Forskolin potentiates calcium-dependent amylase secretion from rat pancreatic acinar cells

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Abstract
The cellular and molecular effects of forskolin, a direct, nonhormonal activator of adenylate cyclase, were assessed on the enzyme secretory process in dispersed rat pancreatic acinar cells. Forskolin stimulated adenylate cyclase activity in the absence of guanyl nucleotide. It promoted a rapid and marked increase in cellular accumulation of cAMP alone or in combination with vasoactive intestinal peptide (VIP) but was itself a weak pancreatic agonist and did not increase the secretory response to VIP or other cAMP dependent agonists. Somatostatin was a partial antagonist of forskolin stimulated cAMP synthesis and forskolin plus cholecystokinin-octapeptide (CCK-OP) induced amylase release. Forskolin potentiated amylase secretion in response to Ca-dependent agonists such as CCK-OP, carbachol and A-23187, but did not affect the ability of CCK-OP and (or) carbachol to mobilize 45Ca from isotope preloaded cells; forskolin alone did not stimulate 45Ca release. In Ca-poor media, the secretory response to forskolin and CCK-OP was reduced in a absolute and relative manner. Ca may play the primary role as intracellular mediator of enzyme secretion, and the role of cAMP may be to modulate the efficiency of Ca utilization.

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