Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells.
The degradation of type IX collagen, a minor collagen in cartilage, was examined by treatment with three different types of matrix metalloproteinases (MMPs) purified from the culture medium of rheumatoid synovial cells. Neither MMP-1 (collagenase) nor MMP-2 (so-called 'gelatinase') could digest type IX collagen, but MMP-3 (stromelysin) readily degraded it into smaller fragments. This suggests that MMP-3 may be responsible for the pathological degradation and/or normal turnover of type IX collagen.
Okada
Y
Y
Department of Pathology, School of Medicine, Kanazawa University, Ishikawa, Japan.
Konomi
H
H
Yada
T
T
Kimata
K
K
Nagase
H
H
D000818:Animals; D001172:Arthritis, Rheumatoid / Q000201:enzymology*; D002478:Cells, Cultured; D002642:Chick Embryo; D003094:Collagen / Q000378:metabolism*; D006801:Humans; D019278:Matrix Metalloproteinase 3; D008666:Metalloendopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity; D013582:Synovial Fluid / Q000201:enzymology*
D003094:Collagen; D008666:Metalloendopeptidases; D019278:Matrix Metalloproteinase 3