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Renal cathepsin G and angiotensin II generation

Standard

Renal cathepsin G and angiotensin II generation. / Rykl, Jana; Thiemann, Joachim; Kurzawski, Sandra; Pohl, Thomas; Gobom, Johan; Zidek, Walter; Schlüter, Hartmut.

in: J HYPERTENS, Jahrgang 24, Nr. 9, 09.2006, S. 1797-807.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Rykl, J, Thiemann, J, Kurzawski, S, Pohl, T, Gobom, J, Zidek, W & Schlüter, H 2006, 'Renal cathepsin G and angiotensin II generation', J HYPERTENS, Jg. 24, Nr. 9, S. 1797-807. https://doi.org/10.1097/01.hjh.0000242404.91332.be

APA

Rykl, J., Thiemann, J., Kurzawski, S., Pohl, T., Gobom, J., Zidek, W., & Schlüter, H. (2006). Renal cathepsin G and angiotensin II generation. J HYPERTENS, 24(9), 1797-807. https://doi.org/10.1097/01.hjh.0000242404.91332.be

Vancouver

Rykl J, Thiemann J, Kurzawski S, Pohl T, Gobom J, Zidek W et al. Renal cathepsin G and angiotensin II generation. J HYPERTENS. 2006 Sep;24(9):1797-807. https://doi.org/10.1097/01.hjh.0000242404.91332.be

Bibtex

@article{47fb09a44dff4a52b74c1d7f3b71dad0,
title = "Renal cathepsin G and angiotensin II generation",
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.",
keywords = "Angiotensin II, Animals, Anions, Cathepsin G, Cathepsins, Chromatography, Ion Exchange, Chromatography, Liquid, Durapatite, Kidney, Lectins, Mass Spectrometry, Oligopeptides, Serine Endopeptidases, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Swine, Journal Article, Research Support, Non-U.S. Gov't",
author = "Jana Rykl and Joachim Thiemann and Sandra Kurzawski and Thomas Pohl and Johan Gobom and Walter Zidek and Hartmut Schl{\"u}ter",
year = "2006",
month = sep,
doi = "10.1097/01.hjh.0000242404.91332.be",
language = "English",
volume = "24",
pages = "1797--807",
journal = "J HYPERTENS",
issn = "0263-6352",
publisher = "Lippincott Williams and Wilkins",
number = "9",

}

RIS

TY - JOUR

T1 - Renal cathepsin G and angiotensin II generation

AU - Rykl, Jana

AU - Thiemann, Joachim

AU - Kurzawski, Sandra

AU - Pohl, Thomas

AU - Gobom, Johan

AU - Zidek, Walter

AU - Schlüter, Hartmut

PY - 2006/9

Y1 - 2006/9

N2 - 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.

AB - 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.

KW - Angiotensin II

KW - Animals

KW - Anions

KW - Cathepsin G

KW - Cathepsins

KW - Chromatography, Ion Exchange

KW - Chromatography, Liquid

KW - Durapatite

KW - Kidney

KW - Lectins

KW - Mass Spectrometry

KW - Oligopeptides

KW - Serine Endopeptidases

KW - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

KW - Swine

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1097/01.hjh.0000242404.91332.be

DO - 10.1097/01.hjh.0000242404.91332.be

M3 - SCORING: Journal article

C2 - 16915029

VL - 24

SP - 1797

EP - 1807

JO - J HYPERTENS

JF - J HYPERTENS

SN - 0263-6352

IS - 9

ER -