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

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 rev...

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Published inBiochimica et biophysica acta Vol. 586; no. 3; pp. 560 - 567
Main Authors Mandl, J., Garzó, T., Mészáros, K., Antoni, F.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 03.09.1979
Subjects
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ISSN0304-4165
0006-3002
1872-8006
DOI10.1016/0304-4165(79)90046-1

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Abstract 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.
AbstractList 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.
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.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.
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.
Author Garzó, T.
Mandl, J.
Antoni, F.
Mészáros, K.
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Snippet 10 mM d-galactosamine inhibited protein synthesis (1 h incubation time) by 67% in isolated mouse liver cells. Counteracting uridylate deficiency induced by...
10 mM D-galactosamine enhibited protein synthesis (1 h incubation time) by 67% in isolated mouse liver cells. Counteracting uridylate deficiency induced by...
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SubjectTerms Amino Sugars - biosynthesis
Animals
Epinephrine - pharmacology
Galactosamine - pharmacology
Glucagon - pharmacology
Liver - drug effects
Liver - metabolism
Liver Glycogen - biosynthesis
Mice
Protein Biosynthesis
Title Epinephrine and glucagon counteract inhibition of protein synthesis induced by d-galactosamine in isolated mouse hepatocytes
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