Epinephrine and glucagon counteract inhibition of protein synthesis induced by d-galactosamine in isolated mouse hepatocytes

• Published in: Biochimica et biophysica acta Vol. 586; no. 3; pp. 560 - 567
• Main Authors: Mandl, J., Garzó, T., Mészáros, K., Antoni, F.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 03.09.1979
• Subjects: Amino Sugars - biosynthesis; Animals; Epinephrine - pharmacology; Galactosamine - pharmacology; Glucagon - pharmacology; Liver - drug effects; Liver - metabolism; Liver Glycogen - biosynthesis; Mice; Protein Biosynthesis
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/0304-4165(79)90046-1

10 mM d-galactosamine inhibited 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 −5M 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-glactosamine effectively. Experimental evidence supports the view that aminoglycogen formed after d-galactosamine treatment is responsible for the inhibition of protein synthesis.