The hormonal control of glycogen metabolism. Phosphorylation of protein phosphatase inhibitor-1 in vivo in response to adrenaline.
Inhibitor-1 has been shown to be phosphorylated in skeletal muscle in vivo. In normal fed animals the degree of phosphorylation was 31 +/- 7% and this value increases to 70 +/- 12% following an intravenous injection of adrenaline. The results imply that the phosphorylation of inhibitor-1 may be equally as important as the phosphorylation of phosphorylase kinase in elevating the levels of phosphorylase a. The role of inhibitor-1 in metabolism is discussed.
D000818:Animals; D004837:Epinephrine / Q000494:pharmacology*; D006003:Glycogen / Q000378:metabolism*; D047908:Intracellular Signaling Peptides and Proteins; D007700:Kinetics; D009124:Muscle Proteins / Q000302:isolation & purification / Q000502:physiology*; D009132:Muscles / Q000187:drug effects / Q000201:enzymology*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010764:Phosphorylase Kinase / Q000378:metabolism; D010762:Phosphorylase a / Q000378:metabolism; D010763:Phosphorylase b / Q000378:metabolism; D010766:Phosphorylation; D011817:Rabbits
D047908:Intracellular Signaling Peptides and Proteins; D009124:Muscle Proteins; C021042:protein phosphatase inhibitor-1; D006003:Glycogen; D010762:Phosphorylase a; D010763:Phosphorylase b; D010764:Phosphorylase Kinase; D010749:Phosphoprotein Phosphatases; D004837:Epinephrine