Insulin stimulates the phosphorylation of the 95,000-dalton subunit of its own receptor
M Kasuga, FA Karlsson, CR Kahn - Science, 1982 - science.org
M Kasuga, FA Karlsson, CR Kahn
Science, 1982•science.orgCultured human lymphocytes and rat hepatoma cells were labeled with [32P]
orthophosphate and the insulin receptor subunits identified by immunoprecipitation and
sodium dodecyl sulfate-gel electrophoresis. In both cell types the 95,000-dalton (β) subunit
of the insulin receptor was selectively phosphorylated. Phosphorylation was specifically
stimulated by insulin in a dose-dependent fashion after 1 and 15 minutes of hormone
treatment, whereas human growth hormone was without effect. This phosphorylation may be …
orthophosphate and the insulin receptor subunits identified by immunoprecipitation and
sodium dodecyl sulfate-gel electrophoresis. In both cell types the 95,000-dalton (β) subunit
of the insulin receptor was selectively phosphorylated. Phosphorylation was specifically
stimulated by insulin in a dose-dependent fashion after 1 and 15 minutes of hormone
treatment, whereas human growth hormone was without effect. This phosphorylation may be …
Cultured human lymphocytes and rat hepatoma cells were labeled with [32P]orthophosphate and the insulin receptor subunits identified by immunoprecipitation and sodium dodecyl sulfate-gel electrophoresis. In both cell types the 95,000-dalton (β) subunit of the insulin receptor was selectively phosphorylated. Phosphorylation was specifically stimulated by insulin in a dose-dependent fashion after 1 and 15 minutes of hormone treatment, whereas human growth hormone was without effect. This phosphorylation may be a very early event in insulin action.
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