The latency of the human fibroblast collagenase precursor depends on an internal cysteine residue.

J. A. Engler, L. Windsor, B. Birkedal-Hansen, H. Birkedal-Hansen

Research output: Contribution to journalArticle

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Abstract

The proenzyme form of human fibroblast collagenase has been expressed in E. coli from its cDNA clone and has been shown to be functionally identical to the human enzyme. Mutants at one of three cysteine residues were constructed by site-directed mutagenesis of the cDNA and their relative activities compared to the wild type enzyme. A cysteine contained in the propeptide domain of procollagenase and other matrix metalloproteinases was shown to be essential for maintaining the proenzyme in an inactive state. A model to explain the importance of this highly conserved cysteine to the maintenance of latency is discussed.

Original languageEnglish (US)
Pages (from-to)231-236
Number of pages6
JournalMatrix (Stuttgart, Germany). Supplement
Volume1
StatePublished - 1992
Externally publishedYes

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Matrix Metalloproteinase 8
Cysteine
Enzyme Precursors
Complementary DNA
Enzymes
Site-Directed Mutagenesis
Matrix Metalloproteinases
Clone Cells
Maintenance
Escherichia coli

ASJC Scopus subject areas

  • Medicine(all)

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The latency of the human fibroblast collagenase precursor depends on an internal cysteine residue. / Engler, J. A.; Windsor, L.; Birkedal-Hansen, B.; Birkedal-Hansen, H.

In: Matrix (Stuttgart, Germany). Supplement, Vol. 1, 1992, p. 231-236.

Research output: Contribution to journalArticle

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