Department of Pharmacology, Weill Cornell Medical College, 1300 York Ave, New York, NY 10065, USA.
J Proteomics. 2011 Oct 19;74(11):2300-12. doi: 10.1016/j.jprot.2011.05.032. Epub 2011 Jun 6.
Reactive nitrogen species are formed during a variety of disease states and have been shown to modify several amino acids on proteins. To date, the majority of research in this area has focused on the nitration of tyrosine residues to form 3-nitrotyrosine. However, emerging evidence suggests that another modification, nitration of tryptophan residues, to form nitrotryptophan (NO(2)-Trp), may also play a significant role in the biology of nitrosative stress. This review takes an in-depth look at NO(2)-Trp, presenting the current research about its formation, prevalence and biological significance, as well as the methods used to identify NO(2)-Trp-modified proteins. Although more research is needed to understand the full biological role of NO(2)-Trp, the data presented herein suggest a contribution to nitrosative stress-induced cell dysregulation and perhaps even in physiological cell processes.
活性氮物种在多种疾病状态下形成,并已被证明可以修饰蛋白质上的几种氨基酸。迄今为止,该领域的大多数研究都集中在酪氨酸残基的硝化上,形成 3-硝基酪氨酸。然而,新出现的证据表明,另一种修饰,即色氨酸残基的硝化,形成硝基色氨酸(NO2-Trp),也可能在硝化应激的生物学中发挥重要作用。这篇综述深入探讨了 NO2-Trp,介绍了目前关于其形成、普遍性和生物学意义的研究,以及用于鉴定 NO2-Trp 修饰蛋白的方法。尽管需要更多的研究来了解 NO2-Trp 的全部生物学作用,但本文提供的数据表明其可能与硝化应激诱导的细胞失调有关,甚至可能与生理细胞过程有关。