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 language | English |
---|---|
Pages (from-to) | 127-133 |
Number of pages | 7 |
Journal | Biomedical Research (Japan) |
Volume | 8 |
Issue number | SUPPL. 1987 |
State | Published - 1987 |
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology