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Oxidation of thioredoxin reductase in HeLa cells stimulated with tumor necrosis factor‐α
Author(s) -
Kim Jae-Ryong,
Lee Seon-Min,
Cho Seung-Hyun,
Kim Jung-Hyun,
Kim Byung-Hak,
Kwon Jaeyul,
Choi Cheol Yong,
Kim Yeong-Dae,
Lee Seung-Rock
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.04.055
Subject(s) - thioredoxin reductase , hela , mitochondrion , apoptosis , peroxiredoxin , thioredoxin , tumor necrosis factor alpha , microbiology and biotechnology , biology , programmed cell death , chemistry , biochemistry , peroxidase , cell , oxidative stress , enzyme , immunology
Stimulation of cells with tumor necrosis factor‐α (TNF‐α) 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‐α on the redox status of selenocysteine (SeCys) residue essential for mitochondrial thioredoxin reductase (TrxR2) was investigated in HeLa cells. TNF‐α 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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