Redox Proteomics: Chemical Principles, Methodological Approaches and Biological/Biomedical Promises

Integrated redox proteomics methodologies have contributed in a significant way to provide a better understanding of the oxidative and nitrosative post translational modifications (PTMs) occurring in prokaryotes and eukaryotes during their life cycle or eventually associated with the development of pathological state. On the other hand, a number of irreversible redox PTMs, including nitration, some oxidations, halogenation, and carbonylation, as detected by dedicated redox proteomics approaches, have been associated with specific stressing conditions, highly affecting protein activity and, ultimately, cell functionality. Quantitative redox proteomic approaches were used to identify and quantify redox PTMs in PTPs (Protein tyrosine phosphatases) expressed in human, mouse, and rat cell lines and tissues or in response to stimulation of growth factor receptors. By applying these novel quantitative methods, authors found that normal and malignant cells display distinctive patterns of PTP expression and redox modification.