Kettenhofen Nicholas J, Broniowska Katarzyna A, Keszler Agnes, Zhang Yanhong, Hogg Neil
Department of Biophysics and Free Radical Research Center, Medical College of Wisconsin, Milwaukee, WI 53226, USA.
J Chromatogr B Analyt Technol Biomed Life Sci. 2007 May 15;851(1-2):152-9. doi: 10.1016/j.jchromb.2007.02.035. Epub 2007 Feb 25.
This review discusses proteomic methods to detect and identify S-nitrosated proteins. Protein S-nitrosation, the post-translational modification of thiol residues to form S-nitrosothiols, has been suggested to be a mechanism of cellular redox signaling by which nitric oxide can alter cellular function through modification of protein thiol residues. It has become apparent that methods that will detect and identify low levels of S-nitrosated protein in complex protein mixtures are required in order to fully appreciate the range, extent and selectivity of this modification in both physiological and pathological conditions. While many advances have been made in the detection of either total cellular S-nitrosation or individual S-nitrosothiols, proteomic methods for the detection of S-nitrosation are in relative infancy. This review will discuss the major methods that have been used for the proteomic analysis of protein S-nitrosation and discuss the pros and cons of this methodology.
本综述讨论了用于检测和鉴定S-亚硝基化蛋白质的蛋白质组学方法。蛋白质S-亚硝基化是硫醇残基的翻译后修饰，形成S-亚硝基硫醇，被认为是一种细胞氧化还原信号传导机制，通过该机制一氧化氮可以通过修饰蛋白质硫醇残基来改变细胞功能。显然，为了充分认识这种修饰在生理和病理条件下的范围、程度和选择性，需要能够检测和鉴定复杂蛋白质混合物中低水平S-亚硝基化蛋白质的方法。虽然在检测总细胞S-亚硝基化或单个S-亚硝基硫醇方面已经取得了许多进展，但用于检测S-亚硝基化的蛋白质组学方法仍处于相对起步阶段。本综述将讨论用于蛋白质S-亚硝基化蛋白质组学分析的主要方法，并讨论该方法的优缺点。
