Articular cartilage and changes in arthritis: Matrix degradation
Open Access
- 1 January 2001
- journal article
- review article
- Published by Springer Nature in Arthritis Research & Therapy
- Vol. 3 (6) , 337-341
- https://doi.org/10.1186/ar325
Abstract
While many proteases in articular cartilage have been described, current studies indicate that members of two families of metalloproteases – MMPs and the ADAMTSs – are responsible for the degradation of the major components of this tissue. Collagenases (MMPs) make the first cleavage in triple-helical collagen, allowing its further degradation by other proteases. Aggrecanases (ADAMTSs), in conjunction with other MMPs, degrade aggrecan, a component of the proteoglycan aggregate. Anti-neoepitope antibodies that recognize the cleavage products of collagen and aggrecan generated by these enzymes are now available and are being used to detect the sites of action and to quantitate degradation products.Keywords
This publication has 28 references indexed in Scilit:
- Inhibition of ADAMTS4 (aggrecanase‐1) by tissue inhibitors of metalloproteinases (TIMP‐1, 2, 3 and 4)FEBS Letters, 2001
- Identification of the 183RWTNNFREY191Region as a Critical Segment of Matrix Metalloproteinase 1 for the Expression of Collagenolytic ActivityJournal of Biological Chemistry, 2000
- The relative importance of cysteine peptidases in osteoarthritis.2000
- The Thrombospondin Motif of Aggrecanase-1 (ADAMTS-4) Is Critical for Aggrecan Substrate Recognition and CleavageJournal of Biological Chemistry, 2000
- ADAMTS‐1 cleaves a cartilage proteoglycan, aggrecanFEBS Letters, 2000
- Type II collagen degradation in spontaneous osteoarthritis in C57BL/6 and BALB/c miceArthritis & Rheumatism, 1999
- N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures. Putative site(s) of enzymic cleavageBiochemical Journal, 1992
- Identification of a stromelysin cleavage site within the interglobular domain of human aggrecan. Evidence for proteolysis at this site in vivo in human articular cartilage.Journal of Biological Chemistry, 1992
- Cathepsin B in synovial cells at the site of joint destruction in rheumatoid arthritisArthritis & Rheumatism, 1991
- Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation.Proceedings of the National Academy of Sciences, 1990