Martínez-Ruiz Antonio, Lamas Santiago
Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas and Instituto Reina Sofía de Investigaciones Nefrológicas, Ramiro de Maeztu, 9, Madrid E-28040, Spain.
Cardiovasc Res. 2007 Jul 15;75(2):220-8. doi: 10.1016/j.cardiores.2007.03.016. Epub 2007 Mar 24.
The role of nitric oxide in several signalling routes has been clearly established. In recent years increasing attention has been paid to its ability to produce covalent protein post-translational modifications in conjunction with other reactive oxygen and nitrogen species. Among these, the modification of cysteine residues has been shown to be of particular importance due to the functional relevance of many of them. In this review, we focus on the modification of the cysteine thiol by incorporation of a NO moiety (S-nitrosylation) or of a glutathione moiety (S-glutathionylation). Both modifications are produced by different reactions induced by nitric oxide-related species. We discuss the differences and similarities of both modifications, and their relationships, in regard to the biochemical mechanisms that produce them, including the enzymatic activities that may catalyze some of them and their subcellular compartmentalization. Even when biochemical knowledge is one step ahead of the demonstration of their pathophysiological relevance, we also describe the potential role of both modifications in several processes in which both post-translational modifications are involved.
一氧化氮在多种信号通路中的作用已得到明确证实。近年来，人们越来越关注它与其他活性氧和氮物种共同产生共价蛋白质翻译后修饰的能力。其中，由于许多半胱氨酸残基具有功能相关性，其修饰已被证明尤为重要。在本综述中，我们重点关注通过结合一氧化氮基团（S-亚硝基化）或谷胱甘肽基团（S-谷胱甘肽化）对半胱氨酸硫醇进行的修饰。这两种修饰均由一氧化氮相关物种诱导的不同反应产生。我们讨论了这两种修饰在产生它们的生化机制方面的差异和相似之处，以及它们之间的关系，包括可能催化其中一些反应的酶活性及其亚细胞定位。即使生化知识在证明它们的病理生理相关性方面领先一步，我们也描述了这两种修饰在涉及这两种翻译后修饰的几个过程中的潜在作用。
