AMPKα2 Deletion Causes Aberrant Expression and Activation of NAD(P)H Oxidase and Consequent Endothelial Dysfunction In Vivo: Role of 26S Proteasomes

Wang, Shuangxi; Zhang, Miao; Liang, Bin; Xu, Jian; Xie, Zhonglin; Liu, Chao; Viollet, Benoit; Yan, Daoguang; Zou, Ming-Hui

doi:10.1161/circresaha.109.212530

Cited by 296Nitric Oxide and Endothelin EffectsRedox biology and oxidative stressNeutrophil, Myeloperoxidase and Oxidative Mechanisms

AMPKα2 Deletion Causes Aberrant Expression and Activation of NAD(P)H Oxidase and Consequent Endothelial Dysfunction In Vivo: Role of 26S Proteasomes

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Wang, Shuangxi, Zhang, Miao, Liang, Bin, Xu, Jian, Xie, Zhonglin, Liu, Chao, Viollet, Benoit, Yan, Daoguang +1 more·2010·Circulation Research

DOI 10.1161/circresaha.109.212530PMC PMC2920052

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Abstract

RATIONALE: AMP-activated protein kinase (AMPK) is an energy sensor and ubiquitously expressed in vascular cells. Recent studies suggest that AMPK activation improves endothelial function by counteracting oxidative stress in endothelial cells. How AMPK suppresses oxidative stress remains to be established. OBJECTIVE: The aim of this study is to examine the effects of AMPK in regulating NAD(P)H oxidase, oxidative stress, and endothelial function. METHODS AND RESULTS: The markers of oxidative stress, NAD(P)H oxidase subunit expression (gp91(phox), p47(phox), p67(phox), NOX1 to -4), NAD(P)H oxidase-mediated superoxide production, 26S proteasome activity, IkappaBalpha degradation, and nuclear translocation of nuclear factor (NF)-kappaB (p50 and p65) were examined in cultured human umbilical vein endothelial cells and mouse aortas isolated from AMPKalpha2 deficient mice. Compared to the wild type, acetylcholine-induced endothelium-dependent relaxation was significantly impaired in parallel with increased production of oxidants in AMPKalpha2(-/-) mice. Further, pretreatment of aorta with either superoxide dismutase (SOD) or tempol or apocynin significantly improved acetylcholine-induced endothelium-dependent relaxation in AMPKalpha2(-/-) mice. Analysis of aortic endothelial cells from AMPKalpha2(-/-) mice and human umbilical vein endothelial cells expressing dominant negative AMPK or AMPKalpha2-specific siRNA revealed that loss of AMPK activity increased NAD(P)H oxidase subunit expression (gp91(phox), p47(phox), p67(phox), NOX1 and -4), NAD(P)H oxidase-mediated superoxide production, 26S proteasome activity, IkappaBalpha degradation, and nuclear translocation of NF-kappaB (p50 and p65), whereas AMPK activation by AICAR or overexpression of constitutively active AMPK had the opposite effect. Consistently, we found that genetic deletion of AMPKalpha2 in low-density lipoprotein receptor knockout (LDLr(-/-)) strain markedly increased 26S proteasome activity, IkappaB degradation, NF-kappaB transactivation, NAD(P)H oxidase subunit overexpression, oxidative stress, and endothelial dysfunction, all of which were largely suppressed by chronic administration of MG132, a potent cell permeable proteasome inhibitor. CONCLUSIONS: We conclude that AMPKalpha2 functions as a physiological suppressor of NAD(P)H oxidase and ROS production in endothelial cells. In this way, AMPK maintains the nonatherogenic and noninflammatory phenotype of endothelial cells.

