Premium
Activation of matrix metalloproteinase 3 (stromelysin) and matrix metalloproteinase 2 (‘gelatinase’) by human neutrophil elastase and cathepsin G
Author(s) -
Okada Yasunori,
Nakanishi Isao
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)80657-x
Subject(s) - cathepsin g , elastase , neutrophil elastase , matrix metalloproteinase , chemistry , matrix metalloproteinase 3 , cathepsin , zymogen , gelatinase , pancreatic elastase , cathepsin l1 , metalloproteinase , biochemistry , microbiology and biotechnology , inflammation , biology , immunology , enzyme
The ability of human neutrophil elastase and cathepsin G to activate matrix metalloproteinase 3 (MMP‐3 = stromelysin) and MMP‐2 (‘gelatinase’) purified from human rheumatoid synovial fibroblasts in culture was examined. The zymogen of MMP‐3 (proMMP‐3) was activated to full activity with elastase and cathepsin G by limited proteolysis of the molecule into two active forms of M r ∼ 45000 and M r ∼ 25000. In contrast, proMMP‐2 was not activated at all by these neutrophil serine proteinases, although it was degraded into small fragments. These data suggest that neutrophil elastase and cathepsin G may play an important role in the activation of proMMP‐3 in vivo in various inflammatory conditions, but proMMP‐2 may be activated in different ways.