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1. We previously reported an endogenous activator of procollagenase from the culture medium of rabbit uterine cervical fibroblasts (Ishibashi et al. (1987) Biochem. J. 241, 527-534). 2. Similar activator was also purified and characterized from rabbit synovial fibroblasts (Vater et al. (1983) J. biol. Chem. 258, 9374-9382), but its mode of activation of procollagenase was reported to be different from that of purified activator from uterine cervical fibroblasts. 3. Here we report the comparative studies of the two activators of procollagenase and demonstrate that they are identified as matrix metalloproteinase 3 (stromelysin) by their immunological and functional criteria. The specific role of the activator in procollagenase activation is also described.

Original publication




Journal article


Comp Biochem Physiol B

Publication Date





381 - 385


Animals, Cells, Cultured, Cervix Uteri, Chromatography, Affinity, Collagenases, Enzyme Precursors, Female, Immunodiffusion, Kinetics, Matrix Metalloproteinase 3, Metalloendopeptidases, Microbial Collagenase, Pregnancy, Rabbits