The inhibitory of glucosamine on the MMP-3 expression in chondrocyte

• Main Authors: Yu-Chen Lin, 林育貞
• Other Authors: Chien-HO Chen, Ph.D.
• Format: Others
• Language: zh-TW
• Published: 2005
• Online Access: http://ndltd.ncl.edu.tw/handle/13079154452310781254

碩士 === 臺北醫學大學 === 醫學技術學系 === 93 === Osteoarthritis（OA） is characterized by loss of the functional intergrity of articular cartilage due to an imbalance between catabolic and anabolic chondrocyte activity. Degradation of the collagenous extracellular matrix by metalloproteases（MMPs）play an important role in the pathogenesis of osteoarthritis. Interleukin-1 (IL-1), a cytokine present which in elevated in OA cartilage and synovial fluid.IL-1is an important mediator of increase matrix degradation and reduced PG synthesis. IL-1 mediates this process by a number of metabolic processes including up-regulating enzymes such as nitric oxide synthase, matrix metalloproteinase. Glucosamine is capable of stimulating PG synthesis, inhibiting the degradation of PGs, and stimulating the regeneration of cartilage in vivo. It showed that the expression of metalloproteases-3（MMP-3）was downregulated by treatment of glucosamine. To examine which signal pathway are involved in the MMP-3 expression by glucosamine, several kinase pathway are investigated the phosphorylation status. The result showed that glucosamine activated Akt, ERK and JNK pathway. Beside, glucosamine inhibited p38 phosphoylation and NF-kB translocated to nucleus. The Akt inhibitors, wortmannin, blocked glucosamine stimulated Akt phosphorylation without blocking ERK phosphorylation. These results provide evidence of glucosamine inhibit IL-1induced NF-kB pathway via Akt phosphorylation regulation in chondrocyte.