Signal transduction mechanisms mediated by tyrosine kinase receptors

M. Kasuga, T. Kadowaki, K. Tobe, T. Izumi, F. Takaku

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

The receptors for insulin, insulin-like growth factor-I (IGF-I) and epidermal growth factor (EGF) possess tyrosine-specific protein kinase activity which becomes activated upon ligand binding. To detect cellular substrates for these tyrosine-specific protein kinases, KB cells were labeled with [32P]orthophosphate and immunoprecipitated with phosphotyrosine-specific antibody. We have found that 1) a 185 kDa protein is rapidly (<10 sec) tyrosine phosphorylated by insulin and IGF-I but not EGF; 2) tyrosine phosphorylation of c-erbB-2 gene product is rapidly (<10 sec) induced by EGF; 3) tyrosine phosphorylation of a 240 kDa protein is stimulated within 30 sec by all three growth factors.

Original languageEnglish
Pages (from-to)127-133
Number of pages7
JournalBiomedical Research (Japan)
Volume8
Issue numberSUPPL. 1987
StatePublished - 1987

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology

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