Effect of CDP-choline on the action of cholecystokinin and carbachol to stimulate amylase secretion from dispersed rat pancreatic acini.

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The effect of CDP-choline, a potent inhibitor of phospholipase A2 (PLA2), on cholecsytokinin (CCK) and carbachol-induced amylase secretion from dispersed rat pancreatic acini was examined. Amylase secretion stimulated by CCK-8 or carbachol increased with increasing concentrations, became maximal at the concentration of 0.1nM CCK-8 or 3μM carbachol respectively, and decreased with further increasing concentrations of secretagogues. CDP-choline inhibited selectively the amylase secretion stimulated by submaximal concentrations of CCK-8 (up to 3nM) or carbachol (up to 10μM) but not by supramaximal concentrations of CCK-8 or carbachol. CDP-choline neither affected the binding of 125I-CCK to its receptors on pancreatic acini nor influenced calcium outflux stimulated by CCK-8.These results indicate that CDP-choline inhibit CCK and carbachol-induced amylase secretions by eliminating subsequent activation of intracellular mechanisms to receptor bindings of secretagogues. Since CDP-choline has been known to a potent inhibitor of PLA2, it seems likely that activation of membrane PL2 will be involved in the action of CCK and carbachol.
財団法人日本消化器病学会の論文