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首页> 外文期刊>Nature >Superoxide dismutase protects calcineurin from inactivation.
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Superoxide dismutase protects calcineurin from inactivation.

机译：超氧化物歧化酶可保护钙调神经磷酸酶免于失活。

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摘要

Calcineurin is the only protein phosphatase known to be under the control of Ca2+ and calmodulin. It is targeted by immunosuppressive drugs and has a critical role in T-cell activation. It is specifically inhibited by immunosuppressant immunophilin complexes, which enabled its function in regulating a wide range of cellular responses to Ca2+-mobilizing signals to be identified. Calcineurin in situ is 10-20 times more active than in the purified form and is subject to a time- and Ca2+/calmodulin-dependent reversible inactivation that is facilitated by small, heat-stable molecules. Here we identify a factor that prevents the inactivation of calcineurin in vitro and in vivo as the enzyme superoxide dismutase, which indicates that inactivation may be the result of oxidative damage to the Fe-Zn active centre of calcineurin. The redox state of iron provides a mechanism to regulate calcineurin activity by desensitizing the enzyme and coupling Ca2+-dependent protein dephosphorylation to the redox state of the cell. The protection of calcineurin against inactivation by superoxide dismutase constitutes a new physiological role for this enzyme which enables the Ca2+-dependent regulation of cellular processes to be modulated by the redox potential.
机译：钙调神经磷酸酶是已知受Ca2 +和钙调蛋白控制的唯一蛋白质磷酸酶。它是免疫抑制药物的靶向，在T细胞活化中起关键作用。它被免疫抑制剂亲免蛋白复合物特异性抑制，从而使其在调节广泛的细胞对Ca2 +动员信号的反应中发挥作用。钙调神经磷酸酶原位活性比纯化形式高10-20倍，并且受时间和Ca2 + /钙调蛋白依赖性可逆失活的影响，这是由小的热稳定分子促进的。在这里，我们确定了一种阻止钙调神经磷酸酶在体外和体内失活的因素，即酶超氧化物歧化酶，这表明该失活可能是钙调神经磷酸酶的Fe-Zn活性中心氧化损伤的结果。铁的氧化还原状态通过使酶脱敏并将Ca2 +依赖性蛋白去磷酸化偶联至细胞的氧化还原状态，提供调节钙调神经磷酸酶活性的机制。保护钙调神经磷酸酶免于超氧化物歧化酶灭活构成了该酶的新的生理学作用，该酶使Ca2 +依赖的细胞过程调节能够被氧化还原电位调节。

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