Quantitative proteomic analysis of S-nitrosated proteins in diabetic mouse liver with ICAT switch method

摘要

In this study we developed a quantitative proteomic method named ICAT switch by introducing isotope-coded affinity tag ( ICAT ) reagents into the biotin-switch method, and used it to investigate S -nitrosation in the liver of normal control C57BL/6J mice and type 2 diabetic KK-Ay mice. We got fifty-eight S -nitrosated peptides with quantitative information in our research, among which thirty-seven had changed S -nitrosation levels in diabetic mouse liver. The S -nitrosated peptides belonged to fortyeight proteins (twenty-eight were new S -nitrosated proteins), some of which were new targets of S -nitrosation and known to be related with diabetes. S -nitrosation patterns were different between diabetic and normal mice. Gene ontology enrichment results suggested that S -nitrosated proteins are more abundant in amino acid metabolic processes. The network constructed for Snitrosated proteins by text-mining technology provided clues about the relationship between S -nitrosation and type 2 diabetes. Our work provides a new approach for quantifying S -nitrosated proteins and suggests that the integrative functions of S -nitrosation may take part in pathophysiological processes of type 2 diabetes.