Insulin-stimulated protein kinase activity in rat skeletal muscle that phosphorylates ribosomal protein S6

Treatment of rats with a single high dose of insulin leads to rapid stimulation of cytosolic protein kinase activity in skeletal muscle that phosphorylates ribosomal protein S6. This stimulation is maximal within 15 minutes after insulin treatment, and the activity remains elevated for at least 90 minutes. The insulin-stimulated protein kinase activity elutes as two peaks from DEAE-Sepharose. Peak I elutes at 0.04-0.06 M KCl and is stimulated by insulin approximately 1.4-fold above the control. Peak II elutes at 0.09-0.11 M KCl and is stimulated 2.8-fold above the control. The peak II activity, which is most strongly stimulated by insulin, is resolved from cyclic AMP-dependent protein kinase on DEAE-Sepharose and appears to be distinct from protein kinase C. These results represent a novel finding of the stimulation of S6 kinase activity by insulin in skeletal muscle tissue in vivo.