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.
Dates
Type | When |
---|---|
Created | 10 years ago (Aug. 10, 2015, 4:57 p.m.) |
Deposited | 3 years, 9 months ago (Nov. 25, 2021, 11:53 a.m.) |
Indexed | 1 month, 4 weeks ago (July 2, 2025, 2:47 p.m.) |
Issued | 38 years, 8 months ago (Dec. 15, 1986) |
Published | 38 years, 8 months ago (Dec. 15, 1986) |
Published Print | 38 years, 8 months ago (Dec. 15, 1986) |
@article{Whitham_1986, title={Comparison of human stromelysin and collagenase by cloning and sequence analysis}, volume={240}, ISSN={1470-8728}, url={http://dx.doi.org/10.1042/bj2400913}, DOI={10.1042/bj2400913}, number={3}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Whitham, S E and Murphy, G and Angel, P and Rahmsdorf, H J and Smith, B J and Lyons, A and Harris, T J R and Reynolds, J J and Herrlich, P and Docherty, A J P}, year={1986}, month=dec, pages={913–916} }