Epinephrine and glucagon counteract inhibition of protein synthesis induced by D-galactosamine in isolated mouse hepatocytes.
10 mM D-galactosamine enhibited protein synthesis (1 h incubation time) by 67% in isolated mouse liver cells. Counteracting uridylate deficiency induced by D-galactosamine by preventive administration of 20 mM uridine did not decrease the extent of protein synthesis inhibition. 20 mM D-galactose reverted the inhibition of protein synthesis by D-galactosamine. 10(-5) M epinephrine and 10(-7) M glucagon decreased the incorporation of D-galactosamine into glycogen to 38% and 26% of the control value, respectively, after a 35 min incubation and reduced the inhibition of protein synthesis by D-galactosamine effectively. Experimental evidence supports the view that aminoglycogen formed after D-galactosamine treatment is responsible for the inhibition of protein synthesis.
D000606:Amino Sugars / Q000096:biosynthesis; D000818:Animals; D004837:Epinephrine / Q000494:pharmacology*; D005688:Galactosamine / Q000494:pharmacology*; D005934:Glucagon / Q000494:pharmacology*; D008099:Liver / Q000187:drug effects / Q000378:metabolism; D008112:Liver Glycogen / Q000096:biosynthesis; D051379:Mice; D014176:Protein Biosynthesis
D000606:Amino Sugars; D008112:Liver Glycogen; C020970:aminoglycogen; D005688:Galactosamine; D005934:Glucagon; D004837:Epinephrine