Enzyme secretion in mouse pancreas mediated by adenosine-3'5'-cyclic phosphate and inhibited by adenosine-3'-phosphate.

A number of hormones and neurohormones have been shown to exert their effect on their target tissues by altering the intracellular level of 3'5'-cyelic AM\IP.1 Among the processes mediated by cyclic AMP is the secretion of macromolecules by various endocrine and exocrine glands.2-5 Of particular interest to investigators studying the exocrine pancreas was the observation of Schramm and his co-workers2' 3that cyclic AMP is an intermediate in the stimulation of parotid secretion by epinephrine. In view of the close morphological and functional resemblance between the parotid gland and the exocrine pancreas, it seemed likely that secretion by the latter, like that by the former, was mediated by cyclic AMP. The present communication shows that secretion by mouse pancreas, which is stimulated by pancreozymin, a gastrin analogue and carbamyl choline, is indeed mediated by cyclic AMP. Furthermore, it is shown that 3'AMIP inhibits secretion, probably by competing with cyclic AMP for its receptor site in the pancreas.