Hydrogen peroxide stimulates tyrosine phosphorylation of the insulin receptor and its tyrosine kinase activity in intact cells

Using the rat hepatoma cell line H-35, in this study we have examined the possibility that H202 elicitates its insulin-like effects by stimulating tyrosine phosphorylation of the insulin receptor and activating its receptor kinase

O Koshio; Y Akanuma; M Kasuga

2015

Scholarcy highlights

  • Insulin receptors consist of a subunits of Mr 135000 and, subunits of Mr 95000 linked together through disulphide bonding to form tetramers(Massague et al, 1980; Van Obberghen et al, 1981)
  • Insulin treatment of intact cells results in autophosphorylation of the /3 subunit of the insulin receptor on tyrosine residues and the rapid activation of its kinase activity
  • Using the rat hepatoma cell line H-35, in this study we have examined the possibility that H202 elicitates its insulin-like effects by stimulating tyrosine phosphorylation of the insulin receptor and activating its receptor kinase
  • H-35 cells were treated with several concentrations of H202 for 10 min and the kinase activity of wheat germ agglutinin-purified fraction toward src-related peptide was examined
  • We have demonstrated that the treatment of H-35 rat hepatoma cells with H202 increased the incorporation of 32p into the tyrosine residues of the, subunit of insulin receptors
  • We have shown that WGA-purified insulin receptors obtained from H202-treated cells demonstrate an increased 32P-labelling of the,l
  • These data provide additional support for the notion that H202 stimulates the tyrosine kinase activity of the insulin receptor in intact cells

Need more features? Save interactive summary cards to your Scholarcy Library.