1
40
2
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Text
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URL Address
<a href="http://doi.org/10.1016/j.freeradbiomed.2013.02.018" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.freeradbiomed.2013.02.018</a>
Rights
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
211-222
Volume
60
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Dublin Core
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Title
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Robust protein nitration contributes to acetaminophen-induced mitochondrial dysfunction and acute liver injury
Publisher
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Free Radical Biology and Medicine
Date
A point or period of time associated with an event in the lifecycle of the resource
2013
2013-07
Subject
The topic of the resource
3-Nitrotyrosine; Acetaminophen; Acute liver injury; Biochemistry & Molecular Biology; covalent binding; CYP2E1; Endocrinology & Metabolism; Free radicals; immunohistochemical localization; induced hepatotoxicity; knockout mice; Mitochondrial dysfunction; mouse-liver; n-acetylcysteine; n-acetylcysteine; nitration; nitric-oxide synthase; oxidative stress; protein; superoxide-dismutase; terminal kinase
Creator
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Abdelmegeed M A; Jang S; Banerjee A; Hardwick J P; Song B J
Description
An account of the resource
Acetaminophen (APAP), a widely used analgesic/antipyretic agent, can cause liver injury through increased nitrative stress, leading to protein nitration. However, the identities of nitrated proteins and their roles in hepatotoxicity are poorly understood. Thus, we aimed at studying the mechanism of APAP-induced hepatotoxicity by systematic identification and characterization of nitrated proteins in the absence or presence of an antioxidant, N-acetylcysteine (NAC). The levels of nitrated proteins markedly increased at 2 h in mice exposed to a single APAP dose (350 mg/kg ip), which caused severe liver necrosis at 24 h. Protein nitration and liver necrosis were minimal in mice exposed to nontoxic 3-hydroxyacetanilide or animals co-treated with APAP and NAC. Mass-spectral analysis of the affinity-purified nitrated proteins identified numerous mitochondrial and cytosolic proteins, including mitochondrial aldehyde dehydrogenase, Mn-superoxide dismutase, glutathione peroxidase, ATP synthase, and 3-ketoacyl-CoA thiolase, involved in antioxidant defense, energy supply, or fatty acid metabolism. Immunoprecipitation followed by immunoblot with anti-3-nitrotyrosine antibody confirmed that the aforementioned proteins were nitrated in APAP-exposed mice but not in NAC-cotreated mice. Consistently, NAC cotreatment significantly restored the suppressed activity of these enzymes. Thus, we demonstrate a new mechanism by which many nitrated proteins with concomitantly suppressed activity promotes APAP-induced mitochondrial dysfunction and hepatotoxicity. Published by Elsevier Inc.
Identifier
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<a href="http://doi.org/10.1016/j.freeradbiomed.2013.02.018" target="_blank" rel="noreferrer noopener">10.1016/j.freeradbiomed.2013.02.018</a>
Format
The file format, physical medium, or dimensions of the resource
Journal Article or Conference Abstract Publication
2013
3-Nitrotyrosine
Abdelmegeed M A
ACETAMINOPHEN
Acute liver injury
Banerjee A
Biochemistry & Molecular Biology
covalent binding
CYP2E1
Endocrinology & Metabolism
Free Radical Biology and Medicine
Free radicals
Hardwick J P
immunohistochemical localization
induced hepatotoxicity
Jang S
Journal Article or Conference Abstract Publication
knockout mice
Mitochondrial dysfunction
mouse-liver
n-acetylcysteine
nitration
nitric-oxide synthase
Oxidative Stress
Protein
Song B J
superoxide-dismutase
terminal kinase
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1002/hep.21372" target="_blank" rel="noreferrer noopener">http://doi.org/10.1002/hep.21372</a>
Rights
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
1218-1230
Issue
5
Volume
44
Search for Full-text
Locate full-text within NEOMED Library's e-journal collections
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The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Inactivation of oxidized and S-nitrosylated mitochondrial proteins in alcoholic fatty liver of rats
Publisher
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Hepatology
Date
A point or period of time associated with an event in the lifecycle of the resource
2006
2006-11
Subject
The topic of the resource
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
An entity primarily responsible for making the resource
Moon K H; Hood B L; Kim B J; Hardwick J P; Conrads T P; Veenstra T D; Song B Y J
Description
An account of the resource
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
The file format, physical medium, or dimensions of the resource
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