. [EU] Albuminuria: More than normal amounts of a protein called albumin in the urine. Albuminuria may be a sign of kidney disease. [NIH] Alertness: A state of readiness to detect and respond to certain specified small changes occurring at random intervals in the environment. [NIH] Alfalfa: A deep-rooted European leguminous plant (Medicago sativa) widely grown for hay and forage. [NIH] Algorithms: A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task. [NIH] Alkaline: Having the reactions of an alkali. [EU] Alkaloid: A member of a large group of chemicals that are made by plants and have nitrogen in them. Some alkaloids have been shown to work against cancer. [NIH] Alkylating Agents: Highly reactive chemicals that introduce alkyl radicals into biologically active molecules and thereby prevent their proper functioning. Many are used as antineoplastic agents, but most are very toxic, with carcinogenic, mutagenic, teratogenic, and immunosuppressant actions. They have also been used as components in poison gases. [NIH]
Allergen: An antigenic substance capable of producing immediate-type hypersensitivity
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(allergy). [EU] Allylamine: Possesses an unusual and selective cytotoxicity for vascular smooth muscle cells in dogs and rats. Useful for experiments dealing with arterial injury, myocardial fibrosis or cardiac decompensation. [NIH] Alpha Particles: Positively charged particles composed of two protons and two neutrons, i.e., helium nuclei, emitted during disintegration of very heavy isotopes; a beam of alpha particles or an alpha ray has very strong ionizing power, but weak penetrability. [NIH] Alpha-1: A protein with the property of inactivating proteolytic enzymes such as leucocyte collagenase and elastase. [NIH] Alpha-Defensins: Defensins found in azurophilic granules of neutrophils and in the secretory granules of intestinal paneth cells. [NIH] Alpha-helix: One of the secondary element of protein. [NIH] Alpha-lactalbumin: A human milk protein which could be used as a nutritional supplement. [NIH] Alternative medicine: Practices not generally recognized by the medical community as standard or conventional medical approaches and used instead of standard treatments. Alternative medicine includes the taking of dietary supplements, megadose vitamins, and herbal preparations; the drinking of special teas; and practices such as massage therapy, magnet therapy, spiritual healing, and meditation. [NIH] Alum: A type of immune adjuvant (a substance used to help boost the immune response to a vaccine). Also called aluminum sulfate. [NIH] Aluminum: A metallic element that has the atomic number 13, atomic symbol Al, and atomic weight 26.98. [NIH] Aluminum Hydroxide: Hydrated aluminum. A compound with many biomedical applications: as a gastric antacid, an antiperspirant, in dentifrices, as an emulsifier, as an adjuvant in bacterins and vaccines, in water purification, etc. [NIH] Alveolar Process: The thickest and spongiest part of the maxilla and mandible hollowed out into deep cavities for the teeth. [NIH] Amelogenesis Imperfecta: Either hereditary enamel hypoplasia or hypocalcification. [NIH] Amine: An organic compound containing nitrogen; any member of a group of chemical compounds formed from ammonia by replacement of one or more of the hydrogen atoms by organic (hydrocarbon) radicals. The amines are distinguished as primary, secondary, and tertiary, according to whether one, two, or three hydrogen atoms are replaced. The amines include allylamine, amylamine, ethylamine, methylamine, phenylamine, propylamine, and many other compounds. [EU] Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining protein conformation. [NIH] Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. [NIH] Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. [NIH] Amitriptyline: Tricyclic antidepressant with anticholinergic and sedative properties. It appears to prevent the re-uptake of norepinephrine and serotonin at nerve terminals, thus
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potentiating the action of these neurotransmitters. Amitriptyline also appears to antaganize cholinergic and alpha-1 adrenergic responses to bioactive amines. [NIH] Ammonia: A colorless alkaline gas. It is formed in the body during decomposition of organic materials during a large number of metabolically important reactions. [NIH] Ammonium Chloride: An acidifying agent that is used as an expectorant and a diuretic. [NIH]
Ampicillin: Semi-synthetic derivative of penicillin that functions as an orally active broadspectrum antibiotic. [NIH] Ampicillin Resistance: Nonsusceptibility of a microbe to the action of ampicillin, a penicillin derivative that interferes with cell wall synthesis. [NIH] Amplification: The production of additional copies of a chromosomal DNA sequence, found as either intrachromosomal or extrachromosomal DNA. [NIH] Amylase: An enzyme that helps the body digest starches. [NIH] Amylose: An unbranched glucan in starch. [NIH] Anabolic: Relating to, characterized by, or promoting anabolism. [EU] Anaesthesia: Loss of feeling or sensation. Although the term is used for loss of tactile sensibility, or of any of the other senses, it is applied especially to loss of the sensation of pain, as it is induced to permit performance of surgery or other painful procedures. [EU] Analgesic: An agent that alleviates pain without causing loss of consciousness. [EU] Analog: In chemistry, a substance that is similar, but not identical, to another. [NIH] Analogous: Resembling or similar in some respects, as in function or appearance, but not in origin or development;. [EU] Anaphylatoxins: The family of peptides C3a, C4a, C5a, and C5a des-arginine produced in the serum during complement activation. They produce smooth muscle contraction, mast cell histamine release, affect platelet aggregation, and act as mediators of the local inflammatory process. The order of anaphylatoxin activity from strongest to weakest is C5a, C3a, C4a, and C5a des-arginine. The latter is the so-called "classical" anaphylatoxin but shows no spasmogenic activity though it contains some chemotactic ability. [NIH] Anatomical: Pertaining to anatomy, or to the structure of the organism. [EU] Androgens: A class of sex hormones associated with the development and maintenance of the secondary male sex characteristics, sperm induction, and sexual differentiation. In addition to increasing virility and libido, they also increase nitrogen and water retention and stimulate skeletal growth. [NIH] Anecdotal report: An incomplete description of the medical and treatment history of one or more patients. Anecdotal reports may be published in places other than peer-reviewed, scientific journals. [NIH] Anemia: A reduction in the number of circulating erythrocytes or in the quantity of hemoglobin. [NIH] Anergy: Absence of immune response to particular substances. [NIH] Anesthesia: A state characterized by loss of feeling or sensation. This depression of nerve function is usually the result of pharmacologic action and is induced to allow performance of surgery or other painful procedures. [NIH] Anesthetics: Agents that are capable of inducing a total or partial loss of sensation, especially tactile sensation and pain. They may act to induce general anesthesia, in which an unconscious state is achieved, or may act locally to induce numbness or lack of sensation at
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a targeted site. [NIH] Anginal: Pertaining to or characteristic of angina. [EU] Angiogenesis: Blood vessel formation. Tumor angiogenesis is the growth of blood vessels from surrounding tissue to a solid tumor. This is caused by the release of chemicals by the tumor. [NIH] Angiotensinogen: An alpha-globulin of which a fragment of 14 amino acids is converted by renin to angiotensin I, the inactive precursor of angiotensin II. It is a member of the serpin superfamily. [NIH] Animal model: An animal with a disease either the same as or like a disease in humans. Animal models are used to study the development and progression of diseases and to test new treatments before they are given to humans. Animals with transplanted human cancers or other tissues are called xenograft models. [NIH] Anions: Negatively charged atoms, radicals or groups of atoms which travel to the anode or positive pole during electrolysis. [NIH] Anode: Electrode held at a positive potential with respect to a cathode. [NIH] Antagonism: Interference with, or inhibition of, the growth of a living organism by another living organism, due either to creation of unfavorable conditions (e. g. exhaustion of food supplies) or to production of a specific antibiotic substance (e. g. penicillin). [NIH] Anterior Cruciate Ligament: A strong ligament of the knee that originates from the posteromedial portion of the lateral condyle of the femur, passes anteriorly and inferiorly between the condyles, and attaches to the depression in front of the intercondylar eminence of the tibia. [NIH] Antibacterial: A substance that destroys bacteria or suppresses their growth or reproduction. [EU] Antibiotic: A drug used to treat infections caused by bacteria and other microorganisms. [NIH]
Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the antigen that induced their synthesis in cells of the lymphoid series (especially plasma cells), or with an antigen closely related to it. [NIH] Antibody: A type of protein made by certain white blood cells in response to a foreign substance (antigen). Each antibody can bind to only a specific antigen. The purpose of this binding is to help destroy the antigen. Antibodies can work in several ways, depending on the nature of the antigen. Some antibodies destroy antigens directly. Others make it easier for white blood cells to destroy the antigen. [NIH] Anticholinergic: An agent that blocks the parasympathetic nerves. Called also parasympatholytic. [EU] Anticoagulant: A drug that helps prevent blood clots from forming. Also called a blood thinner. [NIH] Anticonvulsant: An agent that prevents or relieves convulsions. [EU] Antidepressant: A drug used to treat depression. [NIH] Antidote: A remedy for counteracting a poison. [EU] Antiemetic: An agent that prevents or alleviates nausea and vomiting. Also antinauseant. [EU]
Antifungal: Destructive to fungi, or suppressing their reproduction or growth; effective against fungal infections. [EU] Antifungal Agents: Substances that destroy fungi by suppressing their ability to grow or
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reproduce. They differ from fungicides, industrial because they defend against fungi present in human or animal tissues. [NIH] Antigen: Any substance which is capable, under appropriate conditions, of inducing a specific immune response and of reacting with the products of that response, that is, with specific antibody or specifically sensitized T-lymphocytes, or both. Antigens may be soluble substances, such as toxins and foreign proteins, or particulate, such as bacteria and tissue cells; however, only the portion of the protein or polysaccharide molecule known as the antigenic determinant (q.v.) combines with antibody or a specific receptor on a lymphocyte. Abbreviated Ag. [EU] Antigen-Antibody Complex: The complex formed by the binding of antigen and antibody molecules. The deposition of large antigen-antibody complexes leading to tissue damage causes immune complex diseases. [NIH] Antigen-presenting cell: APC. A cell that shows antigen on its surface to other cells of the immune system. This is an important part of an immune response. [NIH] Anti-infective: An agent that so acts. [EU] Anti-inflammatory: Having to do with reducing inflammation. [NIH] Anti-Inflammatory Agents: Substances that reduce or suppress inflammation. [NIH] Antimetabolite: A chemical that is very similar to one required in a normal biochemical reaction in cells. Antimetabolites can stop or slow down the reaction. [NIH] Antimetastatic: Having to do with reducing inflammation. [NIH] Antimicrobial: Killing microorganisms, or suppressing their multiplication or growth. [EU] Antineoplastic: Inhibiting or preventing the development of neoplasms, checking the maturation and proliferation of malignant cells. [EU] Antioxidant: A substance that prevents damage caused by free radicals. Free radicals are highly reactive chemicals that often contain oxygen. They are produced when molecules are split to give products that have unpaired electrons. This process is called oxidation. [NIH] Antiproliferative: Counteracting a process of proliferation. [EU] Antipruritic: Relieving or preventing itching. [EU] Antipyretic: An agent that relieves or reduces fever. Called also antifebrile, antithermic and febrifuge. [EU] Antiseptic: A substance that inhibits the growth and development of microorganisms without necessarily killing them. [EU] Antiserum: The blood serum obtained from an animal after it has been immunized with a particular antigen. It will contain antibodies which are specific for that antigen as well as antibodies specific for any other antigen with which the animal has previously been immunized. [NIH] Antitussive: An agent that relieves or prevents cough. [EU] Antiviral: Destroying viruses or suppressing their replication. [EU] Anxiety: Persistent feeling of dread, apprehension, and impending disaster. [NIH] Aorta: The main trunk of the systemic arteries. [NIH] Apolipoproteins: The protein components of lipoproteins which remain after the lipids to which the proteins are bound have been removed. They play an important role in lipid transport and metabolism. [NIH] Apoptosis: One of the two mechanisms by which cell death occurs (the other being the pathological process of necrosis). Apoptosis is the mechanism responsible for the
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physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA (DNA fragmentation) at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth. [NIH] Applicability: A list of the commodities to which the candidate method can be applied as presented or with minor modifications. [NIH] Aqueous: Having to do with water. [NIH] Arachidonate 12-Lipoxygenase: An enzyme that catalyzes the oxidation of arachidonic acid to yield 12-hydroperoxyarachidonate (12-HPETE) which is itself rapidly converted by a peroxidase to 12-hydroxy-5,8,10,14-eicosatetraenoate (12-HETE). The 12-hydroperoxides are preferentially formed in platelets. EC 1.13.11.31. [NIH] Arachidonate 15-Lipoxygenase: An enzyme that catalyzes the oxidation of arachidonic acid to yield 15-hydroperoxyarachidonate (15-HPETE) which is rapidly converted to 15-hydroxy5,8,11,13-eicosatetraenoate (15-HETE). The 15-hydroperoxides are preferentially formed in neutrophils and lymphocytes. EC 1.13.11.33. [NIH] Arachidonate Lipoxygenases: Enzymes catalyzing the oxidation of arachidonic acid to hydroperoxyarachidonates (HPETES). These products are then rapidly converted by a peroxidase to hydroxyeicosatetraenoic acids (HETES). The positional specificity of the enzyme reaction varies from tissue to tissue. The final lipoxygenase pathway leads to the leukotrienes. EC 1.13.11.- . [NIH] Arachidonic Acid: An unsaturated, essential fatty acid. It is found in animal and human fat as well as in the liver, brain, and glandular organs, and is a constituent of animal phosphatides. It is formed by the synthesis from dietary linoleic acid and is a precursor in the biosynthesis of prostaglandins, thromboxanes, and leukotrienes. [NIH] Arginine: An essential amino acid that is physiologically active in the L-form. [NIH] Aromatase: An enzyme which converts androgens to estrogens by desaturating ring A of the steroid. This enzyme complex is located in the endoplasmic reticulum of estrogenproducing cells including ovaries, placenta, testicular Sertoli and Leydig cells, adipose, and brain tissues. The enzyme complex has two components, one of which is the CYP19 gene product, the aromatase cytochrome P-450. The other component is NADPH-cytochrome P450 reductase which transfers reducing equivalents to P-450(arom). EC 1.14.13.-. [NIH] Aromatic: Having a spicy odour. [EU] Arterial: Pertaining to an artery or to the arteries. [EU] Arteries: The vessels carrying blood away from the heart. [NIH] Arterioles: The smallest divisions of the arteries located between the muscular arteries and the capillaries. [NIH] Arteriolosclerosis: Sclerosis and thickening of the walls of the smaller arteries (arterioles). Hyaline arteriolosclerosis, in which there is homogeneous pink hyaline thickening of the arteriolar walls, is associated with benign nephrosclerosis. Hyperplastic arteriolosclerosis, in which there is a concentric thickening with progressive narrowing of the lumina may be associated with malignant hypertension, nephrosclerosis, and scleroderma. [EU] Arteriosclerosis: Thickening and loss of elasticity of arterial walls. Atherosclerosis is the most common form of arteriosclerosis and involves lipid deposition and thickening of the intimal cell layers within arteries. Additional forms of arteriosclerosis involve calcification of the media of muscular arteries (Monkeberg medial calcific sclerosis) and thickening of the
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walls of small arteries or arterioles due to cell proliferation or hyaline deposition (arteriolosclerosis). [NIH] Arthroplasty: Surgical reconstruction of a joint to relieve pain or restore motion. [NIH] Arthroscopy: Endoscopic examination, therapy and surgery of the joint. [NIH] Arthrosis: A disease of a joint. [EU] Articular: Of or pertaining to a joint. [EU] Ascorbic Acid: A six carbon compound related to glucose. It is found naturally in citrus fruits and many vegetables. Ascorbic acid is an essential nutrient in human diets, and necessary to maintain connective tissue and bone. Its biologically active form, vitamin C, functions as a reducing agent and coenzyme in several metabolic pathways. Vitamin C is considered an antioxidant. [NIH] Aspergillosis: Infections with fungi of the genus Aspergillus. [NIH] Aspirin: A drug that reduces pain, fever, inflammation, and blood clotting. Aspirin belongs to the family of drugs called nonsteroidal anti-inflammatory agents. It is also being studied in cancer prevention. [NIH] Assay: Determination of the amount of a particular constituent of a mixture, or of the biological or pharmacological potency of a drug. [EU] Astrocytes: The largest and most numerous neuroglial cells in the brain and spinal cord. Astrocytes (from "star" cells) are irregularly shaped with many long processes, including those with "end feet" which form the glial (limiting) membrane and directly and indirectly contribute to the blood brain barrier. They regulate the extracellular ionic and chemical environment, and "reactive astrocytes" (along with microglia) respond to injury. Astrocytes have high- affinity transmitter uptake systems, voltage-dependent and transmitter-gated ion channels, and can release transmitter, but their role in signaling (as in many other functions) is not well understood. [NIH] Ataxia: Impairment of the ability to perform smoothly coordinated voluntary movements. This condition may affect the limbs, trunk, eyes, pharnyx, larnyx, and other structures. Ataxia may result from impaired sensory or motor function. Sensory ataxia may result from posterior column injury or peripheral nerve diseases. Motor ataxia may be associated with cerebellar diseases; cerebral cortex diseases; thalamic diseases; basal ganglia diseases; injury to the red nucleus; and other conditions. [NIH] Atherogenic: Causing the formation of plaque in the lining of the arteries. [NIH] ATP: ATP an abbreviation for adenosine triphosphate, a compound which serves as a carrier of energy for cells. [NIH] Atrophy: Decrease in the size of a cell, tissue, organ, or multiple organs, associated with a variety of pathological conditions such as abnormal cellular changes, ischemia, malnutrition, or hormonal changes. [NIH] Atropine: A toxic alkaloid, originally from Atropa belladonna, but found in other plants, mainly Solanaceae. [NIH] Attenuated: Strain with weakened or reduced virulence. [NIH] Attenuation: Reduction of transmitted sound energy or its electrical equivalent. [NIH] Avian: A plasmodial infection in birds. [NIH] Axillary: Pertaining to the armpit area, including the lymph nodes that are located there. [NIH]
Axillary Artery: The continuation of the subclavian artery; it distributes over the upper limb, axilla, chest and shoulder. [NIH]
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Bacteria: Unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. [NIH] Bacterial Physiology: Physiological processes and activities of bacteria. [NIH] Bacteriophage: A virus whose host is a bacterial cell; A virus that exclusively infects bacteria. It generally has a protein coat surrounding the genome (DNA or RNA). One of the coliphages most extensively studied is the lambda phage, which is also one of the most important. [NIH] Bacterium: Microscopic organism which may have a spherical, rod-like, or spiral unicellular or non-cellular body. Bacteria usually reproduce through asexual processes. [NIH] Basal Ganglia: Large subcortical nuclear masses derived from the telencephalon and located in the basal regions of the cerebral hemispheres. [NIH] Basal Ganglia Diseases: Diseases of the basal ganglia including the putamen; globus pallidus; claustrum; amygdala; and caudate nucleus. Dyskinesias (most notably involuntary movements and alterations of the rate of movement) represent the primary clinical manifestations of these disorders. Common etiologies include cerebrovascular disease; neurodegenerative diseases; and craniocerebral trauma. [NIH] Base: In chemistry, the nonacid part of a salt; a substance that combines with acids to form salts; a substance that dissociates to give hydroxide ions in aqueous solutions; a substance whose molecule or ion can combine with a proton (hydrogen ion); a substance capable of donating a pair of electrons (to an acid) for the formation of a coordinate covalent bond. [EU] Basement Membrane: Ubiquitous supportive tissue adjacent to epithelium and around smooth and striated muscle cells. This tissue contains intrinsic macromolecular components such as collagen, laminin, and sulfated proteoglycans. As seen by light microscopy one of its subdivisions is the basal (basement) lamina. [NIH] Basophils: Granular leukocytes characterized by a relatively pale-staining, lobate nucleus and cytoplasm containing coarse dark-staining granules of variable size and stainable by basic dyes. [NIH] Baths: The immersion or washing of the body or any of its parts in water or other medium for cleansing or medical treatment. It includes bathing for personal hygiene as well as for medical purposes with the addition of therapeutic agents, such as alkalines, antiseptics, oil, etc. [NIH] Behavioral Sciences: Disciplines concerned with the study of human and animal behavior. [NIH]
Belladonna: A species of very poisonous Solanaceous plants yielding atropine (hyoscyamine), scopolamine, and other belladonna alkaloids, used to block the muscarinic autonomic nervous system. [NIH] Benign: Not cancerous; does not invade nearby tissue or spread to other parts of the body. [NIH]
Benign tumor: A noncancerous growth that does not invade nearby tissue or spread to other parts of the body. [NIH] Benzene: Toxic, volatile, flammable liquid hydrocarbon biproduct of coal distillation. It is used as an industrial solvent in paints, varnishes, lacquer thinners, gasoline, etc. Benzene causes central nervous system damage acutely and bone marrow damage chronically and is carcinogenic. It was formerly used as parasiticide. [NIH] Benzocaine: A surface anesthetic that acts by preventing transmission of impulses along nerve fibers and at nerve endings. [NIH]
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Benzoic Acid: A fungistatic compound that is widely used as a food preservative. It is conjugated to glycine in the liver and excreted as hippuric acid. [NIH] Berberine: An alkaloid from Hydrastis canadensis L., Berberidaceae. It is also found in many other plants. It is relatively toxic parenterally, but has been used orally for various parasitic and fungal infections and as antidiarrheal. [NIH] Beta-Defensins: Defensins found mainly in epithelial cells. [NIH] Beta-glucans: Polysaccharides made by several types of mushrooms. Beta-glucans have been used to treat patients with gastric cancer and colorectal cancer. They may be able to stimulate the immune system. [NIH] Bewilderment: Impairment or loss of will power. [NIH] Bifidobacterium: A rod-shaped, gram-positive, non-acid-fast, non-spore-forming, nonmotile bacterium that is a genus of the family Actinomycetaceae. It inhabits the intestines and feces of humans as well as the human vagina. [NIH] Bile: An emulsifying agent produced in the liver and secreted into the duodenum. Its composition includes bile acids and salts, cholesterol, and electrolytes. It aids digestion of fats in the duodenum. [NIH] Bile Acids: Acids made by the liver that work with bile to break down fats. [NIH] Bile Acids and Salts: Steroid acids and salts. The primary bile acids are derived from cholesterol in the liver and usually conjugated with glycine or taurine. The secondary bile acids are further modified by bacteria in the intestine. They play an important role in the digestion and absorption of fat. They have also been used pharmacologically, especially in the treatment of gallstones. [NIH] Bile Ducts: Tubes that carry bile from the liver to the gallbladder for storage and to the small intestine for use in digestion. [NIH] Biliary: Having to do with the liver, bile ducts, and/or gallbladder. [NIH] Bilirubin: A bile pigment that is a degradation product of heme. [NIH] Binding Sites: The reactive parts of a macromolecule that directly participate in its specific combination with another molecule. [NIH] Bioavailability: The degree to which a drug or other substance becomes available to the target tissue after administration. [EU] Biochemical: Relating to biochemistry; characterized by, produced by, or involving chemical reactions in living organisms. [EU] Biofilms: Films of bacteria or other microbial organisms, usually embedded in extracellular polymers such as implanted medical devices, which adhere to surfaces submerged in, or subjected to, aquatic environments (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed). Biofilms consist of multilayers of microbial cells glued together to form microbial communities which are highly resistant to both phagocytes and antibiotics. [NIH] Biogenesis: The origin of life. It includes studies of the potential basis for life in organic compounds but excludes studies of the development of altered forms of life through mutation and natural selection, which is evolution. [NIH] Biological therapy: Treatment to stimulate or restore the ability of the immune system to fight infection and disease. Also used to lessen side effects that may be caused by some cancer treatments. Also known as immunotherapy, biotherapy, or biological response modifier (BRM) therapy. [NIH] Biological Transport: The movement of materials (including biochemical substances and
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drugs) across cell membranes and epithelial layers, usually by passive diffusion. [NIH] Biomass: Total mass of all the organisms of a given type and/or in a given area. (From Concise Dictionary of Biology, 1990) It includes the yield of vegetative mass produced from any given crop. [NIH] Biosynthesis: The building up of a chemical compound in the physiologic processes of a living organism. [EU] Biotechnology: Body of knowledge related to the use of organisms, cells or cell-derived constituents for the purpose of developing products which are technically, scientifically and clinically useful. Alteration of biologic function at the molecular level (i.e., genetic engineering) is a central focus; laboratory methods used include transfection and cloning technologies, sequence and structure analysis algorithms, computer databases, and gene and protein structure function analysis and prediction. [NIH] Biotin: Hexahydro-2-oxo-1H-thieno(3,4-d)imidazole-4-pentanoic acid. Growth factor present in minute amounts in every living cell. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk.The biotin content of cancerous tissue is higher than that of normal tissue. [NIH] Biotransformation: The chemical alteration of an exogenous substance by or in a biological system. The alteration may inactivate the compound or it may result in the production of an active metabolite of an inactive parent compound. The alteration may be either nonsynthetic (oxidation-reduction, hydrolysis) or synthetic (glucuronide formation, sulfate conjugation, acetylation, methylation). This also includes metabolic detoxication and clearance. [NIH] Bivalent: Pertaining to a group of 2 homologous or partly homologous chromosomes during the zygotene stage of prophase to the first metaphase in meiosis. [NIH] Bladder: The organ that stores urine. [NIH] Blast Crisis: Rapid increase in the proportion of blast cells in the blood and bone marrow. [NIH]
Blastocyst: The mammalian embryo in the post-morula stage in which a fluid-filled cavity, enclosed primarily by trophoblast, contains an inner cell mass which becomes the embryonic disc. [NIH] Blastomycosis: A fungal infection that may appear in two forms: 1) a primary lesion characterized by the formation of a small cutaneous nodule and small nodules along the lymphatics that may heal within several months; and 2) chronic granulomatous lesions characterized by thick crusts, warty growths, and unusual vascularity and infection in the middle or upper lobes of the lung. [NIH] Blasts: Immature blood cells. [NIH] Blood Coagulation: The process of the interaction of blood coagulation factors that results in an insoluble fibrin clot. [NIH] Blood Glucose: Glucose in blood. [NIH] Blood Platelets: Non-nucleated disk-shaped cells formed in the megakaryocyte and found in the blood of all mammals. They are mainly involved in blood coagulation. [NIH] Blood pressure: The pressure of blood against the walls of a blood vessel or heart chamber. Unless there is reference to another location, such as the pulmonary artery or one of the heart chambers, it refers to the pressure in the systemic arteries, as measured, for example, in the forearm. [NIH] Blood vessel: A tube in the body through which blood circulates. Blood vessels include a network of arteries, arterioles, capillaries, venules, and veins. [NIH]
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Body Fluids: Liquid components of living organisms. [NIH] Body Mass Index: One of the anthropometric measures of body mass; it has the highest correlation with skinfold thickness or body density. [NIH] Bolus: A single dose of drug usually injected into a blood vessel over a short period of time. Also called bolus infusion. [NIH] Bolus infusion: A single dose of drug usually injected into a blood vessel over a short period of time. Also called bolus. [NIH] Bone Density: The amount of mineral per square centimeter of bone. This is the definition used in clinical practice. Actual bone density would be expressed in grams per milliliter. It is most frequently measured by photon absorptiometry or x-ray computed tomography. [NIH] Bone Marrow: The soft tissue filling the cavities of bones. Bone marrow exists in two types, yellow and red. Yellow marrow is found in the large cavities of large bones and consists mostly of fat cells and a few primitive blood cells. Red marrow is a hematopoietic tissue and is the site of production of erythrocytes and granular leukocytes. Bone marrow is made up of a framework of connective tissue containing branching fibers with the frame being filled with marrow cells. [NIH] Bone Resorption: Bone loss due to osteoclastic activity. [NIH] Boron: A trace element with the atomic symbol B, atomic number 5, and atomic weight 10.81. Boron-10, an isotope of boron, is used as a neutron absorber in boron neutron capture therapy. [NIH] Boron Neutron Capture Therapy: A technique for the treatment of neoplasms, especially gliomas and melanomas in which boron-10, an isotope, is introduced into the target cells followed by irradiation with thermal neutrons. [NIH] Bowel: The long tube-shaped organ in the abdomen that completes the process of digestion. There is both a small and a large bowel. Also called the intestine. [NIH] Bowel Movement: Body wastes passed through the rectum and anus. [NIH] Brachial: All the nerves from the arm are ripped from the spinal cord. [NIH] Brachial Artery: The continuation of the axillary artery; it branches into the radial and ulnar arteries. [NIH] Brachytherapy: A collective term for interstitial, intracavity, and surface radiotherapy. It uses small sealed or partly-sealed sources that may be placed on or near the body surface or within a natural body cavity or implanted directly into the tissues. [NIH] Bradykinin: A nonapeptide messenger that is enzymatically produced from kallidin in the blood where it is a potent but short-lived agent of arteriolar dilation and increased capillary permeability. Bradykinin is also released from mast cells during asthma attacks, from gut walls as a gastrointestinal vasodilator, from damaged tissues as a pain signal, and may be a neurotransmitter. [NIH] Branch: Most commonly used for branches of nerves, but applied also to other structures. [NIH]
Breakdown: A physical, metal, or nervous collapse. [NIH] Broad-spectrum: Effective against a wide range of microorganisms; said of an antibiotic. [EU] Bronchi: The larger air passages of the lungs arising from the terminal bifurcation of the trachea. [NIH] Bronchial: Pertaining to one or more bronchi. [EU] Bronchiseptica: A small, gram-negative, motile bacillus. A normal inhabitant of the
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respiratory tract in man, dogs, and pigs, but is also associated with canine infectious tracheobronchitis and atrophic rhinitis in pigs. [NIH] Buccal: Pertaining to or directed toward the cheek. In dental anatomy, used to refer to the buccal surface of a tooth. [EU] Bupivacaine: A widely used local anesthetic agent. [NIH] Bursitis: Inflammation of a bursa, occasionally accompanied by a calcific deposit in the underlying supraspinatus tendon; the most common site is the subdeltoid bursa. [EU] Caffeine: A methylxanthine naturally occurring in some beverages and also used as a pharmacological agent. Caffeine's most notable pharmacological effect is as a central nervous system stimulant, increasing alertness and producing agitation. It also relaxes smooth muscle, stimulates cardiac muscle, stimulates diuresis, and appears to be useful in the treatment of some types of headache. Several cellular actions of caffeine have been observed, but it is not entirely clear how each contributes to its pharmacological profile. Among the most important are inhibition of cyclic nucleotide phosphodiesterases, antagonism of adenosine receptors, and modulation of intracellular calcium handling. [NIH] Calcification: Deposits of calcium in the tissues of the breast. Calcification in the breast can be seen on a mammogram, but cannot be detected by touch. There are two types of breast calcification, macrocalcification and microcalcification. Macrocalcifications are large deposits and are usually not related to cancer. Microcalcifications are specks of calcium that may be found in an area of rapidly dividing cells. Many microcalcifications clustered together may be a sign of cancer. [NIH] Calcium: A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. [NIH] Calcium channel blocker: A drug used to relax the blood vessel and heart muscle, causing pressure inside blood vessels to drop. It also can regulate heart rhythm. [NIH] Calcium Channel Blockers: A class of drugs that act by selective inhibition of calcium influx through cell membranes or on the release and binding of calcium in intracellular pools. Since they are inducers of vascular and other smooth muscle relaxation, they are used in the drug therapy of hypertension and cerebrovascular spasms, as myocardial protective agents, and in the relaxation of uterine spasms. [NIH] Calcium Chloride: A salt used to replenish calcium levels, as an acid-producing diuretic, and as an antidote for magnesium poisoning. [NIH] Calculi: An abnormal concretion occurring mostly in the urinary and biliary tracts, usually composed of mineral salts. Also called stones. [NIH] Callus: A callosity or hard, thick skin; the bone-like reparative substance that is formed round the edges and fragments of broken bone. [NIH] Caloric intake: Refers to the number of calories (energy content) consumed. [NIH] Camphor: A bicyclic monoterpene ketone found widely in plant (primarily the camphor tree, Cinnamomum camphora). Natural camphor is used topically as a skin antipruritic and as an anti-infective agent. [NIH] Cancer vaccine: A vaccine designed to prevent or treat cancer. [NIH] Candidiasis: Infection with a fungus of the genus Candida. It is usually a superficial infection of the moist cutaneous areas of the body, and is generally caused by C. albicans; it
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most commonly involves the skin (dermatocandidiasis), oral mucous membranes (thrush, def. 1), respiratory tract (bronchocandidiasis), and vagina (vaginitis). Rarely there is a systemic infection or endocarditis. Called also moniliasis, candidosis, oidiomycosis, and formerly blastodendriosis. [EU] Capillary: Any one of the minute vessels that connect the arterioles and venules, forming a network in nearly all parts of the body. Their walls act as semipermeable membranes for the interchange of various substances, including fluids, between the blood and tissue fluid; called also vas capillare. [EU] Capillary Permeability: Property of blood capillary walls that allows for the selective exchange of substances. Small lipid-soluble molecules such as carbon dioxide and oxygen move freely by diffusion. Water and water-soluble molecules cannot pass through the endothelial walls and are dependent on microscopic pores. These pores show narrow areas (tight junctions) which may limit large molecule movement. [NIH] Capsaicin: Cytotoxic alkaloid from various species of Capsicum (pepper, paprika), of the Solanaceae. [NIH] Capsular: Cataract which is initiated by an opacification at the surface of the lens. [NIH] Capsules: Hard or soft soluble containers used for the oral administration of medicine. [NIH] Carbamazepine: An anticonvulsant used to control grand mal and psychomotor or focal seizures. Its mode of action is not fully understood, but some of its actions resemble those of phenytoin; although there is little chemical resemblance between the two compounds, their three-dimensional structure is similar. [NIH] Carbenoxolone: An agent derived from licorice root. It is used for the treatment of digestive tract ulcers, especially in the stomach. Antidiuretic side effects are frequent, but otherwise the drug is low in toxicity. [NIH] Carbohydrate: An aldehyde or ketone derivative of a polyhydric alcohol, particularly of the pentahydric and hexahydric alcohols. They are so named because the hydrogen and oxygen are usually in the proportion to form water, (CH2O)n. The most important carbohydrates are the starches, sugars, celluloses, and gums. They are classified into mono-, di-, tri-, polyand heterosaccharides. [EU] Carbon Dioxide: A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals. [NIH] Carcinogenic: Producing carcinoma. [EU] Carcinogens: Substances that increase the risk of neoplasms in humans or animals. Both genotoxic chemicals, which affect DNA directly, and nongenotoxic chemicals, which induce neoplasms by other mechanism, are included. [NIH] Carcinoma: Cancer that begins in the skin or in tissues that line or cover internal organs. [NIH]
Cardiac: Having to do with the heart. [NIH] Cardiology: The study of the heart, its physiology, and its functions. [NIH] Cardiorespiratory: Relating to the heart and lungs and their function. [EU] Cardiovascular: Having to do with the heart and blood vessels. [NIH] Cardiovascular disease: Any abnormal condition characterized by dysfunction of the heart and blood vessels. CVD includes atherosclerosis (especially coronary heart disease, which can lead to heart attacks), cerebrovascular disease (e.g., stroke), and hypertension (high blood pressure). [NIH] Carotenoids: Substance found in yellow and orange fruits and vegetables and in dark green,
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leafy vegetables. May reduce the risk of developing cancer. [NIH] Case report: A detailed report of the diagnosis, treatment, and follow-up of an individual patient. Case reports also contain some demographic information about the patient (for example, age, gender, ethnic origin). [NIH] Castor Oil: Oil obtained from seeds of Ricinus communis that is used as a cathartic and as a plasticizer. [NIH] Catabolism: Any destructive metabolic process by which organisms convert substances into excreted compounds. [EU] Catecholamines: A general class of ortho-dihydroxyphenylalkylamines derived from tyrosine. [NIH] Catheterization: Use or insertion of a tubular device into a duct, blood vessel, hollow organ, or body cavity for injecting or withdrawing fluids for diagnostic or therapeutic purposes. It differs from intubation in that the tube here is used to restore or maintain patency in obstructions. [NIH] Catheters: A small, flexible tube that may be inserted into various parts of the body to inject or remove liquids. [NIH] Cathode: An electrode, usually an incandescent filament of tungsten, which emits electrons in an X-ray tube. [NIH] Cations: Postively charged atoms, radicals or groups of atoms which travel to the cathode or negative pole during electrolysis. [NIH] Caudal: Denoting a position more toward the cauda, or tail, than some specified point of reference; same as inferior, in human anatomy. [EU] Causal: Pertaining to a cause; directed against a cause. [EU] Cell: The individual unit that makes up all of the tissues of the body. All living things are made up of one or more cells. [NIH] Cell Adhesion: Adherence of cells to surfaces or to other cells. [NIH] Cell Cycle: The complex series of phenomena, occurring between the end of one cell division and the end of the next, by which cellular material is divided between daughter cells. [NIH] Cell Death: The termination of the cell's ability to carry out vital functions such as metabolism, growth, reproduction, responsiveness, and adaptability. [NIH] Cell Differentiation: Progressive restriction of the developmental potential and increasing specialization of function which takes place during the development of the embryo and leads to the formation of specialized cells, tissues, and organs. [NIH] Cell Division: The fission of a cell. [NIH] Cell membrane: Cell membrane = plasma membrane. The structure enveloping a cell, enclosing the cytoplasm, and forming a selective permeability barrier; it consists of lipids, proteins, and some carbohydrates, the lipids thought to form a bilayer in which integral proteins are embedded to varying degrees. [EU] Cell proliferation: An increase in the number of cells as a result of cell growth and cell division. [NIH] Cell Survival: The span of viability of a cell characterized by the capacity to perform certain functions such as metabolism, growth, reproduction, some form of responsiveness, and adaptability. [NIH] Cellobiose: A disaccharide consisting of two glucose units in beta (1-4) glycosidic linkage.
