Glucagon-like peptide-1 does not mediate amylase release from AR42J cells

J Cell Physiol. 1999 Dec;181(3):470-8. doi: 10.1002/(SICI)1097-4652(199912)181:3<470::AID-JCP11>3.0.CO;2-P.


In this study, AR42J pancreatic acinar cells were used to investigate if glucagon-like peptide-1 (GLP-1) or glucagon might influence amylase release and acinar cell function. We first confirmed the presence of GLP-1 receptors on AR42J cells by reverse trasncriptase-polymerase chain reaction (RT-PCR), Western blotting, and partial sequencing analysis. While cholecystokinin (CCK) increased amylase release from AR42J cells, GLP-1, alone or in the presence of CCK, had no effect on amylase release but both CCK and GLP-1 increased intracellular calcium. Similar to GLP-1, glucagon increased both cyclic adenosine monophosphate (cAMP) and intracellular calcium in AR42J cells but it actually decreased CCK-mediated amylase release (n = 20, P < 0.01). CCK stimulation resulted in an increase in tyrosine phosphorylation of several cellular proteins, unlike GLP-1 treatment, where no such increased phosphorylation was seen. Instead, GLP-1 decreased such protein phosphorylations. Genestein blocked CCK-induced phosphorylation events and amylase secretion while vanadate increased amylase secretion. These results provide evidence that tyrosine phosphorylation is necessary for amylase release and that signaling through GLP-1 receptors does not mediate amylase release in AR42J cells. J. Cell. Physiol. 181:470-478, 1999. Published 1999 Wiley-Liss, Inc.

MeSH terms

  • 8-Bromo Cyclic Adenosine Monophosphate / pharmacology
  • Amylases / metabolism*
  • Animals
  • Base Sequence
  • Calcium Signaling / drug effects
  • Cell Line
  • Cholecystokinin / pharmacology
  • Cyclic AMP / metabolism
  • DNA Primers / genetics
  • Glucagon / pharmacology*
  • Glucagon / physiology
  • Glucagon-Like Peptide 1
  • Glucagon-Like Peptide-1 Receptor
  • Pancreas / cytology
  • Pancreas / drug effects
  • Pancreas / physiology
  • Peptide Fragments / pharmacology*
  • Peptide Fragments / physiology
  • Phosphorylation
  • Protein Precursors / pharmacology*
  • Protein Precursors / physiology
  • Rats
  • Receptors, Glucagon / genetics
  • Receptors, Glucagon / metabolism
  • Reverse Transcriptase Polymerase Chain Reaction
  • Tyrosine / metabolism


  • DNA Primers
  • Glp1r protein, rat
  • Glucagon-Like Peptide-1 Receptor
  • Peptide Fragments
  • Protein Precursors
  • Receptors, Glucagon
  • 8-Bromo Cyclic Adenosine Monophosphate
  • Tyrosine
  • Glucagon-Like Peptide 1
  • Glucagon
  • Cholecystokinin
  • Cyclic AMP
  • Amylases