It is well established that NO, and especially S-nitrosation of cellular proteins play a key role in several toxicities and pathologies. Recently, several groups have developed high throughput mass spectrometric approaches for analysis of the SNO-proteome in different tissues, that has revealed hundreds of proteins associated with a toxic or pathological state. In particular, our method (SNOTRAP, SNO trapping by TriAryl Phosphine) directly traps a SNO-molecule without primary denitrosation, and in addition to mass spec proteomics allows imaging of cells and tissues in fresh, frozen, or fixed states. The discovery that there are hundreds of SNO-proteins in any physiological state has allowed analysis of the role of SNO on a systems level. What is remarkable is that there are major differences for the cognate proteins between organs and tissues, or even between different tissue localizations. Even more remarkable is the complete re-programming of the SNO-proteome in the same tissue localization for different toxicities or pathologies. The large number of proteins identified is conducive to analysis in the Gene Ontology system, providing a visualization of shifting biological processes , protein networks, and biochemical pathways induced by mutant proteins or toxic responses. Examples of mutations in the brain and arsenic in drinking water will be presented.

S-Nitrosation is a systems-wide regulatory process

254th National Meeting (2017)

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