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Obtained from the partial hydrolysis of cellulose. [NIH] Cellular metabolism: The sum of all chemical changes that take place in a cell through which energy and basic components are provided for essential processes, including the synthesis of new molecules and the breakdown and removal of others. [NIH] Cellulase: An enzyme isolated from fungi and bacteria. It catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin, and cereal beta-glucans. EC 3.2.1.4. [NIH] Cellulose: A polysaccharide with glucose units linked as in cellobiose. It is the chief constituent of plant fibers, cotton being the purest natural form of the substance. As a raw material, it forms the basis for many derivatives used in chromatography, ion exchange materials, explosives manufacturing, and pharmaceutical preparations. [NIH] Central Nervous System: The main information-processing organs of the nervous system, consisting of the brain, spinal cord, and meninges. [NIH] Cerebellar: Pertaining to the cerebellum. [EU] Cerebral: Of or pertaining of the cerebrum or the brain. [EU] Cerebrovascular: Pertaining to the blood vessels of the cerebrum, or brain. [EU] Cerebrum: The largest part of the brain. It is divided into two hemispheres, or halves, called the cerebral hemispheres. The cerebrum controls muscle functions of the body and also controls speech, emotions, reading, writing, and learning. [NIH] Cetirizine: A potent second-generation histamine H1 antagonist that is effective in the treatment of allergic rhinitis, chronic urticaria, and pollen-induced asthma. Unlike many traditional antihistamines, it does not cause drowsiness or anticholinergic side effects. [NIH] Character: In current usage, approximately equivalent to personality. The sum of the relatively fixed personality traits and habitual modes of response of an individual. [NIH] Chemotactic Factors: Chemical substances that attract or repel cells or organisms. The concept denotes especially those factors released as a result of tissue injury, invasion, or immunologic activity, that attract leukocytes, macrophages, or other cells to the site of infection or insult. [NIH] Chemotherapy: Treatment with anticancer drugs. [NIH] Chenodeoxycholic Acid: A bile acid, usually conjugated with either glycine or taurine. It acts as a detergent to solubilize fats for intestinal absorption and is reabsorbed by the small intestine. It is used as cholagogue, a choleretic laxative, and to prevent or dissolve gallstones. [NIH] Chiropractic: A system of treating bodily disorders by manipulation of the spine and other parts, based on the belief that the cause is the abnormal functioning of a nerve. [NIH] Chitin Synthase: An enzyme that converts UDP glucosamine into chitin and UDP. EC 2.4.1.16. [NIH] Chlorambucil: An anticancer drug that belongs to the family of drugs called alkylating agents. [NIH] Chlorides: Inorganic compounds derived from hydrochloric acid that contain the Cl- ion. [NIH]
Chlorine: A greenish-yellow, diatomic gas that is a member of the halogen family of elements. It has the atomic symbol Cl, atomic number 17, and atomic weight 70.906. It is a powerful irritant that can cause fatal pulmonary edema. Chlorine is used in manufacturing, as a reagent in synthetic chemistry, for water purification, and in the production of chlorinated lime, which is used in fabric bleaching. [NIH] Chlorophyll: Porphyrin derivatives containing magnesium that act to convert light energy
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in photosynthetic organisms. [NIH] Cholecalciferol: An antirachitic oil-soluble vitamin. [NIH] Cholera: An acute diarrheal disease endemic in India and Southeast Asia whose causative agent is vibrio cholerae. This condition can lead to severe dehydration in a matter of hours unless quickly treated. [NIH] Cholera Toxin: The enterotoxin from Vibrio cholerae. It is a protein that consists of two major components, the heavy (H) or A peptide and the light (L) or B peptide or choleragenoid. The B peptide anchors the protein to intestinal epithelial cells, while the A peptide, enters the cytoplasm, and activates adenylate cyclase, and production of cAMP. Increased levels of cAMP are thought to modulate release of fluid and electrolytes from intestinal crypt cells. [NIH] Choleretic: A choleretic agent. [EU] Cholesterol: The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils. [NIH] Cholesterol Esters: Fatty acid esters of cholesterol which constitute about two-thirds of the cholesterol in the plasma. The accumulation of cholesterol esters in the arterial intima is a characteristic feature of atherosclerosis. [NIH] Cholinergic: Resembling acetylcholine in pharmacological action; stimulated by or releasing acetylcholine or a related compound. [EU] Chondroitin sulfate: The major glycosaminoglycan (a type of sugar molecule) in cartilage. [NIH]
Chromatin: The material of chromosomes. It is a complex of DNA, histones, and nonhistone proteins (chromosomal proteins, non-histone) found within the nucleus of a cell. [NIH] Chromosomal: Pertaining to chromosomes. [EU] Chromosome: Part of a cell that contains genetic information. Except for sperm and eggs, all human cells contain 46 chromosomes. [NIH] Chronic: A disease or condition that persists or progresses over a long period of time. [NIH] Chronic Disease: Disease or ailment of long duration. [NIH] Chronic granulocytic leukemia: A slowly progressing disease in which too many white blood cells are made in the bone marrow. Also called chronic myelogenous leukemia or chronic myeloid leukemia. [NIH] Chronic myelogenous leukemia: CML. A slowly progressing disease in which too many white blood cells are made in the bone marrow. Also called chronic myeloid leukemia or chronic granulocytic leukemia. [NIH] Chronic renal: Slow and progressive loss of kidney function over several years, often resulting in end-stage renal disease. People with end-stage renal disease need dialysis or transplantation to replace the work of the kidneys. [NIH] Chylomicrons: A class of lipoproteins that carry dietary cholesterol and triglycerides from the small intestines to the tissues. [NIH] Cimetidine: A histamine congener, it competitively inhibits histamine binding to H2 receptors. Cimetidine has a range of pharmacological actions. It inhibits gastric acid secretion, as well as pepsin and gastrin output. It also blocks the activity of cytochrome P450. [NIH] CIS: Cancer Information Service. The CIS is the National Cancer Institute's link to the public, interpreting and explaining research findings in a clear and understandable manner, and providing personalized responses to specific questions about cancer. Access the CIS by
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calling 1-800-4-CANCER, or by using the Web site at http://cis.nci.nih.gov. [NIH] Citric Acid: A key intermediate in metabolism. It is an acid compound found in citrus fruits. The salts of citric acid (citrates) can be used as anticoagulants due to their calcium chelating ability. [NIH] Citrus: Any tree or shrub of the Rue family or the fruit of these plants. [NIH] Clamp: A u-shaped steel rod used with a pin or wire for skeletal traction in the treatment of certain fractures. [NIH] Clinical Medicine: The study and practice of medicine by direct examination of the patient. [NIH]
Clinical study: A research study in which patients receive treatment in a clinic or other medical facility. Reports of clinical studies can contain results for single patients (case reports) or many patients (case series or clinical trials). [NIH] Clinical trial: A research study that tests how well new medical treatments or other interventions work in people. Each study is designed to test new methods of screening, prevention, diagnosis, or treatment of a disease. [NIH] Clone: The term "clone" has acquired a new meaning. It is applied specifically to the bits of inserted foreign DNA in the hybrid molecules of the population. Each inserted segment originally resided in the DNA of a complex genome amid millions of other DNA segment. [NIH]
Cloning: The production of a number of genetically identical individuals; in genetic engineering, a process for the efficient replication of a great number of identical DNA molecules. [NIH] Coagulation: 1. The process of clot formation. 2. In colloid chemistry, the solidification of a sol into a gelatinous mass; an alteration of a disperse phase or of a dissolved solid which causes the separation of the system into a liquid phase and an insoluble mass called the clot or curd. Coagulation is usually irreversible. 3. In surgery, the disruption of tissue by physical means to form an amorphous residuum, as in electrocoagulation and photocoagulation. [EU] Coal: A natural fuel formed by partial decomposition of vegetable matter under certain environmental conditions. [NIH] Coal Tar: A by-product of the destructive distillation of coal used as a topical antieczematic. It is an antipruritic and keratoplastic agent used also in the treatment of psoriasis and other skin conditions. Occupational exposure to soots, tars, and certain mineral oils is known to be carcinogenic according to the Fourth Annual Report on Carcinogens (NTP 85-002, 1985) (Merck Index, 11th ed). [NIH] Codons: Any triplet of nucleotides (coding unit) in DNA or RNA (if RNA is the carrier of primary genetic information as in some viruses) that codes for particular amino acid or signals the beginning or end of the message. [NIH] Coenzyme: An organic nonprotein molecule, frequently a phosphorylated derivative of a water-soluble vitamin, that binds with the protein molecule (apoenzyme) to form the active enzyme (holoenzyme). [EU] Cofactor: A substance, microorganism or environmental factor that activates or enhances the action of another entity such as a disease-causing agent. [NIH] Colitis: Inflammation of the colon. [NIH] Collagen: A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of skin, connective tissue, and the organic substance of bones and teeth. Different forms of collagen are produced in the body but all
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consist of three alpha-polypeptide chains arranged in a triple helix. Collagen is differentiated from other fibrous proteins, such as elastin, by the content of proline, hydroxyproline, and hydroxylysine; by the absence of tryptophan; and particularly by the high content of polar groups which are responsible for its swelling properties. [NIH] Collapse: 1. A state of extreme prostration and depression, with failure of circulation. 2. Abnormal falling in of the walls of any part of organ. [EU] Colloidal: Of the nature of a colloid. [EU] Colorectal: Having to do with the colon or the rectum. [NIH] Combinatorial: A cut-and-paste process that churns out thousands of potentially valuable compounds at once. [NIH] Communis: Common tendon of the rectus group of muscles that surrounds the optic foramen and a portion of the superior orbital fissure, to the anterior margin of which it is attached at the spina recti lateralis. [NIH] Competency: The capacity of the bacterium to take up DNA from its surroundings. [NIH] Complement: A term originally used to refer to the heat-labile factor in serum that causes immune cytolysis, the lysis of antibody-coated cells, and now referring to the entire functionally related system comprising at least 20 distinct serum proteins that is the effector not only of immune cytolysis but also of other biologic functions. Complement activation occurs by two different sequences, the classic and alternative pathways. The proteins of the classic pathway are termed 'components of complement' and are designated by the symbols C1 through C9. C1 is a calcium-dependent complex of three distinct proteins C1q, C1r and C1s. The proteins of the alternative pathway (collectively referred to as the properdin system) and complement regulatory proteins are known by semisystematic or trivial names. Fragments resulting from proteolytic cleavage of complement proteins are designated with lower-case letter suffixes, e.g., C3a. Inactivated fragments may be designated with the suffix 'i', e.g. C3bi. Activated components or complexes with biological activity are designated by a bar over the symbol e.g. C1 or C4b,2a. The classic pathway is activated by the binding of C1 to classic pathway activators, primarily antigen-antibody complexes containing IgM, IgG1, IgG3; C1q binds to a single IgM molecule or two adjacent IgG molecules. The alternative pathway can be activated by IgA immune complexes and also by nonimmunologic materials including bacterial endotoxins, microbial polysaccharides, and cell walls. Activation of the classic pathway triggers an enzymatic cascade involving C1, C4, C2 and C3; activation of the alternative pathway triggers a cascade involving C3 and factors B, D and P. Both result in the cleavage of C5 and the formation of the membrane attack complex. Complement activation also results in the formation of many biologically active complement fragments that act as anaphylatoxins, opsonins, or chemotactic factors. [EU] Complementary and alternative medicine: CAM. Forms of treatment that are used in addition to (complementary) or instead of (alternative) standard treatments. These practices are not considered standard medical approaches. CAM includes dietary supplements, megadose vitamins, herbal preparations, special teas, massage therapy, magnet therapy, spiritual healing, and meditation. [NIH] Complementary medicine: Practices not generally recognized by the medical community as standard or conventional medical approaches and used to enhance or complement the standard treatments. Complementary medicine includes the taking of dietary supplements, megadose vitamins, and herbal preparations; the drinking of special teas; and practices such as massage therapy, magnet therapy, spiritual healing, and meditation. [NIH] Complementation: The production of a wild-type phenotype when two different mutations are combined in a diploid or a heterokaryon and tested in trans-configuration. [NIH]
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Complete remission: The disappearance of all signs of cancer. Also called a complete response. [NIH] Computational Biology: A field of biology concerned with the development of techniques for the collection and manipulation of biological data, and the use of such data to make biological discoveries or predictions. This field encompasses all computational methods and theories applicable to molecular biology and areas of computer-based techniques for solving biological problems including manipulation of models and datasets. [NIH] Concomitant: Accompanying; accessory; joined with another. [EU] Confusion: A mental state characterized by bewilderment, emotional disturbance, lack of clear thinking, and perceptual disorientation. [NIH] Conjugated: Acting or operating as if joined; simultaneous. [EU] Conjugation: 1. The act of joining together or the state of being conjugated. 2. A sexual process seen in bacteria, ciliate protozoa, and certain fungi in which nuclear material is exchanged during the temporary fusion of two cells (conjugants). In bacterial genetics a form of sexual reproduction in which a donor bacterium (male) contributes some, or all, of its DNA (in the form of a replicated set) to a recipient (female) which then incorporates differing genetic information into its own chromosome by recombination and passes the recombined set on to its progeny by replication. In ciliate protozoa, two conjugants of separate mating types exchange micronuclear material and then separate, each now being a fertilized cell. In certain fungi, the process involves fusion of two gametes, resulting in union of their nuclei and formation of a zygote. 3. In chemistry, the joining together of two compounds to produce another compound, such as the combination of a toxic product with some substance in the body to form a detoxified product, which is then eliminated. [EU] Conjunctiva: The mucous membrane that lines the inner surface of the eyelids and the anterior part of the sclera. [NIH] Connective Tissue: Tissue that supports and binds other tissues. It consists of connective tissue cells embedded in a large amount of extracellular matrix. [NIH] Connective Tissue: Tissue that supports and binds other tissues. It consists of connective tissue cells embedded in a large amount of extracellular matrix. [NIH] Connective Tissue Cells: A group of cells that includes fibroblasts, cartilage cells, adipocytes, smooth muscle cells, and bone cells. [NIH] Connective Tissue Diseases: A heterogeneous group of disorders, some hereditary, others acquired, characterized by abnormal structure or function of one or more of the elements of connective tissue, i.e., collagen, elastin, or the mucopolysaccharides. [NIH] Consciousness: Sense of awareness of self and of the environment. [NIH] Constipation: Infrequent or difficult evacuation of feces. [NIH] Consultation: A deliberation between two or more physicians concerning the diagnosis and the proper method of treatment in a case. [NIH] Consumption: Pulmonary tuberculosis. [NIH] Contracture: A condition of fixed high resistance to passive stretch of a muscle, resulting from fibrosis of the tissues supporting the muscles or the joints, or from disorders of the muscle fibres. [EU] Contraindications: Any factor or sign that it is unwise to pursue a certain kind of action or treatment, e. g. giving a general anesthetic to a person with pneumonia. [NIH] Control group: In a clinical trial, the group that does not receive the new treatment being studied. This group is compared to the group that receives the new treatment, to see if the
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new treatment works. [NIH] Controlled clinical trial: A clinical study that includes a comparison (control) group. The comparison group receives a placebo, another treatment, or no treatment at all. [NIH] Controlled study: An experiment or clinical trial that includes a comparison (control) group. [NIH]
Coordination: Muscular or motor regulation or the harmonious cooperation of muscles or groups of muscles, in a complex action or series of actions. [NIH] Cornea: The transparent part of the eye that covers the iris and the pupil and allows light to enter the inside. [NIH] Corneum: The superficial layer of the epidermis containing keratinized cells. [NIH] Coronary: Encircling in the manner of a crown; a term applied to vessels; nerves, ligaments, etc. The term usually denotes the arteries that supply the heart muscle and, by extension, a pathologic involvement of them. [EU] Coronary heart disease: A type of heart disease caused by narrowing of the coronary arteries that feed the heart, which needs a constant supply of oxygen and nutrients carried by the blood in the coronary arteries. When the coronary arteries become narrowed or clogged by fat and cholesterol deposits and cannot supply enough blood to the heart, CHD results. [NIH] Coronary Thrombosis: Presence of a thrombus in a coronary artery, often causing a myocardial infarction. [NIH] Cortex: The outer layer of an organ or other body structure, as distinguished from the internal substance. [EU] Corticosteroids: Hormones that have antitumor activity in lymphomas and lymphoid leukemias; in addition, corticosteroids (steroids) may be used for hormone replacement and for the management of some of the complications of cancer and its treatment. [NIH] Coumarin: A fluorescent dye. [NIH] Coumestrol: A coumarin derivative occurring naturally in forage crops which has estrogenic activity. [NIH] Cranial: Pertaining to the cranium, or to the anterior (in animals) or superior (in humans) end of the body. [EU] Creatine: An amino acid that occurs in vertebrate tissues and in urine. In muscle tissue, creatine generally occurs as phosphocreatine. Creatine is excreted as creatinine in the urine. [NIH]
Creatinine: A compound that is excreted from the body in urine. Creatinine levels are measured to monitor kidney function. [NIH] Cromolyn Sodium: A chromone complex that acts by inhibiting the release of chemical mediators from sensitized mast cells. It is used in the prophylactic treatment of both allergic and exercise-induced asthma, but does not affect an established asthmatic attack. [NIH] Crystallins: A heterogeneous family of water-soluble structural proteins found in cells of the vertebrate lens. The presence of these proteins accounts for the transparency of the lens. The family is composed of four major groups, alpha, beta, gamma, and delta, and several minor groups, which are classed on the basis of size, charge, immunological properties, and vertebrate source. Alpha, beta, and delta crystallins occur in avian and reptilian lenses, while alpha, beta, and gamma crystallins occur in all other lenses. [NIH] Curare: Plant extracts from several species, including Strychnos toxifera, S. castelnaei, S. crevauxii, and Chondodendron tomentosum, that produce paralysis of skeletal muscle and
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are used adjunctively with general anesthesia. These extracts are toxic and must be used with the administration of artificial respiration. [NIH] Curative: Tending to overcome disease and promote recovery. [EU] Curcumin: A dye obtained from tumeric, the powdered root of Curcuma longa Linn. It is used in the preparation of curcuma paper and the detection of boron. Curcumin appears to possess a spectrum of pharmacological properties, due primarily to its inhibitory effects on metabolic enzymes. [NIH] Cutaneous: Having to do with the skin. [NIH] Cyanide: An extremely toxic class of compounds that can be lethal on inhaling of ingesting in minute quantities. [NIH] Cyclic: Pertaining to or occurring in a cycle or cycles; the term is applied to chemical compounds that contain a ring of atoms in the nucleus. [EU] Cyclosporine: A drug used to help reduce the risk of rejection of organ and bone marrow transplants by the body. It is also used in clinical trials to make cancer cells more sensitive to anticancer drugs. [NIH] Cyst: A sac or capsule filled with fluid. [NIH] Cysteine: A thiol-containing non-essential amino acid that is oxidized to form cystine. [NIH] Cystine: A covalently linked dimeric nonessential amino acid formed by the oxidation of cysteine. Two molecules of cysteine are joined together by a disulfide bridge to form cystine. [NIH]
Cystitis: Inflammation of the urinary bladder. [EU] Cytochrome: Any electron transfer hemoprotein having a mode of action in which the transfer of a single electron is effected by a reversible valence change of the central iron atom of the heme prosthetic group between the +2 and +3 oxidation states; classified as cytochromes a in which the heme contains a formyl side chain, cytochromes b, which contain protoheme or a closely similar heme that is not covalently bound to the protein, cytochromes c in which protoheme or other heme is covalently bound to the protein, and cytochromes d in which the iron-tetrapyrrole has fewer conjugated double bonds than the hemes have. Well-known cytochromes have been numbered consecutively within groups and are designated by subscripts (beginning with no subscript), e.g. cytochromes c, c1, C2, . New cytochromes are named according to the wavelength in nanometres of the absorption maximum of the a-band of the iron (II) form in pyridine, e.g., c-555. [EU] Cytokine: Small but highly potent protein that modulates the activity of many cell types, including T and B cells. [NIH] Cytomegalovirus: A genus of the family Herpesviridae, subfamily Betaherpesvirinae, infecting the salivary glands, liver, spleen, lungs, eyes, and other organs, in which they produce characteristically enlarged cells with intranuclear inclusions. Infection with Cytomegalovirus is also seen as an opportunistic infection in AIDS. [NIH] Cytoplasm: The protoplasm of a cell exclusive of that of the nucleus; it consists of a continuous aqueous solution (cytosol) and the organelles and inclusions suspended in it (phaneroplasm), and is the site of most of the chemical activities of the cell. [EU] Cytotoxic: Cell-killing. [NIH] Cytotoxicity: Quality of being capable of producing a specific toxic action upon cells of special organs. [NIH] Databases, Bibliographic: Extensive collections, reputedly complete, of references and citations to books, articles, publications, etc., generally on a single subject or specialized
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subject area. Databases can operate through automated files, libraries, or computer disks. The concept should be differentiated from factual databases which is used for collections of data and facts apart from bibliographic references to them. [NIH] Deamination: The removal of an amino group (NH2) from a chemical compound. [NIH] Decarboxylation: The removal of a carboxyl group, usually in the form of carbon dioxide, from a chemical compound. [NIH] Decidua: The epithelial lining of the endometrium that is formed before the fertilized ovum reaches the uterus. The fertilized ovum embeds in the decidua. If the ovum is not fertilized, the decidua is shed during menstruation. [NIH] Defensins: Family of antimicrobial peptides that have been identified in humans, animals, and plants. They are thought to play a role in host defenses against infections, inflammation, wound repair, and acquired immunity. Based on the disulfide pairing of their characteristic six cysteine residues, they are divided into alpha-defensins and beta-defensins. [NIH] Degenerative: Undergoing degeneration : tending to degenerate; having the character of or involving degeneration; causing or tending to cause degeneration. [EU] Dehydration: The condition that results from excessive loss of body water. [NIH] Deletion: A genetic rearrangement through loss of segments of DNA (chromosomes), bringing sequences, which are normally separated, into close proximity. [NIH] Dendrites: Extensions of the nerve cell body. They are short and branched and receive stimuli from other neurons. [NIH] Dendritic: 1. Branched like a tree. 2. Pertaining to or possessing dendrites. [EU] Dendritic cell: A special type of antigen-presenting cell (APC) that activates T lymphocytes. [NIH]
Density: The logarithm to the base 10 of the opacity of an exposed and processed film. [NIH] Dentate Gyrus: Gray matter situated above the gyrus hippocampi. It is composed of three layers. The molecular layer is continuous with the hippocampus in the hippocampal fissure. The granular layer consists of closely arranged spherical or oval neurons, called granule cells, whose axons pass through the polymorphic layer ending on the dendrites of pyramidal cells in the hippocampus. [NIH] Dentifrices: Any preparations used for cleansing teeth; they usually contain an abrasive, detergent, binder and flavoring agent and may exist in the form of liquid, paste or powder; may also contain medicaments and caries preventives. [NIH] Deoxyglucose: 2-Deoxy-D-arabino-hexose. An antimetabolite of glucose with antiviral activity. [NIH] Deoxyribonucleic: A polymer of subunits called deoxyribonucleotides which is the primary genetic material of a cell, the material equivalent to genetic information. [NIH] Deoxyribonucleic acid: A polymer of subunits called deoxyribonucleotides which is the primary genetic material of a cell, the material equivalent to genetic information. [NIH] Depolarization: The process or act of neutralizing polarity. In neurophysiology, the reversal of the resting potential in excitable cell membranes when stimulated, i.e., the tendency of the cell membrane potential to become positive with respect to the potential outside the cell. [EU] Depressive Disorder: An affective disorder manifested by either a dysphoric mood or loss of interest or pleasure in usual activities. The mood disturbance is prominent and relatively persistent. [NIH] Dermal: Pertaining to or coming from the skin. [NIH]
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Dermatitis: Any inflammation of the skin. [NIH] Desensitization: The prevention or reduction of immediate hypersensitivity reactions by administration of graded doses of allergen; called also hyposensitization and immunotherapy. [EU] Detoxification: Treatment designed to free an addict from his drug habit. [EU] Deuterium: Deuterium. The stable isotope of hydrogen. It has one neutron and one proton in the nucleus. [NIH] Diabetes Mellitus: A heterogeneous group of disorders that share glucose intolerance in common. [NIH] Diagnostic procedure: A method used to identify a disease. [NIH] Dialyzer: A part of the hemodialysis machine. (See hemodialysis under dialysis.) The dialyzer has two sections separated by a membrane. One section holds dialysate. The other holds the patient's blood. [NIH] Diarrhea: Passage of excessively liquid or excessively frequent stools. [NIH] Diastolic: Of or pertaining to the diastole. [EU] Diencephalon: The paired caudal parts of the prosencephalon from which the thalamus, hypothalamus, epithalamus, and subthalamus are derived. [NIH] Dietary Fats: Fats present in food, especially in animal products such as meat, meat products, butter, ghee. They are present in lower amounts in nuts, seeds, and avocados. [NIH]
Diffusion: The tendency of a gas or solute to pass from a point of higher pressure or concentration to a point of lower pressure or concentration and to distribute itself throughout the available space; a major mechanism of biological transport. [NIH] Digestion: The process of breakdown of food for metabolism and use by the body. [NIH] Digestive system: The organs that take in food and turn it into products that the body can use to stay healthy. Waste products the body cannot use leave the body through bowel movements. The digestive system includes the salivary glands, mouth, esophagus, stomach, liver, pancreas, gallbladder, small and large intestines, and rectum. [NIH] Digestive tract: The organs through which food passes when food is eaten. These organs are the mouth, esophagus, stomach, small and large intestines, and rectum. [NIH] Dihydroxy: AMPA/Kainate antagonist. [NIH] Dilatation: The act of dilating. [NIH] Dilator: A device used to stretch or enlarge an opening. [NIH] Dimerization: The process by which two molecules of the same chemical composition form a condensation product or polymer. [NIH] Dimethyl: A volatile metabolite of the amino acid methionine. [NIH] Diphenhydramine: A histamine H1 antagonist used as an antiemetic, antitussive, for dermatoses and pruritus, for hypersensitivity reactions, as a hypnotic, an antiparkinson, and as an ingredient in common cold preparations. It has some undesired antimuscarinic and sedative effects. [NIH] Diploid: Having two sets of chromosomes. [NIH] Direct: 1. Straight; in a straight line. 2. Performed immediately and without the intervention of subsidiary means. [EU] Disease Progression: The worsening of a disease over time. This concept is most often used
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for chronic and incurable diseases where the stage of the disease is an important determinant of therapy and prognosis. [NIH] Disinfection: Rendering pathogens harmless through the use of heat, antiseptics, antibacterial agents, etc. [NIH] Disorientation: The loss of proper bearings, or a state of mental confusion as to time, place, or identity. [EU] Dissociation: 1. The act of separating or state of being separated. 2. The separation of a molecule into two or more fragments (atoms, molecules, ions, or free radicals) produced by the absorption of light or thermal energy or by solvation. 3. In psychology, a defense mechanism in which a group of mental processes are segregated from the rest of a person's mental activity in order to avoid emotional distress, as in the dissociative disorders (q.v.), or in which an idea or object is segregated from its emotional significance; in the first sense it is roughly equivalent to splitting, in the second, to isolation. 4. A defect of mental integration in which one or more groups of mental processes become separated off from normal consciousness and, thus separated, function as a unitary whole. [EU] Distal: Remote; farther from any point of reference; opposed to proximal. In dentistry, used to designate a position on the dental arch farther from the median line of the jaw. [EU] Diuresis: Increased excretion of urine. [EU] Diuretic: A drug that increases the production of urine. [NIH] DNA Topoisomerase: An enzyme catalyzing ATP-independent breakage of single-stranded DNA, followed by passage and rejoining of another single-stranded DNA. This enzyme class brings about the conversion of one topological isomer of DNA into another, e.g., the relaxation of superhelical turns in DNA, the interconversion of simple and knotted rings of single-stranded DNA, and the intertwisting of single-stranded rings of complementary sequences. (From Enzyme Nomenclature, 1992) EC 5.99.1.2. [NIH] Domesticated: Species in which the evolutionary process has been influenced by humans to meet their needs. [NIH] Dopamine: An endogenous catecholamine and prominent neurotransmitter in several systems of the brain. In the synthesis of catecholamines from tyrosine, it is the immediate precursor to norepinephrine and epinephrine. Dopamine is a major transmitter in the extrapyramidal system of the brain, and important in regulating movement. A family of dopaminergic receptor subtypes mediate its action. Dopamine is used pharmacologically for its direct (beta adrenergic agonist) and indirect (adrenergic releasing) sympathomimetic effects including its actions as an inotropic agent and as a renal vasodilator. [NIH] Dorsal: 1. Pertaining to the back or to any dorsum. 2. Denoting a position more toward the back surface than some other object of reference; same as posterior in human anatomy; superior in the anatomy of quadrupeds. [EU] Dosage Forms: Completed forms of the pharmaceutical preparation in which prescribed doses of medication are included. They are designed to resist action by gastric fluids, prevent vomiting and nausea, reduce or alleviate the undesirable taste and smells associated with oral administration, achieve a high concentration of drug at target site, or produce a delayed or long-acting drug effect. They include capsules, liniments, ointments, pharmaceutical solutions, powders, tablets, etc. [NIH] Double-blinded: A clinical trial in which neither the medical staff nor the person knows which of several possible therapies the person is receiving. [NIH] Drug Interactions: The action of a drug that may affect the activity, metabolism, or toxicity of another drug. [NIH]
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Drug Tolerance: Progressive diminution of the susceptibility of a human or animal to the effects of a drug, resulting from its continued administration. It should be differentiated from drug resistance wherein an organism, disease, or tissue fails to respond to the intended effectiveness of a chemical or drug. It should also be differentiated from maximum tolerated dose and no-observed-adverse-effect level. [NIH] Duct: A tube through which body fluids pass. [NIH] Duodenal Ulcer: An ulcer in the lining of the first part of the small intestine (duodenum). [NIH]
