Evidence that human rheumatoid synovial matrix metalloproteinase 3 is an endogenous activator of procollagenase |
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Authors: | A Ito H Nagase |
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Institution: | Department of Biochemistry, University of Kansas Medical Center, Kansas City 66103. |
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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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