Schöneich Christian, Sharov Victor S
Department of Pharmaceutical Chemistry, University of Kansas, 2095 Constant Avenue, Lawrence, KS 66047, USA.
Free Radic Biol Med. 2006 Nov 15;41(10):1507-20. doi: 10.1016/j.freeradbiomed.2006.08.013. Epub 2006 Aug 16.
The modification of proteins by reactive oxygen and nitrogen species plays an important role in various biologic processes involving protein activation and inactivation, protein translocation and turnover during signal transduction, stress response, proliferation, and apoptosis. Recent advances in protein and peptide separation and mass spectrometry provide increasingly sophisticated tools for the quantitative analysis of such protein modifications, which are absolutely necessary for their correlation with biologic phenomena. The present review focuses specifically on the qualitative and quantitative mass spectrometric analysis of the most common protein modifications caused by reactive oxygen and nitrogen species in vivo and in vitro and details a case study on a membrane protein the sarco/endoplasmic reticulum Ca-ATPase (SERCA).
活性氧和氮物种对蛋白质的修饰在各种生物过程中发挥着重要作用，这些过程包括蛋白质的激活与失活、信号转导过程中的蛋白质转运与周转、应激反应、增殖以及细胞凋亡。蛋白质和肽分离以及质谱分析方面的最新进展为这类蛋白质修饰的定量分析提供了日益精密的工具，而这些工具对于将蛋白质修饰与生物现象相关联而言是绝对必要的。本综述特别聚焦于体内和体外由活性氧和氮物种引起的最常见蛋白质修饰的定性和定量质谱分析，并详细介绍了一个关于膜蛋白肌浆/内质网钙ATP酶（SERCA）的案例研究。
