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  Renal cathepsin G and angiotensin II generation

Rykl, J., Thiemann, J., Kurzawski, S., Pohl, T., Gobom, J., Zidek, W., et al. (2006). Renal cathepsin G and angiotensin II generation. Journal of Hypertension (London), 24(9), 1797-1807.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-83BB-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-83BC-F
Genre: Journal Article
Alternative Title : J Hypertens

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 Creators:
Rykl, Jana, Author
Thiemann, Joachim, Author
Kurzawski, Sandra, Author
Pohl, Thomas, Author
Gobom, Johan1, Author              
Zidek, Walter, Author
Schlüter, Hartmut, Author
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2006-09
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: eDoc: 312534
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Title: Journal of Hypertension (London)
  Alternative Title : J Hypertens
Source Genre: Journal
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Pages: - Volume / Issue: 24 (9) Sequence Number: - Start / End Page: 1797 - 1807 Identifier: ISSN: 0263-6352