Stable isotope oxidative stress

Yan and his colleagues used a stable isotope labeled proteome internal standard to analyse protein expression alterations during oxidative stress in breast epithelial cells. Affinity chromatography was combined with MS/MS in the proteomic analysis of human 06-methylguanine-DNA methyltransferase. These studies demonstrated that proteomics can elucidate protein expre-ssions associated with the pharmacological and toxic effects of an anticancer drug when integrated with other biochemical methods. 

Yan, Y, Weaver, V. M., Sc Blair, I. A (2005). Analysis of protein expression during oxidative stress in breast epithelial cells using a stable isotope labeled proteome internal standard. Journal of Proteome Research, 4, 2007—2014. 

A dramatic selective enrichment in nitrotyrosine content was observed within apoA-I recovered from serum and human atherosclerotic lesions. The analysis of serum from sequential subjects demonstrates that the nitrotyrosine contents of apoA-I were markedly higher in individuals with cardiovascular disease. An increase in nitrotyrosine was observed in the atherosclerotic lesions and plasma of apolipoprotein A-I-deficient mice (Parastatidis et al., 2007). LC MS/MS studies confirm that nitration of apoA-I occurs specifically on tyrosine-192 (Shao et al., 2005). Similarly, LC—MS/MS methods were used to identify tyrosine residues 292 and 422 at the carboxyl terminus of the 3 chain as the principal sites of fibrinogen nitration in vivo (Parastatidis et al., 2008). Stable isotope dilution LC MRM/MS methodology will likely be employed extensively in the future to assess the role of protein tyrosine nitration in the oxidative stress associated with cardiovascular disease. 

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