An essential first step in the understanding disease and environmental perturbations is the early and quantitative detection of the increased levels of the inflammatory marker nitrotyrosine, as compared with its endogenous levels within the tissue or cellular proteome. Thus, methods that successfully address a proteome-wide quantitation of nitrotyrosine and related oxidative modifications can provide early biomarkers of risk and progression of disease as well as effective strategies for therapy. Multidimensional separations LC coupled with tandem mass spectrometry (LC-MS/MS) has, in recent years, significantly expanded our knowledge of human (and mammalian model system) proteomes including some nascent work in identification of post-translational modifications. In the following review, we discuss the application of LC-MS/MS for quantitation and identification of nitrotyrosine-modified proteins within the context of complex protein mixtures presented in mammalian proteomes.
Revised: May 10, 2010 |
Published: February 10, 2008
Citation
Bigelow D.J., and W. Qian. 2008.Quantitative Proteome Mapping of Nitrotyrosines. In Methods in Enzymology, Nitric Oxide Part F: Oxidative and Nitrosative Stress in Redox Regulation of Cell Signaling. 191-205. Amsterdam:Elsevier.PNNL-SA-56770.