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Am J Physiol Gastrointest Liver Physiol 279: G295-G303, 2000;
0193-1857/00 $5.00
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Vol. 279, Issue 2, G295-G303, August 2000

Cellular mechanism of sodium oleate-stimulated secretion of cholecystokinin and secretin

Cecilia H. Chang, William Y. Chey, and Ta-Min Chang

Konar Center for Digestive and Liver Diseases, Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642

Long-chain fatty acids are potent stimulants of secretin and CCK release. The cellular mechanisms of fatty acid-stimulated secretion of these two hormones are not clear. We studied the stimulatory effect and mechanism of sodium oleate (SO) on secretin- and CCK-producing cells. SO stimulated the release of secretin or CCK from isolated rat mucosal cell preparations enriched in either secretin- or CCK-producing cells, respectively. SO also time- and dose-dependently stimulated secretin and CCK release from STC-1 cells. In STC-1 cells, SO-stimulated secretin and CCK release was potentiated by IBMX and inhibited by a protein kinase A-selective inhibitor and a cAMP-specific antagonist. SO-stimulated releases of the two hormones were also inhibited by downregulation or inhibitors of protein kinase C, a calmodulin antagonist and an inhibitor of calmodulin-dependent protein kinase II. Chelating of extracellular Ca2+ or addition of an L-type calcium channel blocker diminished SO-stimulated hormone releases. SO caused an increase in intracellular Ca2+ concentration that was partially reversed by diltiazem but had no effect on production of cAMP, cGMP, or inositol-1,4,5-triphosphate. These results indicate that SO acts on secretin- and CCK-producing cells. Its stimulatory effect is potentiated by endogenous protein kinase A and mediated by activation of Ca2+ influx through the L-type channels and of protein kinase C and Ca2+/calmodulin-dependent protein kinase II.

intracellular calcium; protein kinases; calmodulin; STC-1 cells


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