CARBONYL-COMPOUNDS CROSS-LINK CELLULAR PROTEINS AND ACTIVATE PROTEIN-TYROSINE KINASE P60(C-SRC)

Citation
Aa. Akhand et al., CARBONYL-COMPOUNDS CROSS-LINK CELLULAR PROTEINS AND ACTIVATE PROTEIN-TYROSINE KINASE P60(C-SRC), Journal of cellular biochemistry, 72(1), 1999, pp. 1-7
Citations number
28
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biology,"Cell Biology
ISSN journal
0730-2312
Volume
72
Issue
1
Year of publication
1999
Pages
1 - 7
Database
ISI
SICI code
0730-2312(1999)72:1<1:CCCPAA>2.0.ZU;2-M
Abstract
Glyoxal, a dicarbonyl compound, is produced under oxidative stress by the autoxidation of glucose and reacts with the protein amino group to form Schiff base. In vitro treatment of murine thymocytes and fibrobl asts with glyoxal induced extensive tyrosine phosphorylation of multip le proteins, which was drastically inhibited by the addition of OPB-91 95, an inhibitor of the carbonyl reaction with proteins. Glyoxal induc ed cross-linking of a number of cellular proteins, including glycosylp hosphatidylinositol (GPI)-anchored cell surface Thy-1. We then demonst rated that treatment of cells with glyoxal promptly induced activation of non-receptor protein-tyrosine kinase c-Src, which was partially in hibited by OPB-9195. It is suggested from these results that carbonyl amine reaction quickly activates c-Src, possibly through cross-linkage of GPI-anchored proteins or putative specific receptors. J. Cell. Bio chem. 72:1-7, 1999. (C) 1999 Wiley-Liss, Inc.