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Carbonyl compounds cross-link cellular proteins and activate protein-tyrosine kinase p60c-Src

✍ Scribed by Anwarul A. Akhand; Masashi Kato; Haruhiko Suzuki; Wei Liu; Jun Du; Michinari Hamaguchi; Toshio Miyata; Kiyoshi Kurokawa; Izumi Nakashima

Publisher: John Wiley and Sons
Year: 1999
Tongue: English
Weight: 124 KB
Volume: 72
Category: Article
ISSN: 0730-2312
DOI: 10.1002/(sici)1097-4644(19990101)72:1<1::aid-jcb1>3.0.co;2-y

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✦ Synopsis

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 fibroblasts with glyoxal induced extensive tyrosine phosphorylation of multiple proteins, which was drastically inhibited by the addition of OPB-9195, an inhibitor of the carbonyl reaction with proteins. Glyoxal induced cross-linking of a number of cellular proteins, including glycosylphosphatidylinositol (GPI)-anchored cell surface Thy-1. We then demonstrated that treatment of cells with glyoxal promptly induced activation of non-receptor protein-tyrosine kinase c-Src, which was partially inhibited 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.

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