Role of Cyclic Adenosine 3',5'-Monophosphate in the Induction of Hepatic Enzymes

Abstract

Serine dehydratase formation was induced by cyclic 3',5'-AMP and not by other cyclic nucleotides or adenosine monophosphates. A single injection of cyclic 3',5'-AMP (or its dibutyryl derivative) increased the rate of incorporation of 3H-leucine into serine dehydratase. Under the same experimental conditions the rate of synthesis of serum albumin did not change. A single administration of either glucagon or a mixture of amino acids (also an inducer of serine dehydratase) led, within 20 min, to a 40-fold and a 19-fold increase, respectively, in the concentration of cyclic 3',5'-AMP. The concentration of this nucleotide dropped to the original level within 1 hour after the beginning of the inducer administration. The induction of serine dehydratase by N6,O2'-dibutyryl cyclic 3',5'-AMP was fully inhibited by actinomycin D only if the drug was injected 30 to 15 min prior to the injection of the cyclic nucleotide. The uptake of 3H-dibutyryl cyclic 3',5'-AMP by the liver was not inhibited by actinomycin D.