Thioredoxin and thioredoxin reductase: Current research with special reference to human disease

被引：458
作者：
Holmgren, Arne [1 ]
Lu, Jun [1 ]
机构：
[1] Karolinska Inst, Div Biochem, Dept Med Biochem & Biophys, SE-17177 Stockholm, Sweden
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2010年 / 396卷 / 01期
基金：
瑞典研究理事会;
关键词：
Thioredoxin; Thioredoxin reductase; Redox regulation; Thiol; Disulfide; Selenocysteine; MOLECULAR-MECHANISM; INHIBITION; EXPRESSION; CATALYSIS; OXIDATION;
D O I：
10.1016/j.bbrc.2010.03.083
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：
Thioredoxin (Trx) and thioredoxin reductase (TrxR) plus NADPH, comprising the thioredoxin system, has a large number of functions in DNA synthesis, defense against oxidative stress and apoptosis or redox signaling with reference to many diseases. All three isoenzymes of mammalian TrxR contain an essential selenocysteine residue, which is the target of several drugs in cancer treatment or mercury intoxication. The cytosolic Trx1 acting as the cells' protein disulfide reductase is itself reversibly redox regulated via three structural Cys residues. The evolution of mammalian Trx system compared to its prokaryotic counterparts may be an adaptation to the use of hydrogen peroxide and nitric oxide in redox regulation and signal transduction. (C) 2010 Elsevier Inc. All rights reserved.
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收藏
页码：120 / 124
页数：5
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