Duodenum: The first part of the small intestine. [NIH] Dyes: Chemical substances that are used to stain and color other materials. The coloring may or may not be permanent. Dyes can also be used as therapeutic agents and test reagents in medicine and scientific research. [NIH] Dysplasia: Cells that look abnormal under a microscope but are not cancer. [NIH] Dystrophy: Any disorder arising from defective or faulty nutrition, especially the muscular dystrophies. [EU] Echinacea: A genus of perennial herbs used topically and internally. It contains echinacoside, glycosides, inulin, isobutyl amides, resin, and sesquiterpenes. [NIH] Ectoderm: The outer of the three germ layers of the embryo. [NIH] Eczema: A pruritic papulovesicular dermatitis occurring as a reaction to many endogenous and exogenous agents (Dorland, 27th ed). [NIH] Effector: It is often an enzyme that converts an inactive precursor molecule into an active second messenger. [NIH] Efficacy: The extent to which a specific intervention, procedure, regimen, or service produces a beneficial result under ideal conditions. Ideally, the determination of efficacy is based on the results of a randomized control trial. [NIH] Elasticity: Resistance and recovery from distortion of shape. [NIH] Elastin: The protein that gives flexibility to tissues. [NIH] Elective: Subject to the choice or decision of the patient or physician; applied to procedures that are advantageous to the patient but not urgent. [EU] Electrocoagulation: Electrosurgical procedures used to treat hemorrhage (e.g., bleeding ulcers) and to ablate tumors, mucosal lesions, and refractory arrhythmias. [NIH] Electrolysis: Destruction by passage of a galvanic electric current, as in disintegration of a chemical compound in solution. [NIH] Electrolyte: A substance that dissociates into ions when fused or in solution, and thus becomes capable of conducting electricity; an ionic solute. [EU] Electrons: Stable elementary particles having the smallest known negative charge, present in all elements; also called negatrons. Positively charged electrons are called positrons. The numbers, energies and arrangement of electrons around atomic nuclei determine the chemical identities of elements. Beams of electrons are called cathode rays or beta rays, the latter being a high-energy biproduct of nuclear decay. [NIH] Electroplating: Coating with a metal or alloy by electrolysis. [NIH] Electroporation: A technique in which electric pulses of intensity in kilovolts per centimeter and of microsecond-to-millisecond duration cause a temporary loss of the semipermeability of cell membranes, thus leading to ion leakage, escape of metabolites, and increased uptake by cells of drugs, molecular probes, and DNA. Some applications of electroporation include
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introduction of plasmids or foreign DNA into living cells for transfection, fusion of cells to prepare hybridomas, and insertion of proteins into cell membranes. [NIH] Embryo: The prenatal stage of mammalian development characterized by rapid morphological changes and the differentiation of basic structures. [NIH] Embryogenesis: The process of embryo or embryoid formation, whether by sexual (zygotic) or asexual means. In asexual embryogenesis embryoids arise directly from the explant or on intermediary callus tissue. In some cases they arise from individual cells (somatic cell embryoge). [NIH] Emollient: Softening or soothing; called also malactic. [EU] Emulsions: Colloids of two immiscible liquids where either phase may be either fatty or aqueous; lipid-in-water emulsions are usually liquid, like milk or lotion and water-in-lipid emulsions tend to be creams. [NIH] Enamel: A very hard whitish substance which covers the dentine of the anatomical crown of a tooth. [NIH] Encephalopathy: A disorder of the brain that can be caused by disease, injury, drugs, or chemicals. [NIH] Endemic: Present or usually prevalent in a population or geographical area at all times; said of a disease or agent. Called also endemial. [EU] Endothelial cell: The main type of cell found in the inside lining of blood vessels, lymph vessels, and the heart. [NIH] Endothelium: A layer of epithelium that lines the heart, blood vessels (endothelium, vascular), lymph vessels (endothelium, lymphatic), and the serous cavities of the body. [NIH] Endothelium-derived: Small molecule that diffuses to the adjacent muscle layer and relaxes it. [NIH] Endotoxic: Of, relating to, or acting as an endotoxin (= a heat-stable toxin, associated with the outer membranes of certain gram-negative bacteria. Endotoxins are not secreted and are released only when the cells are disrupted). [EU] Endotoxin: Toxin from cell walls of bacteria. [NIH] End-stage renal: Total chronic kidney failure. When the kidneys fail, the body retains fluid and harmful wastes build up. A person with ESRD needs treatment to replace the work of the failed kidneys. [NIH] Enhancer: Transcriptional element in the virus genome. [NIH] Entorhinal Cortex: Cortex where the signals are combined with those from other sensory systems. [NIH] Environmental Exposure: The exposure to potentially harmful chemical, physical, or biological agents in the environment or to environmental factors that may include ionizing radiation, pathogenic organisms, or toxic chemicals. [NIH] Environmental Health: The science of controlling or modifying those conditions, influences, or forces surrounding man which relate to promoting, establishing, and maintaining health. [NIH]
Enzymatic: Phase where enzyme cuts the precursor protein. [NIH] Enzyme: A protein that speeds up chemical reactions in the body. [NIH] Eosinophils: Granular leukocytes with a nucleus that usually has two lobes connected by a slender thread of chromatin, and cytoplasm containing coarse, round granules that are uniform in size and stainable by eosin. [NIH]
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Epidermal: Pertaining to or resembling epidermis. Called also epidermic or epidermoid. [EU] Epidermal Growth Factor: A 6 kD polypeptide growth factor initially discovered in mouse submaxillary glands. Human epidermal growth factor was originally isolated from urine based on its ability to inhibit gastric secretion and called urogastrone. epidermal growth factor exerts a wide variety of biological effects including the promotion of proliferation and differentiation of mesenchymal and epithelial cells. [NIH] Epidermis: Nonvascular layer of the skin. It is made up, from within outward, of five layers: 1) basal layer (stratum basale epidermidis); 2) spinous layer (stratum spinosum epidermidis); 3) granular layer (stratum granulosum epidermidis); 4) clear layer (stratum lucidum epidermidis); and 5) horny layer (stratum corneum epidermidis). [NIH] Epinephrine: The active sympathomimetic hormone from the adrenal medulla in most species. It stimulates both the alpha- and beta- adrenergic systems, causes systemic vasoconstriction and gastrointestinal relaxation, stimulates the heart, and dilates bronchi and cerebral vessels. It is used in asthma and cardiac failure and to delay absorption of local anesthetics. [NIH] Epithelial: Refers to the cells that line the internal and external surfaces of the body. [NIH] Epithelial Cells: Cells that line the inner and outer surfaces of the body. [NIH] Epithelium: One or more layers of epithelial cells, supported by the basal lamina, which covers the inner or outer surfaces of the body. [NIH] Epitope: A molecule or portion of a molecule capable of binding to the combining site of an antibody. For every given antigenic determinant, the body can construct a variety of antibody-combining sites, some of which fit almost perfectly, and others which barely fit. [NIH]
Erythrocytes: Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing hemoglobin whose function is to transport oxygen. [NIH] Erythropoietin: Glycoprotein hormone, secreted chiefly by the kidney in the adult and the liver in the fetus, that acts on erythroid stem cells of the bone marrow to stimulate proliferation and differentiation. [NIH] Esophageal: Having to do with the esophagus, the muscular tube through which food passes from the throat to the stomach. [NIH] Esophageal Varices: Stretched veins in the esophagus that occur when the liver is not working properly. If the veins burst, the bleeding can cause death. [NIH] Esophagus: The muscular tube through which food passes from the throat to the stomach. [NIH]
Essential Tremor: A rhythmic, involuntary, purposeless, oscillating movement resulting from the alternate contraction and relaxation of opposing groups of muscles. [NIH] Estradiol: The most potent mammalian estrogenic hormone. It is produced in the ovary, placenta, testis, and possibly the adrenal cortex. [NIH] Estrogen: One of the two female sex hormones. [NIH] Estrogen receptor: ER. Protein found on some cancer cells to which estrogen will attach. [NIH]
Ethanol: A clear, colorless liquid rapidly absorbed from the gastrointestinal tract and distributed throughout the body. It has bactericidal activity and is used often as a topical disinfectant. It is widely used as a solvent and preservative in pharmaceutical preparations as well as serving as the primary ingredient in alcoholic beverages. [NIH] Ether: One of a class of organic compounds in which any two organic radicals are attached
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directly to a single oxygen atom. [NIH] Ethylene Glycol: A colorless, odorless, viscous dihydroxy alcohol. It has a sweet taste, but is poisonous if ingested. Ethylene glycol is the most important glycol commercially available and is manufactured on a large scale in the United States. It is used as an antifreeze and coolant, in hydraulic fluids, and in the manufacture of low-freezing dynamites and resins. [NIH]
Eukaryotic Cells: Cells of the higher organisms, containing a true nucleus bounded by a nuclear membrane. [NIH] Evacuation: An emptying, as of the bowels. [EU] Excitatory: When cortical neurons are excited, their output increases and each new input they receive while they are still excited raises their output markedly. [NIH] Exogenous: Developed or originating outside the organism, as exogenous disease. [EU] Exons: Coding regions of messenger RNA included in the genetic transcript which survive the processing of RNA in cell nuclei to become part of a spliced messenger of structural RNA in the cytoplasm. They include joining and diversity exons of immunoglobulin genes. [NIH]
Expectorant: 1. Promoting the ejection, by spitting, of mucus or other fluids from the lungs and trachea. 2. An agent that promotes the ejection of mucus or exudate from the lungs, bronchi, and trachea; sometimes extended to all remedies that quiet cough (antitussives). [EU]
Extensor: A muscle whose contraction tends to straighten a limb; the antagonist of a flexor. [NIH]
External-beam radiation: Radiation therapy that uses a machine to aim high-energy rays at the cancer. Also called external radiation. [NIH] Extracellular: Outside a cell or cells. [EU] Extracellular Matrix: A meshwork-like substance found within the extracellular space and in association with the basement membrane of the cell surface. It promotes cellular proliferation and provides a supporting structure to which cells or cell lysates in culture dishes adhere. [NIH] Extracellular Matrix Proteins: Macromolecular organic compounds that contain carbon, hydrogen, oxygen, nitrogen, and usually, sulfur. These macromolecules (proteins) form an intricate meshwork in which cells are embedded to construct tissues. Variations in the relative types of macromolecules and their organization determine the type of extracellular matrix, each adapted to the functional requirements of the tissue. The two main classes of macromolecules that form the extracellular matrix are: glycosaminoglycans, usually linked to proteins (proteoglycans), and fibrous proteins (e.g., collagen, elastin, fibronectins and laminin). [NIH] Extracellular Space: Interstitial space between cells, occupied by fluid as well as amorphous and fibrous substances. [NIH] Extraction: The process or act of pulling or drawing out. [EU] Extravasation: A discharge or escape, as of blood, from a vessel into the tissues. [EU] Eye Infections: Infection, moderate to severe, caused by bacteria, fungi, or viruses, which occurs either on the external surface of the eye or intraocularly with probable inflammation, visual impairment, or blindness. [NIH] Family Planning: Programs or services designed to assist the family in controlling reproduction by either improving or diminishing fertility. [NIH] Fat: Total lipids including phospholipids. [NIH]
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Fatty acids: A major component of fats that are used by the body for energy and tissue development. [NIH] Feces: The excrement discharged from the intestines, consisting of bacteria, cells exfoliated from the intestines, secretions, chiefly of the liver, and a small amount of food residue. [EU] Femur: The longest and largest bone of the skeleton, it is situated between the hip and the knee. [NIH] Fermentation: An enzyme-induced chemical change in organic compounds that takes place in the absence of oxygen. The change usually results in the production of ethanol or lactic acid, and the production of energy. [NIH] Fertilizers: Substances or mixtures that are added to the soil to supply nutrients or to make available nutrients already present in the soil, in order to increase plant growth and productivity. [NIH] Fetus: The developing offspring from 7 to 8 weeks after conception until birth. [NIH] Fibroblast Growth Factor: Peptide isolated from the pituitary gland and from the brain. It is a potent mitogen which stimulates growth of a variety of mesodermal cells including chondrocytes, granulosa, and endothelial cells. The peptide may be active in wound healing and animal limb regeneration. [NIH] Fibroblasts: Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules. [NIH] Fibronectin: An adhesive glycoprotein. One form circulates in plasma, acting as an opsonin; another is a cell-surface protein which mediates cellular adhesive interactions. [NIH] Fibrosis: Any pathological condition where fibrous connective tissue invades any organ, usually as a consequence of inflammation or other injury. [NIH] Fixatives: Agents employed in the preparation of histologic or pathologic specimens for the purpose of maintaining the existing form and structure of all of the constituent elements. Great numbers of different agents are used; some are also decalcifying and hardening agents. They must quickly kill and coagulate living tissue. [NIH] Flatus: Gas passed through the rectum. [NIH] Fluconazole: Triazole antifungal agent that is used to treat oropharyngeal candidiasis and cryptococcal meningitis in AIDS. [NIH] Fluorescence: The property of emitting radiation while being irradiated. The radiation emitted is usually of longer wavelength than that incident or absorbed, e.g., a substance can be irradiated with invisible radiation and emit visible light. X-ray fluorescence is used in diagnosis. [NIH] Fluorouracil: A pyrimidine analog that acts as an antineoplastic antimetabolite and also has immunosuppressant. It interferes with DNA synthesis by blocking the thymidylate synthetase conversion of deoxyuridylic acid to thymidylic acid. [NIH] Folate: A B-complex vitamin that is being studied as a cancer prevention agent. Also called folic acid. [NIH] Fold: A plication or doubling of various parts of the body. [NIH] Folic Acid: N-(4-(((2-Amino-1,4-dihydro-4-oxo-6-pteridinyl)methyl)amino)benzoyl)-Lglutamic acid. A member of the vitamin B family that stimulates the hematopoietic system. It is present in the liver and kidney and is found in mushrooms, spinach, yeast, green leaves, and grasses. Folic acid is used in the treatment and prevention of folate deficiencies and megaloblastic anemia. [NIH] Forearm: The part between the elbow and the wrist. [NIH]
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Fractionation: Dividing the total dose of radiation therapy into several smaller, equal doses delivered over a period of several days. [NIH] Frameshift: A type of mutation which causes out-of-phase transcription of the base sequence; such mutations arise from the addition or delection of nucleotide(s) in numbers other than 3 or multiples of 3. [NIH] Frameshift Mutation: A type of mutation in which a number of nucleotides not divisible by three is deleted from or inserted into a coding sequence, thereby causing an alteration in the reading frame of the entire sequence downstream of the mutation. These mutations may be induced by certain types of mutagens or may occur spontaneously. [NIH] Freeze-dried: A method used to dry substances, such as food, to make them last longer. The substance is frozen and then dried in a vacuum. [NIH] Friction: Surface resistance to the relative motion of one body against the rubbing, sliding, rolling, or flowing of another with which it is in contact. [NIH] Fructose: A type of sugar found in many fruits and vegetables and in honey. Fructose is used to sweeten some diet foods. It is considered a nutritive sweetener because it has calories. [NIH] Fucose: Deoxysugar. [NIH] Fungi: A kingdom of eukaryotic, heterotrophic organisms that live as saprobes or parasites, including mushrooms, yeasts, smuts, molds, etc. They reproduce either sexually or asexually, and have life cycles that range from simple to complex. Filamentous fungi refer to those that grow as multicelluar colonies (mushrooms and molds). [NIH] Fungicides, Industrial: Chemicals that kill or inhibit the growth of fungi in agricultural applications, on wood, plastics, or other materials, in swimming pools, etc. [NIH] Fungistatic: Inhibiting the growth of fungi. [EU] Fungus: A general term used to denote a group of eukaryotic protists, including mushrooms, yeasts, rusts, moulds, smuts, etc., which are characterized by the absence of chlorophyll and by the presence of a rigid cell wall composed of chitin, mannans, and sometimes cellulose. They are usually of simple morphological form or show some reversible cellular specialization, such as the formation of pseudoparenchymatous tissue in the fruiting body of a mushroom. The dimorphic fungi grow, according to environmental conditions, as moulds or yeasts. [EU] Gait: Manner or style of walking. [NIH] Galactosyltransferases: Enzymes that catalyze the transfer of galactose from a nucleoside diphosphate galactose to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-. [NIH] Gallbladder: The pear-shaped organ that sits below the liver. Bile is concentrated and stored in the gallbladder. [NIH] Gallstones: The solid masses or stones made of cholesterol or bilirubin that form in the gallbladder or bile ducts. [NIH] Ganglion: 1. A knot, or knotlike mass. 2. A general term for a group of nerve cell bodies located outside the central nervous system; occasionally applied to certain nuclear groups within the brain or spinal cord, e.g. basal ganglia. 3. A benign cystic tumour occurring on a aponeurosis or tendon, as in the wrist or dorsum of the foot; it consists of a thin fibrous capsule enclosing a clear mucinous fluid. [EU] Gas: Air that comes from normal breakdown of food. The gases are passed out of the body through the rectum (flatus) or the mouth (burp). [NIH]
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Gastric: Having to do with the stomach. [NIH] Gastric Acid: Hydrochloric acid present in gastric juice. [NIH] Gastric Mucosa: Surface epithelium in the stomach that invaginates into the lamina propria, forming gastric pits. Tubular glands, characteristic of each region of the stomach (cardiac, gastric, and pyloric), empty into the gastric pits. The gastric mucosa is made up of several different kinds of cells. [NIH] Gastrin: A hormone released after eating. Gastrin causes the stomach to produce more acid. [NIH]
Gastritis: Inflammation of the stomach. [EU] Gastrointestinal: Refers to the stomach and intestines. [NIH] Gastrointestinal tract: The stomach and intestines. [NIH] Gelatin: A product formed from skin, white connective tissue, or bone collagen. It is used as a protein food adjuvant, plasma substitute, hemostatic, suspending agent in pharmaceutical preparations, and in the manufacturing of capsules and suppositories. [NIH] Gene: The functional and physical unit of heredity passed from parent to offspring. Genes are pieces of DNA, and most genes contain the information for making a specific protein. [NIH]
Gene Expression: The phenotypic manifestation of a gene or genes by the processes of gene action. [NIH] Gene Silencing: Interruption or suppression of the expression of a gene at transcriptional or translational levels. [NIH] Genetic Code: The specifications for how information, stored in nucleic acid sequence (base sequence), is translated into protein sequence (amino acid sequence). The start, stop, and order of amino acids of a protein is specified by consecutive triplets of nucleotides called codons (codon). [NIH] Genetic Engineering: Directed modification of the gene complement of a living organism by such techniques as altering the DNA, substituting genetic material by means of a virus, transplanting whole nuclei, transplanting cell hybrids, etc. [NIH] Genetics: The biological science that deals with the phenomena and mechanisms of heredity. [NIH] Genistein: An isoflavonoid derived from soy products. It inhibits protein-tyrosine kinase and topoisomerase-ii (dna topoisomerase (atp-hydrolysing)) activity and is used as an antineoplastic and antitumor agent. Experimentally, it has been shown to induce G2 phase arrest in human and murine cell lines. [NIH] Genotype: The genetic constitution of the individual; the characterization of the genes. [NIH] Germ Cells: The reproductive cells in multicellular organisms. [NIH] Gestation: The period of development of the young in viviparous animals, from the time of fertilization of the ovum until birth. [EU] Giardiasis: An infection of the small intestine caused by the flagellated protozoan Giardia lamblia. It is spread via contaminated food and water and by direct person-to-person contact. [NIH] Gland: An organ that produces and releases one or more substances for use in the body. Some glands produce fluids that affect tissues or organs. Others produce hormones or participate in blood production. [NIH] Glioma: A cancer of the brain that comes from glial, or supportive, cells. [NIH]
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Glomerular: Pertaining to or of the nature of a glomerulus, especially a renal glomerulus. [EU]
Glomeruli: Plural of glomerulus. [NIH] Glomerulonephritis: Glomerular disease characterized by an inflammatory reaction, with leukocyte infiltration and cellular proliferation of the glomeruli, or that appears to be the result of immune glomerular injury. [NIH] Glomerulosclerosis: Scarring of the glomeruli. It may result from diabetes mellitus (diabetic glomerulosclerosis) or from deposits in parts of the glomerulus (focal segmental glomerulosclerosis). The most common signs of glomerulosclerosis are proteinuria and kidney failure. [NIH] Glomerulus: A tiny set of looping blood vessels in the nephron where blood is filtered in the kidney. [NIH] Glottis: The vocal apparatus of the larynx, consisting of the true vocal cords (plica vocalis) and the opening between them (rima glottidis). [NIH] Glucokinase: A group of enzymes that catalyzes the conversion of ATP and D-glucose to ADP and D-glucose 6-phosphate. They are found in invertebrates and microorganisms and are highly specific for glucose. (Enzyme Nomenclature, 1992) EC 2.7.1.2. [NIH] Glucose: D-Glucose. A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement. [NIH] Glucose Intolerance: A pathological state in which the fasting plasma glucose level is less than 140 mg per deciliter and the 30-, 60-, or 90-minute plasma glucose concentration following a glucose tolerance test exceeds 200 mg per deciliter. This condition is seen frequently in diabetes mellitus but also occurs with other diseases. [NIH] Glucuronic Acid: Derivatives of uronic acid found throughout the plant and animal kingdoms. They detoxify drugs and toxins by conjugating with them to form glucuronides in the liver which are more water-soluble metabolites that can be easily eliminated from the body. [NIH] Glucuronides: Glycosides of glucuronic acid formed by the reaction of uridine diphosphate glucuronic acid with certain endogenous and exogenous substances. Their formation is important for the detoxification of drugs, steroid excretion and bilirubin metabolism to a more water-soluble compound that can be eliminated in the urine and bile. [NIH] Glucuronosyltransferase: A family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines, and fatty acids. They function as drug-metabolizing enzymes that catalyze the conjugation of UDPglucuronic acid to a variety of endogenous and exogenous compounds. EC 2.4.1.17. [NIH] Glutamate: Excitatory neurotransmitter of the brain. [NIH] Glutamic Acid: A non-essential amino acid naturally occurring in the L-form. Glutamic acid (glutamate) is the most common excitatory neurotransmitter in the central nervous system. [NIH]
Glutamine: A non-essential amino acid present abundantly throught the body and is involved in many metabolic processes. It is synthesized from glutamic acid and ammonia. It is the principal carrier of nitrogen in the body and is an important energy source for many cells. [NIH] Glutathione Peroxidase: An enzyme catalyzing the oxidation of 2 moles of glutathione in the presence of hydrogen peroxide to yield oxidized glutathione and water. EC 1.11.1.9. [NIH]
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Glycerol: A trihydroxy sugar alcohol that is an intermediate in carbohydrate and lipid metabolism. It is used as a solvent, emollient, pharmaceutical agent, and sweetening agent. [NIH]
Glycine: A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter. [NIH] Glycogen: A sugar stored in the liver and muscles. It releases glucose into the blood when cells need it for energy. Glycogen is the chief source of stored fuel in the body. [NIH] Glycogen Synthase: An enzyme that catalyzes the transfer of D-glucose from UDPglucose into 1,4-alpha-D-glucosyl chains. EC 2.4.1.11. [NIH] Glycopeptides: Proteins which contain carbohydrate groups attached covalently to the polypeptide chain. The protein moiety is the predominant group with the carbohydrate making up only a small percentage of the total weight. [NIH] Glycoprotein: A protein that has sugar molecules attached to it. [NIH] Glycosaminoglycan: A type of long, unbranched polysaccharide molecule. Glycosaminoglycans are major structural components of cartilage and are also found in the cornea of the eye. [NIH] Glycoside: Any compound that contains a carbohydrate molecule (sugar), particularly any such natural product in plants, convertible, by hydrolytic cleavage, into sugar and a nonsugar component (aglycone), and named specifically for the sugar contained, as glucoside (glucose), pentoside (pentose), fructoside (fructose) etc. [EU] Glycosidic: Formed by elimination of water between the anomeric hydroxyl of one sugar and a hydroxyl of another sugar molecule. [NIH] Glycosylation: The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction. [NIH] Glycosyltransferases: Enzymes that catalyze the transfer of glycosyl groups to an acceptor. Most often another carbohydrate molecule acts as an acceptor, but inorganic phosphate can also act as an acceptor, such as in the case of phosphorylases. Some of the enzymes in this group also catalyze hydrolysis, which can be regarded as transfer of a glycosyl group from the donor to water. Subclasses include the hexosyltransferases, pentosyltransferases, sialyltransferases, and those transferring other glycosyl groups. EC 2.4. [NIH] Glycyrrhetinic Acid: 3-beta-Hydroxy-11-oxoolean-12-en-30-oic acid. A product from Glycyrrhiza glabra L. Leguminosae with some antiallergic, antibacterial, and antiviral properties. It is used topically for allergic or infectious skin inflammation and orally for its aldosterone effects in electrolyte regulation. [NIH] Glycyrrhiza: A genus of leguminous herbs or shrubs whose roots yield glycyrrhetinic acid and its derivatives, carbenoxolone for example. Licorice toxicity is manifested as hypokalemia, low blood potassium. Licorice is used as flavoring and aromatic in pharmaceuticals and as candy. [NIH] Goats: Any of numerous agile, hollow-horned ruminants of the genus Capra, closely related to the sheep. [NIH] Gonadal: Pertaining to a gonad. [EU] Gout: Hereditary metabolic disorder characterized by recurrent acute arthritis, hyperuricemia and deposition of sodium urate in and around the joints, sometimes with formation of uric acid calculi. [NIH] Governing Board: The group in which legal authority is vested for the control of healthrelated institutions and organizations. [NIH]
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Gp120: 120-kD HIV envelope glycoprotein which is involved in the binding of the virus to its membrane receptor, the CD4 molecule, found on the surface of certain cells in the body. [NIH]
Grade: The grade of a tumor depends on how abnormal the cancer cells look under a microscope and how quickly the tumor is likely to grow and spread. Grading systems are different for each type of cancer. [NIH] Graft: Healthy skin, bone, or other tissue taken from one part of the body and used to replace diseased or injured tissue removed from another part of the body. [NIH] Grafting: The operation of transfer of tissue from one site to another. [NIH] Gram-negative: Losing the stain or decolorized by alcohol in Gram's method of staining, a primary characteristic of bacteria having a cell wall composed of a thin layer of peptidoglycan covered by an outer membrane of lipoprotein and lipopolysaccharide. [EU] Gram-Negative Bacteria: Bacteria which lose crystal violet stain but are stained pink when treated by Gram's method. [NIH] Gram-positive: Retaining the stain or resisting decolorization by alcohol in Gram's method of staining, a primary characteristic of bacteria whose cell wall is composed of a thick layer of peptidologlycan with attached teichoic acids. [EU] Granule: A small pill made from sucrose. [EU] Granulocytes: Leukocytes with abundant granules in the cytoplasm. They are divided into three groups: neutrophils, eosinophils, and basophils. [NIH] Grasses: A large family, Gramineae, of narrow-leaved herbaceous monocots. Many grasses produce highly allergenic pollens and are hosts to cattle parasites and toxic fungi. [NIH] Group Structure: The informal or formal organization of a group of people based on a network of personal relationships which is influenced by the size and composition, etc., of the group. [NIH] Growth: The progressive development of a living being or part of an organism from its earliest stage to maturity. [NIH] Growth factors: Substances made by the body that function to regulate cell division and cell survival. Some growth factors are also produced in the laboratory and used in biological therapy. [NIH] Guanylate Cyclase: An enzyme that catalyzes the conversion of GTP to 3',5'-cyclic GMP and pyrophosphate. It also acts on ITP and dGTP. (From Enzyme Nomenclature, 1992) EC 4.6.1.2. [NIH] Guinea Pigs: A common name used for the family Caviidae. The most common species is Cavia porcellus which is the domesticated guinea pig used for pets and biomedical research. [NIH]
Haploid: An organism with one basic chromosome set, symbolized by n; the normal condition of gametes in diploids. [NIH] Haptens: Small antigenic determinants capable of eliciting an immune response only when coupled to a carrier. Haptens bind to antibodies but by themselves cannot elicit an antibody response. [NIH] Headache: Pain in the cranial region that may occur as an isolated and benign symptom or as a manifestation of a wide variety of conditions including subarachnoid hemorrhage; craniocerebral trauma; central nervous system infections; intracranial hypertension; and other disorders. In general, recurrent headaches that are not associated with a primary disease process are referred to as headache disorders (e.g., migraine). [NIH]
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Health Promotion: Encouraging consumer behaviors most likely to optimize health potentials (physical and psychosocial) through health information, preventive programs, and access to medical care. [NIH] Heart attack: A seizure of weak or abnormal functioning of the heart. [NIH] Hematoma: An extravasation of blood localized in an organ, space, or tissue. [NIH] Heme: The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins. [NIH] Hemodialysis: The use of a machine to clean wastes from the blood after the kidneys have failed. The blood travels through tubes to a dialyzer, which removes wastes and extra fluid. The cleaned blood then flows through another set of tubes back into the body. [NIH] Hemoglobin: One of the fractions of glycosylated hemoglobin A1c. Glycosylated hemoglobin is formed when linkages of glucose and related monosaccharides bind to hemoglobin A and its concentration represents the average blood glucose level over the previous several weeks. HbA1c levels are used as a measure of long-term control of plasma glucose (normal, 4 to 6 percent). In controlled diabetes mellitus, the concentration of glycosylated hemoglobin A is within the normal range, but in uncontrolled cases the level may be 3 to 4 times the normal conentration. Generally, complications are substantially lower among patients with Hb levels of 7 percent or less than in patients with HbA1c levels of 9 percent or more. [NIH] Hemoglobinuria: The presence of free hemoglobin in the urine. [NIH] Hemorrhage: Bleeding or escape of blood from a vessel. [NIH] Hemorrhaging: A copious discharge of blood from the blood vessels. [NIH] Hemostasis: The process which spontaneously arrests the flow of blood from vessels carrying blood under pressure. It is accomplished by contraction of the vessels, adhesion and aggregation of formed blood elements, and the process of blood or plasma coagulation. [NIH]
Heparan Sulfate Proteoglycan: A substance released by astrocytes, which is critical in stopping nervous fibers in their tracks. [NIH] Heparin: Heparinic acid. A highly acidic mucopolysaccharide formed of equal parts of sulfated D-glucosamine and D-glucuronic acid with sulfaminic bridges. The molecular weight ranges from six to twenty thousand. Heparin occurs in and is obtained from liver, lung, mast cells, etc., of vertebrates. Its function is unknown, but it is used to prevent blood clotting in vivo and vitro, in the form of many different salts. [NIH] Hepatocellular: Pertaining to or affecting liver cells. [EU] Hepatocyte: A liver cell. [NIH] Hepatoma: A liver tumor. [NIH] Hereditary: Of, relating to, or denoting factors that can be transmitted genetically from one generation to another. [NIH] Heredity: 1. The genetic transmission of a particular quality or trait from parent to offspring. 2. The genetic constitution of an individual. [EU] Heterogeneity: The property of one or more samples or populations which implies that they are not identical in respect of some or all of their parameters, e. g. heterogeneity of variance. [NIH]
Heterotrophic: Pertaining to organisms that are consumers and dependent on other organisms for their source of energy (food). [NIH] Hexosyltransferases: Enzymes that catalyze the transfer of hexose groups. EC 2.4.1.-. [NIH]
