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. 1988 Nov 15;267(1):211-6.
doi: 10.1016/0003-9861(88)90025-2.

Evidence that human rheumatoid synovial matrix metalloproteinase 3 is an endogenous activator of procollagenase

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Evidence that human rheumatoid synovial matrix metalloproteinase 3 is an endogenous activator of procollagenase

A Ito et al. Arch Biochem Biophys. .

Abstract

The treatment of crude culture medium from human rheumatoid synovial cells with 4-aminophenylmercuric acetate (APMA) or trypsin results in the activation of procollagenase. This process was shown to be dependent on the presence of matrix metalloproteinase 3 (MMP-3). MMP-3 can directly activate procollagenase without changing the apparent molecular weight of procollagenase. This activity was accelerated in the presence of APMA. We propose that MMP-3 plays an important role in connective tissue destruction through the activation of procollagenase in addition to its direct action on components of the extracellular matrix.

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