| Literature DB >> 3030290 |
S E Whitham, G Murphy, P Angel, H J Rahmsdorf, B J Smith, A Lyons, T J Harris, J J Reynolds, P Herrlich, A J Docherty.
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.Entities:
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Year: 1986 PMID： 3030290 PMCID： PMC1147507 DOI： 10.1042/bj2400913
Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857