Cell Biology Department, Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Hospital Reina Sofía, Universidad de Córdoba, Spain.
Expert Rev Proteomics. 2012;9(1):59-69. doi: 10.1586/epr.11.74.
Nitric oxide (NO) can modulate cell function by the coupling of a nitroso moiety to a reactive cysteine in target proteins leading to the formation of a S-nitrosothiol (SNO), a process commonly known as S-nitrosylation. Aberrant S-nitrosylation of proteins, caused by altered production of NO and/or impaired SNO homeostasis, constitutes a mechanism that has been recently postulated in numerous pathophysiological settings. The thiol microenvironment, cellular redox environment, and activity of transnitrosylases and denitrosylases have been proposed as determinant factors for the specificity of S-nitrosylation. A number of methodological approaches have recently been developed for the proteomic identification of S-nitrosylated proteins and/or the identification of specific sites of nitrosylation. This review will consider novel aspects of SNO homeostasis and S-nitrosylation, the latest proteomic methods for the identification of S-nitrosylated cysteines in proteins, and how these novel technologies will impact our current knowledge of the role of deregulated S-nitrosylation in disease.
一氧化氮（NO）可以通过将硝基部分与靶蛋白中的反应性半胱氨酸偶联来调节细胞功能，导致形成 S-亚硝基硫醇（SNO），这一过程通常被称为 S-亚硝基化。由于 NO 产生的改变和/或 SNO 动态平衡受损导致的蛋白质异常 S-亚硝基化，是最近在许多病理生理情况下提出的一种机制。巯基微环境、细胞氧化还原环境以及转亚硝基酶和去亚硝基酶的活性被认为是 S-亚硝基化特异性的决定因素。最近已经开发了许多方法学方法来用于蛋白质组学鉴定 S-亚硝基化蛋白质和/或鉴定特定的亚硝酰化位点。这篇综述将考虑 SNO 动态平衡和 S-亚硝基化的新方面、用于鉴定蛋白质中 S-亚硝基化半胱氨酸的最新蛋白质组学方法，以及这些新技术将如何影响我们对失调的 S-亚硝基化在疾病中的作用的现有知识。
