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|
|Copyright:||© 2007, Lippincott Williams & Wilkins|
|Review Status:||not specified|
|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|
|Communicated by:||Martin Vingron|
|Affiliations:||MPI für molekulare Genetik|
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