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Review
. 2002 Nov;61 Suppl 2(Suppl 2):ii78-81.
doi: 10.1136/ard.61.suppl_2.ii78.

Type II collagen degradation and its regulation in articular cartilage in osteoarthritis

A R Poole  1 , M Kobayashi, T Yasuda, S Laverty, F Mwale, T Kojima, T Sakai, C Wahl, S El-Maadawy, G Webb, E Tchetina, W Wu
Affiliations
Review

Type II collagen degradation and its regulation in articular cartilage in osteoarthritis

A R Poole et al. Ann Rheum Dis. 2002 Nov.
No abstract available

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Figures

Figure 1
Figure 1
Diagrammatic representation of some of the elements of cartilage structure and matrix turnover. Type II collagen fibrils form an endoskeleton and associated with them in interfibrillar sites resides the proteoglycan aggrecan aggregated with hyaluronic acid. In physiology there is active pericellular turnover of extracellular matrix involving proteolysis mediated by matrix metalloproteinases (MMPs). In OA there is increased damage to resident matrix molecules more remote from chondrocytes with up regulation of synthesis of collagen and proteoglycan. These new molecules are also subject to degradation. Degradation products are released to body fluids where they can be detected. Increased proteolysis involves up regulation of interleukin (IL)1 and tumour necrosis factor ß (TNFß) expression by chondrocytes, nitric oxide (NO) production, and receptor activation by matrix degradation products, which is IL1 and TNFα dependent. Reproduced with permission from references 35 and 36.
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