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 in | Biochimica et biophysica acta Vol. 586; no. 3; pp. 560 - 567 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
03.09.1979
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Subjects | |
Online Access | Get full text |
ISSN | 0304-4165 0006-3002 1872-8006 |
DOI | 10.1016/0304-4165(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. |
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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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