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

The DOI matches its Crossref record; 34 of the 35 references it cites were found in a registry or an index.

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
Open this paper in CoChat — free account

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.

Overview

Integrity signals

Registry

Crossref · 10.1161/01.res.0000012569.55432.02

Cites

34 of 34 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Show all 35 references

Research works printed but not linked: 16

  1. 10.1161/res.74.6.8187280 · DOI
  2. 10.1161/res.80.1.45 · DOI
  3. 10.1161/hyp.32.2.331 · DOI
  4. 10.1161/res.87.1.26 · DOI
  5. 10.1161/res.88.9.888 · DOI
  6. 10.1161/res.87.11.999 · DOI
  7. 10.1161/res.88.2.e14 · DOI
  8. 10.1161/circ.96.3.984 · DOI
  9. 10.1161/res.86.1.e7 · DOI
  10. 10.1161/circ.103.17.2188 · DOI
  11. 10.1016/0003-2697(87)90021-2 · DOI
  12. 10.1161/res.86.3.347 · DOI
  13. 10.1161/res.77.3.510 · DOI
  14. 10.1161/circ.103.9.1282 · DOI
  15. Abel K, Lingnau A, Niebuhr K, Wehland J, Walter U. Monoclonal antibodies against the focal adhesion protein VASP revealing epitopes involved in the interaction with two VASP binding proteins and VASP phosphorylation. Eur J Cell Biol. 1996; 69 (suppl 42): 39a.Abstract.
  16. 10.1161/res.85.6.534 · DOI

Cited by

Sorted by citations

Items 501–600 of 669

Related

See all

Metadata

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
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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review