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Proteomic Methodologies to Assess Modifications

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Our laboratory has developed a number of novel gel-based and gel-free proteomic approaches for examining redox-based post-translational protein modifications. As such, we were the first to map specific in situ S-nitrosation and oxidation sites and occupancy levels in the heart at baseline, with cardioprotection, and following ischemia-reperfusion injury (Kohr et al. 2011, Kohr et al. 2011, Kohr et al. 2012).

Our studies utilized these novel proteomic approaches to demonstrate the ability of S-nitrosation to shield critical thiols from the damaging effects of irreversible oxidation, thus leading to the preservation of cellular function and viability. These seminal findings represent important advances toward the development of therapies for disease states where oxidant stress is a critical component of pathogenesis (i.e., ischemic heart disease, diabetes, Parkinson's disease, Alzheimer's disease). These studies also represent important advances in the biology of S-nitrosation, and demonstrate the potential for significant contributions to cellular physiology and function.

We continue to develop novel methodologies to further characterize redox-based modifications in the heart. Current studies are focused on the development of proteomics-based methods to characterize crosslinks induced by the endogenous production of formaldehyde in the heart, especially in the context of ischemia-reperfusion injury. These approaches are critical for defining the role of redox signaling in cardioprotection and ischemic injury.