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Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells
Author(s) -
Okada Yasunori,
Konomi Hiroshi,
Yada Toshikazu,
Kimata Koji,
Nagase Hideaki
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80586-1
Subject(s) - matrix metalloproteinase , metalloproteinase , matrix metalloproteinase 3 , chemistry , degradation (telecommunications) , rheumatoid arthritis , matrix (chemical analysis) , collagen, type i, alpha 1 , biochemistry , immunology , extracellular matrix , medicine , chromatography , telecommunications , computer science
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.