Expression of a Functionally Active gp91phox-Containing Neutrophil-Type NAD(P)H Oxidase in Smooth Muscle Cells From Human Resistance Arteries: Regulation by Angiotensin II
Abstract
A major source of vascular smooth muscle cell (VSMC) superoxide is NAD(P)H oxidase. However, the molecular characteristics and regulation of this enzyme are unclear. We investigated whether VSMCs from human resistance arteries (HVSMCs) possess a functionally active, angiotensin II (Ang II)–regulated NAD(P)H oxidase that contains neutrophil oxidase subunits, including p22phox, gp91phox, p40phox, p47phox, and p67phox. mRNA expression of gp91phox homologues, nox1 and nox4, was also assessed in HVSMCs, human aortic smooth muscle cells, and rat VSMCs. HVSMCs were obtained from resistance arteries from gluteal biopsies of healthy subjects. gp91phox and nox4, but not nox1, were detected in HVSMCs. Nox1 and nox4, but not gp91phox, were expressed in human aortic smooth muscle cells and rat VSMCs. All NAD(P)H oxidase subunits were present in HVSMCs as detected by reverse transcriptase–polymerase chain reaction and immunoblotting. Ang II increased NAD(P)H oxidase subunit abundance. These effects were inhibited by cycloheximide. Acute Ang II stimulation (10 to 15 minutes) increased p47phox serine phosphorylation and induced p47phox and p67phox translocation. This was associated with NAD(P)H oxidase activation. In cells transfected with gp91phox antisense oligonucleotides, Ang II–mediated actions were abrogated. NADPH-induced superoxide generation was reduced by gp91ds-tat and apocynin, inhibitors of p47phox-gp91phox interactions. Our results suggest that HVSMCs possess a functionally active gp91phox-containing neutrophil-like NAD(P)H oxidase. Ang II regulates the enzyme by inducing phosphorylation of p47phox, translocation of cytosolic subunits, and de novo protein synthesis. These novel findings provide insight into the molecular regulation of NAD(P)H oxidase by Ang II in HVSMCs. Furthermore, we identify differences in gp91phox homologue expression in VSMCs from rats and human small and large arteries.
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Mitochondrial ROS are required for the differentiation of some hematopoietic stem cells and human mesenchymal stem cells.
“On a cellular level, mitochondrial ROS have also been shown to be required for the differentiation of some hematopoietic stem cells as well as human mesenchymal stem cells (707, 948).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [948]
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- Authors
- Touyz, R. M., Chen, X., Tabet, F., Yao, G., He, G., Quinn, M. T., Pagano, P. J., & Schiffrin, E. L.
- Affiliations
- Montana State University (US)
- Venue
- Circulation Research
- Published
- 2002-06-14
- Volume
- 90
- Issue
- 11
- Pages
- 1205-1213
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- OpenAlex
- W2132039169
- Cited by
- 590
- References
- 42
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 3 · 2023: 10 · 2022: 15 · 2021: 11 · 2020: 11 · 2019: 12 · 2018: 7 · 2017: 14 · 2016: 17 · 2015: 24 · 2014: 30 · 2013: 35 · 2012: 43
- FWCI
- 25.91
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Circulation Research (publishedVersion)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- Funders
- National Institutes of Health
- Canadian Institutes of Health Research
- Fonds de Recherche du Québec - Santé
- National Heart, Lung, and Blood Institute (HL66575, R01HL066575, R01HL055425)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- NADPH oxidase, gp91phox, vascular smooth muscle cells, resistance arteries, angiotensin II, p47phox phosphorylation, p47phox translocation, p67phox, NOX4, NOX1, superoxide production, apocynin, human aortic smooth muscle cells
- MeSH terms
- NADPH Oxidase 2, Adult, Angiotensin II, Animals, Arteries, Biological Transport, Enzyme Activation, Female, Humans, Male, Membrane Glycoproteins, Microscopy, Fluorescence, Middle Aged, Muscle, Smooth, Vascular, NADH, NADPH Oxidoreductases, NADPH Dehydrogenase, Neutrophils, Phosphoproteins, Phosphorylation, Rats, Inbred WKY, RNA, Messenger, Serine, Tumor Cells, Cultured, Vascular Resistance, Reactive Oxygen Species, Microscopy, Confocal, NADPH Oxidases, Reverse Transcriptase Polymerase Chain Reaction, Membrane Transport Proteins, Rats
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