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. 1986 Dec 15;240(3):913–916. doi: 10.1042/bj2400913

Comparison of human stromelysin and collagenase by cloning and sequence analysis.

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
PMCID: PMC1147507  PMID: 3030290

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.

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Selected References

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