Generation by insulin of a chemical mediator that controls protein phosphorylation and dephosphorylation.
Deproteinized skeletal muscle extracts free of major nucleotides from control and insulin-treated rats were fractionated and assayed for inhibition of protein phosphorylation by cyclic adenosine monophosphate (AMP)-dependent and -independent protein kinases. A differential effect of insulin on a particular fraction was observed on cyclic AMP-dependent protein kinase but not on cyclic AMP-independent protein kinases. This fraction that inhibited cyclic AMP-dependent protein kinase also stimulated glycogen synthase phosphoprotein phosphatase. It is proposed that this fraction may contain a mediator substance generateed in the presence of insulin.
D000818:Animals; D000242:Cyclic AMP / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D006007:Glycogen-Synthase-D Phosphatase / Q000378:metabolism*; D007328:Insulin / Q000494:pharmacology*; D008970:Molecular Weight; D009124:Muscle Proteins / Q000302:isolation & purification / Q000494:pharmacology; D009132:Muscles / Q000187:drug effects*; D010455:Peptides / Q000494:pharmacology; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D047428:Protein Kinase Inhibitors; D051381:Rats
D007328:Insulin; D009124:Muscle Proteins; D010455:Peptides; D047428:Protein Kinase Inhibitors; D000242:Cyclic AMP; D010749:Phosphoprotein Phosphatases; D006007:Glycogen-Synthase-D Phosphatase