The dual functions of thiol-based peroxidases in H2O2 scavenging and signaling

被引:126
作者
Fourquet, Simon [1 ]
Huang, Meng-Er [2 ]
D'Autreaux, Benoit [1 ]
Toledano, Michel B. [1 ]
机构
[1] CEA Saclay, DSV, IBITECS, Lab Stress Oxydants & Canc,CEA, F-91191 Gif Sur Yvette, France
[2] Ctr Univ Orsay, Inst Curie, CNRS, UMR2027, F-91405 Orsay, France
关键词
D O I
10.1089/ars.2008.2049
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
Thiol-based peroxidases consist of the peroxiredoxins (Prx) and the related glutathione peroxidase (GPx)-like enzymes. Their catalytic function is to reduce peroxides by using the reactivity of the cysteine residue, and their presumed primary physiologic role is to protect living organisms from peroxide toxicity. However, as peroxide-metabolizing enzymes, they also regulate hydrogen peroxide (H2O2) signaling. We review here enzymatic and biochemical attributes of thiol peroxidases that specify both distinctive peroxide-scavenging functions and the property of regulating H2O2 signaling. We then discuss possible thiol peroxidase physiologic functions, based on selected observations made in microorganisms and mammals.
引用
收藏
页码:1565 / 1575
页数:11
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