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Hippocampus: A curved elevation of gray matter extending the entire length of the floor of the temporal horn of the lateral ventricle (Dorland, 28th ed). The hippocampus, subiculum, and dentate gyrus constitute the hippocampal formation. Sometimes authors include the entorhinal cortex in the hippocampal formation. [NIH] Histamine: 1H-Imidazole-4-ethanamine. A depressor amine derived by enzymatic decarboxylation of histidine. It is a powerful stimulant of gastric secretion, a constrictor of bronchial smooth muscle, a vasodilator, and also a centrally acting neurotransmitter. [NIH] Histidine: An essential amino acid important in a number of metabolic processes. It is required for the production of histamine. [NIH] Homeostasis: The processes whereby the internal environment of an organism tends to remain balanced and stable. [NIH] Homogeneous: Consisting of or composed of similar elements or ingredients; of a uniform quality throughout. [EU] Homologous: Corresponding in structure, position, origin, etc., as (a) the feathers of a bird and the scales of a fish, (b) antigen and its specific antibody, (c) allelic chromosomes. [EU] Hormonal: Pertaining to or of the nature of a hormone. [EU] Hormone: A substance in the body that regulates certain organs. Hormones such as gastrin help in breaking down food. Some hormones come from cells in the stomach and small intestine. [NIH] Horny layer: The superficial layer of the epidermis containing keratinized cells. [NIH] Host: Any animal that receives a transplanted graft. [NIH] Humoral: Of, relating to, proceeding from, or involving a bodily humour - now often used of endocrine factors as opposed to neural or somatic. [EU] Humour: 1. A normal functioning fluid or semifluid of the body (as the blood, lymph or bile) especially of vertebrates. 2. A secretion that is itself an excitant of activity (as certain hormones). [EU] Hybrid: Cross fertilization between two varieties or, more usually, two species of vines, see also crossing. [NIH] Hybridization: The genetic process of crossbreeding to produce a hybrid. Hybrid nucleic acids can be formed by nucleic acid hybridization of DNA and RNA molecules. Protein hybridization allows for hybrid proteins to be formed from polypeptide chains. [NIH] Hybridomas: Cells artificially created by fusion of activated lymphocytes with neoplastic cells. The resulting hybrid cells are cloned and produce pure or "monoclonal" antibodies or T-cell products, identical to those produced by the immunologically competent parent, and continually grow and divide as the neoplastic parent. [NIH] Hydrochloric Acid: A strong corrosive acid that is commonly used as a laboratory reagent. It is formed by dissolving hydrogen chloride in water. Gastric acid is the hydrochloric acid component of gastric juice. [NIH] Hydrogel: A network of cross-linked hydrophilic macromolecules used in biomedical applications. [NIH] Hydrogen: The first chemical element in the periodic table. It has the atomic symbol H, atomic number 1, and atomic weight 1. It exists, under normal conditions, as a colorless, odorless, tasteless, diatomic gas. Hydrogen ions are protons. Besides the common H1 isotope, hydrogen exists as the stable isotope deuterium and the unstable, radioactive isotope tritium. [NIH] Hydrogen Peroxide: A strong oxidizing agent used in aqueous solution as a ripening agent,
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bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials. [NIH] Hydrolases: Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., esterases, glycosidases (glycoside hydrolases), lipases, nucleotidases, peptidases (peptide hydrolases), and phosphatases (phosphoric monoester hydrolases). EC 3. [NIH] Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water. [NIH] Hydrophilic: Readily absorbing moisture; hygroscopic; having strongly polar groups that readily interact with water. [EU] Hydrophobic: Not readily absorbing water, or being adversely affected by water, as a hydrophobic colloid. [EU] Hydroxylation: Hydroxylate, to introduce hydroxyl into (a compound or radical) usually by replacement of hydrogen. [EU] Hydroxylysine: A hydroxylated derivative of the amino acid lysine that is present in certain collagens. [NIH] Hydroxyproline: A hydroxylated form of the imino acid proline. A deficiency in ascorbic acid can result in impaired hydroxyproline formation. [NIH] Hydroxyzine: A histamine H1 receptor antagonist that is effective in the treatment of chronic urticaria, dermatitis, and histamine-mediated pruritus. Unlike its major metabolite cetirizine, it does cause drowsiness. It is also effective as an antiemetic, for relief of anxiety and tension, and as a sedative. [NIH] Hyperbilirubinemia: Pathologic process consisting of an abnormal increase in the amount of bilirubin in the circulating blood, which may result in jaundice. [NIH] Hyperglycaemia: Abnormally increased content of sugar in the blood. [EU] Hyperglycemia: Abnormally high blood sugar. [NIH] Hyperlipoproteinemia: Metabolic disease characterized by elevated plasma cholesterol and/or triglyceride levels. The inherited form is attributed to a single gene mechanism. [NIH] Hyperplasia: An increase in the number of cells in a tissue or organ, not due to tumor formation. It differs from hypertrophy, which is an increase in bulk without an increase in the number of cells. [NIH] Hypersensitivity: Altered reactivity to an antigen, which can result in pathologic reactions upon subsequent exposure to that particular antigen. [NIH] Hypersensitivity, Immediate: Hypersensitivity reactions which occur within minutes of exposure to challenging antigen due to the release of histamine which follows the antigenantibody reaction and causes smooth muscle contraction and increased vascular permeability. [NIH] Hypertension: Persistently high arterial blood pressure. Currently accepted threshold levels are 140 mm Hg systolic and 90 mm Hg diastolic pressure. [NIH] Hypertrophy: General increase in bulk of a part or organ, not due to tumor formation, nor to an increase in the number of cells. [NIH] Hyperuricemia: A buildup of uric acid (a byproduct of metabolism) in the blood; a side effect of some anticancer drugs. [NIH] Hypnotic: A drug that acts to induce sleep. [EU] Hypochlorous Acid: HClO. An oxyacid of chlorine containing monovalent chlorine that acts
230 Glucosamine
as an oxidizing or reducing agent. [NIH] Hypoglycemia: Abnormally low blood sugar [NIH] Hypoglycemic: An orally active drug that produces a fall in blood glucose concentration. [NIH]
Hypoglycemic Agents: Agents which lower the blood glucose level. [NIH] Hypoplasia: Incomplete development or underdevelopment of an organ or tissue. [EU] Hypothalamus: Ventral part of the diencephalon extending from the region of the optic chiasm to the caudal border of the mammillary bodies and forming the inferior and lateral walls of the third ventricle. [NIH] Ibuprofen: A nonsteroidal anti-inflammatory agent with analgesic properties used in the therapy of rheumatism and arthritis. [NIH] Id: The part of the personality structure which harbors the unconscious instinctive desires and strivings of the individual. [NIH] Iduronic Acid: Component of dermatan sulfate. Differs in configuration from glucuronic acid only at the C-5 position. [NIH] Imidazole: C3H4N2. The ring is present in polybenzimidazoles. [NIH] Immersion: The placing of a body or a part thereof into a liquid. [NIH] Immune adjuvant: A drug that stimulates the immune system to respond to disease. [NIH] Immune response: The activity of the immune system against foreign substances (antigens). [NIH]
Immune system: The organs, cells, and molecules responsible for the recognition and disposal of foreign ("non-self") material which enters the body. [NIH] Immunity: Nonsusceptibility to the invasive or pathogenic microorganisms or to the toxic effect of antigenic substances. [NIH]
effects
of
foreign
Immunization: Deliberate stimulation of the host's immune response. Active immunization involves administration of antigens or immunologic adjuvants. Passive immunization involves administration of immune sera or lymphocytes or their extracts (e.g., transfer factor, immune RNA) or transplantation of immunocompetent cell producing tissue (thymus or bone marrow). [NIH] Immunocompromised: Having a weakened immune system caused by certain diseases or treatments. [NIH] Immunodeficiency: The decreased ability of the body to fight infection and disease. [NIH] Immunogenic: Producing immunity; evoking an immune response. [EU] Immunoglobulin: A protein that acts as an antibody. [NIH] Immunohistochemistry: Histochemical localization of immunoreactive substances using labeled antibodies as reagents. [NIH] Immunologic: The ability of the antibody-forming system to recall a previous experience with an antigen and to respond to a second exposure with the prompt production of large amounts of antibody. [NIH] Immunology: The study of the body's immune system. [NIH] Immunosuppressant: An agent capable of suppressing immune responses. [EU] Immunotherapy: Manipulation of the host's immune system in treatment of disease. It includes both active and passive immunization as well as immunosuppressive therapy to prevent graft rejection. [NIH]
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Impairment: In the context of health experience, an impairment is any loss or abnormality of psychological, physiological, or anatomical structure or function. [NIH] Implant radiation: A procedure in which radioactive material sealed in needles, seeds, wires, or catheters is placed directly into or near the tumor. Also called [NIH] Implantation: The insertion or grafting into the body of biological, living, inert, or radioactive material. [EU] In situ: In the natural or normal place; confined to the site of origin without invasion of neighbouring tissues. [EU] In Situ Hybridization: A technique that localizes specific nucleic acid sequences within intact chromosomes, eukaryotic cells, or bacterial cells through the use of specific nucleic acid-labeled probes. [NIH] In vitro: In the laboratory (outside the body). The opposite of in vivo (in the body). [NIH] In vivo: In the body. The opposite of in vitro (outside the body or in the laboratory). [NIH] Incision: A cut made in the body during surgery. [NIH] Incubation: The development of an infectious disease from the entrance of the pathogen to the appearance of clinical symptoms. [EU] Incubation period: The period of time likely to elapse between exposure to the agent of the disease and the onset of clinical symptoms. [NIH] Indicative: That indicates; that points out more or less exactly; that reveals fairly clearly. [EU] Induction: The act or process of inducing or causing to occur, especially the production of a specific morphogenetic effect in the developing embryo through the influence of evocators or organizers, or the production of anaesthesia or unconsciousness by use of appropriate agents. [EU] Infarction: A pathological process consisting of a sudden insufficient blood supply to an area, which results in necrosis of that area. It is usually caused by a thrombus, an embolus, or a vascular torsion. [NIH] Infection: 1. Invasion and multiplication of microorganisms in body tissues, which may be clinically unapparent or result in local cellular injury due to competitive metabolism, toxins, intracellular replication, or antigen-antibody response. The infection may remain localized, subclinical, and temporary if the body's defensive mechanisms are effective. A local infection may persist and spread by extension to become an acute, subacute, or chronic clinical infection or disease state. A local infection may also become systemic when the microorganisms gain access to the lymphatic or vascular system. 2. An infectious disease. [EU]
Infiltration: The diffusion or accumulation in a tissue or cells of substances not normal to it or in amounts of the normal. Also, the material so accumulated. [EU] Inflammation: A pathological process characterized by injury or destruction of tissues caused by a variety of cytologic and chemical reactions. It is usually manifested by typical signs of pain, heat, redness, swelling, and loss of function. [NIH] Inflammatory bowel disease: A general term that refers to the inflammation of the colon and rectum. Inflammatory bowel disease includes ulcerative colitis and Crohn's disease. [NIH]
Influenza: An acute viral infection involving the respiratory tract. It is marked by inflammation of the nasal mucosa, the pharynx, and conjunctiva, and by headache and severe, often generalized, myalgia. [NIH] Infusion: A method of putting fluids, including drugs, into the bloodstream. Also called
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intravenous infusion. [NIH] Ingestion: Taking into the body by mouth [NIH] Initiation: Mutation induced by a chemical reactive substance causing cell changes; being a step in a carcinogenic process. [NIH] Inlay: In dentistry, a filling first made to correspond with the form of a dental cavity and then cemented into the cavity. [NIH] Inner ear: The labyrinth, comprising the vestibule, cochlea, and semicircular canals. [NIH] Inorganic: Pertaining to substances not of organic origin. [EU] Inositol: An isomer of glucose that has traditionally been considered to be a B vitamin although it has an uncertain status as a vitamin and a deficiency syndrome has not been identified in man. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1379) Inositol phospholipids are important in signal transduction. [NIH] Insulator: Material covering the metal conductor of the lead. It is usually polyurethane or silicone. [NIH] Insulin: A protein hormone secreted by beta cells of the pancreas. Insulin plays a major role in the regulation of glucose metabolism, generally promoting the cellular utilization of glucose. It is also an important regulator of protein and lipid metabolism. Insulin is used as a drug to control insulin-dependent diabetes mellitus. [NIH] Insulin-dependent diabetes mellitus: A disease characterized by high levels of blood glucose resulting from defects in insulin secretion, insulin action, or both. Autoimmune, genetic, and environmental factors are involved in the development of type I diabetes. [NIH] Insulin-like: Muscular growth factor. [NIH] Interleukin-1: A soluble factor produced by monocytes, macrophages, and other cells which activates T-lymphocytes and potentiates their response to mitogens or antigens. IL-1 consists of two distinct forms, IL-1 alpha and IL-1 beta which perform the same functions but are distinct proteins. The biological effects of IL-1 include the ability to replace macrophage requirements for T-cell activation. The factor is distinct from interleukin-2. [NIH] Interleukin-10: Factor that is a coregulator of mast cell growth. It is produced by T-cells and B-cells and shows extensive homology with the Epstein-Barr virus BCRFI gene. [NIH] Interleukin-2: Chemical mediator produced by activated T lymphocytes and which regulates the proliferation of T cells, as well as playing a role in the regulation of NK cell activity. [NIH] Intermittent: Occurring at separated intervals; having periods of cessation of activity. [EU] Internal Medicine: A medical specialty concerned with the diagnosis and treatment of diseases of the internal organ systems of adults. [NIH] Internal radiation: A procedure in which radioactive material sealed in needles, seeds, wires, or catheters is placed directly into or near the tumor. Also called brachytherapy, implant radiation, or interstitial radiation therapy. [NIH] Interstitial: Pertaining to or situated between parts or in the interspaces of a tissue. [EU] Intestinal: Having to do with the intestines. [NIH] Intestine: A long, tube-shaped organ in the abdomen that completes the process of digestion. There is both a large intestine and a small intestine. Also called the bowel. [NIH] Intracellular: Inside a cell. [NIH] Intracellular Membranes: Membranes of subcellular structures. [NIH] Intramuscular: IM. Within or into muscle. [NIH]
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Intraperitoneal: IP. Within the peritoneal cavity (the area that contains the abdominal organs). [NIH] Intravenous: IV. Into a vein. [NIH] Intrinsic: Situated entirely within or pertaining exclusively to a part. [EU] Intubation: Introduction of a tube into a hollow organ to restore or maintain patency if obstructed. It is differentiated from catheterization in that the insertion of a catheter is usually performed for the introducing or withdrawing of fluids from the body. [NIH] Inulin: A starch found in the tubers and roots of many plants. Since it is hydrolyzable to fructose, it is classified as a fructosan. It has been used in physiologic investigation for determination of the rate of glomerular function. [NIH] Invasive: 1. Having the quality of invasiveness. 2. Involving puncture or incision of the skin or insertion of an instrument or foreign material into the body; said of diagnostic techniques. [EU]
Invertebrates: Animals that have no spinal column. [NIH] Involuntary: Reaction occurring without intention or volition. [NIH] Iodine: A nonmetallic element of the halogen group that is represented by the atomic symbol I, atomic number 53, and atomic weight of 126.90. It is a nutritionally essential element, especially important in thyroid hormone synthesis. In solution, it has anti-infective properties and is used topically. [NIH] Ions: An atom or group of atoms that have a positive or negative electric charge due to a gain (negative charge) or loss (positive charge) of one or more electrons. Atoms with a positive charge are known as cations; those with a negative charge are anions. [NIH] Irradiation: The use of high-energy radiation from x-rays, neutrons, and other sources to kill cancer cells and shrink tumors. Radiation may come from a machine outside the body (external-beam radiation therapy) or from materials called radioisotopes. Radioisotopes produce radiation and can be placed in or near the tumor or in the area near cancer cells. This type of radiation treatment is called internal radiation therapy, implant radiation, interstitial radiation, or brachytherapy. Systemic radiation therapy uses a radioactive substance, such as a radiolabeled monoclonal antibody, that circulates throughout the body. Irradiation is also called radiation therapy, radiotherapy, and x-ray therapy. [NIH] Irrigation: The washing of a body cavity or surface by flowing solution which is inserted and then removed. Any drug in the irrigation solution may be absorbed. [NIH] Ischemia: Deficiency of blood in a part, due to functional constriction or actual obstruction of a blood vessel. [EU] Islet: Cell producing insulin in pancreas. [NIH] Isoflavones: 3-Phenylchromones. Isomeric form of flavones in which the benzene group is attached to the 3 position of the benzopyran ring instead of the 2 position. [NIH] Itraconazole: An antifungal agent that has been used in the treatment of histoplasmosis, blastomycosis, cryptococcal meningitis, and aspergillosis. [NIH] Jaundice: A clinical manifestation of hyperbilirubinemia, consisting of deposition of bile pigments in the skin, resulting in a yellowish staining of the skin and mucous membranes. [NIH]
Joint: The point of contact between elements of an animal skeleton with the parts that surround and support it. [NIH] Joint Capsule: The sac enclosing a joint. It is composed of an outer fibrous articular capsule and an inner synovial membrane. [NIH]
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Kb: A measure of the length of DNA fragments, 1 Kb = 1000 base pairs. The largest DNA fragments are up to 50 kilobases long. [NIH] Keratan Sulfate: A sulfated mucopolysaccharide initially isolated from bovine cornea. At least two types are known. Type I, found mostly in the cornea, contains D-galactose and Dglucosamine-6-O-sulfate as the repeating unit; type II, found in skeletal tissues, contains Dgalactose and D-galactosamine-6-O-sulfate as the repeating unit. [NIH] Keratin: A class of fibrous proteins or scleroproteins important both as structural proteins and as keys to the study of protein conformation. The family represents the principal constituent of epidermis, hair, nails, horny tissues, and the organic matrix of tooth enamel. Two major conformational groups have been characterized, alpha-keratin, whose peptide backbone forms an alpha-helix, and beta-keratin, whose backbone forms a zigzag or pleated sheet structure. [NIH] Keratinocytes: Epidermal cells which synthesize keratin and undergo characteristic changes as they move upward from the basal layers of the epidermis to the cornified (horny) layer of the skin. Successive stages of differentiation of the keratinocytes forming the epidermal layers are basal cell, spinous or prickle cell, and the granular cell. [NIH] Keratoconjunctivitis: Simultaneous inflammation of the cornea and conjunctiva. [NIH] Keratoconjunctivitis Sicca: Drying and inflammation of the conjunctiva as a result of insufficient lacrimal secretion. When found in association with xerostomia and polyarthritis, it is called Sjogren's syndrome. [NIH] Keratolytic: An agent that promotes keratolysis. [EU] Ketone Bodies: Chemicals that the body makes when there is not enough insulin in the blood and it must break down fat for its energy. Ketone bodies can poison and even kill body cells. When the body does not have the help of insulin, the ketones build up in the blood and then "spill" over into the urine so that the body can get rid of them. The body can also rid itself of one type of ketone, called acetone, through the lungs. This gives the breath a fruity odor. Ketones that build up in the body for a long time lead to serious illness and coma. [NIH] Kidney Disease: Any one of several chronic conditions that are caused by damage to the cells of the kidney. People who have had diabetes for a long time may have kidney damage. Also called nephropathy. [NIH] Kinetic: Pertaining to or producing motion. [EU] Labile: 1. Gliding; moving from point to point over the surface; unstable; fluctuating. 2. Chemically unstable. [EU] Lacrimal: Pertaining to the tears. [EU] Lactation: The period of the secretion of milk. [EU] Lactobacillus: A genus of gram-positive, microaerophilic, rod-shaped bacteria occurring widely in nature. Its species are also part of the many normal flora of the mouth, intestinal tract, and vagina of many mammals, including humans. Pathogenicity from this genus is rare. [NIH] Lactobacillus acidophilus: A species of gram-positive, rod-shaped bacteria isolated from the intestinal tract of humans and animals, the human mouth, and vagina. This organism produces the fermented product, acidophilus milk. [NIH] Lactose Synthase: An enzyme of the transferase class that catalyzes the transfer of galactose from UDPgalactose to glucose, forming lactose. The enzyme is a complex of the enzyme Nacetyllactosamine synthase and alpha-lactalbumin; the latter protein is present in lactating mammary gland cells where it alters the usual specificity of the former to make lactose
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synthesis the preferred reaction. (Dorland, 28th ed) EC 2.4.1.22. [NIH] Laminin: Large, noncollagenous glycoprotein with antigenic properties. It is localized in the basement membrane lamina lucida and functions to bind epithelial cells to the basement membrane. Evidence suggests that the protein plays a role in tumor invasion. [NIH] Large Intestine: The part of the intestine that goes from the cecum to the rectum. The large intestine absorbs water from stool and changes it from a liquid to a solid form. The large intestine is 5 feet long and includes the appendix, cecum, colon, and rectum. Also called colon. [NIH] Larynx: An irregularly shaped, musculocartilaginous tubular structure, lined with mucous membrane, located at the top of the trachea and below the root of the tongue and the hyoid bone. It is the essential sphincter guarding the entrance into the trachea and functioning secondarily as the organ of voice. [NIH] Latent: Phoria which occurs at one distance or another and which usually has no troublesome effect. [NIH] Laxative: An agent that acts to promote evacuation of the bowel; a cathartic or purgative. [EU]
Lectin: A complex molecule that has both protein and sugars. Lectins are able to bind to the outside of a cell and cause biochemical changes in it. Lectins are made by both animals and plants. [NIH] Leishmaniasis: A disease caused by any of a number of species of protozoa in the genus Leishmania. There are four major clinical types of this infection: cutaneous (Old and New World), diffuse cutaneous, mucocutaneous, and visceral leishmaniasis. [NIH] Lens: The transparent, double convex (outward curve on both sides) structure suspended between the aqueous and vitreous; helps to focus light on the retina. [NIH] Lesion: An area of abnormal tissue change. [NIH] Lethal: Deadly, fatal. [EU] Leucine: An essential branched-chain amino acid important for hemoglobin formation. [NIH] Leucocyte: All the white cells of the blood and their precursors (myeloid cell series, lymphoid cell series) but commonly used to indicate granulocytes exclusive of lymphocytes. [NIH]
Leukaemia: An acute or chronic disease of unknown cause in man and other warm-blooded animals that involves the blood-forming organs, is characterized by an abnormal increase in the number of leucocytes in the tissues of the body with or without a corresponding increase of those in the circulating blood, and is classified according of the type leucocyte most prominently involved. [EU] Leukemia: Cancer of blood-forming tissue. [NIH] Leukocytes: White blood cells. These include granular leukocytes (basophils, eosinophils, and neutrophils) as well as non-granular leukocytes (lymphocytes and monocytes). [NIH] Leukotrienes: A family of biologically active compounds derived from arachidonic acid by oxidative metabolism through the 5-lipoxygenase pathway. They participate in host defense reactions and pathophysiological conditions such as immediate hypersensitivity and inflammation. They have potent actions on many essential organs and systems, including the cardiovascular, pulmonary, and central nervous system as well as the gastrointestinal tract and the immune system. [NIH] Library Services: Services offered to the library user. They include reference and circulation. [NIH]
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Lidocaine: A local anesthetic and cardiac depressant used as an antiarrhythmia agent. Its actions are more intense and its effects more prolonged than those of procaine but its duration of action is shorter than that of bupivacaine or prilocaine. [NIH] Life cycle: The successive stages through which an organism passes from fertilized ovum or spore to the fertilized ovum or spore of the next generation. [NIH] Ligament: A band of fibrous tissue that connects bones or cartilages, serving to support and strengthen joints. [EU] Ligands: A RNA simulation method developed by the MIT. [NIH] Linkage: The tendency of two or more genes in the same chromosome to remain together from one generation to the next more frequently than expected according to the law of independent assortment. [NIH] Lipase: An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. It is produced by glands on the tongue and by the pancreas and initiates the digestion of dietary fats. (From Dorland, 27th ed) EC 3.1.1.3. [NIH] Lipid: Fat. [NIH] Lipid A: Lipid A is the biologically active component of lipopolysaccharides. It shows strong endotoxic activity and exhibits immunogenic properties. [NIH] Lipid Peroxidation: Peroxidase catalyzed oxidation of lipids using hydrogen peroxide as an electron acceptor. [NIH] Lipopolysaccharide: Substance consisting of polysaccaride and lipid. [NIH] Lipoprotein: Any of the lipid-protein complexes in which lipids are transported in the blood; lipoprotein particles consist of a spherical hydrophobic core of triglycerides or cholesterol esters surrounded by an amphipathic monolayer of phospholipids, cholesterol, and apolipoproteins; the four principal classes are high-density, low-density, and very-lowdensity lipoproteins and chylomicrons. [EU] Lipoprotein Lipase: An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. The enzyme hydrolyzes triacylglycerols in chylomicrons, very-low-density lipoproteins, low-density lipoproteins, and diacylglycerols. It occurs on capillary endothelial surfaces, especially in mammary, muscle, and adipose tissue. Genetic deficiency of the enzyme causes familial hyperlipoproteinemia Type I. (Dorland, 27th ed) EC 3.1.1.34. [NIH] Liposomes: Artificial, single or multilaminar vesicles (made from lecithins or other lipids) that are used for the delivery of a variety of biological molecules or molecular complexes to cells, for example, drug delivery and gene transfer. They are also used to study membranes and membrane proteins. [NIH] Lipoxygenase: An enzyme of the oxidoreductase class that catalyzes reactions between linoleate and other fatty acids and oxygen to form hydroperoxy-fatty acid derivatives. Related enzymes in this class include the arachidonate lipoxygenases, arachidonate 5lipoxygenase, arachidonate 12-lipoxygenase, and arachidonate 15-lipoxygenase. EC 1.13.11.12. [NIH] Lithium: An element in the alkali metals family. It has the atomic symbol Li, atomic number 3, and atomic weight 6.94. Salts of lithium are used in treating manic-depressive disorders. [NIH]
Liver: A large, glandular organ located in the upper abdomen. The liver cleanses the blood and aids in digestion by secreting bile. [NIH] Localization: The process of determining or marking the location or site of a lesion or
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disease. May also refer to the process of keeping a lesion or disease in a specific location or site. [NIH] Localized: Cancer which has not metastasized yet. [NIH] Locomotion: Movement or the ability to move from one place or another. It can refer to humans, vertebrate or invertebrate animals, and microorganisms. [NIH] Low-density lipoprotein: Lipoprotein that contains most of the cholesterol in the blood. LDL carries cholesterol to the tissues of the body, including the arteries. A high level of LDL increases the risk of heart disease. LDL typically contains 60 to 70 percent of the total serum cholesterol and both are directly correlated with CHD risk. [NIH] Lubricants: Oily or slippery substances. [NIH] Lucida: An instrument, invented by Wollaton, consisting essentially of a prism or a mirror through which an object can be viewed so as to appear on a plane surface seen in direct view and on which the outline of the object may be traced. [NIH] Lumen: The cavity or channel within a tube or tubular organ. [EU] Lupus: A form of cutaneous tuberculosis. It is seen predominantly in women and typically involves the nasal, buccal, and conjunctival mucosa. [NIH] Lyases: A class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4. [NIH] Lymph: The almost colorless fluid that travels through the lymphatic system and carries cells that help fight infection and disease. [NIH] Lymphatic: The tissues and organs, including the bone marrow, spleen, thymus, and lymph nodes, that produce and store cells that fight infection and disease. [NIH] Lymphatic system: The tissues and organs that produce, store, and carry white blood cells that fight infection and other diseases. This system includes the bone marrow, spleen, thymus, lymph nodes and a network of thin tubes that carry lymph and white blood cells. These tubes branch, like blood vessels, into all the tissues of the body. [NIH] Lymphoblasts: Interferon produced predominantly by leucocyte cells. [NIH] Lymphocyte: A white blood cell. Lymphocytes have a number of roles in the immune system, including the production of antibodies and other substances that fight infection and diseases. [NIH] Lymphoid: Referring to lymphocytes, a type of white blood cell. Also refers to tissue in which lymphocytes develop. [NIH] Lymphokines: Soluble protein factors generated by activated lymphocytes that affect other cells, primarily those involved in cellular immunity. [NIH] Lymphoma: A general term for various neoplastic diseases of the lymphoid tissue. [NIH] Lysine: An essential amino acid. It is often added to animal feed. [NIH] Macrophage: A type of white blood cell that surrounds and kills microorganisms, removes dead cells, and stimulates the action of other immune system cells. [NIH] Macrophage Activation: The process of altering the morphology and functional activity of macrophages so that they become avidly phagocytic. It is initiated by lymphokines, such as the macrophage activation factor (MAF) and the macrophage migration-inhibitory factor (MMIF), immune complexes, C3b, and various peptides, polysaccharides, and immunologic adjuvants. [NIH] Malabsorption: Impaired intestinal absorption of nutrients. [EU] Malignant: Cancerous; a growth with a tendency to invade and destroy nearby tissue and
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spread to other parts of the body. [NIH] Malnutrition: A condition caused by not eating enough food or not eating a balanced diet. [NIH]
Mammary: Pertaining to the mamma, or breast. [EU] Mandible: The largest and strongest bone of the face constituting the lower jaw. It supports the lower teeth. [NIH] Manic: Affected with mania. [EU] Mannans: Polysaccharides consisting of mannose units. [NIH] Mannosyltransferases: Enzymes that catalyze the transfer of mannose from a nucleoside diphosphate mannose to an acceptor molecule which is frequently another carbohydrate. The group includes EC 2.4.1.32, EC 2.4.1.48, EC 2.4.1.54, and EC 2.4.1.57. [NIH] Matrix metalloproteinase: A member of a group of enzymes that can break down proteins, such as collagen, that are normally found in the spaces between cells in tissues (i.e., extracellular matrix proteins). Because these enzymes need zinc or calcium atoms to work properly, they are called metalloproteinases. Matrix metalloproteinases are involved in wound healing, angiogenesis, and tumor cell metastasis. [NIH] Meat: The edible portions of any animal used for food including domestic mammals (the major ones being cattle, swine, and sheep) along with poultry, fish, shellfish, and game. [NIH]
Medial: Lying near the midsaggital plane of the body; opposed to lateral. [NIH] Mediate: Indirect; accomplished by the aid of an intervening medium. [EU] Mediator: An object or substance by which something is mediated, such as (1) a structure of the nervous system that transmits impulses eliciting a specific response; (2) a chemical substance (transmitter substance) that induces activity in an excitable tissue, such as nerve or muscle; or (3) a substance released from cells as the result of the interaction of antigen with antibody or by the action of antigen with a sensitized lymphocyte. [EU] Medical Staff: Professional medical personnel who provide care to patients in an organized facility, institution or agency. [NIH] Medicament: A medicinal substance or agent. [EU] MEDLINE: An online database of MEDLARS, the computerized bibliographic Medical Literature Analysis and Retrieval System of the National Library of Medicine. [NIH] Megaloblastic: A large abnormal red blood cell appearing in the blood in pernicious anaemia. [EU] Meiosis: A special method of cell division, occurring in maturation of the germ cells, by means of which each daughter nucleus receives half the number of chromosomes characteristic of the somatic cells of the species. [NIH] Melanin: The substance that gives the skin its color. [NIH] Melanocytes: Epidermal dendritic pigment cells which control long-term morphological color changes by alteration in their number or in the amount of pigment they produce and store in the pigment containing organelles called melanosomes. Melanophores are larger cells which do not exist in mammals. [NIH] Melanoma: A form of skin cancer that arises in melanocytes, the cells that produce pigment. Melanoma usually begins in a mole. [NIH] Membrane: A very thin layer of tissue that covers a surface. [NIH] Membrane Proteins: Proteins which are found in membranes including cellular and
