Abstract
Moderate alcohol consumption has beneficial effects on endothelial nitric-oxide synthase (eNOS) activation, which can engender an array of anti-atherogenic actions. Here we show that in human aortic endothelial cells (HAECs), rapid activation of mitochondrial aldehyde dehydrogenase 2 (ALDH2) mediates ethanol-induced eNOS activation by preventing reactive oxygen species (ROS) accumulation. Furthermore, activation of ALDH2 by ethanol is due to its hyperacetylation by SIRT3 inactivation. These data suggest that ethanol-induced eNOS activation in HAECs may be dependent on ALDH2 hyperacetylation by SIRT3 inactivation.
Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylation / drug effects
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Acetyltransferases / genetics
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Acetyltransferases / metabolism
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Aldehyde Dehydrogenase / genetics
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Aldehyde Dehydrogenase / metabolism*
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Aldehyde Dehydrogenase, Mitochondrial
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Cells, Cultured
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Dose-Response Relationship, Drug
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Endothelial Cells / drug effects
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Endothelial Cells / metabolism
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Enzyme Activation / drug effects
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Enzyme Activation / genetics
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Ethanol / pharmacology*
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Gene Expression Regulation, Enzymologic / drug effects
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Humans
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Mitochondria / drug effects
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Mitochondria / enzymology
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Mitochondria / metabolism
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Nitric Oxide Synthase Type III / genetics
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Nitric Oxide Synthase Type III / metabolism*
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Protein Processing, Post-Translational / drug effects
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Protein Processing, Post-Translational / genetics
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RNA, Small Interfering / pharmacology
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Reactive Oxygen Species / metabolism
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Sirtuin 3 / genetics
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Sirtuin 3 / metabolism*
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Transfection
Substances
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RNA, Small Interfering
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Reactive Oxygen Species
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Ethanol
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NOS3 protein, human
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Nitric Oxide Synthase Type III
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ALDH2 protein, human
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Aldehyde Dehydrogenase
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Aldehyde Dehydrogenase, Mitochondrial
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Acetyltransferases
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SIRT3 protein, human
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Sirtuin 3