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Suchschritt : FT=glucosamine AND FT=osteoarthritis
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2/274 von 416 DIMDI: MEDLINE (ME60) © NLM

ND: | ME11290798
PMID: | 11290798
LR: | 20061115
CED: | 20010406
DCO: | 20010628
Autoren: | Shikhman AR; Kuhn K; Alaaeddine N; Lotz M
Titel: | N-acetylglucosamine prevents IL-1 beta-mediated activation of human chondrocytes.
Quelle: | Journal of immunology (Baltimore, Md. : 1950); VOL: 166 (8); p. 5155-60 /20010415/
PM: | Print
SU: | AIM IM
Sprache: | English
CY: | United States
JID: | 2985117R
ISSN: | 0022-1767
CO: | JOIMA3
Institution: | Division of Rheumatology, Scripps Clinic, La Jolla, CA 92037, USA.
DT: | Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.
NG: | AG07996 AG NIA; AT00052 AT NCCAM
Schlagwörter
CT: | ACETYLGALACTOSAMINE/pharmacology; ACETYLGLUCOSAMINE/*pharmacology; ACTIVE TRANSPORT, CELL NUCLEUS/drug effects; ANTI-INFLAMMATORY AGENTS/*pharmacology; CARTILAGE, ARTICULAR/drug effects; CARTILAGE, ARTICULAR/enzymology; CARTILAGE, ARTICULAR/immunology; CARTILAGE, ARTICULAR/metabolism; CELL NUCLEUS/drug effects; CELL NUCLEUS/metabolism; CELLS, CULTURED; CHONDROCYTES/*drug effects; CHONDROCYTES/enzymology; CHONDROCYTES/immunology; CHONDROCYTES/*metabolism; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; ENZYME ACTIVATION/drug effects; GLUCOSAMINE/pharmacology; HUMANS; INTERLEUKIN-1/*antagonists & inhibitors; INTERLEUKIN-1/*physiology; INTERLEUKIN-6/biosynthesis; ISOENZYMES/antagonists & inhibitors; ISOENZYMES/biosynthesis; JNK MITOGEN-ACTIVATED PROTEIN KINASES; MEMBRANE PROTEINS; MITOGEN-ACTIVATED PROTEIN KINASES/metabolism; NF-KAPPA B/metabolism; NITRIC OXIDE/antagonists & inhibitors; NITRIC OXIDE/biosynthesis; NITRIC OXIDE SYNTHASE/antagonists & inhibitors; NITRIC OXIDE SYNTHASE/biosynthesis; NITRIC OXIDE SYNTHASE TYPE II; PHOSPHORYLATION/drug effects; PROSTAGLANDIN-ENDOPEROXIDE SYNTHASES/biosynthesis; P38 MITOGEN-ACTIVATED PROTEIN KINASES
CTG: | ACETYLGALACTOSAMIN/Pharmakologie; ACETYLGLUCOSAMIN/*Pharmakologie; AKTIVER TRANSPORT, ZELLKERN/Arzneimittelwirkungen; ANTIPHLOGISTIKA/*Pharmakologie; KNORPEL, GELENK-/Arzneimittelwirkungen; KNORPEL, GELENK-/Enzymologie; KNORPEL, GELENK-/Immunologie; KNORPEL, GELENK-/Stoffwechsel; ZELLKERN/Arzneimittelwirkungen; ZELLKERN/Stoffwechsel; ZELLEN, KULTIVIERTE; CHONDROZYTEN/*Arzneimittelwirkungen; CHONDROZYTEN/Enzymologie; CHONDROZYTEN/Immunologie; CHONDROZYTEN/*Stoffwechsel; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; ENZYMAKTIVIERUNG/Arzneimittelwirkungen; GLUCOSAMIN/Pharmakologie; MENSCH; INTERLEUKIN-1/*Antagonisten & Inhibitoren; INTERLEUKIN-1/*Physiologie; INTERLEUKIN-6/Biosynthese; ISOENZYME/Antagonisten & Inhibitoren; ISOENZYME/Biosynthese; JNK-MITOGEN-AKTIVIERTE PROTEINKINASEN; MEMBRANPROTEINE; MITOGENAKTIVIERTE PROTEINKINASEN/Stoffwechsel; NF-KAPPA B/Stoffwechsel; STICKSTOFFMONOXID/Antagonisten & Inhibitoren; STICKSTOFFMONOXID/Biosynthese; STICKSTOFFMONOXID-SYNTHASE/Antagonisten & Inhibitoren; STICKSTOFFMONOXID-SYNTHASE/Biosynthese; STICKSTOFFMONOXID-SYNTHASE TYP II; PHOSPHORYLIERUNG/Arzneimittelwirkungen; PROSTAGLANDIN-ENDOPEROXID-SYNTHASE/Biosynthese; P38-MITOGEN-AKTIVIERTE PROTEINKINASEN
