Quantitative proteomic analysis of S-nitrosated proteins in diabetic mouse liver with ICAT switch method.
10.1007/s13238-010-0087-x
- Author:
Xu ZHANG
1
;
Bo HUANG
;
Xixi ZHOU
;
Chang CHEN
Author Information
1. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Animals;
Computational Biology;
Diabetes Mellitus, Experimental;
metabolism;
pathology;
Female;
Isotope Labeling;
Liver;
chemistry;
pathology;
Mice;
Mice, Inbred C57BL;
Molecular Sequence Data;
Nitrosation;
Peptides;
analysis;
Proteome;
chemistry
- From:
Protein & Cell
2010;1(7):675-687
- CountryChina
- Language:English
-
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 forty-eight 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 S-nitrosated 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.
