Are endogenous glucocorticoids involved in short-term regulation of hepatic glycogen metabolism?
The release of endogenous corticosterone was stimulated by intraperitoneal administration of ACTH to conscious rats. Corticosterone had no reproducible stimulatory effect either on the activation of synthase or inactivation of phosphorylase. On the other hand, an induction of the synthesis of total synthase enzyme protein was observed which could be blocked by actinomycin D. In Sephadex-filtered liver homogenates, a particularly impaired pattern of phosphorylase inactivation/synthase activation was observed during incubation at 20 degrees C in the ACTH-treated rats.
D000324:Adrenocorticotropic Hormone / Q000494:pharmacology*; D000818:Animals; D003345:Corticosterone / Q000502:physiology*; D006006:Glycogen Synthase / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000187:drug effects / Q000201:enzymology; D008112:Liver Glycogen / Q000378:metabolism*; D008297:Male; D010762:Phosphorylase a / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains
D008112:Liver Glycogen; D000324:Adrenocorticotropic Hormone; D010762:Phosphorylase a; D006006:Glycogen Synthase; D003345:Corticosterone