Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE 68198, USA.
Amino Acids. 2012 May;42(5):1541-51. doi: 10.1007/s00726-012-1279-x. Epub 2012 Apr 5.
Protein S-nitrosylation is the covalent redox-related modification of cysteine sulfhydryl groups with nitric oxide, creating a regulatory impact similar to phosphorylation. Recent studies have reported a growing number of proteins to be S-nitrosylated in vivo resulting in altered functions. These studies support S-nitrosylation as a critical regulatory mechanism, fine-tuning protein activities within diverse cellular processes and biochemical pathways. In addition, S-nitrosylation appears to have key roles in the etiology of a broad range of human diseases. In this review, we discuss recent advances in proteomic approaches for the enrichment, identification, and quantitation of cysteine S-nitrosylated proteins and peptides. These advances have provided analytical tools with the power to interpret the impact of S-nitrosylation at the system level, providing a new platform for drug discovery and the identification of diagnostic markers for human diseases.
蛋白质 S-亚硝基化是指一氧化氮与半胱氨酸巯基发生共价氧化还原相关修饰，从而产生类似磷酸化的调节作用。最近的研究报告称，体内有越来越多的蛋白质发生 S-亚硝基化，导致其功能改变。这些研究支持 S-亚硝基化作为一种关键的调节机制，精细调节多种细胞过程和生化途径中的蛋白质活性。此外，S-亚硝基化似乎在广泛的人类疾病的发病机制中起着关键作用。在这篇综述中，我们讨论了用于富集、鉴定和定量半胱氨酸 S-亚硝基化蛋白质和肽的蛋白质组学方法的最新进展。这些进展提供了具有在系统水平上解释 S-亚硝基化影响的分析工具，为药物发现和鉴定人类疾病的诊断标志物提供了新的平台。
