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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...
Tissue inhibitor of metalloproteinases (TIMP) from cultured bovine dental pulp inhibits human rheumatoid synovial matrix metalloproteinase 3 (MMP-3) with a stoichiometry of 1:1 on a molar basis. Among the serine proteinases examined, human neutrophil elastase, trypsin and α-chymotrypsin destroyed the inhibitory activity of TIMP against MMP-3 by degrading the inhibitor molecule into small fragments...
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