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intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. [NIH] Meningitis: Inflammation of the meninges. When it affects the dura mater, the disease is termed pachymeningitis; when the arachnoid and pia mater are involved, it is called leptomeningitis, or meningitis proper. [EU] Menopause: Permanent cessation of menstruation. [NIH] Menstruation: The normal physiologic discharge through the vagina of blood and mucosal tissues from the nonpregnant uterus. [NIH] Mental Disorders: Psychiatric illness or diseases manifested by breakdowns in the adaptational process expressed primarily as abnormalities of thought, feeling, and behavior producing either distress or impairment of function. [NIH] Menthol: An alcohol produced from mint oils or prepared synthetically. [NIH] Mesenchymal: Refers to cells that develop into connective tissue, blood vessels, and lymphatic tissue. [NIH] Mesentery: A layer of the peritoneum which attaches the abdominal viscera to the abdominal wall and conveys their blood vessels and nerves. [NIH] Mesoderm: The middle germ layer of the embryo. [NIH] Mesothelial: It lines the peritonealla and pleural cavities. [NIH] Meta-Analysis: A quantitative method of combining the results of independent studies (usually drawn from the published literature) and synthesizing summaries and conclusions which may be used to evaluate therapeutic effectiveness, plan new studies, etc., with application chiefly in the areas of research and medicine. [NIH] Metabolic disorder: A condition in which normal metabolic processes are disrupted, usually because of a missing enzyme. [NIH] Metabolite: Any substance produced by metabolism or by a metabolic process. [EU] Metaphase: The second phase of cell division, in which the chromosomes line up across the equatorial plane of the spindle prior to separation. [NIH] Metastasis: The spread of cancer from one part of the body to another. Tumors formed from cells that have spread are called "secondary tumors" and contain cells that are like those in the original (primary) tumor. The plural is metastases. [NIH] Methicillin Resistance: Non-susceptibility of a microbe to the action of methicillin, a semisynthetic penicillin derivative. [NIH] Methionine: A sulfur containing essential amino acid that is important in many body functions. It is a chelating agent for heavy metals. [NIH] Methylene Blue: A compound consisting of dark green crystals or crystalline powder, having a bronze-like luster. Solutions in water or alcohol have a deep blue color. Methylene blue is used as a bacteriologic stain and as an indicator. It inhibits Guanylate cyclase, and has been used to treat cyanide poisoning and to lower levels of methemoglobin. [NIH] MI: Myocardial infarction. Gross necrosis of the myocardium as a result of interruption of the blood supply to the area; it is almost always caused by atherosclerosis of the coronary arteries, upon which coronary thrombosis is usually superimposed. [NIH] Microbe: An organism which cannot be observed with the naked eye; e. g. unicellular animals, lower algae, lower fungi, bacteria. [NIH] Microbiology: The study of microorganisms such as fungi, bacteria, algae, archaea, and
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viruses. [NIH] Microorganism: An organism that can be seen only through a microscope. Microorganisms include bacteria, protozoa, algae, and fungi. Although viruses are not considered living organisms, they are sometimes classified as microorganisms. [NIH] Micro-organism: An organism which cannot be observed with the naked eye; e. g. unicellular animals, lower algae, lower fungi, bacteria. [NIH] Microscopy: The application of microscope magnification to the study of materials that cannot be properly seen by the unaided eye. [NIH] Microspheres: Small uniformly-sized spherical particles frequently radioisotopes or various reagents acting as tags or markers. [NIH]
labeled
with
Microtubule-Associated Proteins: High molecular weight proteins found in the microtubules of the cytoskeletal system. Under certain conditions they are required for tubulin assembly into the microtubules and stabilize the assembled microtubules. [NIH] Microtubules: Slender, cylindrical filaments found in the cytoskeleton of plant and animal cells. They are composed of the protein tubulin. [NIH] Microvillus: A minute process or protrusion from the free surface of a cell. [EU] Migration: The systematic movement of genes between populations of the same species, geographic race, or variety. [NIH] Milligram: A measure of weight. A milligram is approximately 450,000-times smaller than a pound and 28,000-times smaller than an ounce. [NIH] Milliliter: A measure of volume for a liquid. A milliliter is approximately 950-times smaller than a quart and 30-times smaller than a fluid ounce. A milliliter of liquid and a cubic centimeter (cc) of liquid are the same. [NIH] Mineral Oil: A mixture of liquid hydrocarbons obtained from petroleum. It is used as laxative, lubricant, ointment base, and emollient. [NIH] Miotic: 1. Pertaining to, characterized by, or producing miosis : contraction of the pupil. 2. An agent that causes the pupil to contract. 3. Meiotic: characterized by cell division. [EU] Mitomycin: An antineoplastic antibiotic produced by Streptomyces caespitosus. It acts as a bi- or trifunctional alkylating agent causing cross-linking of DNA and inhibition of DNA synthesis. [NIH] Mitosis: A method of indirect cell division by means of which the two daughter nuclei normally receive identical complements of the number of chromosomes of the somatic cells of the species. [NIH] Mitotic: Cell resulting from mitosis. [NIH] Mobility: Capability of movement, of being moved, or of flowing freely. [EU] Modification: A change in an organism, or in a process in an organism, that is acquired from its own activity or environment. [NIH] Molecular: Of, pertaining to, or composed of molecules : a very small mass of matter. [EU] Molecular Evolution: Multiple rounds of selection, amplification, and mutation leading to molecules with the desired properties. [NIH] Molecular mass: The sum of the atomic masses of all atoms in a molecule, based on a scale in which the atomic masses of hydrogen, carbon, nitrogen, and oxygen are 1, 12, 14, and 16, respectively. For example, the molecular mass of water, which has two atoms of hydrogen and one atom of oxygen, is 18 (i.e., 2 + 16). [NIH] Molecular Probes: A group of atoms or molecules attached to other molecules or cellular
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structures and used in studying the properties of these molecules and structures. Radioactive DNA or RNA sequences are used in molecular genetics to detect the presence of a complementary sequence by molecular hybridization. [NIH] Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds. [NIH] Molecule: A chemical made up of two or more atoms. The atoms in a molecule can be the same (an oxygen molecule has two oxygen atoms) or different (a water molecule has two hydrogen atoms and one oxygen atom). Biological molecules, such as proteins and DNA, can be made up of many thousands of atoms. [NIH] Monensin: An antiprotozoal agent produced by Streptomyces cinnamonensis. It exerts its effect during the development of first-generation trophozoites into first-generation schizonts within the intestinal epithelial cells. It does not interfere with hosts' development of acquired immunity to the majority of coccidial species. Monensin is a sodium and proton selective ionophore and is widely used as such in biochemical studies. [NIH] Monitor: An apparatus which automatically records such physiological signs as respiration, pulse, and blood pressure in an anesthetized patient or one undergoing surgical or other procedures. [NIH] Monoamine: Enzyme that breaks down dopamine in the astrocytes and microglia. [NIH] Monoamine Oxidase: An enzyme that catalyzes the oxidative deamination of naturally occurring monoamines. It is a flavin-containing enzyme that is localized in mitochondrial membranes, whether in nerve terminals, the liver, or other organs. Monoamine oxidase is important in regulating the metabolic degradation of catecholamines and serotonin in neural or target tissues. Hepatic monoamine oxidase has a crucial defensive role in inactivating circulating monoamines or those, such as tyramine, that originate in the gut and are absorbed into the portal circulation. (From Goodman and Gilman's, The Pharmacological Basis of Therapeutics, 8th ed, p415) EC 1.4.3.4. [NIH] Monoclonal: An antibody produced by culturing a single type of cell. It therefore consists of a single species of immunoglobulin molecules. [NIH] Monoclonal antibodies: Laboratory-produced substances that can locate and bind to cancer cells wherever they are in the body. Many monoclonal antibodies are used in cancer detection or therapy; each one recognizes a different protein on certain cancer cells. Monoclonal antibodies can be used alone, or they can be used to deliver drugs, toxins, or radioactive material directly to a tumor. [NIH] Monocyte: A type of white blood cell. [NIH] Morphine: The principal alkaloid in opium and the prototype opiate analgesic and narcotic. Morphine has widespread effects in the central nervous system and on smooth muscle. [NIH] Morphological: Relating to the configuration or the structure of live organs. [NIH] Morphology: The science of the form and structure of organisms (plants, animals, and other forms of life). [NIH] Motility: The ability to move spontaneously. [EU] Motor nerve: An efferent nerve conveying an impulse that excites muscular contraction. [NIH]
Mucocutaneous: Pertaining to or affecting the mucous membrane and the skin. [EU] Mucolytic: Destroying or dissolving mucin; an agent that so acts : a mucopolysaccharide or glycoprotein, the chief constituent of mucus. [EU] Mucosa: A mucous membrane, or tunica mucosa. [EU]
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Mucosal Lining: The lining of GI tract organs that makes mucus. [NIH] Mucositis: A complication of some cancer therapies in which the lining of the digestive system becomes inflamed. Often seen as sores in the mouth. [NIH] Mucus: The viscous secretion of mucous membranes. It contains mucin, white blood cells, water, inorganic salts, and exfoliated cells. [NIH] Multiple Organ Failure: A progressive condition usually characterized by combined failure of several organs such as the lungs, liver, kidney, along with some clotting mechanisms, usually postinjury or postoperative. [NIH] Muscle Contraction: A process leading to shortening and/or development of tension in muscle tissue. Muscle contraction occurs by a sliding filament mechanism whereby actin filaments slide inward among the myosin filaments. [NIH] Muscle Fibers: Large single cells, either cylindrical or prismatic in shape, that form the basic unit of muscle tissue. They consist of a soft contractile substance enclosed in a tubular sheath. [NIH] Muscle relaxant: An agent that specifically aids in reducing muscle tension, as those acting at the polysynaptic neurons of motor nerves (e.g. meprobamate) or at the myoneural junction (curare and related compounds). [EU] Muscle tension: A force in a material tending to produce extension; the state of being stretched. [NIH] Muscular Atrophy: Derangement in size and number of muscle fibers occurring with aging, reduction in blood supply, or following immobilization, prolonged weightlessness, malnutrition, and particularly in denervation. [NIH] Muscular Dystrophies: A general term for a group of inherited disorders which are characterized by progressive degeneration of skeletal muscles. [NIH] Musculoskeletal System: Themuscles, bones, and cartilage of the body. [NIH] Mutagenesis: Process of generating genetic mutations. It may occur spontaneously or be induced by mutagens. [NIH] Mutagens: Chemical agents that increase the rate of genetic mutation by interfering with the function of nucleic acids. A clastogen is a specific mutagen that causes breaks in chromosomes. [NIH] Myalgia: Pain in a muscle or muscles. [EU] Myelogenous: Produced by, or originating in, the bone marrow. [NIH] Myocardial infarction: Gross necrosis of the myocardium as a result of interruption of the blood supply to the area; it is almost always caused by atherosclerosis of the coronary arteries, upon which coronary thrombosis is usually superimposed. [NIH] Myocardium: The muscle tissue of the heart composed of striated, involuntary muscle known as cardiac muscle. [NIH] Myosin: Chief protein in muscle and the main constituent of the thick filaments of muscle fibers. In conjunction with actin, it is responsible for the contraction and relaxation of muscles. [NIH] Myotonic Dystrophy: A condition presenting muscle weakness and wasting which may be progressive. [NIH] N-acetyl: Analgesic agent. [NIH] Narcosis: A general and nonspecific reversible depression of neuronal excitability, produced by a number of physical and chemical aspects, usually resulting in stupor. [NIH]
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Narcotic: 1. Pertaining to or producing narcosis. 2. An agent that produces insensibility or stupor, applied especially to the opioids, i.e. to any natural or synthetic drug that has morphine-like actions. [EU] Nasal Mucosa: The mucous membrane lining the nasal cavity. [NIH] Natural selection: A part of the evolutionary process resulting in the survival and reproduction of the best adapted individuals. [NIH] Nausea: An unpleasant sensation in the stomach usually accompanied by the urge to vomit. Common causes are early pregnancy, sea and motion sickness, emotional stress, intense pain, food poisoning, and various enteroviruses. [NIH] NCI: National Cancer Institute. NCI, part of the National Institutes of Health of the United States Department of Health and Human Services, is the federal government's principal agency for cancer research. NCI conducts, coordinates, and funds cancer research, training, health information dissemination, and other programs with respect to the cause, diagnosis, prevention, and treatment of cancer. Access the NCI Web site at http://cancer.gov. [NIH] Necrosis: A pathological process caused by the progressive degradative action of enzymes that is generally associated with severe cellular trauma. It is characterized by mitochondrial swelling, nuclear flocculation, uncontrolled cell lysis, and ultimately cell death. [NIH] Need: A state of tension or dissatisfaction felt by an individual that impels him to action toward a goal he believes will satisfy the impulse. [NIH] Neonatal: Pertaining to the first four weeks after birth. [EU] Neoplasia: Abnormal and uncontrolled cell growth. [NIH] Neoplasm: A new growth of benign or malignant tissue. [NIH] Neoplastic: Pertaining to or like a neoplasm (= any new and abnormal growth); pertaining to neoplasia (= the formation of a neoplasm). [EU] Nephropathy: Disease of the kidneys. [EU] Nerve: A cordlike structure of nervous tissue that connects parts of the nervous system with other tissues of the body and conveys nervous impulses to, or away from, these tissues. [NIH] Nerve Endings: Specialized terminations of peripheral neurons. Nerve endings include neuroeffector junction(s) by which neurons activate target organs and sensory receptors which transduce information from the various sensory modalities and send it centrally in the nervous system. Presynaptic nerve endings are presynaptic terminals. [NIH] Nerve Fibers: Slender processes of neurons, especially the prolonged axons that conduct nerve impulses. [NIH] Nervous System: The entire nerve apparatus composed of the brain, spinal cord, nerves and ganglia. [NIH] Neural: 1. Pertaining to a nerve or to the nerves. 2. Situated in the region of the spinal axis, as the neutral arch. [EU] Neural Crest: A strip of specialized ectoderm flanking each side of the embryonal neural plate, which after the closure of the neural tube, forms a column of isolated cells along the dorsal aspect of the neural tube. Most of the cranial and all of the spinal sensory ganglion cells arise by differentiation of neural crest cells. [NIH] Neuraminidase: An enzyme that catalyzes the hydrolysis of alpha-2,3, alpha-2,6-, and alpha-2,8-glycosidic linkages (at a decreasing rate, respectively) of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid, and synthetic substrate. (From Enzyme Nomenclature, 1992) EC 3.2.1.18. [NIH] Neuroblastoma: Cancer that arises in immature nerve cells and affects mostly infants and
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children. [NIH] Neurofilaments: Bundle of neuronal fibers. [NIH] Neuronal: Pertaining to a neuron or neurons (= conducting cells of the nervous system). [EU] Neurons: The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the nervous system. [NIH] Neurotransmitters: Endogenous signaling molecules that alter the behavior of neurons or effector cells. Neurotransmitter is used here in its most general sense, including not only messengers that act directly to regulate ion channels, but also those that act through second messenger systems, and those that act at a distance from their site of release. Included are neuromodulators, neuroregulators, neuromediators, and neurohumors, whether or not acting at synapses. [NIH] Neutrons: Electrically neutral elementary particles found in all atomic nuclei except light hydrogen; the mass is equal to that of the proton and electron combined and they are unstable when isolated from the nucleus, undergoing beta decay. Slow, thermal, epithermal, and fast neutrons refer to the energy levels with which the neutrons are ejected from heavier nuclei during their decay. [NIH] Neutrophil: A type of white blood cell. [NIH] Niacin: Water-soluble vitamin of the B complex occurring in various animal and plant tissues. Required by the body for the formation of coenzymes NAD and NADP. Has pellagra-curative, vasodilating, and antilipemic properties. [NIH] Nickel: A trace element with the atomic symbol Ni, atomic number 28, and atomic weight 58.69. It is a cofactor of the enzyme urease. [NIH] Nifedipine: A potent vasodilator agent with calcium antagonistic action. It is a useful antianginal agent that also lowers blood pressure. The use of nifedipine as a tocolytic is being investigated. [NIH] Nitric Oxide: A free radical gas produced endogenously by a variety of mammalian cells. It is synthesized from arginine by a complex reaction, catalyzed by nitric oxide synthase. Nitric oxide is endothelium-derived relaxing factor. It is released by the vascular endothelium and mediates the relaxation induced by some vasodilators such as acetylcholine and bradykinin. It also inhibits platelet aggregation, induces disaggregation of aggregated platelets, and inhibits platelet adhesion to the vascular endothelium. Nitric oxide activates cytosolic guanylate cyclase and thus elevates intracellular levels of cyclic GMP. [NIH]
Nitrogen: An element with the atomic symbol N, atomic number 7, and atomic weight 14. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells. [NIH] Nocodazole: Nocodazole is an antineoplastic agent which exerts its effect by depolymerizing microtubules. [NIH] Norepinephrine: Precursor of epinephrine that is secreted by the adrenal medulla and is a widespread central and autonomic neurotransmitter. Norepinephrine is the principal transmitter of most postganglionic sympathetic fibers and of the diffuse projection system in the brain arising from the locus ceruleus. It is also found in plants and is used pharmacologically as a sympathomimetic. [NIH] Nosocomial: Pertaining to or originating in the hospital, said of an infection not present or incubating prior to admittance to the hospital, but generally occurring 72 hours after admittance; the term is usually used to refer to patient disease, but hospital personnel may
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also acquire nosocomial infection. [EU] Novobiocin: An antibiotic drug used to treat infection. [NIH] Nuclear: A test of the structure, blood flow, and function of the kidneys. The doctor injects a mildly radioactive solution into an arm vein and uses x-rays to monitor its progress through the kidneys. [NIH] Nuclear Pore: An opening through the nuclear envelope formed by the nuclear pore complex which transports nuclear proteins or RNA into or out of the cell nucleus and which, under some conditions, acts as an ion channel. [NIH] Nuclear Proteins: Proteins found in the nucleus of a cell. Do not confuse with nucleoproteins which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus. [NIH] Nuclei: A body of specialized protoplasm found in nearly all cells and containing the chromosomes. [NIH] Nucleic acid: Either of two types of macromolecule (DNA or RNA) formed by polymerization of nucleotides. Nucleic acids are found in all living cells and contain the information (genetic code) for the transfer of genetic information from one generation to the next. [NIH] Nucleolus: A small dense body (sub organelle) within the nucleus of eukaryotic cells, visible by phase contrast and interference microscopy in live cells throughout interphase. Contains RNA and protein and is the site of synthesis of ribosomal RNA. [NIH] Nucleoproteins: Proteins conjugated with nucleic acids. [NIH] Nucleotidases: A class of enzymes that catalyze the conversion of a nucleotide and water to a nucleoside and orthophosphate. EC 3.1.3.-. [NIH] Nucleus: A body of specialized protoplasm found in nearly all cells and containing the chromosomes. [NIH] Nursing Care: Care given to patients by nursing service personnel. [NIH] Odour: A volatile emanation that is perceived by the sense of smell. [EU] Ointments: Semisolid preparations used topically for protective emollient effects or as a vehicle for local administration of medications. Ointment bases are various mixtures of fats, waxes, animal and plant oils and solid and liquid hydrocarbons. [NIH] Oligosaccharides: Carbohydrates consisting of between two and ten monosaccharides connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form. [NIH] Omega-3 fatty acid: A type of fat obtained in the diet and involved in immunity. [NIH] Oncogene: A gene that normally directs cell growth. If altered, an oncogene can promote or allow the uncontrolled growth of cancer. Alterations can be inherited or caused by an environmental exposure to carcinogens. [NIH] On-line: A sexually-reproducing population derived from a common parentage. [NIH] Oocytes: Female germ cells in stages between the prophase of the first maturation division and the completion of the second maturation division. [NIH] Opacity: Degree of density (area most dense taken for reading). [NIH] Open Reading Frames: Reading frames where successive nucleotide triplets can be read as codons specifying amino acids and where the sequence of these triplets is not interrupted by stop codons. [NIH] Operon: The genetic unit consisting of a feedback system under the control of an operator
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gene, in which a structural gene transcribes its message in the form of mRNA upon blockade of a repressor produced by a regulator gene. Included here is the attenuator site of bacterial operons where transcription termination is regulated. [NIH] Ophthalmic: Pertaining to the eye. [EU] Optic Chiasm: The X-shaped structure formed by the meeting of the two optic nerves. At the optic chiasm the fibers from the medial part of each retina cross to project to the other side of the brain while the lateral retinal fibers continue on the same side. As a result each half of the brain receives information about the contralateral visual field from both eyes. [NIH]
Organ Transplantation: Transference of an organ between individuals of the same species or between individuals of different species. [NIH] Organelles: Specific particles of membrane-bound organized living substances present in eukaryotic cells, such as the mitochondria; the golgi apparatus; endoplasmic reticulum; lysomomes; plastids; and vacuoles. [NIH] Osmosis: Tendency of fluids (e.g., water) to move from the less concentrated to the more concentrated side of a semipermeable membrane. [NIH] Osmotic: Pertaining to or of the nature of osmosis (= the passage of pure solvent from a solution of lesser to one of greater solute concentration when the two solutions are separated by a membrane which selectively prevents the passage of solute molecules, but is permeable to the solvent). [EU] Ossification: The formation of bone or of a bony substance; the conversion of fibrous tissue or of cartilage into bone or a bony substance. [EU] Osteoarthritis: A progressive, degenerative joint disease, the most common form of arthritis, especially in older persons. The disease is thought to result not from the aging process but from biochemical changes and biomechanical stresses affecting articular cartilage. In the foreign literature it is often called osteoarthrosis deformans. [NIH] Osteoblasts: Bone-forming cells which secrete an extracellular matrix. Hydroxyapatite crystals are then deposited into the matrix to form bone. [NIH] Osteoclasts: A large multinuclear cell associated with the absorption and removal of bone. An odontoclast, also called cementoclast, is cytomorphologically the same as an osteoclast and is involved in cementum resorption. [NIH] Osteogenesis: The histogenesis of bone including ossification. It occurs continuously but particularly in the embryo and child and during fracture repair. [NIH] Osteoporosis: Reduction of bone mass without alteration in the composition of bone, leading to fractures. Primary osteoporosis can be of two major types: postmenopausal osteoporosis and age-related (or senile) osteoporosis. [NIH] Osteotomy: The surgical cutting of a bone. [EU] Outpatient: A patient who is not an inmate of a hospital but receives diagnosis or treatment in a clinic or dispensary connected with the hospital. [NIH] Ovaries: The pair of female reproductive glands in which the ova, or eggs, are formed. The ovaries are located in the pelvis, one on each side of the uterus. [NIH] Ovary: Either of the paired glands in the female that produce the female germ cells and secrete some of the female sex hormones. [NIH] Overweight: An excess of body weight but not necessarily body fat; a body mass index of 25 to 29.9 kg/m2. [NIH] Ovulation: The discharge of a secondary oocyte from a ruptured graafian follicle. [NIH]
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Ovum: A female germ cell extruded from the ovary at ovulation. [NIH] Oxidation: The act of oxidizing or state of being oxidized. Chemically it consists in the increase of positive charges on an atom or the loss of negative charges. Most biological oxidations are accomplished by the removal of a pair of hydrogen atoms (dehydrogenation) from a molecule. Such oxidations must be accompanied by reduction of an acceptor molecule. Univalent o. indicates loss of one electron; divalent o., the loss of two electrons. [EU]
Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). [NIH] Oxidative metabolism: A chemical process in which oxygen is used to make energy from carbohydrates (sugars). Also known as aerobic respiration, cell respiration, or aerobic metabolism. [NIH] Oxides: Binary compounds of oxygen containing the anion O(2-). The anion combines with metals to form alkaline oxides and non-metals to form acidic oxides. [NIH] Oxygenation: The process of supplying, treating, or mixing with oxygen. No:1245 oxygenation the process of supplying, treating, or mixing with oxygen. [EU] Pacemaker: An object or substance that influences the rate at which a certain phenomenon occurs; often used alone to indicate the natural cardiac pacemaker or an artificial cardiac pacemaker. In biochemistry, a substance whose rate of reaction sets the pace for a series of interrelated reactions. [EU] Paediatric: Of or relating to the care and medical treatment of children; belonging to or concerned with paediatrics. [EU] Palliative: 1. Affording relief, but not cure. 2. An alleviating medicine. [EU] Pancreas: A mixed exocrine and endocrine gland situated transversely across the posterior abdominal wall in the epigastric and hypochondriac regions. The endocrine portion is comprised of the Islets of Langerhans, while the exocrine portion is a compound acinar gland that secretes digestive enzymes. [NIH] Pancreatic: Having to do with the pancreas. [NIH] Pancreatic cancer: Cancer of the pancreas, a salivary gland of the abdomen. [NIH] Parasite: An animal or a plant that lives on or in an organism of another species and gets at least some of its nutrition from that other organism. [NIH] Parasitic: Having to do with or being a parasite. A parasite is an animal or a plant that lives on or in an organism of another species and gets at least some of its nutrients from it. [NIH] Parietal: 1. Of or pertaining to the walls of a cavity. 2. Pertaining to or located near the parietal bone, as the parietal lobe. [EU] Paroxysmal: Recurring in paroxysms (= spasms or seizures). [EU] Partial remission: The shrinking, but not complete disappearance, of a tumor in response to therapy. Also called partial response. [NIH] Patch: A piece of material used to cover or protect a wound, an injured part, etc.: a patch over the eye. [NIH] Pathogen: Any disease-producing microorganism. [EU] Pathogenesis: The cellular events and reactions that occur in the development of disease. [NIH]
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Pathologic: 1. Indicative of or caused by a morbid condition. 2. Pertaining to pathology (= branch of medicine that treats the essential nature of the disease, especially the structural and functional changes in tissues and organs of the body caused by the disease). [EU] Pathologic Processes: The abnormal mechanisms and forms involved in the dysfunctions of tissues and organs. [NIH] Pathophysiology: Altered functions in an individual or an organ due to disease. [NIH] Patient Compliance: Voluntary cooperation of the patient in following a prescribed regimen. [NIH] Patient Education: The teaching or training of patients concerning their own health needs. [NIH]
Pelvic: Pertaining to the pelvis. [EU] Penicillin: An antibiotic drug used to treat infection. [NIH] Pentosan polysulfate: A drug used to relieve pain or discomfort associated with chronic inflammation of the bladder. It is also being evaluated for its protective effects on the gastrointestinal tract in people undergoing radiation therapy. [NIH] Pentosyltransferases: Enzymes of the transferase class that catalyze the transfer of a pentose group from one compound to another. (Dorland, 28th ed) EC 2.4.2. [NIH] Pepsin: An enzyme made in the stomach that breaks down proteins. [NIH] Pepsin A: Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice. [NIH] Peptide: Any compound consisting of two or more amino acids, the building blocks of proteins. Peptides are combined to make proteins. [NIH] Peptide Hydrolases: A subclass of enzymes from the hydrolase class that catalyze the hydrolysis of peptide bonds. Exopeptidases and endopeptidases make up the sub-subclasses for this group. EC 3.4. [NIH] Perennial: Lasting through the year of for several years. [EU] Perfusion: Bathing an organ or tissue with a fluid. In regional perfusion, a specific area of the body (usually an arm or a leg) receives high doses of anticancer drugs through a blood vessel. Such a procedure is performed to treat cancer that has not spread. [NIH] Periplasm: The space between the inner and outer membranes of a cell that is shared with the cell wall. [NIH] Peritoneal: Having to do with the peritoneum (the tissue that lines the abdominal wall and covers most of the organs in the abdomen). [NIH] Peritoneal Cavity: The space enclosed by the peritoneum. It is divided into two portions, the greater sac and the lesser sac or omental bursa, which lies behind the stomach. The two sacs are connected by the foramen of Winslow, or epiploic foramen. [NIH] Peritoneal Dialysis: Dialysis fluid being introduced into and removed from the peritoneal cavity as either a continuous or an intermittent procedure. [NIH] Peritoneum: Endothelial lining of the abdominal cavity, the parietal peritoneum covering the inside of the abdominal wall and the visceral peritoneum covering the bowel, the mesentery, and certain of the organs. The portion that covers the bowel becomes the serosal layer of the bowel wall. [NIH] Pertussis: An acute, highly contagious infection of the respiratory tract, most frequently
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affecting young children, usually caused by Bordetella pertussis; a similar illness has been associated with infection by B. parapertussis and B. bronchiseptica. It is characterized by a catarrhal stage, beginning after an incubation period of about two weeks, with slight fever, sneezing, running at the nose, and a dry cough. In a week or two the paroxysmal stage begins, with the characteristic paroxysmal cough, consisting of a deep inspiration, followed by a series of quick, short coughs, continuing until the air is expelled from the lungs; the close of the paroxysm is marked by a long-drawn, shrill, whooping inspiration, due to spasmodic closure of the glottis. This stage lasts three to four weeks, after which the convalescent stage begins, in which paroxysms grow less frequent and less violent, and finally cease. Called also whooping cough. [EU] Petroleum: Naturally occurring complex liquid hydrocarbons which, after distillation, yield combustible fuels, petrochemicals, and lubricants. [NIH] PH: The symbol relating the hydrogen ion (H+) concentration or activity of a solution to that of a given standard solution. Numerically the pH is approximately equal to the negative logarithm of H+ concentration expressed in molarity. pH 7 is neutral; above it alkalinity increases and below it acidity increases. [EU] Phagocytosis: The engulfing of microorganisms, other cells, and foreign particles by phagocytic cells. [NIH] Pharmaceutical Preparations: Drugs intended for human or veterinary use, presented in their finished dosage form. Included here are materials used in the preparation and/or formulation of the finished dosage form. [NIH] Pharmaceutical Solutions: Homogeneous liquid preparations that contain one or more chemical substances dissolved, i.e., molecularly dispersed, in a suitable solvent or mixture of mutually miscible solvents. For reasons of their ingredients, method of preparation, or use, they do not fall into another group of products. [NIH] Pharmacokinetic: The mathematical analysis of the time courses of absorption, distribution, and elimination of drugs. [NIH] Pharmacologic: Pertaining to pharmacology or to the properties and reactions of drugs. [EU] Pharynx: The hollow tube about 5 inches long that starts behind the nose and ends at the top of the trachea (windpipe) and esophagus (the tube that goes to the stomach). [NIH] Phenazopyridine: A local anesthetic that has been used in urinary tract disorders. Its use is limited by problems with toxicity (primarily blood disorders) and potential carcinogenicity. [NIH]
Phenotype: The outward appearance of the individual. It is the product of interactions between genes and between the genotype and the environment. This includes the killer phenotype, characteristic of yeasts. [NIH] Phenyl: Ingredient used in cold and flu remedies. [NIH] Phenylalanine: An aromatic amino acid that is essential in the animal diet. It is a precursor of melanin, dopamine, noradrenalin, and thyroxine. [NIH] Phosphates: Inorganic salts of phosphoric acid. [NIH] Phospholipases: A class of enzymes that catalyze the hydrolysis of phosphoglycerides or glycerophosphatidates. EC 3.1.-. [NIH] Phospholipids: Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides; glycerophospholipids) or sphingosine (sphingolipids). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system. [NIH]
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Phosphoric Monoester Hydrolases: A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3. [NIH] Phosphorus: A non-metallic element that is found in the blood, muscles, nevers, bones, and teeth, and is a component of adenosine triphosphate (ATP; the primary energy source for the body's cells.) [NIH] Phosphorylated: Attached to a phosphate group. [NIH] Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. [NIH] Photocoagulation: Using a special strong beam of light (laser) to seal off bleeding blood vessels such as in the eye. The laser can also burn away blood vessels that should not have grown in the eye. This is the main treatment for diabetic retinopathy. [NIH] Physical Examination: Systematic and thorough inspection of the patient for physical signs of disease or abnormality. [NIH] Physiologic: Having to do with the functions of the body. When used in the phrase "physiologic age," it refers to an age assigned by general health, as opposed to calendar age. [NIH]
