title: Comparison of human stromelysin and collagenase by cloning and sequence analysis.
abstract: A comparison of the cDNA-derived amino acid sequences of human stromelysin and collagenase with the N-terminal sequences of purified enzymes reveals that these metalloproteinases are highly conserved and that they are secreted as proenzymes. A putative zinc-binding site was identified by its homology with the zinc-chelating sequence of thermolysin. These sequences permitted the identification of: transin, a protein induced in rat fibroblasts either exposed to growth factors or transformed by oncogenic viruses, as the rat homologue of stromelysin, and XHF1, a protein induced in human fibroblasts after treatment with tumourigenic agents, as collagenase.
mesh_terms: D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D004247:DNA; D010450:Endopeptidases; D006801:Humans; D019278:Matrix Metalloproteinase 3; D003012:Microbial Collagenase; D010662:Phenylmercuric Acetate / Q000031:analogs & derivatives
chemical_list: C010024:4-aminophenylmercuriacetate; D004247:DNA; D010450:Endopeptidases; D019278:Matrix Metalloproteinase 3; D003012:Microbial Collagenase; D010662:Phenylmercuric Acetate