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Text
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URL Address
<a href="http://doi.org/10.1002/hep.21372" target="_blank" rel="noreferrer noopener">http://doi.org/10.1002/hep.21372</a>
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Pages
1218-1230
Issue
5
Volume
44
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Title
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Inactivation of oxidized and S-nitrosylated mitochondrial proteins in alcoholic fatty liver of rats
Publisher
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Hepatology
Date
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2006
2006-11
Subject
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oxidative stress; nitric-oxide; Gastroenterology & Hepatology; activated receptor-alpha; mouse-liver; Aldehyde dehydrogenase; cytochrome-p450 cyp2e1; dependent hepatotoxicity; ethanol-consumption; hepatic mitochondria; nitrosative stress
Creator
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Moon K H; Hood B L; Kim B J; Hardwick J P; Conrads T P; Veenstra T D; Song B Y J
Description
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Increased oxidative/nitrosative stress is a major contributing factor to alcohol-mediated mitochondrial dysfunction. However, which mitochondrial proteins are oxidatively modified under alcohol-induced oxidative/nitrosative stress is poorly understood. The aim of this study was to systematically investigate oxidized and/or S-nitrosylated mitochondrial proteins and to use a biotin-N-maleimide probe to evaluate their inactivation in alcoholic fatty livers of rats. Binge or chronic alcohol exposure significantly elevated nitric oxide, inducible nitric oxide synthase, and ethanol-inducible CYP21. The biotin-N-maleimide-labeled oxidized and/or S-nitrosylated mitochondrial proteins from pair-fed controls or alcohol-fed rat livers were subsequently purified with streptavidin-agarose. The overall patterns of oxidized and/or S-nitrosylated proteins resolved by 2-dimensional polyacrylamide gel electrophoresis were very similar in the chronic and binge alcohol treatment groups. Seventy-nine proteins that displayed differential spot intensities from those of control rats were identified by mass spectrometry. These include mitochondrial aldehyde dehydrogenase 2 (ALDH2), ATP synthase, acyl-CoA dehydrogenase, 3-ketoacyl-CoA thiolase, and many proteins involved in chaperone activity, mitochondrial electron transfer, and ion transport. The activity of 3-ketoacyl-CoA thiolase involved in mitochondrial beta-oxidation of fatty acids was significantly inhibited in alcohol-exposed rat livers, consistent with hepatic fat accumulation, as determined by biochemical and histological analyses. Measurement of activity and immunoblot results showed that ALDH2 and ATP synthase were also inhibited through oxidative modification of their cysteine or tyrosine residues in alcoholic fatty livers of rats. (In conclusion) under bar our results help to explain the underlying mechanism for mitochondrial dysfunction and increased susceptibility to alcohol-mediated liver damage.
Identifier
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<a href="http://doi.org/10.1002/hep.21372" target="_blank" rel="noreferrer noopener">10.1002/hep.21372</a>
Format
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Journal Article or Conference Abstract Publication
2006
activated receptor-alpha
Aldehyde Dehydrogenase
Conrads T P
cytochrome-p450 cyp2e1
dependent hepatotoxicity
ethanol-consumption
Gastroenterology & Hepatology
Hardwick J P
hepatic mitochondria
Hepatology
Hood B L
Journal Article or Conference Abstract Publication
Kim B J
Moon K H
mouse-liver
nitric-oxide
nitrosative stress
Oxidative Stress
Song B Y J
Veenstra T D