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PMID: 2920840 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells.

FEBS letters ·Vol. 244 ·No. 2 ·1989-02-27 ·Pages 473-6

Okada Y, Konomi H, Yada T, Kimata K, Nagase H

Abstract

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.

MeSH Terms
Animals Arthritis, Rheumatoid/enzymology Cells, Cultured Chick Embryo Collagen/metabolism Humans Matrix Metalloproteinase 3 Metalloendopeptidases/isolation & purification,metabolism Substrate Specificity Synovial Fluid/enzymology
Chemicals
Collagen Metalloendopeptidases Matrix Metalloproteinase 3
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Okada Y
Department of Pathology, School of Medicine, Kanazawa University, Ishikawa, Japan.
Konomi H
Yada T
Kimata K
Nagase H
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1989-02-27
Pages
473-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
Grants
NIAMS NIH HHS · AR 39189 · United States
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