Contemporary techniques for detecting and identifying proteins susceptible to reversible thiol oxidation
Contemporary techniques for detecting and identifying proteins susceptible to reversible thiol oxidation
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DOI：
10.1042/bst0391260
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发表时间：
2011-10-01
影响因子：
3.9
通讯作者：
Eaton, Philip
中科院分区：
文献类型：
--
作者：
Burgoyne, Joseph R.;Eaton, Philip
蛋白质氧化升高是大多数主要疾病的一个广泛报道的标志。从历史上看，这种“氧化应激”被认为是有害的，因为蛋白质氧化事件被简单地解释为损伤。然而，最近的进展改变了这种过时的观点。用于检测和识别易氧化蛋白质的灵敏方法揭示了健康期间生理细胞信号传导中这种修饰的基本作用。与细胞还原系统动态耦合的可逆蛋白质氧化允许氧化蛋白质修饰来调节蛋白质功能，类似于磷酸调节。然而，许多可逆蛋白质氧化态的相对不稳定性质阻碍了修饰蛋白质的可靠检测和鉴定。因此，已经开发出了稳定蛋白质氧化的专门方法以及检测特定类型修饰的技术。在这里，我们讨论了这些技术，并严格评估了它们的灵敏度、选择性和可靠识别可逆氧化蛋白质的能力。
Elevated protein oxidation is a widely reported hallmark of most major diseases. Historically, this 'oxidative stress' has been considered causatively detrimental, as the protein oxidation events were interpreted simply as damage. However, recent advances have changed this antiquated view; sensitive methodology for detecting and identifying proteins susceptible to oxidation has revealed a fundamental role for this modification in physiological cell signalling during health. Reversible protein oxidation that is dynamically coupled with cellular reducing systems allows oxidative protein modifications to regulate protein function, analogous to phosphoregulation. However, the relatively labile nature of many reversible protein oxidation states hampers the reliable detection and identification of modified proteins. Consequently, specialized methods to stabilize protein oxidation in combination with techniques to detect specific types of modification have been developed. Here, these techniques are discussed, and their sensitivity, selectivity and ability to reliably identify reversibly oxidized proteins are critically assessed.