Secretin potentiates cholecystokinin-stimulated amylase release by AR4-2J cells via a stimulation of phospholipase C

Richard J Bold, Jin Ishizuka, Courtney M. Townsend, James C. Thompson

Research output: Contribution to journalArticle

11 Scopus citations


Alterations in the activity of phospholipase C (PLC) are thought to be the primary intracellular events leading to pancreatic acinar cell exocytosis of zymogen granules. When multiple hormones, each of which may stimulate different signal transduction pathways, bind to cell surface receptors, the cell must integrate these signals into a common response through communication (cross-talk) among intracellular second messengers. We show that cholecystokinin (CCK) induces amylase secretion from AR4-2J pancreatic acinar cells via stimulation of PLC activity. Secretin indirectly stimulated the PLC pathway through cross-talk of the activated cAMP pathway to potentiate the CCK-stimulated amylase secretion. Therefore, secretin potentiated the acinar cell secretory response to CCK by cAMP-mediated cross-talk with the PLC signal transduction pathway.

Original languageEnglish (US)
Pages (from-to)172-176
Number of pages5
JournalJournal of Cellular Physiology
Issue number1
StatePublished - Oct 1995


ASJC Scopus subject areas

  • Clinical Biochemistry
  • Cell Biology
  • Physiology

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