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. 2010 Jul 29;1(7):675–687. doi: 10.1007/s13238-010-0087-x

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

Xu Zhang 1,2, Bo Huang 1,2, Xixi Zhou 1,2, Chang Chen 1,✉
PMCID: PMC4875280  PMID: 21203939

Abstract

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.

Keywords: ICAT switch, mass spectrometry, quantitative, S-nitrosation, type 2 diabetes

Footnotes

These authors contributed equally to the work.

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