Literature DB >> 3305933

Proteoglycans from experimental osteoarthritic cartilage: degradation by neutral metalloproteases.

J P Pelletier, J Martel-Pelletier, C J Malemud.   

Abstract

This study deals with the analysis of the structure of cartilage proteoglycans in experimental osteoarthritis. We have demonstrated that chondrocytes in osteoarthritic cartilage synthesize proteoglycans which have the same functional characteristics as those of normal cartilage. Osteoarthritic cartilage contains metallodependent proteoglycan degrading enzymes, in both active and latent forms. These enzymes degrade both synthesized and endogenous proteoglycan macromolecules, as indicated by the reduced hydrodynamic size found in both proteoglycan populations in osteoarthritic cartilage treated with APMA. Our results also suggest the possibility that proteolytic degradation can occur at both the hyaluronate-binding region and in the chondroitin-sulfate-rich region of the proteoglycan core protein.

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Year:  1987        PMID: 3305933

Source DB:  PubMed          Journal:  J Rheumatol        ISSN: 0315-162X            Impact factor:   4.666


  3 in total

1.  Gene expression of matrix metalloproteinases 1, 3, and 9 by chondrocytes in osteoarthritic human knee articular cartilage is zone and grade specific.

Authors:  A J Freemont; V Hampson; R Tilman; P Goupille; Y Taiwo; J A Hoyland
Journal:  Ann Rheum Dis       Date:  1997-09       Impact factor: 19.103

2.  In situ zymographic localisation of type II collagen degrading activity in osteoarthritic human articular cartilage.

Authors:  A J Freemont; R J Byers; Y O Taiwo; J A Hoyland
Journal:  Ann Rheum Dis       Date:  1999-06       Impact factor: 19.103

3.  The Novartis-ILAR Rheumatology Prize 2001 Osteoarthritis: from molecule to man.

Authors:  Jean-Pierre Pelletier; Johanne Martel-Pelletier
Journal:  Arthritis Res       Date:  2001-11-02
  3 in total

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