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AMPK negatively regulates NOX by reducing its phosphorylation and preventing P47phox's translocation to membrane.
“Additional evidence supporting AMPK protection against oxidative stress is that AMPK negatively regulates NOX by reducing its phosphorylation and preventing P47phox’s translocation to membrane [70,151].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [70]

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Abstract 1149: Endothelial Dysfunction in AMP-activated Kinase {alpha}2 Knockout Mice: Role of NAD(P)H oxidase-derived Superoxide Anions
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Abstract 18473: Oxidative Stress Improves Coronary Endothelial Function Through Activation of the Pro-Survival Kinase AMPK
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1AMP-Activated Protein Kinase Preserves Endothelial Function During Chronic Angiotensin II Treatment by Limiting
Upregulation, N., Schuhmacher, S., Foretz, M., Knorr, M., Jansen, T., Hortmann, M., Wenzel, P., Oelze, M., Kleschyov, A. L., Daiber, A., et al. (2016)

Authors: Wang, S., Zhang, M., Liang, B., Xu, J., Xie, Z., Liu, C., Viollet, B., Yan, D., & Zou, M.-H.
Affiliations: Centre National de la Recherche Scientifique (FR)
From the Section of Endocrinology and Diabetes (S.W., M.Z., B.L., J.X., Z.X., C.L., D.Y., M.-H.Z.), Department of Medicine, University of Oklahoma Health Sciences Center, Oklahoma City; Institut Cochin (B.V.), Centre National de la Recherche Scientifique (Unité Mixte de Recherche 8104), University Paris Descartes, Paris, France; Institut National de la Santé et de la Recherche Médicale (B.V.), U1016, Paris, France; and College of Life Science (B.V.), Jinan University, Guangzhou, China.
ORCID: Wang, Shuangxi
Zhang, Miao
Xu, Jian
Liu, Chao
Zou, Ming-Hui
Venue: Circulation Research
Publisher: Ovid Technologies (Wolters Kluwer Health)
Published: 2010-04-02
Volume: 106
Issue: 6
Pages: 1117-1128
ISSN: 0009-7330 (ISSN-L)
1524-4571
DOI: 10.1161/circresaha.109.212530
PMC: PMC2920052
OpenAlex: W1964266642
Cited by: 296
References: 41
Citations by year: 2026: 4 · 2025: 3 · 2024: 9 · 2023: 12 · 2022: 8 · 2021: 13 · 2020: 24 · 2019: 18 · 2018: 26 · 2017: 28 · 2016: 34 · 2015: 27 · 2014: 26 · 2013: 20 · 2012: 20
FWCI: 13.63
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Circulation Research (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Heart, Lung, and Blood Institute (R01HL105157, HL 079584, R01HL079584, HL-080499, HL096032, HL074399, R01HL074399, R01HL080499, HL-089920, R01HL110488, R01HL089920, R01HL096032)
Topics: Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Keywords: AMPKα2, AMPK, NADPH oxidase, endothelial dysfunction, oxidative stress, NF-κB signaling, 26S proteasome, superoxide production, NOX1, NOX4, LDL receptor, atherosclerosis, acetylcholine-induced relaxation, AICAR, tempol, apocynin, superoxide dismutase, p47phox, p67phox, gp91phox, LDL oxidation
MeSH terms: NF-KappaB Inhibitor alpha, Acetophenones, Acetylcholine, Aminoimidazole Carboxamide, Animals, Antioxidants, Cells, Cultured, Cyclic N-Oxides, Dose-Response Relationship, Drug, Endothelium, Vascular, Enzyme Activation, Enzyme Inhibitors, Humans, Interferon-gamma, Interleukin-2, Isoenzymes, Leupeptins, Male, Mice, Inbred C57BL, Nitroprusside, Receptors, LDL, Ribonucleotides, Spin Labels, Superoxides, Superoxide Dismutase, Transfection, Vasodilation, Vasodilator Agents, Gene Expression Regulation, Enzymologic, NF-kappa B, Gene Deletion, Mice, Knockout, Oxidative Stress, Inflammation Mediators, NADPH Oxidases, I-kappa B Proteins, RNA Interference, Endothelial Cells, Proteasome Endopeptidase Complex, Mice, AMP-Activated Protein Kinases, Proteasome Inhibitors

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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 ›

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AMPKα2 Deletion Causes Aberrant Expression and Activation of NAD(P)H Oxidase and Consequent Endothelial Dysfunction In Vivo: Role of 26S Proteasomes

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