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Studies on the role of cAMP-dependent protein kinase in the actions of glucagon and catecholamines on liver glycogen metabolism.

Cherrington AD, Exton JH
Metabolism. 1976 25 (11 Suppl 1): 1351-4

PMID: 185493 · DOI:10.1016/s0026-0495(76)80140-0

Glucagon causes a rapid activation of cAMP-dependent protein kinase in rat liver parenchymal cells which correlates well with the accumulation of cAMP. Full activation of phosphorylase or inactivation of glycogen synthase is achieved with half-maximal or less activation of protein kinase. Epinephrine stimulates glycogen breakdown in these cells mainly by mechanisms involving alpha-adrenergic receptors and not beta-receptors. Activition of alpha-receptors results in rapid activation of phosphorylase and inactivation of glycogen synthase without accumulation of cAMP or activation of cAMP-dependent protein kinase. Activation of beta-receptors causes a transient rise in cAMP and a short-lived activation of protein kinase with correspondingly little stimulation of glycogenolysis.

MeSH Terms (11)

Animals Cyclic AMP Dose-Response Relationship, Drug Epinephrine Glucagon Liver Glycogen Phenylephrine Phosphorylases Protein Kinases Rats Receptors, Adrenergic

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