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首页> 外文期刊>American Journal of Physiology >Biological significance of nitric oxide-mediated protein modifications.
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Biological significance of nitric oxide-mediated protein modifications.

机译：一氧化氮介导的蛋白质修饰的生物学意义。

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摘要

Nitric oxide (NO), despite an apparently simple diatomic structure, has a wide variety of functions in both physiology and pathology and within every major organ system. It has become an increasingly important scientific challenge to decipher how this wide range of activity is achieved. To this end a number of investigators have begun to explore how NO-mediated posttranslational modifications of proteins may represent mechanisms of cellular signaling. These modifications include: 1). binding to metal centers; 2). nitrosylation of thiol and amine groups; 3). nitration of tyrosine, tryptophan, amine, carboxylic acid, and phenylalanine groups; and 4). oxidation of thiols (both cysteine and methionine residues) and tyrosine. However, two particular modifications have recently received much attention, nitrosylation of thiols to produce S-nitrosothiol and nitration of tyrosine residues to produce nitrotyrosine. It is the purpose of this review to examine the possibility that these modifications may play a role in NO-mediated signaling.
机译：一氧化氮（NO）尽管表面看似简单的双原子结构，但在生理和病理学以及每个主要器官系统中均具有多种功能。解密如何实现如此广泛的活动已成为越来越重要的科学挑战。为此，许多研究人员已开始探索NO介导的蛋白质翻译后修饰如何代表细胞信号转导的机制。这些修改包括：1）。绑定到金属中心; 2）。巯基和胺基的亚硝基化; 3）。酪氨酸，色氨酸，胺，羧酸和苯丙氨酸的硝化作用;和4）。氧化硫醇（半胱氨酸和蛋氨酸残基）和酪氨酸。但是，最近有两个特别的修饰引起了人们的注意：硫醇的亚硝化作用产生S-亚硝基硫醇和酪氨酸残基的硝化作用产生硝基酪氨酸。这篇综述的目的是研究这些修饰可能在NO介导的信号传导中起作用的可能性。

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