Source:http://linkedlifedata.com/resource/pubmed/id/21319188
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2011-3-4
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pubmed:abstractText |
Peroxiredoxins (Prxs) are peroxidases that catalyze the reduction of reactive oxygen species (ROS). The active site cysteine residue of members of the 2-Cys Prx subgroup (Prx I to IV) of Prxs is hyperoxidized to cysteine sulfinic acid (Cys-SO(2) ) during catalysis with concomitant loss of peroxidase activity. Reactivation of the hyperoxidized Prx is catalyzed by sulfiredoxin (Srx). Ethanol consumption induces the accumulation of cytochrome P450 2E1 (CYP2E1), a major contributor to ethanol-induced ROS production in the liver. We now show that chronic ethanol feeding markedly increased the expression of Srx in the liver of mice in a largely Nrf2-dependent manner. Among Prx I to IV, only Prx I was found to be hyperoxidized in the liver of ethanol-fed wildtype mice, and the level of Prx I-SO(2) increased to ?30% to 50% of total Prx I in the liver of ethanol-fed Srx(-/-) mice. This result suggests that Prx I is the most active 2-Cys Prx in elimination of ROS from the liver of ethanol-fed mice and that, despite the up-regulation of Srx expression by ethanol, the capacity of Srx is not sufficient to counteract the hyperoxidation of Prx I that occurs during ROS reduction. A protease protection assay revealed that a large fraction of Prx I is located together with CYP2E1 at the cytosolic side of the endoplasmic reticulum membrane. The selective role of Prx I in ROS removal is thus likely attributable to the proximity of Prx I and CYP2E1. CONCLUSION: The pivotal functions of Srx and Prx I in protection of the liver in ethanol-fed mice was evident from the severe oxidative damage observed in mice lacking either Srx or Prx I.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 CYP2E1,
http://linkedlifedata.com/resource/pubmed/chemical/Ethanol,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases Acting on Sulfur...,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxiredoxin III,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxiredoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Prdx1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Prdx3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species,
http://linkedlifedata.com/resource/pubmed/chemical/sulfiredoxin protein, mouse
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1527-3350
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2010 American Association for the Study of Liver Diseases.
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pubmed:issnType |
Electronic
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pubmed:volume |
53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
945-53
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:21319188-Animals,
pubmed-meshheading:21319188-Cytochrome P-450 CYP2E1,
pubmed-meshheading:21319188-Drug-Induced Liver Injury,
pubmed-meshheading:21319188-Ethanol,
pubmed-meshheading:21319188-Male,
pubmed-meshheading:21319188-Mice,
pubmed-meshheading:21319188-Oxidation-Reduction,
pubmed-meshheading:21319188-Oxidoreductases Acting on Sulfur Group Donors,
pubmed-meshheading:21319188-Peroxiredoxin III,
pubmed-meshheading:21319188-Peroxiredoxins,
pubmed-meshheading:21319188-Reactive Oxygen Species
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pubmed:year |
2011
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pubmed:articleTitle |
Concerted action of sulfiredoxin and peroxiredoxin I protects against alcohol-induced oxidative injury in mouse liver.
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pubmed:affiliation |
Department of Life Science, Division of Life and Pharmaceutical Sciences, Ewha Womans University, Seoul, Korea. soohanbae@ewha.ac.kr
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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