Activation of matrix metalloproteinase 3 (stromelysin) and matrix metalloproteinase 2 ('gelatinase') by human neutrophil elastase and cathepsin G
Y Okada, I Nakanishi - FEBS letters, 1989 - Elsevier
Y Okada, I Nakanishi
FEBS letters, 1989•ElsevierThe 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 …
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 …
Abstract
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 Mr ∼ 45000 and Mr ∼ 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.
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