Characterization of prorenin activation using a synthetic peptide substrate.

Journal Article (Journal Article)

Human renin is synthesized as an inactive zymogen (prorenin) which is processed to the active form. We synthesized an 11-amino acid peptide which spans the human prorenin processing site in order to develop a simple assay to study human prorenin activation. Six enzymes which are capable of activating recombinant prorenin in vitro were studied. Four of these enzymes digested the synthetic peptide in a specific fashion, as analyzed by reverse-phase high-performance liquid chromatography. Amino acid analysis of the purified digestion products revealed that trypsin cleaves between Arg-Leu, the authentic processing site, while kallikrein, plasmin and elastase all cleaved at alternate sites. On the other hand, pepsin and cathepsin D did not cleave this substrate, suggesting that the activation of prorenin by these proteases might occur at a site distinct from the authentic processing site. Our data suggest that this synthetic peptide may be used as a simple and specific assay for prorenin activation.

Full Text

Duke Authors

Cited Authors

  • Dubin, D; Pratt, RE; Hui, KY; Dzau, VJ

Published Date

  • June 1991

Published In

Volume / Issue

  • 9 / 6

Start / End Page

  • 483 - 486

PubMed ID

  • 1653285

International Standard Serial Number (ISSN)

  • 0263-6352

Digital Object Identifier (DOI)

  • 10.1097/00004872-199106000-00001


  • eng

Conference Location

  • England