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

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

Research output: Contribution to journalArticlepeer-review

62 Citations (Scopus)

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 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. Clyoxal 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.

Original languageEnglish
Pages (from-to)1-7
Number of pages7
JournalJournal of Cellular Biochemistry
Volume72
Issue number1
DOIs
Publication statusPublished - 1999 Jan 1
Externally publishedYes

Keywords

  • Glyoxal
  • Thy-1
  • Tyrosine phosphorylation
  • c-Src

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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