Role of glucagon in increase of hepatic glycerate kinase of adult and neonatal rats.
An increase of rat liver glycerate kinase [ATP: D-glycerate 2-phosphotransferase EC 2.7.1.31] on protein feeding, on starvation or during fetal and neonatal development was studied from the viewpoint of the role of glucagon as the mediator. On starvation and during fetal and neonatal development, glycerate kinase in the cytosolic and mitochondrial fractions increased approximately in the same ratio. Glucagon in plasma increased under these conditions and glucagon administration increased glycerate kinase in both intracellular fractions approximately in the same ratio. The above results suggested that glucagon functions as at least one of the mediators for these processes. In diabetic rats, only a slight increase of the enzyme in both intracellular fractions was observed. Protein feeding, however, strongly increased the mitochondrial enzyme. Glucagon failed to mediate this function of dietary protein for the mitochondrial enzyme.
D000367:Age Factors; D000818:Animals; D003994:Bucladesine / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology; D003921:Diabetes Mellitus, Experimental / Q000201:enzymology; D005934:Glucagon / Q000502:physiology*; D005943:Gluconeogenesis; D008099:Liver / Q000201:enzymology*; D008928:Mitochondria / Q000201:enzymology; D010770:Phosphotransferases / Q000378:metabolism*; D017853:Phosphotransferases (Alcohol Group Acceptor); D051381:Rats; D014221:Triamcinolone / Q000494:pharmacology
D014221:Triamcinolone; D003994:Bucladesine; D005934:Glucagon; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C020670:glycerate kinase