Institute of Chemistry, Academia Sinica, Taipei, Taiwan.
Methods. 2013 Aug 1;62(2):138-50. doi: 10.1016/j.ymeth.2013.04.016. Epub 2013 Apr 27.
Reversible protein S-nitrosylation, defined as the covalent addition of a nitroso moiety to the reactive thiol group on a cysteine residue, has received increasing recognition as a critical post-translational modification that exerts ubiquitous influence in a wide range of cellular pathways and physiological processes. Due to the lability of the S-NO bond, which is a dynamic modification, and the low abundance of endogenously S-nitrosylated proteins in vivo, unambiguous identification of S-nitrosylated proteins and S-nitrosylation sites remains methodologically challenging. In this review, we summarize recent advancements and the use of state-of-art approaches for the enrichment, systematic identification and quantitation of S-nitrosylation protein targets and their modification sites at the S-nitrosoproteome scale. These advancements have facilitated the global identification of >3000 S-nitrosylated proteins that are associated with wide range of human diseases. These strategies hold promise to site-specifically unravel potential molecular targets and to change S-nitrosylation-based pathophysiology, which may further the understanding of the potential role of S-nitrosylation in diseases.
蛋白质可逆的 S-亚硝基化作用，定义为一个硝基部分共价添加到半胱氨酸残基的反应性巯基上，已被越来越多地认为是一种关键的翻译后修饰，它在广泛的细胞途径和生理过程中产生普遍的影响。由于 S-NO 键的不稳定性，这是一种动态修饰，以及体内内源性 S-亚硝基化蛋白质的低丰度，S-亚硝基化蛋白质和 S-亚硝基化位点的明确鉴定在方法学上仍然具有挑战性。在这篇综述中，我们总结了最近的进展，并概述了用于 S-亚硝酰化蛋白质靶标及其在 S-亚硝酰蛋白组水平上的修饰位点的富集、系统鉴定和定量的最先进方法。这些进展促进了>3000 种与多种人类疾病相关的 S-亚硝基化蛋白质的全局鉴定。这些策略有望特异性地揭示潜在的分子靶标，并改变基于 S-亚硝基化的病理生理学，这可能进一步了解 S-亚硝基化在疾病中的潜在作用。
