Forrester Michael T, Foster Matthew W, Benhar Moran, Stamler Jonathan S
Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Free Radic Biol Med. 2009 Jan 15;46(2):119-26. doi: 10.1016/j.freeradbiomed.2008.09.034. Epub 2008 Oct 17.
Protein S-nitrosylation, the posttranslational modification of cysteine thiols to form S-nitrosothiols, is a principle mechanism of nitric oxide-based signaling. Studies have demonstrated myriad roles for S-nitrosylation in organisms from bacteria to humans, and recent efforts have greatly advanced our scientific understanding of how this redox-based modification is dynamically regulated during physiological and pathophysiological conditions. The focus of this review is the biotin-switch technique (BST), which has become a mainstay assay for detecting S-nitrosylated proteins in complex biological systems. Potential pitfalls and modern adaptations of the BST are discussed, as are future directions for this assay in the burgeoning field of protein S-nitrosylation.
蛋白质S-亚硝基化是指半胱氨酸硫醇发生翻译后修饰形成S-亚硝基硫醇，它是基于一氧化氮的信号传导的主要机制。研究表明，从细菌到人类，S-亚硝基化在生物体中发挥着多种作用，最近的研究极大地增进了我们对这种基于氧化还原的修饰在生理和病理生理条件下如何动态调节的科学理解。本综述的重点是生物素转换技术（BST），它已成为在复杂生物系统中检测S-亚硝基化蛋白质的主要检测方法。文中讨论了BST的潜在缺陷和现代改进方法，以及该检测方法在新兴的蛋白质S-亚硝基化领域的未来发展方向。
