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一氧化氮与过氧化物酶之间的相互作用。

The interplay between nitric oxide and peroxiredoxins.

作者信息

Abbas Kahina, Breton Jacques, Drapier Jean-Claude

机构信息

Institut de Chimie des Substances Naturelles, CNRS, Avenue de la Terrasse, 91, 190 Gif-sur-Yvette, France.

出版信息

Immunobiology. 2008;213(9-10):815-22. doi: 10.1016/j.imbio.2008.07.029. Epub 2008 Sep 13.

DOI:10.1016/j.imbio.2008.07.029
PMID:18926296
Abstract

Peroxiredoxins participate in the antioxidant response by reducing H(2)O(2), organic peroxides and peroxynitrite. Peroxiredoxins have a conserved NH(2)-terminal cysteine residue that is oxidized to sulfenic acid during catalysis of peroxide reduction. In eukaryotes, the sulfenic acid can be further oxidized to a sulfinic acid. Resulting inactivation of peroxiredoxins favors H(2)O(2) signaling but may eventually result in oxidative stress. Interestingly, it has recently been shown that overoxidized peroxiredoxins progressively recover activity owing to sulfiredoxin, an enzyme recently characterized in yeast and mammals. This reversible peroxide-sensitive switch represents a new type of regulation that controls reactive oxygen species-mediated cytoxicity and signaling. This report presents a brief overview of the regulation by peroxiredoxins of the messenger function of H(2)O(2) and comments on the results of recent studies that addressed the consequence of nitric oxide production on both expression and redox state of peroxiredoxins in various physiopathological processes including macrophage immunostimulation, the response of dopaminergic neurons to N-methyl-d-aspartate-stimulation and the plant hypersensitive response.

摘要

过氧化物酶通过还原过氧化氢、有机过氧化物和过氧亚硝酸根参与抗氧化反应。过氧化物酶有一个保守的氨基末端半胱氨酸残基,在过氧化物还原催化过程中被氧化成亚磺酸。在真核生物中,亚磺酸可进一步氧化成亚磺酸。由此导致的过氧化物酶失活有利于过氧化氢信号传导,但最终可能导致氧化应激。有趣的是,最近研究表明,由于硫氧还蛋白(一种最近在酵母和哺乳动物中得到鉴定的酶),过度氧化的过氧化物酶会逐渐恢复活性。这种可逆的过氧化物敏感开关代表了一种新型调控机制,可控制活性氧介导的细胞毒性和信号传导。本报告简要概述了过氧化物酶对过氧化氢信使功能的调控,并对近期研究结果进行了评论,这些研究探讨了一氧化氮生成对过氧化物酶在各种生理病理过程(包括巨噬细胞免疫刺激、多巴胺能神经元对N-甲基-D-天冬氨酸刺激的反应以及植物超敏反应)中的表达和氧化还原状态的影响。

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