Cathepsin D-mediated processing of procollagen: Lysosomal enzyme involvement in secretory processing of procollagen

D. L. Helseth, A. Veis

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40 Scopus citations

Abstract

The proteolytic removal of the extension COOH-terminal propeptide from procollagen has been examined in vitro. A crude enzyme activity was identified in a whole-chicken-embryo extract that acted at acid pH and appeared to be similar to one identified previously [Davidson, J.M., McEneany, L.S.G. & Bornstein, P. (1979) Eur J. Biochem. 100, 551-558]. This activity was inhibitable by pepstatin but not by leupeptin, suggesting that it might be cathepsin D. Cathepsin D was purified 907-fold from chicken livers by affinity chromatography on pepstatin-aminohexyl-Sepharose 4B and was found to remove the COOH propeptides from procollagen. At pH 6.0, the site of cleavage appeared to shift from the COOH telopeptide to the COOH telopeptide/propeptide junction, based upon the difference in electrophoretic migration of the cleavage products, although determining the actual cleavage site will require end-group analysis. A model for the involvement of cathepsin D in the in vivo processing of procollagen is presented.

Original languageEnglish (US)
Pages (from-to)3302-3306
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume81
Issue number11 I
DOIs
StatePublished - Jan 1 1984

ASJC Scopus subject areas

  • General

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