The latent forms of stromelysin and collagenase from human gingival fibroblasts were purified to homogeneity. These latent proenzymes underwent serial small reductions in Mr upon activation by treatment with either 4-aminophenylmercuric acetate or trypsin. Similar shifts in Mr and activation kinetics were observed upon identical treatments of either recombinant prostromelysin or procollagenase. Prostromelysin showed a lag between activation and Mr fall, suggesting an initial activation by conformational change. Collagenase activity was enhanced up to 12-fold by either natural or recombinant stromelysin in the presence of trypsin or 4-aminophenylmercuric acetate. Stromelysin caused a further apparent decrease in the Mr of procollagenase. Since these important connective-tissue-degrading enzymes are usually co-ordinately produced by cells, a cascade mechanism is proposed in which collagenase is activated by stromelysin.
Stromelysin is an activator of procollagenase. A study with natural and recombinant enzymes
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G Murphy, M I Cockett, P E Stephens, B J Smith, A J P Docherty; Stromelysin is an activator of procollagenase. A study with natural and recombinant enzymes. Biochem J 15 November 1987; 248 (1): 265–268. doi: https://doi.org/10.1042/bj2480265
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