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Regulation of hepatic tyrosine amino transferase ec 2.6.1.5


, : Regulation of hepatic tyrosine amino transferase ec 2.6.1.5. Biochimica et Biophysica Acta 677(3-4): 433-444

Tyrosine aminotransferase induction was studied in hepatocytes from untreated, partially and fully glucocorticoid[dexamethasone]-induced rats: enzyme activities were initially 12.9 .+-. 1.7 (n = 16), 41.4 .+-. 3.2 (n = 6) and 117.9 .+-. 10.5 (n = 7) mU/mg protein, respectively. Untreated or fully induced hepatocytes maintain initial levels, whereas partially induced hepatocytes increase their tyrosine aminotransferase activity even in the presence of actinomycin D. Fully induced hepatocytes possess a normal protein synthesizing machinery and the mechanisms to degrade selectively tyrosine aminotransferase. The effect of progesterone treatment is consistent with these cells retaining a high dexamethasone level. Glucagon induces tyrosine aminotransferase via its 2nd messenger, cAMP. This induction decreases dramatically with in vivo glucocorticoid treatment. Time courses and effects of inhibitors are consistent with these in vivo and in vitro treatments being alternative methods of inducing tyrosine aminotransferase by the same basic pretranslational step.

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