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Am J Physiol Gastrointest Liver Physiol 279: G605-G612, 2000;
0193-1857/00 $5.00
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Vol. 279, Issue 3, G605-G612, September 2000

Control of CCK gene transcription by PACAP in STC-1 cells

Damian G. Deavall1, Raktima Raychowdhury2, Graham J. Dockray1, and Rod Dimaline1

1 Physiological Laboratory, University of Liverpool, Liverpool L69 3BX, United Kingdom; and 2 Massachusetts General Hospital, Boston, Massachusetts 02114

The mechanisms by which neuroendocrine stimulants regulate CCK gene transcription are unclear. We examined promoter activation by pituitary adenylate cyclase-activating polypeptide (PACAP), a known CCK secretagogue, in the enteroendocrine cell line STC-1. The promoter region from -70 to -87 bp, relative to the transcriptional start site, contains a composite calcium/cyclic AMP response element (CRE)/activator protein 1 (AP1) site that may bind CRE binding protein (CREB) and AP1. PACAP (with IBMX) stimulated expression of an 87-bp construct 3.35 ± 0.36-fold but had no effect on a -70 construct. The effect was blocked by the protein kinase A inhibitor H-89 and by a dominant-negative CREB plasmid. Mutation of the CRE/AP1 site to a canonical CRE site did not affect the response to PACAP, but mutation to a canonical AP1 site prevented it. CREB phosphorylation was increased after PACAP treatment. Electrophoretic mobility shift assay and supershift analysis revealed that CREB and not AP1 bound to the CRE/AP1 site and that PACAP increased the proportion of phosphorylated CREB that was bound. We conclude that PACAP increases CCK gene expression via a cAMP-mediated pathway involving CREB phosphorylation by protein kinase A and activation of a composite CRE/AP1 site.

cholecystokinin; pituitary adenylate cyclase-activating polypeptide; calcium/cyclic AMP response element; calcium/3,5'-monophosphate response element binding protein; adenosine 3',5'-cyclic monophosphate


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