Evidence that human rheumatoid synovial matrix metalloproteinase 3 is an endogenous activator of procollagenase.
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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Department of Biochemistry, University of Kansas Medical Center, Kansas City 66103.
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D001172:Arthritis, Rheumatoid / Q000201:enzymology*; D002478:Cells, Cultured; D017364:Collagenases; D004789:Enzyme Activation / Q000187:drug effects; D004792:Enzyme Precursors / Q000378:metabolism*; D006801:Humans; D019278:Matrix Metalloproteinase 3; D008666:Metalloendopeptidases / Q000378:metabolism*; D003012:Microbial Collagenase / Q000378:metabolism*; D008970:Molecular Weight; D010662:Phenylmercuric Acetate / Q000031:analogs & derivatives / Q000494:pharmacology; D013583:Synovial Membrane / Q000201:enzymology*; D014357:Trypsin / Q000494:pharmacology
D004792:Enzyme Precursors; C010024:4-aminophenylmercuriacetate; D014357:Trypsin; D017364:Collagenases; D008666:Metalloendopeptidases; C022440:procollagenase; D019278:Matrix Metalloproteinase 3; D003012:Microbial Collagenase; D010662:Phenylmercuric Acetate