Physiology: The science that deals with the life processes and functions of organismus, their cells, tissues, and organs. [NIH] Pigment: A substance that gives color to tissue. Pigments are responsible for the color of skin, eyes, and hair. [NIH] Pilocarpine: A slowly hydrolyzed muscarinic agonist with no nicotinic effects. Pilocarpine is used as a miotic and in the treatment of glaucoma. [NIH] Pilot study: The initial study examining a new method or treatment. [NIH] Pituitary Gland: A small, unpaired gland situated in the sella turcica tissue. It is connected to the hypothalamus by a short stalk. [NIH] Placenta: A highly vascular fetal organ through which the fetus absorbs oxygen and other nutrients and excretes carbon dioxide and other wastes. It begins to form about the eighth day of gestation when the blastocyst adheres to the decidua. [NIH] Plants: Multicellular, eukaryotic life forms of the kingdom Plantae. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (meristems); cellulose within cells providing rigidity; the absence of organs of locomotion; absense of nervous and sensory systems; and an alteration of haploid and diploid generations. [NIH] Plaque: A clear zone in a bacterial culture grown on an agar plate caused by localized destruction of bacterial cells by a bacteriophage. The concentration of infective virus in a fluid can be estimated by applying the fluid to a culture and counting the number of. [NIH] Plasma: The clear, yellowish, fluid part of the blood that carries the blood cells. The proteins that form blood clots are in plasma. [NIH] Plasma cells: A type of white blood cell that produces antibodies. [NIH] Plasma protein: One of the hundreds of different proteins present in blood plasma, including carrier proteins ( such albumin, transferrin, and haptoglobin), fibrinogen and other coagulation factors, complement components, immunoglobulins, enzyme inhibitors, precursors of substances such as angiotension and bradykinin, and many other types of proteins. [EU] Plasmids: Any extrachromosomal hereditary determinant. Plasmids are self-replicating circular molecules of DNA that are found in a variety of bacterial, archaeal, fungal, algal,
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and plant species. [NIH] Platelet Activation: A series of progressive, overlapping events triggered by exposure of the platelets to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug. [NIH] Platelet Aggregation: The attachment of platelets to one another. This clumping together can be induced by a number of agents (e.g., thrombin, collagen) and is part of the mechanism leading to the formation of a thrombus. [NIH] Platelets: A type of blood cell that helps prevent bleeding by causing blood clots to form. Also called thrombocytes. [NIH] Platinum: Platinum. A heavy, soft, whitish metal, resembling tin, atomic number 78, atomic weight 195.09, symbol Pt. (From Dorland, 28th ed) It is used in manufacturing equipment for laboratory and industrial use. It occurs as a black powder (platinum black) and as a spongy substance (spongy platinum) and may have been known in Pliny's time as "alutiae". [NIH]
Pleated: Particular three-dimensional pattern of amyloidoses. [NIH] Pleural: A circumscribed area of hyaline whorled fibrous tissue which appears on the surface of the parietal pleura, on the fibrous part of the diaphragm or on the pleura in the interlobar fissures. [NIH] Point Mutation: A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair. [NIH] Poisoning: A condition or physical state produced by the ingestion, injection or inhalation of, or exposure to a deleterious agent. [NIH] Pollen: The male fertilizing element of flowering plants analogous to sperm in animals. It is released from the anthers as yellow dust, to be carried by insect or other vectors, including wind, to the ovary (stigma) of other flowers to produce the embryo enclosed by the seed. The pollens of many plants are allergenic. [NIH] Polyarthritis: An inflammation of several joints together. [EU] Polycystic: An inherited disorder characterized by many grape-like clusters of fluid-filled cysts that make both kidneys larger over time. These cysts take over and destroy working kidney tissue. PKD may cause chronic renal failure and end-stage renal disease. [NIH] Polymerase: An enzyme which catalyses the synthesis of DNA using a single DNA strand as a template. The polymerase copies the template in the 5'-3'direction provided that sufficient quantities of free nucleotides, dATP and dTTP are present. [NIH] Polymers: Compounds formed by the joining of smaller, usually repeating, units linked by covalent bonds. These compounds often form large macromolecules (e.g., polypeptides, proteins, plastics). [NIH] Polymorphism: The occurrence together of two or more distinct forms in the same population. [NIH] Polypeptide: A peptide which on hydrolysis yields more than two amino acids; called tripeptides, tetrapeptides, etc. according to the number of amino acids contained. [EU] Polysaccharide: A type of carbohydrate. It contains sugar molecules that are linked together chemically. [NIH] Posterior: Situated in back of, or in the back part of, or affecting the back or dorsal surface of the body. In lower animals, it refers to the caudal end of the body. [EU] Postmenopausal: Refers to the time after menopause. Menopause is the time in a woman's
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life when menstrual periods stop permanently; also called "change of life." [NIH] Postoperative: After surgery. [NIH] Postsynaptic: Nerve potential generated by an inhibitory hyperpolarizing stimulation. [NIH] Post-translational: The cleavage of signal sequence that directs the passage of the protein through a cell or organelle membrane. [NIH] Potassium: An element that is in the alkali group of metals. It has an atomic symbol K, atomic number 19, and atomic weight 39.10. It is the chief cation in the intracellular fluid of muscle and other cells. Potassium ion is a strong electrolyte and it plays a significant role in the regulation of fluid volume and maintenance of the water-electrolyte balance. [NIH] Potentiate: A degree of synergism which causes the exposure of the organism to a harmful substance to worsen a disease already contracted. [NIH] Potentiating: A degree of synergism which causes the exposure of the organism to a harmful substance to worsen a disease already contracted. [NIH] Potentiation: An overall effect of two drugs taken together which is greater than the sum of the effects of each drug taken alone. [NIH] Practice Guidelines: Directions or principles presenting current or future rules of policy for the health care practitioner to assist him in patient care decisions regarding diagnosis, therapy, or related clinical circumstances. The guidelines may be developed by government agencies at any level, institutions, professional societies, governing boards, or by the convening of expert panels. The guidelines form a basis for the evaluation of all aspects of health care and delivery. [NIH] Precursor: Something that precedes. In biological processes, a substance from which another, usually more active or mature substance is formed. In clinical medicine, a sign or symptom that heralds another. [EU] Predisposition: A latent susceptibility to disease which may be activated under certain conditions, as by stress. [EU] Prenatal: Existing or occurring before birth, with reference to the fetus. [EU] Prevalence: The total number of cases of a given disease in a specified population at a designated time. It is differentiated from incidence, which refers to the number of new cases in the population at a given time. [NIH] Prickle: Several layers of the epidermis where the individual cells are connected by cell bridges. [NIH] Probe: An instrument used in exploring cavities, or in the detection and dilatation of strictures, or in demonstrating the potency of channels; an elongated instrument for exploring or sounding body cavities. [NIH] Procaine: A local anesthetic of the ester type that has a slow onset and a short duration of action. It is mainly used for infiltration anesthesia, peripheral nerve block, and spinal block. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1016). [NIH] Prodrug: A substance that gives rise to a pharmacologically active metabolite, although not itself active (i. e. an inactive precursor). [NIH] Progeny: The offspring produced in any generation. [NIH] Progesterone: Pregn-4-ene-3,20-dione. The principal progestational hormone of the body, secreted by the corpus luteum, adrenal cortex, and placenta. Its chief function is to prepare the uterus for the reception and development of the fertilized ovum. It acts as an antiovulatory agent when administered on days 5-25 of the menstrual cycle. [NIH] Progression: Increase in the size of a tumor or spread of cancer in the body. [NIH]
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Progressive: Advancing; going forward; going from bad to worse; increasing in scope or severity. [EU] Proline: A non-essential amino acid that is synthesized from glutamic acid. It is an essential component of collagen and is important for proper functioning of joints and tendons. [NIH] Promoter: A chemical substance that increases the activity of a carcinogenic process. [NIH] Pronase: A proteolytic enzyme obtained from Streptomyces griseus. [NIH] Prophase: The first phase of cell division, in which the chromosomes become visible, the nucleus starts to lose its identity, the spindle appears, and the centrioles migrate toward opposite poles. [NIH] Prophylaxis: An attempt to prevent disease. [NIH] Prostaglandins: A group of compounds derived from unsaturated 20-carbon fatty acids, primarily arachidonic acid, via the cyclooxygenase pathway. They are extremely potent mediators of a diverse group of physiological processes. [NIH] Prostaglandins A: (13E,15S)-15-Hydroxy-9-oxoprosta-10,13-dien-1-oic acid (PGA(1)); (5Z,13E,15S)-15-hydroxy-9-oxoprosta-5,10,13-trien-1-oic acid (PGA(2)); (5Z,13E,15S,17Z)-15hydroxy-9-oxoprosta-5,10,13,17-tetraen-1-oic acid (PGA(3)). A group of naturally occurring secondary prostaglandins derived from PGE. PGA(1) and PGA(2) as well as their 19hydroxy derivatives are found in many organs and tissues. [NIH] Prostaglandins D: Physiologically active prostaglandins found in many tissues and organs. They show pressor activity, are mediators of inflammation, and have potential antithrombotic effects. [NIH] Prostate: A gland in males that surrounds the neck of the bladder and the urethra. It secretes a substance that liquifies coagulated semen. It is situated in the pelvic cavity behind the lower part of the pubic symphysis, above the deep layer of the triangular ligament, and rests upon the rectum. [NIH] Protease: Proteinase (= any enzyme that catalyses the splitting of interior peptide bonds in a protein). [EU] Protective Agents: Synthetic or natural substances which are given to prevent a disease or disorder or are used in the process of treating a disease or injury due to a poisonous agent. [NIH]
Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific proteinbinding measures are often used as assays in diagnostic assessments. [NIH] Protein C: A vitamin-K dependent zymogen present in the blood, which, upon activation by thrombin and thrombomodulin exerts anticoagulant properties by inactivating factors Va and VIIIa at the rate-limiting steps of thrombin formation. [NIH] Protein S: The vitamin K-dependent cofactor of activated protein C. Together with protein C, it inhibits the action of factors VIIIa and Va. A deficiency in protein S can lead to recurrent venous and arterial thrombosis. [NIH] Proteins: Polymers of amino acids linked by peptide bonds. The specific sequence of amino acids determines the shape and function of the protein. [NIH] Protein-Tyrosine Kinase: An enzyme that catalyzes the phosphorylation of tyrosine residues in proteins with ATP or other nucleotides as phosphate donors. EC 2.7.1.112. [NIH] Proteinuria: The presence of protein in the urine, indicating that the kidneys are not working properly. [NIH] Proteoglycan: A molecule that contains both protein and glycosaminoglycans, which are a
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type of polysaccharide. Proteoglycans are found in cartilage and other connective tissues. [NIH]
Proteolytic: 1. Pertaining to, characterized by, or promoting proteolysis. 2. An enzyme that promotes proteolysis (= the splitting of proteins by hydrolysis of the peptide bonds with formation of smaller polypeptides). [EU] Protocol: The detailed plan for a clinical trial that states the trial's rationale, purpose, drug or vaccine dosages, length of study, routes of administration, who may participate, and other aspects of trial design. [NIH] Protons: Stable elementary particles having the smallest known positive charge, found in the nuclei of all elements. The proton mass is less than that of a neutron. A proton is the nucleus of the light hydrogen atom, i.e., the hydrogen ion. [NIH] Protozoa: A subkingdom consisting of unicellular organisms that are the simplest in the animal kingdom. Most are free living. They range in size from submicroscopic to macroscopic. Protozoa are divided into seven phyla: Sarcomastigophora, Labyrinthomorpha, Apicomplexa, Microspora, Ascetospora, Myxozoa, and Ciliophora. [NIH] Proximal: Nearest; closer to any point of reference; opposed to distal. [EU] Pruritic: Pertaining to or characterized by pruritus. [EU] Pruritus: An intense itching sensation that produces the urge to rub or scratch the skin to obtain relief. [NIH] Psoriasis: A common genetically determined, chronic, inflammatory skin disease characterized by rounded erythematous, dry, scaling patches. The lesions have a predilection for nails, scalp, genitalia, extensor surfaces, and the lumbosacral region. Accelerated epidermopoiesis is considered to be the fundamental pathologic feature in psoriasis. [NIH] Psychomotor: Pertaining to motor effects of cerebral or psychic activity. [EU] Psyllium: Dried, ripe seeds of Plantago psyllium, P. indica, and P. ovata (Plantaginaceae). Plantain seeds swell in water and are used as demulcents and bulk laxatives. [NIH] Public Policy: A course or method of action selected, usually by a government, from among alternatives to guide and determine present and future decisions. [NIH] Publishing: "The business or profession of the commercial production and issuance of literature" (Webster's 3d). It includes the publisher, publication processes, editing and editors. Production may be by conventional printing methods or by electronic publishing. [NIH]
Pulmonary: Relating to the lungs. [NIH] Pulse: The rhythmical expansion and contraction of an artery produced by waves of pressure caused by the ejection of blood from the left ventricle of the heart as it contracts. [NIH]
Purifying: Respiratory equipment whose function is to remove contaminants from otherwise wholesome air. [NIH] Purines: A series of heterocyclic compounds that are variously substituted in nature and are known also as purine bases. They include adenine and guanine, constituents of nucleic acids, as well as many alkaloids such as caffeine and theophylline. Uric acid is the metabolic end product of purine metabolism. [NIH] Pustular: Pertaining to or of the nature of a pustule; consisting of pustules (= a visible collection of pus within or beneath the epidermis). [EU] Quality of Life: A generic concept reflecting concern with the modification and
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enhancement of life attributes, e.g., physical, political, moral and social environment. [NIH] Quaternary: 1. Fourth in order. 2. Containing four elements or groups. [EU] Quercetin: Aglucon of quercetrin, rutin, and other glycosides. It is widely distributed in the plant kingdom, especially in rinds and barks, clover blossoms, and ragweed pollen. [NIH] Quiescent: Marked by a state of inactivity or repose. [EU] Race: A population within a species which exhibits general similarities within itself, but is both discontinuous and distinct from other populations of that species, though not sufficiently so as to achieve the status of a taxon. [NIH] Radiation: Emission or propagation of electromagnetic energy (waves/rays), or the waves/rays themselves; a stream of electromagnetic particles (electrons, neutrons, protons, alpha particles) or a mixture of these. The most common source is the sun. [NIH] Radiation therapy: The use of high-energy radiation from x-rays, gamma rays, neutrons, and other sources to kill cancer cells and shrink tumors. Radiation may come from a machine outside the body (external-beam radiation therapy), or it may come from radioactive material placed in the body in the area near cancer cells (internal radiation therapy, implant radiation, or brachytherapy). Systemic radiation therapy uses a radioactive substance, such as a radiolabeled monoclonal antibody, that circulates throughout the body. Also called radiotherapy. [NIH] Radioactive: Giving off radiation. [NIH] Radiolabeled: Any compound that has been joined with a radioactive substance. [NIH] Radiology: A specialty concerned with the use of x-ray and other forms of radiant energy in the diagnosis and treatment of disease. [NIH] Radiotherapy: The use of ionizing radiation to treat malignant neoplasms and other benign conditions. The most common forms of ionizing radiation used as therapy are x-rays, gamma rays, and electrons. A special form of radiotherapy, targeted radiotherapy, links a cytotoxic radionuclide to a molecule that targets the tumor. When this molecule is an antibody or other immunologic molecule, the technique is called radioimmunotherapy. [NIH] Randomized: Describes an experiment or clinical trial in which animal or human subjects are assigned by chance to separate groups that compare different treatments. [NIH] Randomized clinical trial: A study in which the participants are assigned by chance to separate groups that compare different treatments; neither the researchers nor the participants can choose which group. Using chance to assign people to groups means that the groups will be similar and that the treatments they receive can be compared objectively. At the time of the trial, it is not known which treatment is best. It is the patient's choice to be in a randomized trial. [NIH] Rationalize: To attribute one's actions to rational and creditable motives without adequate analysis of the true and unconscious motives. [NIH] Reactive Oxygen Species: Reactive intermediate oxygen species including both radicals and non-radicals. These substances are constantly formed in the human body and have been shown to kill bacteria and inactivate proteins, and have been implicated in a number of diseases. Scientific data exist that link the reactive oxygen species produced by inflammatory phagocytes to cancer development. [NIH] Receptor: A molecule inside or on the surface of a cell that binds to a specific substance and causes a specific physiologic effect in the cell. [NIH] Receptors, Serotonin: Cell-surface proteins that bind serotonin and trigger intracellular changes which influence the behavior of cells. Several types of serotonin receptors have been
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recognized which differ in their pharmacology, molecular biology, and mode of action. [NIH] Recombinant: A cell or an individual with a new combination of genes not found together in either parent; usually applied to linked genes. [EU] Recombinant Proteins: Proteins prepared by recombinant DNA technology. [NIH] Recombination: The formation of new combinations of genes as a result of segregation in crosses between genetically different parents; also the rearrangement of linked genes due to crossing-over. [NIH] Rectum: The last 8 to 10 inches of the large intestine. [NIH] Red blood cells: RBCs. Cells that carry oxygen to all parts of the body. Also called erythrocytes. [NIH] Red Nucleus: A pinkish-yellow portion of the midbrain situated in the rostral mesencephalic tegmentum. It receives a large projection from the contralateral half of the cerebellum via the superior cerebellar peduncle and a projection from the ipsilateral motor cortex. [NIH] Reductase: Enzyme converting testosterone to dihydrotestosterone. [NIH] Refer: To send or direct for treatment, aid, information, de decision. [NIH] Refraction: A test to determine the best eyeglasses or contact lenses to correct a refractive error (myopia, hyperopia, or astigmatism). [NIH] Regeneration: The natural renewal of a structure, as of a lost tissue or part. [EU] Regimen: A treatment plan that specifies the dosage, the schedule, and the duration of treatment. [NIH] Relapse: The return of signs and symptoms of cancer after a period of improvement. [NIH] Relaxant: 1. Lessening or reducing tension. 2. An agent that lessens tension. [EU] Remission: A decrease in or disappearance of signs and symptoms of cancer. In partial remission, some, but not all, signs and symptoms of cancer have disappeared. In complete remission, all signs and symptoms of cancer have disappeared, although there still may be cancer in the body. [NIH] Renin: An enzyme which is secreted by the kidney and is formed from prorenin in plasma and kidney. The enzyme cleaves the Leu-Leu bond in angiotensinogen to generate angiotensin I. EC 3.4.23.15. (Formerly EC 3.4.99.19). [NIH] Repressor: Any of the specific allosteric protein molecules, products of regulator genes, which bind to the operator of operons and prevent RNA polymerase from proceeding into the operon to transcribe messenger RNA. [NIH] Research Support: Financial support of research activities. [NIH] Resorption: The loss of substance through physiologic or pathologic means, such as loss of dentin and cementum of a tooth, or of the alveolar process of the mandible or maxilla. [EU] Respiration: The act of breathing with the lungs, consisting of inspiration, or the taking into the lungs of the ambient air, and of expiration, or the expelling of the modified air which contains more carbon dioxide than the air taken in (Blakiston's Gould Medical Dictionary, 4th ed.). This does not include tissue respiration (= oxygen consumption) or cell respiration (= cell respiration). [NIH] Respiratory distress syndrome: A lung disease that occurs primarily in premature infants; the newborn must struggle for each breath and blueing of its skin reflects the baby's inability to get enough oxygen. [NIH] Respiratory Distress Syndrome, Adult: A syndrome of life-threatening progressive
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pulmonary insufficiency in the absence of known pulmonary disease, usually following a systemic insult such as surgery or major trauma. [NIH] Respiratory Mucosa: The mucous membrane lining the respiratory tract. [NIH] Response rate: The percentage of patients whose cancer shrinks or disappears after treatment. [NIH] Restoration: Broad term applied to any inlay, crown, bridge or complete denture which restores or replaces loss of teeth or oral tissues. [NIH] Retina: The ten-layered nervous tissue membrane of the eye. It is continuous with the optic nerve and receives images of external objects and transmits visual impulses to the brain. Its outer surface is in contact with the choroid and the inner surface with the vitreous body. The outer-most layer is pigmented, whereas the inner nine layers are transparent. [NIH] Retinoblastoma: An eye cancer that most often occurs in children younger than 5 years. It occurs in hereditary and nonhereditary (sporadic) forms. [NIH] Retinoids: Derivatives of vitamin A. Used clinically in the treatment of severe cystic acne, psoriasis, and other disorders of keratinization. Their possible use in the prophylaxis and treatment of cancer is being actively explored. [NIH] Retinol: Vitamin A. It is essential for proper vision and healthy skin and mucous membranes. Retinol is being studied for cancer prevention; it belongs to the family of drugs called retinoids. [NIH] Reversion: A return to the original condition, e. g. the reappearance of the normal or wild type in previously mutated cells, tissues, or organisms. [NIH] Rhamnose: A methylpentose whose L- isomer is found naturally in many plant glycosides and some gram-negative bacterial lipopolysaccharides. [NIH] Rheumatism: A group of disorders marked by inflammation or pain in the connective tissue structures of the body. These structures include bone, cartilage, and fat. [NIH] Rheumatoid: Resembling rheumatism. [EU] Rheumatoid arthritis: A form of arthritis, the cause of which is unknown, although infection, hypersensitivity, hormone imbalance and psychologic stress have been suggested as possible causes. [NIH] Rheumatology: A subspecialty of internal medicine concerned with the study of inflammatory or degenerative processes and metabolic derangement of connective tissue structures which pertain to a variety of musculoskeletal disorders, such as arthritis. [NIH] Ribonucleic acid: RNA. One of the two nucleic acids found in all cells. The other is deoxyribonucleic acid (DNA). Ribonucleic acid transfers genetic information from DNA to proteins produced by the cell. [NIH] Ribose: A pentose active in biological systems usually in its D-form. [NIH] Ribosome: A granule of protein and RNA, synthesized in the nucleolus and found in the cytoplasm of cells. Ribosomes are the main sites of protein synthesis. Messenger RNA attaches to them and there receives molecules of transfer RNA bearing amino acids. [NIH] Rigidity: Stiffness or inflexibility, chiefly that which is abnormal or morbid; rigor. [EU] Risk factor: A habit, trait, condition, or genetic alteration that increases a person's chance of developing a disease. [NIH] Ristocetin: An antibiotic mixture of two components, A and B, obtained from Nocardia lurida (or the same substance produced by any other means). It is no longer used clinically because of its toxicity. It causes platelet agglutination and blood coagulation and is used to assay those functions in vitro. [NIH]
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Rod: A reception for vision, located in the retina. [NIH] Rubber: A high-molecular-weight polymeric elastomer derived from the milk juice (latex) of Hevea brasiliensis and other trees. It is a substance that can be stretched at room temperature to atleast twice its original length and after releasing the stress, retractrapidly, and recover its original dimensions fully. Synthetic rubber is made from many different chemicals, including styrene, acrylonitrile, ethylene, propylene, and isoprene. [NIH] Rutin: 3-((6-O-(6-Deoxy-alpha-L-mannopyranosyl)-beta-D-glucopyranosyl)oxy)-2-(3,4dihydroxyphenyl)-5,7-dihydroxy-4H-1-benzopyran-4-one. Found in many plants, including buckwheat, tobacco, forsythia, hydrangea, pansies, etc. It has been used therapeutically to decrease capillary fragility. [NIH] Salicylate: Non-steroidal anti-inflammatory drugs. [NIH] Salicylic: A tuberculosis drug. [NIH] Saline: A solution of salt and water. [NIH] Saliva: The clear, viscous fluid secreted by the salivary glands and mucous glands of the mouth. It contains mucins, water, organic salts, and ptylin. [NIH] Salivary: The duct that convey saliva to the mouth. [NIH] Salivary glands: Glands in the mouth that produce saliva. [NIH] Saponins: Sapogenin glycosides. A type of glycoside widely distributed in plants. Each consists of a sapogenin as the aglycon moiety, and a sugar. The sapogenin may be a steroid or a triterpene and the sugar may be glucose, galactose, a pentose, or a methylpentose. Sapogenins are poisonous towards the lower forms of life and are powerful hemolytics when injected into the blood stream able to dissolve red blood cells at even extreme dilutions. [NIH] Sarcoma: A connective tissue neoplasm formed by proliferation of mesodermal cells; it is usually highly malignant. [NIH] Scleroproteins: Simple proteins characterized by their insolubility and fibrous structure. Within the body, they perform a supportive or protective function. [NIH] Sclerosis: A pathological process consisting of hardening or fibrosis of an anatomical structure, often a vessel or a nerve. [NIH] Screening: Checking for disease when there are no symptoms. [NIH] Secondary tumor: Cancer that has spread from the organ in which it first appeared to another organ. For example, breast cancer cells may spread (metastasize) to the lungs and cause the growth of a new tumor. When this happens, the disease is called metastatic breast cancer, and the tumor in the lungs is called a secondary tumor. Also called secondary cancer. [NIH] Secretion: 1. The process of elaborating a specific product as a result of the activity of a gland; this activity may range from separating a specific substance of the blood to the elaboration of a new chemical substance. 2. Any substance produced by secretion. [EU] Secretory: Secreting; relating to or influencing secretion or the secretions. [NIH] Sedative: 1. Allaying activity and excitement. 2. An agent that allays excitement. [EU] Sedentary: 1. Sitting habitually; of inactive habits. 2. Pertaining to a sitting posture. [EU] Segmental: Describing or pertaining to a structure which is repeated in similar form in successive segments of an organism, or which is undergoing segmentation. [NIH] Seizures: Clinical or subclinical disturbances of cortical function due to a sudden, abnormal, excessive, and disorganized discharge of brain cells. Clinical manifestations include
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abnormal motor, sensory and psychic phenomena. Recurrent seizures are usually referred to as epilepsy or "seizure disorder." [NIH] Selenium: An element with the atomic symbol Se, atomic number 34, and atomic weight 78.96. It is an essential micronutrient for mammals and other animals but is toxic in large amounts. Selenium protects intracellular structures against oxidative damage. It is an essential component of glutathione peroxidase. [NIH] Self Care: Performance of activities or tasks traditionally performed by professional health care providers. The concept includes care of oneself or one's family and friends. [NIH] Sella: A deep depression in the shape of a Turkish saddle in the upper surface of the body of the sphenoid bone in the deepest part of which is lodged the hypophysis cerebri. [NIH] Semen: The thick, yellowish-white, viscid fluid secretion of male reproductive organs discharged upon ejaculation. In addition to reproductive organ secretions, it contains spermatozoa and their nutrient plasma. [NIH] Senile: Relating or belonging to old age; characteristic of old age; resulting from infirmity of old age. [NIH] Sensor: A device designed to respond to physical stimuli such as temperature, light, magnetism or movement and transmit resulting impulses for interpretation, recording, movement, or operating control. [NIH] Sepsis: The presence of bacteria in the bloodstream. [NIH] Septal: An abscess occurring at the root of the tooth on the proximal surface. [NIH] Septic: Produced by or due to decomposition by microorganisms; putrefactive. [EU] Septum: A dividing wall or partition; a general term for such a structure. The term is often used alone to refer to the septal area or to the septum pellucidum. [EU] Septum Pellucidum: A triangular double membrane separating the anterior horns of the lateral ventricles of the brain. It is situated in the median plane and bounded by the corpus callosum and the body and columns of the fornix. [NIH] Sequence Homology: The degree of similarity between sequences. Studies of amino acid and nucleotide sequences provide useful information about the genetic relatedness of certain species. [NIH] Sequencing: The determination of the order of nucleotides in a DNA or RNA chain. [NIH] Serine: A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from glycine or threonine. It is involved in the biosynthesis of purines, pyrimidines, and other amino acids. [NIH] Serotonin: A biochemical messenger and regulator, synthesized from the essential amino acid L-tryptophan. In humans it is found primarily in the central nervous system, gastrointestinal tract, and blood platelets. Serotonin mediates several important physiological functions including neurotransmission, gastrointestinal motility, hemostasis, and cardiovascular integrity. Multiple receptor families (receptors, serotonin) explain the broad physiological actions and distribution of this biochemical mediator. [NIH] Serum: The clear liquid part of the blood that remains after blood cells and clotting proteins have been removed. [NIH] Serum Albumin: A major plasma protein that serves in maintaining the plasma colloidal osmotic pressure and transporting large organic anions. [NIH] Sex Determination: The biological characteristics which distinguish human beings as female or male. [NIH] Shedding: Release of infectious particles (e. g., bacteria, viruses) into the environment, for
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example by sneezing, by fecal excretion, or from an open lesion. [NIH] Shock: The general bodily disturbance following a severe injury; an emotional or moral upset occasioned by some disturbing or unexpected experience; disruption of the circulation, which can upset all body functions: sometimes referred to as circulatory shock. [NIH]
Sialic Acids: A group of naturally occurring N-and O-acyl derivatives of the deoxyamino sugar neuraminic acid. They are ubiquitously distributed in many tissues. [NIH] Sialyltransferases: A group of enzymes with the general formula CMP-Nacetylneuraminate:acceptor N-acetylneuraminyl transferase. They catalyze the transfer of Nacetylneuraminic acid from CMP-N-acetylneuraminic acid to an acceptor, which is usually the terminal sugar residue of an oligosaccharide, a glycoprotein, or a glycolipid. EC 2.4.99.-. [NIH]
Sicca: Failure of lacrimal secretion, keratoconjunctivitis sicca, failure of secretion of the salivary glands and mucous glands of the upper respiratory tract and polyarthritis. [NIH] Side effect: A consequence other than the one(s) for which an agent or measure is used, as the adverse effects produced by a drug, especially on a tissue or organ system other than the one sought to be benefited by its administration. [EU] Signal Transduction: The intercellular or intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GABA-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptormediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway. [NIH] Signs and Symptoms: Clinical manifestations that can be either objective when observed by a physician, or subjective when perceived by the patient. [NIH] Skeletal: Having to do with the skeleton (boney part of the body). [NIH] Skeleton: The framework that supports the soft tissues of vertebrate animals and protects many of their internal organs. The skeletons of vertebrates are made of bone and/or cartilage. [NIH] Skull: The skeleton of the head including the bones of the face and the bones enclosing the brain. [NIH] Small cell lung cancer: A type of lung cancer in which the cells appear small and round when viewed under the microscope. Also called oat cell lung cancer. [NIH] Small intestine: The part of the digestive tract that is located between the stomach and the large intestine. [NIH] Smooth muscle: Muscle that performs automatic tasks, such as constricting blood vessels. [NIH]
Sneezing: Sudden, forceful, involuntary expulsion of air from the nose and mouth caused by irritation to the mucous membranes of the upper respiratory tract. [NIH] Social Environment: The aggregate of social and cultural institutions, forms, patterns, and
