Quantitative proteomic analysis of S-nitrosated proteins in diabetic mouse liver with ICAT switch method
Protein & Cell
;
(12): 675-687, 2010.
Article
in English
| WPRIM
| ID: wpr-757421
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Pathology
/
Peptides
/
Molecular Sequence Data
/
Nitrosation
/
Chemistry
/
Amino Acid Sequence
/
Computational Biology
/
Proteome
/
Diabetes Mellitus, Experimental
/
Isotope Labeling
Limits:
Animals
Language:
English
Journal:
Protein & Cell
Year:
2010
Type:
Article
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