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首页> 外文期刊>Molecular cell >Inactivation of a Peroxiredoxin by Hydrogen Peroxide Is Critical for Thioredoxin-Mediated Repair of Oxidized Proteins and Cell Survival
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Inactivation of a Peroxiredoxin by Hydrogen Peroxide Is Critical for Thioredoxin-Mediated Repair of Oxidized Proteins and Cell Survival

机译：过氧化氢灭活过氧化物酶对于硫氧还蛋白介导的氧化蛋白修复和细胞存活至关重要。

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摘要

Eukaryotic 2-Cys peroxiredoxins (Prx) are abundant antioxidant enzymes whose thioredoxin peroxidase activity plays an important role in protecting against oxidative stress, aging, and cancer. Paradoxically, this thioredoxin peroxidase activity is highly sensitive to inactivation by peroxide-induced Prx hyperoxidation. However, any possible advantage in preventing Prx from removing peroxides under oxidative stress conditions has remained obscure. Here we demonstrate that, in cells treated with hydrogen peroxide, the Prx Tpx1 is a major substrate for thioredoxin in the fission yeast Schizosaccharomyces pombe and, as such, competitively inhibits thioredoxin-mediated reduction of other oxidized proteins.Consequently, we reveal that the hyperoxidation of Tpx1 is critical to allow thioredoxin to act onother substrates ensuring repair of oxidized proteins and cell survival following exposure to toxiclevels of hydrogen peroxide. We conclude that the inactivation of the thioredoxin peroxidase activity of Prx is important to maintain thioredoxin activity and cell viability under oxidative stress conditions.
机译：真核2-Cys过氧化物酶（Prx）是丰富的抗氧化酶，其硫氧还蛋白过氧化物酶的活性在防止氧化应激，衰老和癌症中起着重要的作用。矛盾的是，这种硫氧还蛋白过氧化物酶活性对由过氧化物诱导的Prx过氧化引起的失活非常敏感。但是，在氧化应激条件下防止Prx去除过氧化物的任何可能的优点仍然不清楚。在这里，我们证明了在过氧化氢处理的细胞中，Prx Tpx1是裂殖酵母裂殖酵母中硫氧还蛋白的主要底物，因此，竞争性抑制了硫氧还蛋白介导的其他氧化蛋白的还原。 Tpx1的暴露对于使硫氧还蛋白能够作用于其他底物至关重要，从而确保了氧化蛋白的修复和暴露于过氧化氢的毒性水平后的细胞存活。我们得出的结论是，Prx的硫氧还蛋白过氧化物酶活性的失活对于在氧化应激条件下维持硫氧还蛋白的活性和细胞活力很重要。

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