Oxidation of thioredoxin reductase in HeLa cells stimulated with tumor necrosis factor-α

被引：25

作者：

Kim, JR

Lee, SM

Cho, SH

Kim, JH

Kim, BH

Kwon, J

Choi, CY

Kim, YD

Lee, SR ^{[1
]}

机构：

[1] Ewha Womans Univ, Dept Biol Sci, Div Mol Life Sci, Ctr Cell Signaling Res, Seoul 120750, South Korea

[2] Yeungnam Univ, Coll Med, Taejon 705717, South Korea

[3] Natl Heart Lung & Blood Inst, Lab Cell Signaling, NIH, Bethesda, MD 20892 USA

[4] Sungkyunkwan Univ, Dept Biol Sci, Suwon 440746, South Korea

[5] Pusan Natl Univ, Dept Thorac & Cardiovasc Surg, Pusan 602739, South Korea

来源：

FEBS LETTERS | 2004年 / 567卷 / 2-3期

基金：

新加坡国家研究基金会;

关键词：

thioredoxin reductase; selenocysteine; reactive oxygen species; apoptosis;

D O I：

10.1016/j.febslet.2004.04.055

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Stimulation of cells with tumor necrosis factor-alpha (TNF-alpha) results in the increase in generation of H2O2 in mitochondria that leads to apoptosis. The effect of H2O2 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 H2O2 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 H2O2 in mitochondria. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：189 / 196

页数：8

共 54 条

[1] Rapid induction of cell death by selenium-compromised thioredoxin reductase 1 but not by the fully active enzyme containing selenocysteine [J].