Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein

G. I. Goldberg, S. M. Wilhelm, A. Kronberger, E. A. Bauer, G. A. Grant, A. Z. Eisen

Research output: Contribution to journalArticlepeer-review

535 Scopus citations

Abstract

We have determined the complete sequence of the cDNA clone representing the full size human skin collagenase mRNA. Collagenase is synthesized in pre-proenzyme form M(r) 54,092, with a 19 amino acid long signal peptide. The primary secretion products of the enzyme consist of a minor glycosylated form, M(r) 57,000, and a major unmodified polypeptide of predirected M(r) 51,929. Proteolytic activation of human skin procollagenase results in removal of 81 amino acid residues from the amino-terminal portion of the proenzyme. Both potential N-glycosylation sites are contained within the proteolytically activated form of the enzyme. The primary structure of the coding region of the presented clone is homologous to an oncogene-induced rat protein whose function is still unknown, although preliminary observations suggest that it is not rat skin collagenase.

Original languageEnglish
Pages (from-to)6600-6605
Number of pages6
JournalJournal of Biological Chemistry
Volume261
Issue number14
StatePublished - 1986

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