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Comparison of human stromelysin and collagenase by cloning and sequence analysis.
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.
PMID: 3030290 [PubMed - indexed for MEDLINE]
PMCID: PMC1147507
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Cited by 61 PubMed Central articles
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Genome-wide identification of Xenopus matrix metalloproteinases: conservation and unique duplications in amphibians.
Fu L, Das B, Mathew S, Shi YB.
BMC Genomics. 2009 Feb 17; 10:81. Epub 2009 Feb 17.
[BMC Genomics. 2009]
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Chronic ultraviolet B irradiation causes loss of hyaluronic acid from mouse dermis because of down-regulation of hyaluronic acid synthases.
Dai G, Freudenberger T, Zipper P, Melchior A, Grether-Beck S, Rabausch B, de Groot J, Twarock S, Hanenberg H, Homey B, et al.
Am J Pathol. 2007 Nov; 171(5):1451-61.
[Am J Pathol. 2007]
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Sequencing and Characterization of the Soybean Leaf Metalloproteinase : Structural and Functional Similarity to the Matrix Metalloproteinase Family.
McGeehan G, Burkhart W, Anderegg R, Becherer JD, Gillikin JW, Graham JS.
Plant Physiol. 1992 Jul; 99(3):1179-1183.
[Plant Physiol. 1992]
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