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processes that influence the life of an individual or community. [NIH] Sodium: An element that is a member of the alkali group of metals. It has the atomic symbol Na, atomic number 11, and atomic weight 23. With a valence of 1, it has a strong affinity for oxygen and other nonmetallic elements. Sodium provides the chief cation of the extracellular body fluids. Its salts are the most widely used in medicine. (From Dorland, 27th ed) Physiologically the sodium ion plays a major role in blood pressure regulation, maintenance of fluid volume, and electrolyte balance. [NIH] Soft tissue: Refers to muscle, fat, fibrous tissue, blood vessels, or other supporting tissue of the body. [NIH] Solid tumor: Cancer of body tissues other than blood, bone marrow, or the lymphatic system. [NIH] Solvent: 1. Dissolving; effecting a solution. 2. A liquid that dissolves or that is capable of dissolving; the component of a solution that is present in greater amount. [EU] Somatic: 1. Pertaining to or characteristic of the soma or body. 2. Pertaining to the body wall in contrast to the viscera. [EU] Somite: One of the paired blocks of mesoderm present in each segment of the early embryo. [NIH]
Sorbitol: A polyhydric alcohol with about half the sweetness of sucrose. Sorbitol occurs naturally and is also produced synthetically from glucose. It was formerly used as a diuretic and may still be used as a laxative and in irrigating solutions for some surgical procedures. It is also used in many manufacturing processes, as a pharmaceutical aid, and in several research applications. [NIH] Soybean Oil: Oil from soybean or soybean plant. [NIH] Spasmodic: Of the nature of a spasm. [EU] Specialist: In medicine, one who concentrates on 1 special branch of medical science. [NIH] Species: A taxonomic category subordinate to a genus (or subgenus) and superior to a subspecies or variety, composed of individuals possessing common characters distinguishing them from other categories of individuals of the same taxonomic level. In taxonomic nomenclature, species are designated by the genus name followed by a Latin or Latinized adjective or noun. [EU] Specificity: Degree of selectivity shown by an antibody with respect to the number and types of antigens with which the antibody combines, as well as with respect to the rates and the extents of these reactions. [NIH] Spectrum: A charted band of wavelengths of electromagnetic vibrations obtained by refraction and diffraction. By extension, a measurable range of activity, such as the range of bacteria affected by an antibiotic (antibacterial s.) or the complete range of manifestations of a disease. [EU] Sperm: The fecundating fluid of the male. [NIH] Sperm Head: The anterior, usually ovoid, nucleus-containing part of spermatozoa. [NIH] Spermatozoa: Mature male germ cells that develop in the seminiferous tubules of the testes. Each consists of a head, a body, and a tail that provides propulsion. The head consists mainly of chromatin. [NIH] Spermatozoon: The mature male germ cell. [NIH] Spinal cord: The main trunk or bundle of nerves running down the spine through holes in the spinal bone (the vertebrae) from the brain to the level of the lower back. [NIH] Spinous: Like a spine or thorn in shape; having spines. [NIH]
262 Glucosamine
Spleen: An organ that is part of the lymphatic system. The spleen produces lymphocytes, filters the blood, stores blood cells, and destroys old blood cells. It is located on the left side of the abdomen near the stomach. [NIH] Sporadic: Neither endemic nor epidemic; occurring occasionally in a random or isolated manner. [EU] Sputa: The material expelled from the respiratory passages by coughing or clearing the throat. [NIH] Stabilizer: A device for maintaining constant X-ray tube voltage or current. [NIH] Staphylococcal Infections: Infections with bacteria of the genus Staphylococcus. [NIH] Steel: A tough, malleable, iron-based alloy containing up to, but no more than, two percent carbon and often other metals. It is used in medicine and dentistry in implants and instrumentation. [NIH] Stem Cells: Relatively undifferentiated cells of the same lineage (family type) that retain the ability to divide and cycle throughout postnatal life to provide cells that can become specialized and take the place of those that die or are lost. [NIH] Stent: A device placed in a body structure (such as a blood vessel or the gastrointestinal tract) to provide support and keep the structure open. [NIH] Sterilization: The destroying of all forms of life, especially microorganisms, by heat, chemical, or other means. [NIH] Steroid: A group name for lipids that contain a hydrogenated cyclopentanoperhydrophenanthrene ring system. Some of the substances included in this group are progesterone, adrenocortical hormones, the gonadal hormones, cardiac aglycones, bile acids, sterols (such as cholesterol), toad poisons, saponins, and some of the carcinogenic hydrocarbons. [EU] Stimulant: 1. Producing stimulation; especially producing stimulation by causing tension on muscle fibre through the nervous tissue. 2. An agent or remedy that produces stimulation. [EU]
Stimulus: That which can elicit or evoke action (response) in a muscle, nerve, gland or other excitable issue, or cause an augmenting action upon any function or metabolic process. [NIH] Stomach: An organ of digestion situated in the left upper quadrant of the abdomen between the termination of the esophagus and the beginning of the duodenum. [NIH] Strand: DNA normally exists in the bacterial nucleus in a helix, in which two strands are coiled together. [NIH] Stress: Forcibly exerted influence; pressure. Any condition or situation that causes strain or tension. Stress may be either physical or psychologic, or both. [NIH] Stringency: Experimental conditions (e. g. temperature, salt concentration) used during the hybridization of nucleic acids. [NIH] Stroke: Sudden loss of function of part of the brain because of loss of blood flow. Stroke may be caused by a clot (thrombosis) or rupture (hemorrhage) of a blood vessel to the brain. [NIH] Stupor: Partial or nearly complete unconsciousness, manifested by the subject's responding only to vigorous stimulation. Also, in psychiatry, a disorder marked by reduced responsiveness. [EU] Styrene: A colorless, toxic liquid with a strong aromatic odor. It is used to make rubbers, polymers and copolymers, and polystyrene plastics. [NIH] Subacute: Somewhat acute; between acute and chronic. [EU]
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Subclinical: Without clinical manifestations; said of the early stage(s) of an infection or other disease or abnormality before symptoms and signs become apparent or detectable by clinical examination or laboratory tests, or of a very mild form of an infection or other disease or abnormality. [EU] Subcutaneous: Beneath the skin. [NIH] Subiculum: A region of the hippocampus that projects to other areas of the brain. [NIH] Submaxillary: Four to six lymph glands, located between the lower jaw and the submandibular salivary gland. [NIH] Subspecies: A category intermediate in rank between species and variety, based on a smaller number of correlated characters than are used to differentiate species and generally conditioned by geographical and/or ecological occurrence. [NIH] Substance P: An eleven-amino acid neurotransmitter that appears in both the central and peripheral nervous systems. It is involved in transmission of pain, causes rapid contractions of the gastrointestinal smooth muscle, and modulates inflammatory and immune responses. [NIH]
Substrate: A substance upon which an enzyme acts. [EU] Sulfates: Inorganic salts of sulfuric acid. [NIH] Sulfotransferases: Enzymes which transfer sulfate groups to various acceptor molecules. They are involved in posttranslational sulfation of proteins and sulfate conjugation of exogenous chemicals and bile acids. EC 2.8.2. [NIH] Sulfur: An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight 32.066. It is found in the amino acids cysteine and methionine. [NIH] Sulfuric acid: A strong acid that, when concentrated is extemely corrosive to the skin and mucous membranes. It is used in making fertilizers, dyes, electroplating, and industrial explosives. [NIH] Superoxide: Derivative of molecular oxygen that can damage cells. [NIH] Superoxide Dismutase: An oxidoreductase that catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. EC 1.15.1.1. [NIH] Supplementation: Adding nutrients to the diet. [NIH] Suppression: A conscious exclusion of disapproved desire contrary with repression, in which the process of exclusion is not conscious. [NIH] Surfactant: A fat-containing protein in the respiratory passages which reduces the surface tension of pulmonary fluids and contributes to the elastic properties of pulmonary tissue. [NIH]
Swainsonine: An indolizidine alkaloid from the plant Swainsona canescens that is a potent alpha-mannosidase inhibitor. Swainsonine also exhibits antimetastatic, antiproliferative, and immunomodulatory activity. [NIH] Symbiosis: The living together of organisms of different species. [NIH] Sympathomimetic: 1. Mimicking the effects of impulses conveyed by adrenergic postganglionic fibres of the sympathetic nervous system. 2. An agent that produces effects similar to those of impulses conveyed by adrenergic postganglionic fibres of the sympathetic nervous system. Called also adrenergic. [EU] Symphysis: A secondary cartilaginous joint. [NIH] Symptomatic: Having to do with symptoms, which are signs of a condition or disease. [NIH]
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Synaptic: Pertaining to or affecting a synapse (= site of functional apposition between neurons, at which an impulse is transmitted from one neuron to another by electrical or chemical means); pertaining to synapsis (= pairing off in point-for-point association of homologous chromosomes from the male and female pronuclei during the early prophase of meiosis). [EU] Synergistic: Acting together; enhancing the effect of another force or agent. [EU] Synovial: Of pertaining to, or secreting synovia. [EU] Synovial Fluid: The clear, viscous fluid secreted by the synovial membrane. It contains mucin, albumin, fat, and mineral salts and serves to lubricate joints. [NIH] Synovial Membrane: The inner membrane of a joint capsule surrounding a freely movable joint. It is loosely attached to the external fibrous capsule and secretes synovial fluid. [NIH] Systemic: Affecting the entire body. [NIH] Systolic: Indicating the maximum arterial pressure during contraction of the left ventricle of the heart. [EU] Telangiectasia: The permanent enlargement of blood vessels, causing redness in the skin or mucous membranes. [NIH] Temporal: One of the two irregular bones forming part of the lateral surfaces and base of the skull, and containing the organs of hearing. [NIH] Tendinitis: Inflammation of tendons and of tendon-muscle attachments. [EU] Testicular: Pertaining to a testis. [EU] Testis: Either of the paired male reproductive glands that produce the male germ cells and the male hormones. [NIH] Thalamic: Cell that reaches the lateral nucleus of amygdala. [NIH] Thalamic Diseases: Disorders of the centrally located thalamus, which integrates a wide range of cortical and subcortical information. Manifestations include sensory loss, movement disorders; ataxia, pain syndromes, visual disorders, a variety of neuropsychological conditions, and coma. Relatively common etiologies include cerebrovascular disorders; craniocerebral trauma; brain neoplasms; brain hypoxia; intracranial hemorrhages; and infectious processes. [NIH] Therapeutics: The branch of medicine which is concerned with the treatment of diseases, palliative or curative. [NIH] Thermal: Pertaining to or characterized by heat. [EU] Third Ventricle: A narrow cleft inferior to the corpus callosum, within the diencephalon, between the paired thalami. Its floor is formed by the hypothalamus, its anterior wall by the lamina terminalis, and its roof by ependyma. It communicates with the fourth ventricle by the cerebral aqueduct, and with the lateral ventricles by the interventricular foramina. [NIH] Threonine: An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins. [NIH] Threshold: For a specified sensory modality (e. g. light, sound, vibration), the lowest level (absolute threshold) or smallest difference (difference threshold, difference limen) or intensity of the stimulus discernible in prescribed conditions of stimulation. [NIH] Thrombin: An enzyme formed from prothrombin that converts fibrinogen to fibrin. (Dorland, 27th ed) EC 3.4.21.5. [NIH] Thrombocytopenia: A decrease in the number of blood platelets. [NIH] Thrombomodulin: A cell surface glycoprotein of endothelial cells that binds thrombin and
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serves as a cofactor in the activation of protein C and its regulation of blood coagulation. [NIH]
Thrombosis: The formation or presence of a blood clot inside a blood vessel. [NIH] Thromboxanes: Physiologically active compounds found in many organs of the body. They are formed in vivo from the prostaglandin endoperoxides and cause platelet aggregation, contraction of arteries, and other biological effects. Thromboxanes are important mediators of the actions of polyunsaturated fatty acids transformed by cyclooxygenase. [NIH] Thymidine: A chemical compound found in DNA. Also used as treatment for mucositis. [NIH]
Thyroid: A gland located near the windpipe (trachea) that produces thyroid hormone, which helps regulate growth and metabolism. [NIH] Tin: A trace element that is required in bone formation. It has the atomic symbol Sn, atomic number 50, and atomic weight 118.71. [NIH] Tissue: A group or layer of cells that are alike in type and work together to perform a specific function. [NIH] Tissue Distribution: Accumulation of a drug or chemical substance in various organs (including those not relevant to its pharmacologic or therapeutic action). This distribution depends on the blood flow or perfusion rate of the organ, the ability of the drug to penetrate organ membranes, tissue specificity, protein binding. The distribution is usually expressed as tissue to plasma ratios. [NIH] Tolerance: 1. The ability to endure unusually large doses of a drug or toxin. 2. Acquired drug tolerance; a decreasing response to repeated constant doses of a drug or the need for increasing doses to maintain a constant response. [EU] Tomography: Imaging methods that result in sharp images of objects located on a chosen plane and blurred images located above or below the plane. [NIH] Tooth Preparation: Procedures carried out with regard to the teeth or tooth structures preparatory to specified dental therapeutic and surgical measures. [NIH] Topical: On the surface of the body. [NIH] Toxic: Having to do with poison or something harmful to the body. Toxic substances usually cause unwanted side effects. [NIH] Toxicity: The quality of being poisonous, especially the degree of virulence of a toxic microbe or of a poison. [EU] Toxicokinetics: Study of the absorption, distribution, metabolism, and excretion of test substances. [NIH] Toxicology: The science concerned with the detection, chemical composition, and pharmacologic action of toxic substances or poisons and the treatment and prevention of toxic manifestations. [NIH] Toxins: Specific, characterizable, poisonous chemicals, often proteins, with specific biological properties, including immunogenicity, produced by microbes, higher plants, or animals. [NIH] Trace element: Substance or element essential to plant or animal life, but present in extremely small amounts. [NIH] Trachea: The cartilaginous and membranous tube descending from the larynx and branching into the right and left main bronchi. [NIH] Traction: The act of pulling. [NIH] Transcription Factors: Endogenous substances, usually proteins, which are effective in the
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initiation, stimulation, or termination of the genetic transcription process. [NIH] Transdermal: Entering through the dermis, or skin, as in administration of a drug applied to the skin in ointment or patch form. [EU] Transduction: The transfer of genes from one cell to another by means of a viral (in the case of bacteria, a bacteriophage) vector or a vector which is similar to a virus particle (pseudovirion). [NIH] Transfection: The uptake of naked or purified DNA into cells, usually eukaryotic. It is analogous to bacterial transformation. [NIH] Transferases: Transferases are enzymes transferring a group, for example, the methyl group or a glycosyl group, from one compound (generally regarded as donor) to another compound (generally regarded as acceptor). The classification is based on the scheme "donor:acceptor group transferase". (Enzyme Nomenclature, 1992) EC 2. [NIH] Translation: The process whereby the genetic information present in the linear sequence of ribonucleotides in mRNA is converted into a corresponding sequence of amino acids in a protein. It occurs on the ribosome and is unidirectional. [NIH] Translational: The cleavage of signal sequence that directs the passage of the protein through a cell or organelle membrane. [NIH] Translocation: The movement of material in solution inside the body of the plant. [NIH] Transmitter: A chemical substance which effects the passage of nerve impulses from one cell to the other at the synapse. [NIH] Transplantation: Transference of a tissue or organ, alive or dead, within an individual, between individuals of the same species, or between individuals of different species. [NIH] Trauma: Any injury, wound, or shock, must frequently physical or structural shock, producing a disturbance. [NIH] Trees: Woody, usually tall, perennial higher plants (Angiosperms, Gymnosperms, and some Pterophyta) having usually a main stem and numerous branches. [NIH] Triglyceride: A lipid carried through the blood stream to tissues. Most of the body's fat tissue is in the form of triglycerides, stored for use as energy. Triglycerides are obtained primarily from fat in foods. [NIH] Tryptophan: An essential amino acid that is necessary for normal growth in infants and for nitrogen balance in adults. It is a precursor serotonin and niacin. [NIH] Tuberculosis: Any of the infectious diseases of man and other animals caused by species of Mycobacterium. [NIH] Tuberous Sclerosis: A rare congenital disease in which the essential pathology is the appearance of multiple tumors in the cerebrum and in other organs, such as the heart or kidneys. [NIH] Tubulin: A microtubule subunit protein found in large quantities in mammalian brain. It has also been isolated from sperm flagella, cilia, and other sources. Structurally, the protein is a dimer with a molecular weight of approximately 120,000 and a sedimentation coefficient of 5.8S. It binds to colchicine, vincristine, and vinblastine. [NIH] Tunicamycin: An N-acetylglycosamine containing antiviral antibiotic obtained from Streptomyces lysosuperificus. It is also active against some bacteria and fungi, because it inhibits the glucosylation of proteins. Tunicamycin is used as tool in the study of microbial biosynthetic mechanisms. [NIH] Type 2 diabetes: Usually characterized by a gradual onset with minimal or no symptoms of metabolic disturbance and no requirement for exogenous insulin. The peak age of onset is 50
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to 60 years. Obesity and possibly a genetic factor are usually present. [NIH] Typhimurium: Microbial assay which measures his-his+ reversion by chemicals which cause base substitutions or frameshift mutations in the genome of this organism. [NIH] Tyramine: An indirect sympathomimetic. Tyramine does not directly activate adrenergic receptors, but it can serve as a substrate for adrenergic uptake systems and monoamine oxidase so it prolongs the actions of adrenergic transmitters. It also provokes transmitter release from adrenergic terminals. Tyramine may be a neurotransmitter in some invertebrate nervous systems. [NIH] Tyrosine: A non-essential amino acid. In animals it is synthesized from phenylalanine. It is also the precursor of epinephrine, thyroid hormones, and melanin. [NIH] Ulcer: A localized necrotic lesion of the skin or a mucous surface. [NIH] Unconscious: Experience which was once conscious, but was subsequently rejected, as the "personal unconscious". [NIH] Uracil: An anticancer drug that belongs to the family of drugs called alkylating agents. [NIH] Urethra: The tube through which urine leaves the body. It empties urine from the bladder. [NIH]
Uric: A kidney stone that may result from a diet high in animal protein. When the body breaks down this protein, uric acid levels rise and can form stones. [NIH] Uridine Diphosphate: A uracil nucleotide containing a pyrophosphate group esterified to C5 of the sugar moiety. [NIH] Urinary: Having to do with urine or the organs of the body that produce and get rid of urine. [NIH] Urinary tract: The organs of the body that produce and discharge urine. These include the kidneys, ureters, bladder, and urethra. [NIH] Urine: Fluid containing water and waste products. Urine is made by the kidneys, stored in the bladder, and leaves the body through the urethra. [NIH] Urokinase: A drug that dissolves blood clots or prevents them from forming. [NIH] Ursodeoxycholic Acid: An epimer of chenodeoxycholic acid. It is a mammalian bile acid found first in the bear and is apparently either a precursor or a product of chenodeoxycholate. Its administration changes the composition of bile and may dissolve gallstones. It is used as a cholagogue and choleretic. [NIH] Urticaria: A vascular reaction of the skin characterized by erythema and wheal formation due to localized increase of vascular permeability. The causative mechanism may be allergy, infection, or stress. [NIH] Uterus: The small, hollow, pear-shaped organ in a woman's pelvis. This is the organ in which a fetus develops. Also called the womb. [NIH] Vaccination: Administration of vaccines to stimulate the host's immune response. This includes any preparation intended for active immunological prophylaxis. [NIH] Vaccine: A substance or group of substances meant to cause the immune system to respond to a tumor or to microorganisms, such as bacteria or viruses. [NIH] Vagina: The muscular canal extending from the uterus to the exterior of the body. Also called the birth canal. [NIH] Vancomycin: Antibacterial obtained from Streptomyces orientalis. It is a glycopeptide related to ristocetin that inhibits bacterial cell wall assembly and is toxic to kidneys and the inner ear. [NIH]
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Varices: Stretched veins such as those that form in the esophagus from cirrhosis. [NIH] Vascular: Pertaining to blood vessels or indicative of a copious blood supply. [EU] Vasoconstriction: Narrowing of the blood vessels without anatomic change, for which constriction, pathologic is used. [NIH] Vasodilator: An agent that widens blood vessels. [NIH] Vector: Plasmid or other self-replicating DNA molecule that transfers DNA between cells in nature or in recombinant DNA technology. [NIH] Vegetative: 1. Concerned with growth and with nutrition. 2. Functioning involuntarily or unconsciously, as the vegetative nervous system. 3. Resting; denoting the portion of a cell cycle during which the cell is not involved in replication. 4. Of, pertaining to, or characteristic of plants. [EU] Vein: Vessel-carrying blood from various parts of the body to the heart. [NIH] Venous: Of or pertaining to the veins. [EU] Ventricle: One of the two pumping chambers of the heart. The right ventricle receives oxygen-poor blood from the right atrium and pumps it to the lungs through the pulmonary artery. The left ventricle receives oxygen-rich blood from the left atrium and pumps it to the body through the aorta. [NIH] Ventricular: Pertaining to a ventricle. [EU] Venules: The minute vessels that collect blood from the capillary plexuses and join together to form veins. [NIH] Veterinarians: Individuals with a degree in veterinary medicine that provides them with training and qualifications to treat diseases and injuries of animals. [NIH] Veterinary Medicine: The medical science concerned with the prevention, diagnosis, and treatment of diseases in animals. [NIH] Vibrio: A genus of Vibrionaceae, made up of short, slightly curved, motile, gram-negative rods. Various species produce cholera and other gastrointestinal disorders as well as abortion in sheep and cattle. [NIH] Vibrio cholerae: The etiologic agent of cholera. [NIH] Vinblastine: An anticancer drug that belongs to the family of plant drugs called vinca alkaloids. It is a mitotic inhibitor. [NIH] Vinca Alkaloids: A class of alkaloids from the genus of apocyanaceous woody herbs including periwinkles. They are some of the most useful antineoplastic agents. [NIH] Viral: Pertaining to, caused by, or of the nature of virus. [EU] Virulence: The degree of pathogenicity within a group or species of microorganisms or viruses as indicated by case fatality rates and/or the ability of the organism to invade the tissues of the host. [NIH] Virus: Submicroscopic organism that causes infectious disease. In cancer therapy, some viruses may be made into vaccines that help the body build an immune response to, and kill, tumor cells. [NIH] Visceral: , from viscus a viscus) pertaining to a viscus. [EU] Visceral fat: One of the three compartments of abdominal fat. Retroperitoneal and subcutaneous are the other two compartments. [NIH] Viscosity: A physical property of fluids that determines the internal resistance to shear forces. [EU]
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Vitamin A: A substance used in cancer prevention; it belongs to the family of drugs called retinoids. [NIH] Vitamin E: Vitamin found largely in plant materials, especially wheat germ, corn, sunflower seed, rapeseed, soybean oils, alfalfa, and lettuce. It is used as an antioxidant in vegetable oils and shortenings. [NIH] Vitro: Descriptive of an event or enzyme reaction under experimental investigation occurring outside a living organism. Parts of an organism or microorganism are used together with artificial substrates and/or conditions. [NIH] Vivo: Outside of or removed from the body of a living organism. [NIH] Weight Gain: Increase in body weight over existing weight. [NIH] Weight-Bearing: The physical state of supporting an applied load. This often refers to the weight-bearing bones or joints that support the body's weight, especially those in the spine, hip, knee, and foot. [NIH] White blood cell: A type of cell in the immune system that helps the body fight infection and disease. White blood cells include lymphocytes, granulocytes, macrophages, and others. [NIH]
Whooping Cough: A respiratory infection caused by Bordetella pertussis and characterized by paroxysmal coughing ending in a prolonged crowing intake of breath. [NIH] Whooping Cough: A respiratory infection caused by Bordetella pertussis and characterized by paroxysmal coughing ending in a prolonged crowing intake of breath. [NIH] Windpipe: A rigid tube, 10 cm long, extending from the cricoid cartilage to the upper border of the fifth thoracic vertebra. [NIH] Wound Healing: Restoration of integrity to traumatized tissue. [NIH] Xenograft: The cells of one species transplanted to another species. [NIH] X-ray: High-energy radiation used in low doses to diagnose diseases and in high doses to treat cancer. [NIH] X-ray therapy: The use of high-energy radiation from x-rays to kill cancer cells and shrink tumors. Radiation may come from a machine outside the body (external-beam radiation therapy) or from materials called radioisotopes. Radioisotopes produce radiation and can be placed in or near the tumor or in the area near cancer cells. This type of radiation treatment is called internal radiation therapy, implant radiation, interstitial radiation, or brachytherapy. Systemic radiation therapy uses a radioactive substance, such as a radiolabeled monoclonal antibody, that circulates throughout the body. X-ray therapy is also called radiation therapy, radiotherapy, and irradiation. [NIH] Yeasts: A general term for single-celled rounded fungi that reproduce by budding. Brewers' and bakers' yeasts are Saccharomyces cerevisiae; therapeutic dried yeast is dried yeast. [NIH] Zygote: The fertilized ovum. [NIH] Zymogen: Inactive form of an enzyme which can then be converted to the active form, usually by excision of a polypeptide, e. g. trypsinogen is the zymogen of trypsin. [NIH]
271
INDEX A Abdominal, 191, 192, 233, 239, 247, 248, 268 Abdominal fat, 191, 268 Abrasion, 3, 191 Acceptor, 12, 71, 113, 124, 152, 191, 222, 225, 236, 238, 247, 260, 263, 266 Acetaminophen, 4, 156, 191 Acetone, 133, 191, 234 Acetylcholine, 191, 208, 244 Acetylcysteine, 105, 191 Acetylgalactosamine, 13, 39, 60, 69, 70, 128, 143, 191 Acetylglucosamine, 8, 13, 14, 20, 22, 24, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 43, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 82, 83, 84, 85, 87, 88, 89, 90, 118, 123, 125, 143, 173, 191 Acetylglucosaminidase, 59, 191 Acrosome, 32, 191 Acrosome Reaction, 32, 191 Acrylonitrile, 191, 258 Actin, 191, 242 Acyl, 7, 24, 58, 65, 90, 111, 191, 192, 260 Acyl Carrier Protein, 7, 192 Acylation, 111, 192 Adaptation, 84, 192 Adenine, 192, 254 Adenosine, 122, 192, 199, 204, 250 Adenosine Diphosphate, 122, 192 Adenosine Triphosphate, 122, 192, 199, 250 Adenylate Cyclase, 192, 208 Adipocytes, 10, 192, 211 Adipose Tissue, 24, 191, 192, 236 Adjustment, 192 Adjuvant, 7, 31, 89, 102, 111, 192, 194, 223 Adoptive Transfer, 16, 192 Adrenal Medulla, 192, 219, 244 Adrenergic, 192, 195, 216, 219, 263, 267 Adverse Effect, 4, 21, 118, 143, 156, 192, 260 Aerobic, 12, 155, 192, 247 Aerobic Exercise, 155, 192 Aetiology, 105, 193 Affinity, 18, 23, 25, 34, 52, 109, 121, 136, 193, 199, 261
Agar, 193, 250 Age of Onset, 193, 266 Agonist, 119, 193, 216, 250 Albumin, 193, 250, 264 Albuminuria, 26, 193 Alertness, 193, 204 Alfalfa, 193, 269 Algorithms, 193, 202 Alkaline, 108, 193, 195, 204, 247 Alkaloid, 193, 199, 201, 205, 241, 263 Alkylating Agents, 193, 207, 267 Allergen, 193, 215 Allylamine, 194 Alpha Particles, 194, 255 Alpha-1, 194, 195 Alpha-Defensins, 194, 214 Alpha-helix, 194, 234 Alpha-lactalbumin, 194, 234 Alternative medicine, 161, 194 Alum, 102, 194 Aluminum, 102, 194 Aluminum Hydroxide, 102, 194 Alveolar Process, 194, 256 Amelogenesis Imperfecta, 18, 194 Amine, 135, 194, 228 Amino Acid Sequence, 194, 196, 223 Amino Acids, 10, 68, 89, 122, 194, 196, 223, 245, 248, 251, 253, 257, 259, 263, 266 Amitriptyline, 157, 194 Ammonia, 40, 43, 194, 195, 224 Ammonium Chloride, 135, 195 Ampicillin, 23, 195 Ampicillin Resistance, 23, 195 Amplification, 195, 240 Amylase, 107, 140, 195 Amylose, 120, 195 Anabolic, 13, 150, 195 Anaesthesia, 195, 231 Analgesic, 33, 74, 82, 145, 191, 195, 230, 241, 242 Analog, 22, 162, 195, 221 Analogous, 19, 117, 146, 195, 251, 266 Anaphylatoxins, 195, 210 Anatomical, 195, 218, 231, 258 Androgens, 195, 198 Anecdotal report, 119, 147, 195 Anemia, 174, 195, 221 Anergy, 16, 195
272 Glucosamine
Anesthesia, 195, 213, 252 Anesthetics, 157, 195, 219 Anginal, 196, 244 Angiogenesis, 139, 196, 238 Angiotensinogen, 196, 256 Animal model, 19, 24, 26, 196 Anions, 193, 196, 233, 259, 263 Anode, 127, 196 Antagonism, 196, 204 Anterior Cruciate Ligament, 122, 196 Antibacterial, 10, 20, 196, 216, 225, 261, 267 Antibiotic, 6, 66, 88, 143, 195, 196, 203, 240, 245, 248, 257, 261, 266 Antibodies, 29, 35, 38, 49, 102, 113, 119, 144, 196, 197, 226, 228, 230, 237, 241, 250 Anticholinergic, 157, 194, 196, 207 Anticoagulant, 139, 196, 253 Anticonvulsant, 196, 205 Antidepressant, 194, 196 Antidote, 196, 204 Antiemetic, 196, 215, 229 Antifungal, 75, 140, 196, 221, 233 Antifungal Agents, 140, 196 Antigen, 12, 16, 27, 125, 193, 196, 197, 210, 214, 228, 229, 230, 231, 238 Antigen-Antibody Complex, 197, 210 Antigen-presenting cell, 197, 214 Anti-infective, 197, 204, 229, 233 Anti-Inflammatory Agents, 197, 199 Antimetabolite, 197, 214, 221 Antimetastatic, 197, 263 Antimicrobial, 114, 197, 214 Antineoplastic, 193, 197, 221, 223, 240, 244, 268 Antioxidant, 149, 197, 199, 269 Antiproliferative, 197, 263 Antipruritic, 197, 204, 209 Antipyretic, 191, 197 Antiseptic, 191, 197 Antiserum, 70, 197 Antitussive, 197, 215 Antiviral, 69, 88, 90, 191, 197, 214, 225, 266 Anxiety, 197, 229 Aorta, 86, 197, 268 Apolipoproteins, 197, 236 Apoptosis, 14, 22, 197 Applicability, 162, 198 Aqueous, 20, 108, 114, 126, 127, 135, 198, 200, 213, 218, 228, 235 Arachidonate 12-Lipoxygenase, 198, 236 Arachidonate 15-Lipoxygenase, 198, 236
Arachidonate Lipoxygenases, 198, 236 Arachidonic Acid, 110, 198, 235, 253 Arginine, 122, 157, 195, 198, 244 Aromatase, 75, 198 Aromatic, 10, 12, 58, 113, 198, 225, 249, 262 Arterial, 14, 194, 198, 208, 229, 253, 264 Arteries, 104, 197, 198, 199, 202, 203, 212, 237, 239, 242, 265 Arterioles, 198, 199, 202, 205 Arteriolosclerosis, 198, 199 Arteriosclerosis, 104, 198 Arthroplasty, 44, 86, 170, 199 Arthroscopy, 170, 171, 199 Arthrosis, 125, 199 Articular, 3, 14, 20, 28, 46, 49, 66, 75, 76, 105, 108, 117, 122, 171, 199, 233, 246 Ascorbic Acid, 148, 149, 199, 229 Aspergillosis, 141, 199, 233 Aspirin, 5, 199 Assay, 18, 32, 42, 199, 257, 267 Astrocytes, 199, 227, 241 Ataxia, 174, 199, 264 Atherogenic, 14, 199 ATP, 122, 192, 199, 216, 223, 224, 250, 253 Atrophy, 129, 174, 199 Atropine, 157, 199, 200 Attenuated, 102, 125, 199 Attenuation, 28, 128, 199 Avian, 136, 199, 212 Axillary, 199, 203 Axillary Artery, 199, 203 B Bacterial Physiology, 192, 200 Bacteriophage, 200, 250, 266 Bacterium, 200, 201, 210, 211 Basal Ganglia, 199, 200, 222 Basal Ganglia Diseases, 199, 200 Base, 7, 103, 108, 127, 131, 132, 149, 192, 200, 214, 222, 223, 234, 240, 251, 264, 267 Basement Membrane, 26, 200, 220, 235 Basophils, 200, 226, 235 Baths, 135, 200 Behavioral Sciences, 6, 200 Belladonna, 199, 200 Benign, 139, 198, 200, 222, 226, 243, 255 Benign tumor, 139, 200 Benzene, 200, 233 Benzocaine, 146, 200 Benzoic Acid, 157, 201 Berberine, 149, 201 Beta-Defensins, 201, 214 Beta-glucans, 201, 207
Index 273
Bewilderment, 201, 211 Bifidobacterium, 116, 201 Bile, 13, 63, 201, 207, 222, 224, 228, 233, 236, 262, 263, 267 Bile Acids, 63, 201, 262, 263 Bile Acids and Salts, 201 Bile Ducts, 201, 222 Biliary, 16, 64, 201, 204 Bilirubin, 16, 193, 201, 222, 224, 229 Binding Sites, 12, 29, 39, 144, 201 Bioavailability, 77, 115, 201 Biofilms, 135, 201 Biogenesis, 31, 201 Biological therapy, 201, 226 Biological Transport, 201, 215 Biomass, 134, 142, 202 Biosynthesis, 6, 7, 8, 10, 14, 15, 19, 20, 24, 30, 35, 51, 64, 66, 123, 151, 198, 202, 259 Biotechnology, 6, 28, 31, 35, 40, 72, 75, 88, 124, 152, 161, 169, 170, 173, 174, 175, 202 Biotin, 116, 202 Biotransformation, 202 Bivalent, 19, 202 Bladder, 157, 202, 213, 248, 253, 267 Blast Crisis, 53, 202 Blastocyst, 202, 250 Blastomycosis, 202, 233 Blasts, 137, 202 Blood Coagulation, 202, 204, 257, 265 Blood Glucose, 26, 97, 118, 202, 227, 230, 232 Blood Platelets, 202, 259, 264 Blood pressure, 202, 205, 229, 241, 244, 261 Body Fluids, 203, 217, 261 Body Mass Index, 203, 246 Bolus, 8, 203 Bolus infusion, 203 Bone Density, 6, 130, 203 Bone Marrow, 137, 200, 202, 203, 208, 213, 219, 230, 237, 242, 261 Bone Resorption, 130, 203 Boron, 79, 105, 203, 213 Boron Neutron Capture Therapy, 203 Bowel, 91, 203, 215, 231, 232, 235, 248 Bowel Movement, 203, 215 Brachial, 98, 203 Brachial Artery, 98, 203 Brachytherapy, 203, 232, 233, 255, 269 Bradykinin, 203, 244, 250 Branch, 187, 203, 237, 248, 261, 264 Breakdown, 16, 119, 148, 151, 203, 207, 215, 222
