Cited by 676Nitric Oxide and Endothelin EffectsRenin-Angiotensin System StudiesRedox biology and oxidative stress

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Effects of Angiotensin II Infusion on the Expression and Function of NAD(P)H Oxidase and Components of Nitric Oxide/cGMP Signaling

Mollnau, Hanke, Wendt, Maria, Szöcs, Katalin, Lassègue, Bernard, Schulz, Eberhard, Oelze, Mathias, Li, Huige, Bodenschatz, Martin, August, Michael, Kleschyov, Andrei L., Tsilimingas, Nikolaus, Walter, Ulrich, Förstermann, Ulrich, Meinertz, Thomas, Griendling, Kathy, Münzel, Thomas·2002·Circulation Research

DOI 10.1161/01.res.0000012569.55432.02

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Abstract

Angiotensin II infusion causes endothelial dysfunction by increasing NAD(P)H oxidase-mediated vascular superoxide production. However, it remains to be elucidated how in vivo angiotensin II treatment may alter the expression of the gp91 phox isoforms and the endothelial nitric oxide synthase (NOS III) and subsequent signaling events and whether, in addition to the NAD(P)H oxidase, NOS III contributes to vascular superoxide formation. We therefore studied the influence of in vivo angiotensin II treatment (7 days) in rats on endothelial function and on the expression of the NAD(P)H oxidase subunits p22 phox , nox1, nox4, and gp91 phox and NOS III. Further analysis included the expression of NO-downstream targets, the soluble guanylyl cyclase (sGC), the cGMP-dependent protein kinase I (cGK-I), and the expression and phosphorylation of the vasodilator-stimulated phosphoprotein (VASP) at Ser239 (P-VASP). Angiotensin II caused endothelial dysfunction and increased vascular superoxide. Likewise, we found an increase in vascular protein kinase C (PKC) activity, in the expression of nox1 (6- to 7-fold), gp91 phox (3-fold), p22 phox (3-fold), NOS III mRNA, and protein. NOS-inhibition with N G -nitro- l -arginine decreased superoxide in vessels from angiotensin II-treated animals, compatible with NOS-uncoupling. Vascular NO assessed with electron paramagnetic resonance was markedly reduced. Likewise, a decrease in sGC-expression and P-VASP levels was found. In vivo PKC-inhibition with chelerythrine reduced angiotensin II-induced superoxide production and markedly inhibited upregulation of NAD(P)H oxidase subunits. We therefore conclude that angiotensin II-induced increases in the activity and the expression of NAD(P)H oxidase are at least in part PKC-dependent. NADPH oxidase-induced superoxide production may trigger NOS III uncoupling, leading to impaired NO/cGMP signaling and to endothelial dysfunction in this animal model. The full text of this article is available at http://www.circresaha.org.

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Authors: Mollnau, H., Wendt, M., Szöcs, K., Lassègue, B., Schulz, E., Oelze, M., Li, H., Bodenschatz, M., August, M., Kleschyov, A. L., Tsilimingas, N., Walter, U., Förstermann, U., Meinertz, T., Griendling, K., & Münzel, T.
Affiliations: Emory University (US)
From the Division of Cardiology (H.M., M.W., E.S., M.O., M.B., M.A., A.L.K., T. Meinertz., T. Münzel) and Cardiovascular Surgery (N.T.), University Hospital Eppendorf, Hamburg, Germany; the Department of Clinical Biochemistry and Pathobiochemistry (U.W.), University of Würzburg, Germany; the Department of Pharmacology (H.L., U.F.), Johannes Gutenberg University, Mainz, Germany; and the Department of Cardiology (K.S., B.L., K.G.), Emory University, Atlanta, Ga.
ORCID: Wendt, Maria
Schulz, Eberhard
Li, Huige
Kleschyov, Andrei L.
Walter, Ulrich
Griendling, Kathy
Venue: Circulation Research
Publisher: Ovid Technologies (Wolters Kluwer Health)
Published: 2002-03-08
Volume: 90
Issue: 4
Pages: E58-65
ISSN: 0009-7330 (ISSN-L)
1524-4571
DOI: 10.1161/01.res.0000012569.55432.02
OpenAlex: W2114547396
Cited by: 676
References: 35
Citations by year: 2026: 5 · 2025: 4 · 2024: 9 · 2023: 15 · 2022: 10 · 2021: 13 · 2020: 20 · 2019: 14 · 2018: 15 · 2017: 24 · 2016: 21 · 2015: 29 · 2014: 26 · 2013: 25 · 2012: 38
FWCI: 32.37
Type: journal article
Language: en
Open access: closed
Locations: Circulation Research (publishedVersion)
PubMed (publishedVersion)
Funders: Deutsche Forschungsgemeinschaft
Topics: Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Renin-Angiotensin System Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: angiotensin II, NADPH oxidase, endothelial dysfunction, nitric oxide synthase uncoupling, nitric oxide/cGMP signaling, superoxide production, gp91phox, NOX1, NOX4, p22phox, soluble guanylate cyclase, cGMP-dependent protein kinase I, VASP phosphorylation, protein kinase C, chelerythrine, L-NNA
MeSH terms: Soluble Guanylyl Cyclase, NADPH Oxidase 1, NADPH Oxidase 2, NADPH Oxidase 4, Vasodilator-Stimulated Phosphoprotein, Angiotensin II, Animals, Aorta, Blood Pressure, Disease Models, Animal, Enzyme Activation, Cyclic GMP, Guanylate Cyclase, Infusions, Parenteral, Membrane Glycoproteins, Microfilament Proteins, NAD, NADH, NADPH Oxidoreductases, NADP, NADPH Dehydrogenase, Nitric Oxide, Phosphoproteins, Protein Kinase C, Superoxides, Vasodilation, Vasodilator Agents, Signal Transduction, Cell Adhesion Molecules, Rats, Wistar, Cyclic GMP-Dependent Protein Kinases, Receptors, Cytoplasmic and Nuclear, Nitric Oxide Synthase, NADPH Oxidases, Membrane Transport Proteins, Rats, Nitric Oxide Synthase Type III, Cyclic GMP-Dependent Protein Kinase Type I, In Vitro Techniques

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Effects of Angiotensin II Infusion on the Expression and Function of NAD(P)H Oxidase and Components of Nitric Oxide/cGMP Signaling

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