Characterization of cAMP-dependent protein kinase activation by CCK in rat pancreas

Christopher R. Marino, Steven D. Leach, Jean F. Schaefer, Laurence J. Miller, Fred S. Gorelick

Research output: Contribution to journalArticlepeer-review

34 Scopus citations


This study reports on the use of a new sensitive assay of cAMP-dependent protein kinase activity to examine the effect of cholecystokinin (CCK) on the cAMP second messenger cascade in rat pancreatic acini. Treatment of acini with both low (pM) and high (nM) concentrations of CCK was associated with an increase in cAMP-dependent protein kinase activity. The increases in kinase activity were detected in the absence of phosphodiesterase inhibition, a condition required to detect a measurable increase in cellular cAMP in these cells. Furthermore, the cAMP cascade was dissociated from the secretory effects of CCK, since the CCK analogue, OPE, mediates enzyme secretion but does not increase cellular cAMP levels or kinase activity.

Original languageEnglish (US)
Pages (from-to)48-52
Number of pages5
JournalFEBS Letters
Issue number1
StatePublished - Jan 18 1993


  • Adenosine 3′,5′ cyclic monophosphate
  • CCK receptor
  • Cholecystokinin
  • Pancreatic acini
  • Phosphodiesterase inhibitor
  • Protein kinase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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