The effect of insulin on the glycogenolytic cascade and on the activity of glycogen synthase in the liver of anaesthetized rabbits.
1. The administration of insulin to anaesthetized rabbits caused the inactivation of liver phosphorylase and phosphorylase kinase, but did not change either the hepatic concentration of cyclic AMP or the activity of cyclic AMP-dependent histone kinase. All measured parameters were increased by the subsequent administration of glucagon. 2. Activation of glycogen synthase by insulin was only observed when phosphorylase had been strongly inactivated.
D000818:Animals; D000242:Cyclic AMP / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D005934:Glucagon / Q000494:pharmacology; D006006:Glycogen Synthase / Q000378:metabolism*; D007328:Insulin / Q000494:pharmacology*; D008099:Liver / Q000187:drug effects* / Q000201:enzymology / Q000378:metabolism; D008297:Male; D010764:Phosphorylase Kinase / Q000378:metabolism; D006005:Phosphorylases / Q000378:metabolism; D006656:Protamine Kinase / Q000378:metabolism; D011817:Rabbits
D007328:Insulin; D005934:Glucagon; D000242:Cyclic AMP; D006005:Phosphorylases; D006006:Glycogen Synthase; D010764:Phosphorylase Kinase; D006656:Protamine Kinase