Enhancement of epidermal growth factor (EGF) and insulin-stimulated tyrosine phosphorylation of endogenous substrates by sodium selenate.
Sodium selenate stimulated tyrosine phosphorylation of the epidermal growth factor (EGF) receptor in A431 cells and enhanced the tyrosine phosphorylation of endogenous proteins in response to EGF in A431 cells and insulin in NIH 3T3 HIR3.5 cells. These effects occurred without changes in ligand binding, were not abolished by mercaptoethanol in the case of the EGF receptor, and appeared distinct from the effects of vanadate. These results support a role for selenium or selenoproteins in regulating EGF and insulin receptor tyrosine kinase activity and suggest a mechanism whereby selenium-containing compounds contribute to cell growth.
Pillay
T S
TS
Department of Chemical Pathology, Royal Postgraduate Medical School, University of London, Hammersmith Hospital, UK.
Makgoba
M W
MW
D016475:3T3 Cells; D000818:Animals; D015153:Blotting, Western; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D004815:Epidermal Growth Factor / Q000494:pharmacology*; D007328:Insulin / Q000494:pharmacology*; D051379:Mice; D010766:Phosphorylation; D064586:Selenic Acid; D012643:Selenium / Q000494:pharmacology*; D018036:Selenium Compounds; D013379:Substrate Specificity; D014443:Tyrosine / Q000378:metabolism*
D007328:Insulin; D018036:Selenium Compounds; D014443:Tyrosine; D004815:Epidermal Growth Factor; D012643:Selenium; D064586:Selenic Acid