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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2-3
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pubmed:dateCreated |
2004-6-4
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pubmed:abstractText |
Stimulation of cells with tumor necrosis factor-alpha (TNF-alpha) results in the increase in generation of H(2)O(2) in mitochondria that leads to apoptosis. The effect of H(2)O(2) produced by TNF-alpha on the redox status of selenocysteine (SeCys) residue essential for mitochondrial thioredoxin reductase (TrxR2) was investigated in HeLa cells. TNF-alpha caused accumulation of oxidized TrxR2 with a thioselenide bond. The conditional induction of SeCys-deficient TrxR2 resulted in the increased production of H(2)O(2) and apoptosis. These results suggest that the SeCys residue of TrxR2 plays a critical role in cell survival by serving as an electron donor for Trx-II and subsequent peroxiredoxin-III, which is a primary line of defense against H(2)O(2) in mitochondria.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/NADP,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Selenocysteine,
http://linkedlifedata.com/resource/pubmed/chemical/TXNRD1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/TXNRD2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Thioredoxin Reductase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Thioredoxin Reductase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Thioredoxin-Disulfide Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Txnrd1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Txnrd2 protein, rat
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
567
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
189-96
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:15178321-Animals,
pubmed-meshheading:15178321-Apoptosis,
pubmed-meshheading:15178321-Cysteine,
pubmed-meshheading:15178321-Cytoplasm,
pubmed-meshheading:15178321-DNA Fragmentation,
pubmed-meshheading:15178321-Disulfides,
pubmed-meshheading:15178321-Genes, Dominant,
pubmed-meshheading:15178321-HeLa Cells,
pubmed-meshheading:15178321-Humans,
pubmed-meshheading:15178321-Hydrogen Peroxide,
pubmed-meshheading:15178321-Mitochondria, Liver,
pubmed-meshheading:15178321-Mutation,
pubmed-meshheading:15178321-NADP,
pubmed-meshheading:15178321-Oxidation-Reduction,
pubmed-meshheading:15178321-Rats,
pubmed-meshheading:15178321-Recombinant Proteins,
pubmed-meshheading:15178321-Selenocysteine,
pubmed-meshheading:15178321-Thioredoxin Reductase 1,
pubmed-meshheading:15178321-Thioredoxin Reductase 2,
pubmed-meshheading:15178321-Thioredoxin-Disulfide Reductase,
pubmed-meshheading:15178321-Tumor Necrosis Factor-alpha
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pubmed:year |
2004
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pubmed:articleTitle |
Oxidation of thioredoxin reductase in HeLa cells stimulated with tumor necrosis factor-alpha.
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pubmed:affiliation |
Biochemistry and Molecular Biology, College of Medicine, Yeungnam University, Daegu 705-717, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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