Comparison of human stromelysin and collagenase by cloning and sequence analysis

作者：S. E. Whitham, Gillian Murphy, Peter E. Angel, Hans J. Rahmsdorf, Bryan John Smith, A. Bruce Lyons, T J R Harris, John J. Reynolds, Peter A. Herrlich, Andrew Docherty · 发表于：Biochemical Journal · 年份：1986 · DOI：10.1042/bj2400913 · 被引用次数：441 · 研究领域：Ubiquitin and proteasome pathways、Cancer-related Molecular Pathways、Protease and Inhibitor Mechanisms

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.