SECRETIN POTENTIATES CHOLECYSTOKININ-STIMULATED AMYLASE RELEASE BY AR4-2J CELLS VIA A STIMULATION OF PHOSPHOLIPASE-C

Alterations in the activity of phospholipase C (PLC) are thought to be the primary intracellular events leading to pancreatic acinar cell ex ocytosis of zymogen granules. When multiple hormones, each of which ma y stimulate different signal transduction pathways, bind to cell surfa ce receptors, the cell must integrate these signals into a common resp onse through communication (cross-talk) among intracellular second mes sengers. We show that cholecystokinin (CCK) induces amylase secretion from AR4-2J pancreatic acinar cells via stimulation of PLC activity. S ecretin indirectly stimulated the PLC pathway through cross-talk of th e activated cAMP pathway to potentiate the CCK-stimulated amylase secr etion. Therefore, secretin potentiated the acinar cell secretory respo nse to CCK by cAMP-mediated cross-talk with the PLC signal transductio n pathway. (C) 1995 Wiley-Liss, Inc.