TE: | Anti-Inflammatory Agents; Interleukin-1; Interleukin-6; Isoenzymes; Membrane Proteins; NF-kappa B; Nitric Oxide/10102-43-9; Acetylgalactosamine/31022-50-1; Glucosamine/3416-24-8; Acetylglucosamine/7512-17-6; NOS2A protein, human/E.C. 1.14.13.39; Nitric Oxide Synthase/E.C. 1.14.13.39; Nitric Oxide Synthase Type II/E.C. 1.14.13.39; Cyclooxygenase 1/E.C. 1.14.99.1; Cyclooxygenase 2/E.C. 1.14.99.1; PTGS1 protein, human/E.C. 1.14.99.1; PTGS2 protein, human/E.C. 1.14.99.1; Prostaglandin-Endoperoxide Synthases/E.C. 1.14.99.1; JNK Mitogen-Activated Protein Kinases/E.C. 2.7.1.37; Mitogen-Activated Protein Kinases/E.C. 2.7.1.37; p38 Mitogen-Activated Protein Kinases/E.C. 2.7.1.37
CR: | 10102-43-9; 31022-50-1; 3416-24-8; 7512-17-6; E.C. 1.14.13.39; E.C. 1.14.13.39; E.C. 1.14.13.39; E.C. 1.14.99.1; E.C. 1.14.99.1; E.C. 1.14.99.1; E.C. 1.14.99.1; E.C. 1.14.99.1; E.C. 2.7.1.37; E.C. 2.7.1.37; E.C. 2.7.1.37
AB: | Glucosamine represents one of the most commonly used drugs to treat osteoarthritis. However, mechanisms of its antiarthritic activities are still poorly understood. The present study identifies a novel mechanism of glucosamine-mediated anti-inflammatory activity. It is shown that both glucosamine and N-acetylglucosamine inhibit IL-1beta- and TNF-alpha-induced NO production in normal human articular chondrocytes. The effect of the sugars on NO production is specific, since several other monosaccharides, including glucose, glucuronic acid, and N-acetylmannosamine, do not express this activity. Furthermore, N-acetylglucosamine polymers, including the dimer and the trimer, also do not affect NO production. The observed suppression of IL-1beta-induced NO production is associated with inhibition of inducible NO synthase mRNA and protein expression. In addition, N-acetylglucosamine also suppresses the production of IL-1beta-induced cyclooxygenase-2 and IL-6. The constitutively expressed cyclooxygenase-1, however, was not affected by the sugar. N-acetylglucosamine-mediated inhibition of the IL-1beta response of human chondrocytes was not associated with the decreased inhibition of the mitogen-activated protein kinases c-Jun N-terminal kinase, extracellular signal-related kinase, and p38, nor with activation of the transcription factor NF-kappaB. In conclusion, these results demonstrate that N-acetylglucosamine expresses a unique range of activities and identifies a novel mechanism for the inhibition of inflammatory processes.

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