The increase in hepatic tyrosine aminotransferase activity by ethanol administration involves an acceleration of enzyme synthesis.
The present study was conducted to examine the nature of the increase in tyrosine aminotransferase (TAT) activity by acute ethanol administration. A significant rise in aminotransferase activity was observed as early as 1 hr after intact rats were gavaged with ethanol. Ethanol administration also increased TAT activity in adrenalectomized rats. Inhibition of ethanol metabolism by pyrazole administration had no effect on the ethanol-induced increase in TAT activity. Immunochemical analyses revealed that the enhancement of TAT activity in ethanol-fed rats correlated with an increase in aminotransferase protein. Measurement of the rate of TAT synthesis showed that in ethanol-fed rats, [3H]leucine was incorporated into the aminotransferase protein at a higher rate than in controls by a factor which was similar to the enhancement in enzyme activity. Our findings indicate that an acceleration of TAT synthesis fully accounts for the increase in TAT activity during the early stage of enzyme induction. TAT induction by ethanol administration is not dependent upon an increase in adrenal corticosteroid production, nor does it require ethanol metabolism.
D000818:Animals; D004790:Enzyme Induction; D000431:Ethanol / Q000494:pharmacology*; D005947:Glucose / Q000494:pharmacology; D008099:Liver / Q000201:enzymology*; D008297:Male; D011720:Pyrazoles / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D014444:Tyrosine Transaminase / Q000096:biosynthesis*
D011720:Pyrazoles; D000431:Ethanol; C031280:pyrazole; D014444:Tyrosine Transaminase; D005947:Glucose