Adrenal glucocorticoid permissive regulation of muscle glycogenolysis: action on protein phosphatase(s) and its inhibitor(s).
Adrenal glucocorticoids exert a permissive action on the glycogen phosphorylase cascade. Epinephrine activation of muscle phosphorylase and phosphorylase b kinase is depressed in adrenalectomized rats. Phosphorylase phosphatase activity is increased by steroid lack, and normal epinephrine inhibition of the enzyme does not occur. Phosphorylase b kinase phosphatase activity is also increased; epinephrine, however, does not inhibit activity in muscle from normal or adrenalectomized rats. Protein phosphatase inhibitor activity is depressed in boiled dialyzed preparations made from adrenalectomized rat muscle. Cortisol resplacement therapy restores protein phosphatase inhibitor activity, decreases increased protein phosphatase activity, and restores normal epinephrine-induced activation of phosphorylase b kinase and phosphorylase and epinephrine inhibition of phosphorylase phosphatase.
D000315:Adrenalectomy; D000818:Animals; D004837:Epinephrine / Q000494:pharmacology; D006003:Glycogen / Q000378:metabolism*; D006854:Hydrocortisone / Q000494:pharmacology*; D008297:Male; D009132:Muscles / Q000187:drug effects / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010764:Phosphorylase Kinase / Q000378:metabolism; D010765:Phosphorylase Phosphatase / Q000037:antagonists & inhibitors / Q000378:metabolism; D010762:Phosphorylase a / Q000378:metabolism; D051381:Rats
D006003:Glycogen; D010762:Phosphorylase a; D010764:Phosphorylase Kinase; D010749:Phosphoprotein Phosphatases; D010765:Phosphorylase Phosphatase; D006854:Hydrocortisone; D004837:Epinephrine