Generation by insulin of a chemical mediator that controls protein phosphorylation and dephosphorylation.
Science, 1979/12/21;206(4425):1408-10.
Larner J, Galasko G, Cheng K, DePaoli-Roach AA, Huang L, Daggy P, Kellogg J
PMID: 228395
Impact factor: 63.714
Abstract
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.
MeSH terms
Animals; Cyclic AMP; Enzyme Activation; Glycogen-Synthase-D Phosphatase; Insulin; Molecular Weight; Muscle Proteins; Muscles; Peptides; Phosphoprotein Phosphatases; Protein Kinase Inhibitors; Rats
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