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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1984 Jun;81(11):3302–3306. doi: 10.1073/pnas.81.11.3302

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

D L Helseth Jr, A Veis
PMCID: PMC345495  PMID: 6587351

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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