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1 Department of Medicine, VA Healthcare Connecticut, West Haven, CT, USA
2 Department of Medicine, Yale University School of Medicine, New Haven, CT, USA
3 Department of Medicine, VA Healthcare Connecticut, West Haven, CT, USA; Department of Medicine, Yale University School of Medicine, New Haven, CT, USA
* To whom correspondence should be addressed. E-mail: fred.Gorelick{at}yale.edu.
The pathologic activation of proteases within the pancreatic acinar cell is critical to initiating pancreatitis. Stimulation of acinar cells with supraphysiologic concentrations of the cholecystokinin (CCK) analogue, caerulein (CER) leads to protease activation and pancreatitis. Agents that sensitize the acinar cell to the effects of CCK might contribute to disease. The effects of physiologic ligands that increase acinar cell cAMP [secretin, vasoactive intestinal polypeptide (VIP), and pituitary adenylate cyclase activating peptide (PACAP)] on CER-induced responses were examined in isolated rat pancreatic acini. Each ligand sensitized the acinar cell to zymogen activation by physiologic concentrations of CER [0.1nM]. VIP and PACAP, but not secretin, also enhanced activation by supraphysiologic concentrations of CER [0.1 µM]. A cell permeable cAMP analogue also sensitized the acinar cell to CER-induced activation. The cAMP antagonist Rp-8-Br-cAMP inhibited these sensitizing effects. These findings suggest that ligands that increase acinar cell cAMP levels can sensitize the acinar cell to the effects of CCK-induced zymogen activation.
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