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ID: 312534.0, MPI für molekulare Genetik / Department of Computational Molecular Biology
Renal cathepsin G and angiotensin II generation
Authors:Rykl, Jana; Thiemann, Joachim; Kurzawski, Sandra; Pohl, Thomas; Gobom, Johan; Zidek, Walter; Schlüter, Hartmut
Date of Publication (YYYY-MM-DD):2006-09
Title of Journal:Journal of Hypertension (London)
Journal Abbrev.:J Hypertens
Issue / Number:9
Start Page:1797
End Page:1807
Copyright:© 2007, Lippincott Williams & Wilkins
Review Status:not specified
Audience:Experts Only
Abstract / Description:Background: Alternative pathways of angiotensin II biosynthesis play a significant role in the renin-angiotensin system. In this study porcine renal tissue was investigated for angiotensin II-generating enzymes.

Methods and results: Protein extracts from porcine renal tissue were fractionated by liquid chromatography and tested for their angiotensin II-generating activity by the mass-spectrometry-assisted enzyme screening system (MES) and the active fractions were purified to near homogeneity. In one of these active fractions, inhibitable by an angiotensin-converting enzyme specific inhibitor, purified by anion-exchange chromatography, followed by hydroxyapatite chromatography, lectin affinity chromatography, size-exclusion chromatography and two-dimensional electrophoresis, angiotensin-converting enzyme was identified by a tryptic peptide matrix-assisted-laser-desorption/ionization (MALDI) mass fingerprint analysis. In a second active fraction, which was inhibited by chymostatin and antipain, yielded by anion-exchange chromatography, followed by hydroxyapatite chromatography, lectin affinity chromatography, chymostatin-antipain chromatography and one-dimensional electrophoresis, cathepsin G was identified by electro-spray ionization (ESI)-ion-trap mass spectrometry. The angiotensin-generating activities of the fraction containing angiotensin-converting enzyme and the fraction containing cathepsin G were in the same order of magnitude, thus showing that the contribution of cathepsin G towards the production of angiotensin II is significant.

Conclusion: This is the first time that cathepsin G has been identified in mammalian renal tissue.
External Publication Status:published
Document Type:Article
Communicated by:Martin Vingron
Affiliations:MPI für molekulare Genetik
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