Broad-spectrum, 195, 203 Bronchi, 203, 219, 220, 265 Bronchial, 203, 228 Bronchiseptica, 203, 249 Buccal, 204, 237 Bupivacaine, 204, 236 Bursitis, 91, 110, 204 C Caffeine, 119, 204, 254 Calcification, 198, 204 Calcium, 108, 130, 157, 204, 209, 210, 238, 244, 260 Calcium channel blocker, 157, 204 Calcium Channel Blockers, 157, 204 Calcium Chloride, 108, 204 Calculi, 204, 225 Callus, 204, 218 Caloric intake, 104, 204 Camphor, 33, 82, 204 Cancer vaccine, 15, 204 Candidiasis, 204, 221 Capillary, 121, 139, 203, 205, 236, 258, 268 Capillary Permeability, 121, 203, 205 Capsaicin, 156, 171, 205 Capsular, 27, 56, 205 Capsules, 107, 121, 143, 205, 216, 223 Carbamazepine, 157, 205 Carbenoxolone, 205, 225 Carbohydrate, 11, 17, 25, 33, 36, 38, 43, 63, 67, 69, 70, 113, 144, 205, 222, 225, 238, 251 Carbon Dioxide, 205, 214, 250, 256 Carcinogenic, 193, 200, 205, 209, 232, 253, 262 Carcinogens, 16, 104, 205, 209, 245 Carcinoma, 56, 205 Cardiac, 31, 65, 194, 204, 205, 219, 223, 236, 242, 247, 262 Cardiology, 136, 205 Cardiorespiratory, 193, 205 Cardiovascular, 15, 119, 205, 235, 259 Cardiovascular disease, 15, 205 Carotenoids, 112, 205 Case report, 29, 86, 171, 206, 209 Castor Oil, 145, 206 Catabolism, 3, 206 Catecholamines, 192, 206, 216, 241 Catheterization, 138, 206, 233 Catheters, 27, 98, 141, 147, 206, 231, 232 Cathode, 196, 206, 217 Cations, 206, 233 Caudal, 206, 215, 230, 251
274 Glucosamine
Causal, 24, 206 Cell Adhesion, 56, 206 Cell Cycle, 206, 268 Cell Death, 197, 206, 243 Cell Differentiation, 206, 260 Cell Division, 173, 200, 206, 226, 238, 239, 240, 250, 253 Cell membrane, 12, 35, 88, 202, 204, 206, 214, 217, 249 Cell proliferation, 139, 199, 206, 260 Cell Survival, 206, 226 Cellobiose, 206, 207 Cellular metabolism, 122, 207 Cellulase, 107, 140, 207 Cellulose, 29, 108, 145, 207, 222, 250 Central Nervous System, 191, 200, 204, 207, 222, 224, 226, 235, 241, 259 Cerebellar, 199, 207, 256 Cerebral, 85, 199, 200, 207, 219, 254, 264 Cerebrovascular, 200, 204, 205, 207, 264 Cerebrum, 207, 266 Cetirizine, 207, 229 Character, 207, 214 Chemotactic Factors, 207, 210 Chemotherapy, 141, 207 Chenodeoxycholic Acid, 207, 267 Chiropractic, 38, 83, 92, 207 Chitin Synthase, 8, 207 Chlorambucil, 74, 207 Chlorides, 108, 207 Chlorine, 207, 229 Chlorophyll, 207, 222 Cholecalciferol, 130, 208 Cholera, 125, 208, 268 Cholera Toxin, 125, 208 Choleretic, 207, 208, 267 Cholesterol, 86, 103, 104, 128, 201, 208, 212, 222, 229, 236, 237, 262 Cholesterol Esters, 208, 236 Cholinergic, 195, 208 Chromatin, 198, 208, 218, 261 Chromosomal, 69, 195, 208 Chromosome, 59, 208, 211, 226, 236 Chronic, 6, 21, 33, 53, 70, 82, 87, 105, 106, 108, 114, 146, 149, 150, 153, 173, 202, 207, 208, 216, 218, 229, 231, 234, 235, 248, 251, 254, 262 Chronic Disease, 149, 150, 208, 235 Chronic granulocytic leukemia, 208 Chronic myelogenous leukemia, 53, 208 Chronic renal, 208, 251 Chylomicrons, 208, 236
Cimetidine, 157, 208 CIS, 8, 17, 208 Citric Acid, 135, 145, 209 Citrus, 199, 209 Clamp, 97, 209 Clinical Medicine, 209, 252 Clinical study, 209, 212 Clone, 32, 209 Cloning, 7, 8, 20, 37, 59, 69, 123, 151, 202, 209 Coagulation, 24, 202, 209, 227, 250 Coal, 149, 200, 209 Coal Tar, 149, 209 Codons, 209, 223, 245 Coenzyme, 112, 140, 199, 209 Cofactor, 209, 244, 253, 265 Colitis, 92, 209, 231 Collapse, 203, 210 Colloidal, 193, 210, 259 Colorectal, 54, 201, 210 Combinatorial, 7, 210 Communis, 206, 210 Competency, 18, 210 Complement, 27, 74, 195, 210, 223, 250 Complementary and alternative medicine, 81, 82, 93, 210 Complementary medicine, 82, 210 Complementation, 6, 210 Complete remission, 211, 256 Computational Biology, 169, 173, 211 Concomitant, 102, 211 Confusion, 46, 211, 216 Conjugated, 19, 69, 201, 207, 211, 213, 245 Conjugation, 63, 202, 211, 224, 263 Conjunctiva, 211, 231, 234 Connective Tissue Cells, 211 Connective Tissue Diseases, 117, 211 Consciousness, 195, 211, 216 Constipation, 107, 140, 211 Consultation, 6, 211 Consumption, 132, 134, 211, 256 Contracture, 56, 211 Contraindications, ii, 211 Control group, 17, 21, 211 Controlled clinical trial, 58, 87, 162, 212 Controlled study, 21, 38, 212 Coordination, 12, 212 Cornea, 212, 225, 234 Corneum, 128, 212, 219 Coronary, 205, 212, 239, 242 Coronary heart disease, 205, 212 Coronary Thrombosis, 212, 239, 242
Index 275
Cortex, 85, 199, 212, 218, 219, 252, 256 Corticosteroids, 141, 156, 171, 212 Coumarin, 212 Coumestrol, 115, 212 Cranial, 212, 226, 243 Creatine, 122, 212 Creatinine, 212 Cromolyn Sodium, 157, 212 Crystallins, 72, 212 Curare, 212, 242 Curative, 213, 244, 264 Curcumin, 105, 213 Cutaneous, 68, 89, 202, 204, 213, 235, 237 Cyanide, 213, 239 Cyclic, 192, 204, 213, 226, 244 Cyclosporine, 37, 213 Cyst, 13, 213 Cysteine, 30, 55, 191, 213, 214, 263 Cystine, 213 Cystitis, 157, 213 Cytochrome, 198, 208, 213 Cytokine, 16, 36, 102, 213 Cytomegalovirus, 69, 90, 213 Cytoplasm, 8, 12, 128, 198, 200, 206, 208, 213, 218, 220, 226, 257 Cytotoxic, 102, 205, 213, 255, 260 Cytotoxicity, 36, 68, 194, 213 D Databases, Bibliographic, 169, 213 Deamination, 90, 214, 241 Decarboxylation, 214, 228 Decidua, 214, 250 Defensins, 143, 194, 201, 214 Degenerative, 51, 70, 77, 90, 105, 106, 112, 122, 131, 150, 214, 246, 257 Dehydration, 208, 214 Deletion, 123, 151, 198, 214 Dendrites, 214, 244 Dendritic, 16, 214, 238 Dendritic cell, 16, 214 Density, 127, 203, 214, 236, 245 Dentate Gyrus, 214, 228 Dentifrices, 194, 214 Deoxyglucose, 118, 214 Deoxyribonucleic, 214, 257 Deoxyribonucleic acid, 214, 257 Depolarization, 214, 260 Depressive Disorder, 214, 236 Dermal, 129, 214 Dermatitis, 215, 217, 229 Desensitization, 10, 215 Detoxification, 107, 140, 215, 224
Deuterium, 215, 228 Diabetes Mellitus, 26, 215, 224, 227 Diagnostic procedure, 101, 161, 215 Dialyzer, 215, 227 Diarrhea, 29, 36, 215 Diastolic, 215, 229 Diencephalon, 215, 230, 264 Dietary Fats, 215, 236 Diffusion, 75, 129, 146, 202, 205, 215, 231 Digestion, 25, 116, 201, 203, 215, 232, 236, 262 Digestive system, 99, 116, 215, 242 Digestive tract, 116, 205, 215, 260 Dihydroxy, 215, 220, 258 Dilatation, 215, 252 Dilator, 138, 215 Dimerization, 16, 215 Dimethyl, 144, 215 Diphenhydramine, 147, 215 Diploid, 210, 215, 250 Direct, iii, 9, 13, 22, 29, 39, 209, 215, 216, 223, 237, 256 Disease Progression, 38, 160, 215 Disinfection, 127, 216 Disorientation, 211, 216 Dissociation, 193, 216 Distal, 216, 254 Diuresis, 204, 216 Diuretic, 195, 204, 216, 261 DNA Topoisomerase, 216, 223 Domesticated, 216, 226 Dopamine, 216, 241, 249 Dorsal, 216, 243, 251 Dosage Forms, 107, 216 Double-blinded, 21, 68, 89, 216 Drug Interactions, 216 Drug Tolerance, 217, 265 Duct, 206, 217, 258 Duodenal Ulcer, 20, 217 Duodenum, 201, 217, 262 Dyes, 12, 200, 217, 263 Dysplasia, 110, 174, 217 Dystrophy, 58, 174, 217 E Echinacea, 110, 217 Ectoderm, 217, 243 Eczema, 125, 217 Effector, 106, 107, 191, 210, 217, 244 Elasticity, 198, 217 Elastin, 121, 129, 136, 210, 211, 217, 220 Elective, 65, 217 Electrocoagulation, 209, 217
276 Glucosamine
Electrolysis, 127, 196, 206, 217 Electrolyte, 127, 217, 225, 252, 261 Electrons, 197, 200, 206, 217, 233, 247, 255 Electroplating, 217, 263 Electroporation, 27, 217 Embryo, 27, 202, 206, 217, 218, 231, 239, 246, 251, 261 Embryogenesis, 27, 30, 218 Emollient, 149, 218, 225, 240, 245 Emulsions, 111, 193, 218 Enamel, 17, 69, 194, 218, 234 Encephalopathy, 119, 136, 218 Endemic, 208, 218, 262 Endothelial cell, 63, 139, 218, 221, 264 Endothelium, 218, 244 Endothelium-derived, 218, 244 Endotoxic, 218, 236 Endotoxin, 7, 19, 24, 218 End-stage renal, 208, 218, 251 Enhancer, 145, 146, 218 Entorhinal Cortex, 218, 228 Environmental Exposure, 218, 245 Environmental Health, 168, 170, 218 Enzymatic, 7, 9, 19, 26, 71, 85, 109, 111, 123, 143, 151, 171, 204, 210, 218, 228 Eosinophils, 218, 226, 235 Epidermal, 43, 128, 219, 234, 238 Epidermal Growth Factor, 43, 219 Epidermis, 128, 149, 212, 219, 228, 234, 252, 254 Epinephrine, 114, 192, 216, 219, 244, 267 Epithelial, 22, 124, 201, 202, 208, 214, 219, 235, 241 Epithelial Cells, 201, 208, 219, 235, 241 Epithelium, 8, 59, 200, 218, 219, 223 Epitope, 31, 42, 70, 219 Erythrocytes, 44, 60, 85, 195, 203, 219, 256 Erythropoietin, 40, 219 Esophageal, 75, 219 Esophageal Varices, 75, 219 Esophagus, 215, 219, 249, 262, 268 Essential Tremor, 174, 219 Estradiol, 115, 219 Estrogen, 16, 34, 115, 130, 198, 219 Estrogen receptor, 34, 115, 219 Ethanol, 219, 221 Ether, 12, 135, 219 Ethylene Glycol, 147, 220 Eukaryotic Cells, 118, 220, 231, 245, 246 Evacuation, 211, 220, 235 Excitatory, 220, 224
Exogenous, 121, 143, 202, 217, 220, 224, 253, 263, 266 Exons, 123, 151, 220 Expectorant, 195, 220 Extensor, 220, 254 External-beam radiation, 220, 233, 255, 269 Extracellular, 8, 14, 18, 26, 136, 143, 199, 201, 211, 220, 221, 238, 246, 261 Extracellular Matrix, 14, 26, 136, 211, 220, 221, 238, 246 Extracellular Matrix Proteins, 220, 238 Extracellular Space, 8, 220 Extraction, 8, 220 Extravasation, 220, 227 Eye Infections, 114, 220 F Family Planning, 169, 220 Fatty acids, 24, 86, 104, 193, 221, 224, 236, 253, 265 Feces, 201, 211, 221 Femur, 196, 221 Fermentation, 117, 146, 221 Fertilizers, 221, 263 Fetus, 219, 221, 250, 252, 267 Fibroblast Growth Factor, 109, 221 Fibroblasts, 68, 211, 221 Fibronectin, 136, 221 Fibrosis, 26, 60, 174, 194, 211, 221, 258 Fixatives, 69, 221 Flatus, 221, 222 Fluconazole, 141, 221 Fluorescence, 11, 221 Fluorouracil, 39, 75, 221 Folate, 221 Fold, 77, 124, 152, 221 Folic Acid, 116, 126, 221 Forearm, 98, 202, 221 Fractionation, 107, 222 Frameshift, 222, 267 Frameshift Mutation, 222, 267 Freeze-dried, 129, 222 Friction, 117, 222 Fructose, 8, 10, 26, 41, 51, 57, 63, 65, 118, 222, 225, 233 Fucose, 56, 68, 143, 222 Fungi, 124, 140, 196, 199, 207, 211, 220, 222, 226, 239, 240, 266, 269 Fungicides, Industrial, 197, 222 Fungistatic, 141, 201, 222 Fungus, 116, 133, 204, 222
Index 277
G Gait, 22, 222 Galactosyltransferases, 32, 123, 151, 222 Gallbladder, 191, 201, 215, 222 Gallstones, 201, 207, 222, 267 Ganglion, 222, 243 Gas, 98, 179, 195, 205, 207, 215, 221, 222, 228, 244 Gastric, 20, 77, 84, 194, 201, 208, 216, 219, 223, 228, 248 Gastric Acid, 208, 223 Gastric Mucosa, 84, 223 Gastrin, 208, 223, 228 Gastritis, 20, 223 Gastrointestinal, 47, 107, 119, 163, 203, 219, 223, 235, 248, 259, 262, 263, 268 Gastrointestinal tract, 107, 119, 219, 223, 235, 248, 259, 262 Gelatin, 223, 225, 264 Gene Expression, 16, 24, 29, 175, 223 Gene Silencing, 8, 223 Genetic Code, 223, 245 Genetic Engineering, 202, 209, 223 Genetics, 39, 211, 223, 241 Genistein, 115, 223 Genotype, 61, 223, 249 Germ Cells, 223, 238, 245, 246, 261, 264 Gestation, 223, 250 Giardiasis, 13, 223 Gland, 139, 192, 223, 234, 247, 250, 253, 258, 262, 263, 265 Glioma, 43, 223 Glomerular, 25, 42, 224, 233 Glomeruli, 224 Glomerulonephritis, 42, 224 Glomerulosclerosis, 26, 224 Glomerulus, 224 Glottis, 224, 249 Glucokinase, 48, 52, 224 Glucose Intolerance, 215, 224 Glucuronic Acid, 16, 70, 109, 137, 224, 227, 230 Glucuronides, 224 Glucuronosyltransferase, 16, 224 Glutamate, 224 Glutamic Acid, 147, 221, 224, 253 Glutamine, 8, 10, 26, 41, 57, 63, 65, 115, 116, 118, 224 Glutathione Peroxidase, 224, 259 Glycerol, 104, 225, 249 Glycine, 122, 201, 207, 225, 259 Glycogen, 48, 65, 225
Glycogen Synthase, 48, 65, 225 Glycopeptides, 123, 151, 225 Glycoprotein, 18, 19, 28, 32, 55, 58, 118, 120, 219, 221, 225, 226, 235, 241, 260, 264 Glycosaminoglycan, 14, 33, 70, 82, 109, 114, 126, 129, 145, 208, 225 Glycoside, 115, 225, 229, 258 Glycosidic, 18, 56, 102, 107, 140, 206, 225, 243, 245 Glycosylation, 10, 18, 24, 32, 38, 52, 62, 118, 225 Glycosyltransferases, 7, 18, 225 Glycyrrhetinic Acid, 225 Glycyrrhiza, 148, 225 Goats, 106, 225 Gonadal, 225, 262 Gout, 110, 225 Governing Board, 225, 252 Gp120, 37, 226 Grade, 144, 226 Graft, 226, 228, 230 Grafting, 226, 231 Gram-negative, 7, 19, 24, 203, 218, 226, 257, 268 Gram-Negative Bacteria, 218, 226, 257 Gram-positive, 23, 201, 226, 234 Granule, 214, 226, 257 Granulocytes, 137, 226, 235, 260, 269 Grasses, 221, 226 Group Structure, 114, 226 Growth factors, 109, 136, 226 Guanylate Cyclase, 226, 244 Guinea Pigs, 106, 226 H Haploid, 226, 250 Haptens, 193, 226 Headache, 204, 226, 231 Health Promotion, 6, 227 Heart attack, 104, 205, 227 Hematoma, 139, 227 Heme, 12, 16, 201, 213, 227 Hemodialysis, 138, 215, 227 Hemoglobin, 68, 89, 195, 219, 227, 235 Hemoglobinuria, 30, 34, 66, 174, 227 Hemorrhage, 217, 226, 227, 262 Hemorrhaging, 135, 227 Hemostasis, 77, 135, 136, 138, 139, 227, 259 Heparan Sulfate Proteoglycan, 26, 42, 48, 227 Heparin, 25, 29, 35, 49, 53, 54, 76, 109, 139, 227 Hepatocellular, 17, 227
278 Glucosamine
Hepatocyte, 16, 227 Hepatoma, 17, 227 Hereditary, 194, 211, 225, 227, 250, 257 Heredity, 223, 227 Heterogeneity, 40, 193, 227 Heterotrophic, 222, 227 Hexosyltransferases, 225, 227 Hippocampus, 85, 214, 228, 263 Histamine, 83, 119, 195, 207, 208, 215, 228, 229 Histidine, 62, 228 Homeostasis, 14, 228 Homogeneous, 136, 147, 198, 228, 249 Homologous, 123, 151, 202, 228, 264 Hormonal, 11, 199, 228 Hormone, 17, 97, 115, 212, 219, 223, 228, 232, 233, 239, 252, 257, 260, 265 Horny layer, 219, 228 Host, 12, 13, 20, 89, 102, 131, 200, 214, 228, 230, 235, 267, 268 Humoral, 102, 228 Humour, 228 Hybrid, 27, 47, 69, 89, 209, 228 Hybridization, 228, 241, 262 Hybridomas, 218, 228 Hydrochloric Acid, 207, 228 Hydrogel, 145, 228 Hydrogen Peroxide, 116, 224, 228, 236, 263 Hydrolases, 143, 229, 250 Hydrolysis, 56, 134, 191, 202, 207, 225, 229, 237, 243, 248, 249, 250, 251, 254 Hydrophilic, 27, 129, 228, 229 Hydrophobic, 24, 229, 236 Hydroxylation, 121, 229 Hydroxylysine, 210, 229 Hydroxyproline, 210, 229 Hydroxyzine, 157, 229 Hyperbilirubinemia, 16, 229, 233 Hyperglycaemia, 63, 229 Hyperglycemia, 9, 10, 52, 118, 229 Hyperlipoproteinemia, 229, 236 Hyperplasia, 105, 149, 229 Hypersensitivity, 55, 193, 215, 229, 235, 257 Hypersensitivity, Immediate, 229 Hypertension, 75, 198, 204, 205, 226, 229 Hypertrophy, 26, 229 Hyperuricemia, 225, 229 Hypnotic, 215, 229 Hypochlorous Acid, 127, 229 Hypoglycemia, 98, 230
Hypoglycemic, 118, 230 Hypoglycemic Agents, 118, 230 Hypoplasia, 194, 230 Hypothalamus, 115, 215, 230, 250, 264 I Ibuprofen, 41, 42, 48, 50, 76, 160, 230 Id, 78, 91, 180, 186, 188, 230 Iduronic Acid, 67, 109, 230 Imidazole, 202, 228, 230 Immersion, 200, 230 Immune adjuvant, 194, 230 Immune response, 102, 138, 192, 194, 195, 197, 226, 230, 263, 267, 268 Immune system, 20, 24, 102, 108, 140, 141, 197, 201, 230, 235, 237, 267, 269 Immunity, 27, 31, 36, 62, 89, 102, 125, 214, 230, 237, 241, 245 Immunization, 192, 230 Immunocompromised, 140, 230 Immunodeficiency, 37, 69, 90, 173, 230 Immunogenic, 102, 114, 230, 236 Immunoglobulin, 120, 196, 220, 230, 241 Immunohistochemistry, 27, 230 Immunologic, 27, 192, 207, 230, 237, 255 Immunology, 35, 38, 56, 58, 59, 60, 70, 88, 192, 193, 230 Immunosuppressant, 193, 221, 230 Immunotherapy, 192, 201, 215, 230 Impairment, 48, 199, 201, 220, 231, 239 Implant radiation, 231, 232, 233, 255, 269 Implantation, 139, 231 In situ, 27, 231 In Situ Hybridization, 27, 231 In vitro, 4, 12, 14, 18, 19, 21, 22, 27, 48, 49, 52, 57, 63, 66, 68, 69, 90, 105, 108, 136, 140, 231, 257 In vivo, 11, 12, 15, 16, 19, 22, 26, 38, 48, 59, 74, 85, 87, 105, 108, 137, 140, 227, 231, 265 Incision, 138, 231, 233 Incubation, 22, 231, 249 Incubation period, 231, 249 Indicative, 156, 231, 248, 268 Induction, 9, 17, 22, 24, 26, 32, 102, 105, 137, 195, 231 Infarction, 231 Infiltration, 224, 231, 252 Inflammatory bowel disease, 33, 60, 82, 231 Influenza, 125, 231 Infusion, 40, 66, 75, 231 Ingestion, 8, 114, 121, 232, 251
Index 279
Initiation, 70, 232, 266 Inlay, 232, 257 Inner ear, 232, 267 Inorganic, 127, 132, 207, 225, 232, 242, 249, 263 Inositol, 12, 34, 232 Insulator, 147, 232 Insulin, 9, 10, 23, 34, 40, 47, 48, 66, 97, 118, 160, 232, 233, 234, 266 Insulin-dependent diabetes mellitus, 232 Insulin-like, 47, 232 Interleukin-1, 14, 31, 75, 89, 232 Interleukin-10, 31, 89, 232 Interleukin-2, 232 Intermittent, 232, 248 Internal Medicine, 49, 66, 68, 87, 89, 170, 232, 257 Internal radiation, 232, 233, 255, 269 Interstitial, 157, 203, 220, 232, 233, 269 Intestinal, 13, 116, 119, 148, 179, 194, 207, 208, 232, 234, 237, 241 Intestine, 13, 201, 203, 232, 235 Intracellular, 22, 24, 25, 27, 85, 129, 150, 204, 231, 232, 239, 244, 252, 255, 259, 260 Intracellular Membranes, 232, 239 Intramuscular, 41, 232 Intraperitoneal, 24, 233 Intravenous, 28, 232, 233 Intrinsic, 193, 200, 233 Intubation, 206, 233 Inulin, 106, 107, 217, 233 Invasive, 53, 136, 141, 157, 230, 233 Invertebrates, 224, 233 Involuntary, 200, 219, 233, 242, 260 Iodine, 150, 233 Ions, 136, 150, 200, 216, 217, 228, 233, 241 Irradiation, 120, 203, 233, 269 Irrigation, 156, 233 Ischemia, 199, 233 Islet, 118, 233 Isoflavones, 115, 233 Itraconazole, 141, 233 J Jaundice, 229, 233 Joint Capsule, 105, 122, 233, 264 K Kb, 6, 16, 168, 234 Keratan Sulfate, 14, 58, 234 Keratin, 56, 128, 234 Keratinocytes, 149, 234 Keratoconjunctivitis, 234, 260 Keratoconjunctivitis Sicca, 234, 260
Keratolytic, 149, 234 Ketone Bodies, 191, 234 Kidney Disease, 26, 99, 168, 174, 193, 234 Kinetic, 5, 57, 62, 124, 152, 234 L Labile, 210, 234 Lacrimal, 234, 260 Lactation, 124, 139, 152, 234 Lactobacillus, 116, 234 Lactobacillus acidophilus, 116, 234 Lactose Synthase, 124, 152, 234 Laminin, 136, 200, 220, 235 Large Intestine, 215, 232, 235, 256, 260 Larynx, 224, 235, 265 Latent, 235, 252 Laxative, 193, 207, 235, 240, 261 Lectin, 17, 21, 28, 31, 32, 34, 38, 58, 60, 64, 65, 69, 82, 89, 235, 239 Leishmaniasis, 15, 235 Lens, 72, 205, 212, 235 Lesion, 202, 235, 236, 260, 267 Lethal, 16, 24, 213, 235 Leucine, 136, 235, 248 Leucocyte, 194, 235, 237 Leukaemia, 137, 235 Leukemia, 37, 173, 208, 235 Leukocytes, 27, 57, 72, 143, 200, 203, 207, 218, 226, 235 Leukotrienes, 110, 198, 235 Library Services, 186, 235 Lidocaine, 146, 236 Life cycle, 13, 222, 236 Ligament, 144, 196, 236, 253 Ligands, 18, 21, 236 Linkage, 19, 22, 30, 56, 61, 66, 70, 102, 113, 118, 137, 206, 236 Lipase, 104, 236 Lipid, 7, 15, 19, 24, 63, 90, 133, 197, 198, 205, 218, 225, 232, 236, 266 Lipid A, 7, 15, 19, 24, 236 Lipid Peroxidation, 90, 236 Lipopolysaccharide, 10, 19, 24, 226, 236 Lipoprotein, 14, 109, 226, 236, 237 Lipoprotein Lipase, 109, 236 Liposomes, 125, 236 Lipoxygenase, 110, 198, 235, 236 Lithium, 108, 236 Localization, 16, 19, 52, 59, 69, 230, 236 Localized, 27, 28, 124, 149, 227, 231, 235, 237, 241, 250, 267 Locomotion, 237, 250 Low-density lipoprotein, 236, 237
280 Glucosamine
Lubricants, 106, 107, 237, 249 Lucida, 235, 237 Lumen, 8, 16, 237 Lupus, 110, 237 Lyases, 25, 237 Lymph, 199, 218, 228, 237, 263 Lymphatic, 218, 231, 237, 239, 261, 262 Lymphatic system, 237, 261, 262 Lymphoblasts, 38, 237 Lymphocyte, 197, 237, 238 Lymphoid, 196, 212, 235, 237 Lymphokines, 237 Lymphoma, 34, 173, 237 Lysine, 147, 229, 237 M Macrophage, 16, 28, 102, 232, 237 Macrophage Activation, 16, 237 Malabsorption, 174, 237 Malignant, 37, 139, 173, 197, 198, 237, 243, 255, 258 Malnutrition, 193, 199, 238, 242 Mammary, 139, 234, 236, 238 Mandible, 194, 238, 256 Manic, 236, 238 Mannans, 222, 238 Mannosyltransferases, 18, 238 Matrix metalloproteinase, 49, 238 Meat, 150, 215, 238 Medial, 198, 238, 246 Mediate, 17, 67, 118, 216, 238 Mediator, 34, 105, 232, 238, 259 Medical Staff, 216, 238 Medicament, 107, 114, 238 MEDLINE, 169, 173, 174, 238 Megaloblastic, 221, 238 Meiosis, 202, 238, 264 Melanin, 148, 238, 249, 267 Melanocytes, 238 Melanoma, 173, 203, 238 Membrane Proteins, 125, 236, 238 Meningitis, 221, 233, 239 Menopause, 130, 239, 251 Menstruation, 139, 214, 239 Mental Disorders, 100, 239 Menthol, 131, 149, 239 Mesenchymal, 219, 239 Mesentery, 239, 248 Mesoderm, 239, 261 Mesothelial, 68, 239 Meta-Analysis, 44, 66, 86, 88, 119, 148, 239 Metabolic disorder, 108, 225, 239
Metabolite, 6, 19, 118, 202, 215, 229, 239, 252 Metaphase, 202, 239 Metastasis, 113, 238, 239 Methicillin Resistance, 31, 239 Methionine, 122, 215, 239, 263 Methylene Blue, 157, 239 MI, 59, 189, 239 Microbe, 195, 239, 265 Microbiology, 12, 19, 42, 58, 60, 192, 201, 239 Microorganism, 117, 146, 209, 240, 247, 269 Micro-organism, 124, 240 Microscopy, 18, 84, 200, 240, 245 Microspheres, 125, 240 Microtubule-Associated Proteins, 53, 240 Microtubules, 240, 244 Microvillus, 13, 240 Migration, 76, 237, 240 Milligram, 162, 240 Milliliter, 203, 240 Mineral Oil, 111, 209, 240 Miotic, 240, 250 Mitomycin, 6, 240 Mitosis, 198, 240 Mitotic, 59, 240, 268 Mobility, 8, 17, 106, 141, 240 Modification, 9, 17, 20, 22, 55, 118, 162, 223, 240, 254 Molecular Evolution, 18, 240 Molecular mass, 22, 240 Molecular Probes, 217, 240 Molecular Structure, 115, 241 Monensin, 88, 241 Monitor, 97, 212, 241, 245 Monoamine, 90, 241, 267 Monoamine Oxidase, 90, 241, 267 Monoclonal, 29, 36, 42, 53, 55, 59, 63, 228, 233, 241, 255, 269 Monoclonal antibodies, 42, 59, 241 Monocyte, 58, 241 Morphine, 241, 243 Morphological, 17, 218, 222, 238, 241 Morphology, 26, 28, 237, 241 Motility, 241, 259 Motor nerve, 241, 242 Mucocutaneous, 235, 241 Mucolytic, 191, 241 Mucosa, 54, 223, 237, 241 Mucosal Lining, 116, 242 Mucositis, 242, 265
Index 281
Mucus, 220, 241, 242 Multiple Organ Failure, 24, 242 Muscle Contraction, 122, 242 Muscle Fibers, 242 Muscle relaxant, 157, 242 Muscle tension, 242 Muscular Atrophy, 174, 242 Muscular Dystrophies, 217, 242 Musculoskeletal System, 122, 152, 153, 242 Mutagenesis, 10, 18, 23, 30, 242 Mutagens, 222, 242 Myalgia, 231, 242 Myelogenous, 242 Myocardial infarction, 47, 212, 239, 242 Myocardium, 239, 242 Myosin, 31, 59, 242 Myotonic Dystrophy, 174, 242 N Narcosis, 242, 243 Narcotic, 157, 171, 241, 243 Nasal Mucosa, 231, 243 Natural selection, 201, 243 Nausea, 196, 216, 243 NCI, 1, 71, 99, 167, 209, 243 Necrosis, 197, 231, 239, 242, 243 Neonatal, 17, 243 Neoplasia, 173, 243 Neoplasm, 243, 258 Neoplastic, 53, 228, 237, 243 Nephropathy, 26, 234, 243 Nerve, 192, 194, 195, 199, 200, 207, 214, 222, 238, 241, 243, 252, 257, 258, 262, 266 Nerve Endings, 200, 243 Nerve Fibers, 200, 243 Neural, 26, 228, 241, 243 Neural Crest, 27, 243 Neuraminidase, 12, 107, 140, 243 Neuroblastoma, 35, 40, 243 Neurofilaments, 52, 244 Neuronal, 242, 244 Neurons, 214, 220, 242, 243, 244, 264 Neurotransmitters, 195, 244 Neutrons, 194, 203, 233, 244, 255 Neutrophil, 142, 143, 244 Niacin, 116, 149, 244, 266 Nickel, 83, 244 Nifedipine, 157, 244 Nitric Oxide, 14, 105, 118, 244 Nitrogen, 105, 113, 193, 194, 195, 220, 224, 240, 244, 266 Nocodazole, 59, 244 Norepinephrine, 192, 194, 216, 244
Nosocomial, 23, 244 Novobiocin, 66, 245 Nuclear, 8, 9, 28, 29, 30, 38, 55, 59, 61, 62, 64, 71, 75, 85, 200, 211, 217, 220, 222, 243, 245 Nuclear Pore, 30, 245 Nuclear Proteins, 8, 38, 245 Nuclei, 194, 211, 217, 220, 223, 240, 244, 245, 254 Nucleic acid, 107, 117, 123, 140, 151, 223, 228, 231, 242, 244, 245, 254, 257, 262 Nucleolus, 245, 257 Nucleoproteins, 245 Nucleotidases, 229, 245 Nucleus, 191, 198, 200, 208, 213, 215, 218, 220, 238, 244, 245, 253, 254, 261, 262, 264 Nursing Care, 6, 245 O Odour, 198, 245 Ointments, 131, 216, 245 Omega-3 fatty acid, 112, 245 Oncogene, 173, 245 On-line, 11, 189, 245 Oocytes, 54, 245 Opacity, 214, 245 Open Reading Frames, 23, 245 Operon, 12, 245, 256 Ophthalmic, 114, 246 Optic Chiasm, 230, 246 Organ Transplantation, 141, 246 Organelles, 213, 238, 246 Osmosis, 246 Osmotic, 60, 193, 246, 259 Ossification, 246 Osteoblasts, 130, 246 Osteoclasts, 130, 246 Osteogenesis, 139, 246 Osteoporosis, 130, 246 Osteotomy, 170, 246 Outpatient, 97, 246 Ovaries, 198, 246 Ovary, 219, 246, 247, 251 Overweight, 78, 97, 246 Ovulation, 139, 246, 247 Ovum, 191, 214, 223, 236, 247, 252, 269 Oxidation, 127, 148, 191, 197, 198, 202, 213, 224, 236, 237, 247 Oxidation-Reduction, 127, 202, 247 Oxidative metabolism, 235, 247 Oxides, 135, 247 Oxygenation, 110, 247
282 Glucosamine
P Pacemaker, 147, 247 Paediatric, 33, 82, 247 Palliative, 4, 247, 264 Pancreas, 191, 202, 215, 232, 233, 236, 247 Pancreatic, 118, 173, 247 Pancreatic cancer, 173, 247 Parasite, 15, 21, 247 Parasitic, 201, 247 Parietal, 247, 248, 251 Paroxysmal, 30, 34, 66, 174, 247, 249, 269 Partial remission, 247, 256 Patch, 129, 145, 247, 266 Pathogen, 8, 12, 23, 231, 247 Pathogenesis, 3, 7, 14, 15, 20, 23, 27, 90, 155, 247 Pathologic, 121, 198, 212, 221, 229, 248, 254, 256, 268 Pathologic Processes, 198, 248 Pathophysiology, 24, 248 Patient Compliance, 20, 248 Patient Education, 156, 178, 184, 186, 189, 248 Pelvic, 248, 253 Penicillin, 23, 195, 196, 239, 248 Pentosan polysulfate, 157, 248 Pentosyltransferases, 225, 248 Pepsin, 208, 248 Pepsin A, 208, 248 Peptide, 15, 36, 38, 59, 69, 84, 85, 120, 208, 221, 229, 234, 248, 251, 253, 254 Peptide Hydrolases, 229, 248 Perennial, 217, 248, 266 Perfusion, 248, 265 Periplasm, 12, 248 Peritoneal, 60, 68, 83, 87, 233, 248 Peritoneal Cavity, 233, 248 Peritoneal Dialysis, 60, 87, 248 Peritoneum, 87, 239, 248 Pertussis, 83, 125, 248, 269 Petroleum, 240, 249 PH, 33, 203, 249 Phagocytosis, 58, 249 Pharmaceutical Preparations, 207, 219, 223, 249 Pharmaceutical Solutions, 216, 249 Pharmacokinetic, 249 Pharmacologic, 4, 20, 156, 195, 249, 265 Pharynx, 231, 249 Phenazopyridine, 157, 249 Phenotype, 210, 249 Phenyl, 157, 249
Phenylalanine, 248, 249, 267 Phosphates, 7, 20, 249 Phospholipases, 249, 260 Phospholipids, 220, 232, 236, 249 Phosphoric Monoester Hydrolases, 229, 250 Phosphorus, 130, 204, 250 Phosphorylated, 15, 102, 209, 250 Phosphorylation, 10, 16, 48, 62, 250, 253 Photocoagulation, 209, 250 Physical Examination, 97, 171, 250 Physiologic, 145, 193, 202, 233, 239, 250, 255, 256 Physiology, 26, 47, 62, 83, 205, 250 Pigment, 201, 238, 250 Pilocarpine, 114, 250 Pilot study, 33, 51, 63, 74, 77, 82, 250 Pituitary Gland, 115, 221, 250 Placenta, 62, 148, 198, 219, 250, 252 Plaque, 149, 199, 250 Plasma, 10, 24, 115, 118, 193, 196, 206, 208, 221, 223, 224, 227, 229, 250, 256, 259, 265 Plasma cells, 196, 250 Plasma protein, 193, 250, 259 Plasmids, 123, 151, 218, 250 Platelet Activation, 251, 260 Platelet Aggregation, 195, 244, 251, 265 Platelets, 198, 244, 251 Platinum, 127, 251 Pleated, 234, 251 Pleural, 239, 251 Point Mutation, 23, 251 Poisoning, 204, 239, 243, 251 Pollen, 207, 251, 255 Polyarthritis, 234, 251, 260 Polycystic, 174, 251 Polymerase, 251, 256 Polymers, 28, 125, 147, 201, 251, 253, 262 Polymorphism, 123, 151, 251 Polypeptide, 192, 194, 209, 219, 225, 228, 248, 251, 269 Polysaccharide, 16, 27, 30, 31, 72, 107, 120, 121, 125, 140, 197, 207, 225, 251, 254 Posterior, 199, 216, 247, 251 Postmenopausal, 6, 115, 130, 160, 246, 251 Postoperative, 242, 252 Postsynaptic, 252, 260 Post-translational, 11, 252 Potassium, 97, 108, 150, 225, 252 Potentiate, 102, 252 Potentiating, 195, 252 Potentiation, 252, 260
Index 283
Practice Guidelines, 171, 252 Precursor, 7, 117, 133, 196, 198, 216, 217, 218, 244, 249, 252, 266, 267 Predisposition, 122, 252 Prenatal, 65, 218, 252 Prevalence, 23, 155, 252 Prickle, 234, 252 Probe, 6, 19, 252 Procaine, 236, 252 Prodrug, 138, 252 Progeny, 211, 252 Progesterone, 252, 262 Progression, 40, 49, 58, 86, 87, 137, 162, 170, 196, 252 Progressive, 110, 198, 206, 208, 217, 226, 242, 243, 246, 251, 253, 256 Proline, 121, 210, 229, 253 Promoter, 17, 31, 54, 253 Pronase, 107, 140, 253 Prophase, 202, 245, 253, 264 Prophylaxis, 45, 253, 257, 267 Prostaglandins, 110, 198, 253 Prostaglandins A, 110, 253 Prostaglandins D, 253 Prostate, 173, 253 Protease, 8, 26, 253 Protective Agents, 204, 253 Protein Binding, 253, 265 Protein C, 103, 193, 194, 197, 200, 234, 236, 253 Protein S, 120, 174, 175, 202, 223, 253, 257 Protein-Tyrosine Kinase, 223, 253 Proteinuria, 224, 253 Proteoglycan, 8, 14, 66, 105, 119, 133, 134, 147, 253 Proteolytic, 105, 194, 210, 253, 254 Protocol, 11, 254 Protons, 194, 228, 254, 255 Protozoa, 211, 235, 240, 254 Proximal, 7, 66, 135, 138, 216, 254, 259 Pruritic, 217, 254 Pruritus, 124, 215, 229, 254 Psoriasis, 35, 46, 146, 149, 209, 254, 257 Psychomotor, 205, 254 Psyllium, 92, 254 Public Policy, 169, 254 Publishing, 28, 254 Pulmonary, 202, 207, 211, 235, 254, 257, 263, 268 Pulse, 241, 254 Purifying, 13, 254 Purines, 254, 259
Pustular, 149, 254 Q Quality of Life, 6, 22, 254 Quaternary, 74, 255 Quercetin, 119, 147, 255 Quiescent, 139, 255 R Race, 122, 240, 255 Radiation, 128, 218, 220, 221, 222, 232, 233, 248, 255, 269 Radiation therapy, 220, 222, 232, 233, 248, 255, 269 Radioactive, 228, 231, 232, 233, 241, 245, 255, 269 Radiolabeled, 233, 255, 269 Radiology, 136, 255 Radiotherapy, 203, 233, 255, 269 Randomized, 21, 33, 42, 49, 51, 64, 68, 74, 82, 86, 89, 163, 217, 255 Randomized clinical trial, 68, 89, 255 Rationalize, 25, 255 Reactive Oxygen Species, 12, 70, 255 Receptor, 9, 10, 12, 15, 21, 25, 31, 43, 59, 76, 119, 192, 197, 216, 226, 229, 255, 259, 260 Receptors, Serotonin, 255, 259 Recombinant, 22, 35, 72, 102, 110, 117, 123, 151, 256, 268 Recombinant Proteins, 72, 256 Recombination, 211, 256 Rectum, 203, 210, 215, 221, 222, 231, 235, 253, 256 Red blood cells, 98, 219, 256, 258 Red Nucleus, 199, 256 Reductase, 95, 198, 256 Refer, 1, 204, 210, 222, 237, 244, 256, 259 Refraction, 256, 261 Regeneration, 39, 221, 256 Regimen, 107, 130, 140, 217, 248, 256 Relapse, 137, 256 Relaxant, 256 Remission, 35, 137, 256 Renin, 40, 54, 55, 65, 196, 256 Repressor, 23, 246, 256 Research Support, 6, 256 Resorption, 130, 246, 256 Respiration, 205, 213, 241, 247, 256 Respiratory distress syndrome, 143, 256 Respiratory Distress Syndrome, Adult, 143, 256 Respiratory Mucosa, 36, 257 Response rate, 11, 257 Restoration, 14, 110, 134, 171, 257, 269
284 Glucosamine
Retina, 235, 246, 257, 258 Retinoblastoma, 173, 257 Retinoids, 257, 269 Retinol, 148, 257 Reversion, 257, 267 Rhamnose, 107, 140, 257 Rheumatism, 44, 45, 63, 110, 125, 230, 257 Rheumatoid, 38, 70, 105, 124, 125, 152, 178, 257 Rheumatoid arthritis, 70, 105, 124, 152, 257 Rheumatology, 4, 21, 33, 34, 39, 40, 42, 50, 57, 74, 81, 82, 105, 257 Ribonucleic acid, 107, 140, 257 Ribose, 192, 257 Ribosome, 87, 257, 266 Rigidity, 250, 257 Risk factor, 24, 141, 155, 257 Ristocetin, 257, 267 Rod, 200, 201, 209, 234, 258 Rubber, 147, 191, 258 Rutin, 255, 258 S Salicylate, 157, 258 Salicylic, 149, 258 Saline, 17, 258 Saliva, 258 Salivary, 39, 213, 215, 247, 258, 260, 263 Salivary glands, 39, 213, 215, 258, 260 Saponins, 111, 258, 262 Sarcoma, 55, 258 Scleroproteins, 234, 258 Sclerosis, 174, 198, 258 Screening, 97, 209, 258 Secondary tumor, 239, 258 Secretion, 40, 48, 119, 133, 147, 208, 219, 228, 232, 234, 242, 258, 259, 260 Secretory, 125, 194, 258 Sedative, 194, 215, 229, 258 Sedentary, 104, 258 Segmental, 224, 258 Seizures, 205, 247, 258 Selenium, 131, 132, 259 Self Care, 157, 259 Sella, 250, 259 Semen, 253, 259 Senile, 246, 259 Sensor, 12, 34, 259 Sepsis, 7, 20, 259 Septal, 259 Septic, 24, 259 Septum, 127, 259
Septum Pellucidum, 259 Sequence Homology, 24, 259 Sequencing, 37, 259 Serine, 26, 118, 192, 259 Serotonin, 157, 194, 241, 255, 259, 266 Serum, 27, 47, 58, 84, 120, 125, 192, 193, 195, 197, 210, 237, 259 Serum Albumin, 120, 259 Sex Determination, 174, 259 Shedding, 128, 259 Shock, 24, 260, 266 Sialic Acids, 90, 260 Sialyltransferases, 225, 260 Sicca, 125, 260 Side effect, 122, 125, 149, 157, 163, 179, 192, 201, 205, 207, 229, 260, 265 Signal Transduction, 9, 11, 232, 260 Signs and Symptoms, 256, 260 Skeletal, 48, 120, 130, 195, 209, 212, 234, 242, 260 Skeleton, 191, 221, 233, 260 Skull, 260, 264 Small cell lung cancer, 71, 260 Small intestine, 201, 207, 208, 217, 223, 228, 232, 260 Smooth muscle, 14, 194, 195, 204, 211, 228, 229, 241, 260, 263 Sneezing, 249, 260 Social Environment, 255, 260 Sodium, 41, 108, 114, 145, 150, 157, 225, 241, 261 Soft tissue, 144, 203, 260, 261 Solid tumor, 196, 261 Solvent, 18, 191, 200, 219, 225, 246, 249, 261 Somatic, 30, 218, 228, 238, 240, 261 Somite, 26, 261 Sorbitol, 145, 261 Soybean Oil, 261, 269 Spasmodic, 249, 261 Specialist, 62, 180, 261 Specificity, 7, 17, 19, 24, 70, 89, 193, 198, 234, 261, 265 Spectrum, 141, 213, 261 Sperm, 32, 191, 195, 208, 251, 261, 266 Sperm Head, 191, 261 Spermatozoa, 191, 259, 261 Spermatozoon, 191, 261 Spinal cord, 199, 203, 207, 208, 222, 243, 261 Spinous, 219, 234, 261 Spleen, 36, 213, 237, 262
Index 285
Sporadic, 257, 262 Sputa, 60, 262 Stabilizer, 120, 262 Staphylococcal Infections, 27, 262 Steel, 209, 262 Stem Cells, 219, 262 Stent, 147, 262 Sterilization, 111, 119, 120, 127, 262 Steroid, 4, 115, 198, 201, 224, 258, 262 Stimulant, 130, 204, 228, 262 Stimulus, 262, 264 Stomach, 62, 191, 205, 215, 219, 223, 228, 243, 248, 249, 260, 262 Strand, 74, 251, 262 Stress, 122, 153, 243, 252, 257, 258, 262, 267 Stringency, 123, 151, 262 Stroke, 100, 168, 205, 262 Stupor, 242, 243, 262 Styrene, 258, 262 Subacute, 231, 262 Subclinical, 231, 258, 263 Subcutaneous, 24, 192, 263, 268 Subiculum, 228, 263 Submaxillary, 219, 263 Subspecies, 66, 261, 263 Substance P, 239, 257, 258, 263 Substrate, 18, 22, 25, 33, 68, 71, 82, 118, 144, 146, 147, 229, 243, 263, 267 Sulfates, 25, 45, 70, 72, 77, 90, 108, 114, 263 Sulfotransferases, 58, 263 Sulfur, 132, 220, 239, 263 Sulfuric acid, 108, 263 Superoxide, 12, 57, 105, 263 Superoxide Dismutase, 12, 105, 263 Supplementation, 14, 29, 68, 84, 86, 89, 130, 159, 263 Suppression, 223, 263 Surfactant, 135, 263 Swainsonine, 88, 263 Symbiosis, 7, 263 Sympathomimetic, 216, 219, 244, 263, 267 Symphysis, 253, 263 Symptomatic, 11, 29, 66, 86, 88, 263 Synaptic, 260, 264 Synergistic, 106, 119, 120, 147, 264 Synovial, 42, 67, 75, 77, 105, 117, 121, 150, 155, 233, 264 Synovial Fluid, 105, 117, 155, 264 Synovial Membrane, 105, 233, 264 Systemic, 20, 125, 140, 156, 171, 197, 202, 205, 219, 231, 233, 255, 257, 264, 269 Systolic, 229, 264
T Telangiectasia, 174, 264 Temporal, 8, 228, 264 Tendinitis, 125, 264 Testicular, 198, 264 Testis, 219, 264 Thalamic, 199, 264 Thalamic Diseases, 199, 264 Therapeutics, 33, 38, 63, 82, 83, 241, 264 Thermal, 156, 203, 216, 244, 264 Third Ventricle, 230, 264 Threonine, 118, 259, 264 Threshold, 16, 229, 264 Thrombin, 251, 253, 264 Thrombocytopenia, 49, 264 Thrombomodulin, 253, 264 Thrombosis, 253, 262, 265 Thromboxanes, 198, 265 Thymidine, 136, 265 Thyroid, 59, 233, 265, 267 Tin, 251, 265 Tissue Distribution, 118, 265 Tolerance, 12, 16, 224, 265 Tomography, 203, 265 Tooth Preparation, 192, 265 Toxicity, 10, 63, 110, 111, 118, 205, 216, 225, 249, 257, 265 Toxicokinetics, 265 Toxicology, 170, 265 Toxins, 113, 197, 224, 231, 241, 265 Trace element, 203, 244, 265 Trachea, 119, 148, 203, 220, 235, 249, 265 Traction, 209, 265 Transcription Factors, 24, 265 Transdermal, 149, 150, 266 Transduction, 260, 266 Transfection, 43, 202, 218, 266 Transferases, 18, 123, 151, 225, 266 Translation, 8, 23, 266 Translational, 223, 266 Translocation, 10, 41, 266 Transmitter, 191, 199, 216, 238, 244, 266, 267 Transplantation, 42, 118, 170, 208, 230, 266 Trauma, 130, 153, 200, 226, 243, 257, 264, 266 Trees, 258, 266 Triglyceride, 104, 229, 266 Tryptophan, 210, 259, 266 Tuberculosis, 211, 237, 258, 266 Tuberous Sclerosis, 174, 266 Tubulin, 240, 266
286 Glucosamine
Tunicamycin, 88, 139, 266 Type 2 diabetes, 24, 68, 89, 118, 159, 266 Typhimurium, 111, 267 Tyramine, 241, 267 Tyrosine, 11, 206, 216, 253, 267 U Ulcer, 217, 267 Unconscious, 195, 230, 255, 267 Uracil, 267 Urethra, 253, 267 Uric, 225, 229, 254, 267 Uridine Diphosphate, 8, 9, 224, 267 Urinary, 157, 204, 213, 249, 267 Urinary tract, 249, 267 Urine, 69, 97, 193, 202, 212, 216, 219, 224, 227, 234, 253, 267 Urokinase, 69, 267 Ursodeoxycholic Acid, 69, 267 Urticaria, 207, 229, 267 Uterus, 214, 239, 246, 252, 267 V Vaccination, 16, 36, 107, 114, 140, 267 Vaccine, 16, 27, 72, 102, 125, 192, 194, 204, 254, 267 Vagina, 201, 205, 234, 239, 267 Vancomycin, 23, 267 Varices, 77, 268 Vascular, 14, 24, 26, 29, 72, 121, 141, 194, 204, 218, 229, 231, 244, 250, 267, 268 Vasoconstriction, 219, 268 Vasodilator, 203, 216, 228, 244, 268 Vector, 8, 123, 151, 266, 268 Vegetative, 13, 202, 268 Vein, 97, 233, 245, 268 Venous, 253, 268 Ventricle, 228, 254, 264, 268 Ventricular, 65, 268
Venules, 202, 205, 268 Veterinarians, 106, 268 Veterinary Medicine, 169, 268 Vibrio, 60, 88, 208, 268 Vibrio cholerae, 60, 88, 208, 268 Vinblastine, 88, 266, 268 Vinca Alkaloids, 268 Viral, 102, 191, 231, 266, 268 Virulence, 12, 27, 28, 30, 62, 199, 265, 268 Virus, 9, 37, 69, 90, 125, 200, 218, 223, 226, 232, 250, 266, 268 Visceral, 24, 235, 248, 268 Visceral fat, 24, 268 Viscosity, 191, 268 Vitamin A, 103, 232, 257, 269 Vitamin E, 103, 269 Vitro, 15, 18, 19, 21, 22, 32, 227, 269 Vivo, 12, 14, 19, 269 W Weight Gain, 104, 269 Weight-Bearing, 105, 106, 269 White blood cell, 105, 113, 196, 208, 235, 237, 241, 242, 244, 250, 269 Whooping Cough, 249, 269 Windpipe, 249, 265, 269 Wound Healing, 46, 92, 107, 129, 139, 140, 145, 221, 238, 269 X Xenograft, 196, 269 X-ray, 10, 203, 206, 221, 233, 245, 255, 262, 269 X-ray therapy, 233, 269 Y Yeasts, 222, 249, 269 Z Zygote, 211, 269 Zymogen, 253, 269
Index 287
288 Glucosamine
