In vitro action of bombesin and bombesin-like peptides on amylase secretion, calcium efflux, and adenylate cyclase activity in the rat pancreas: a comparison with other secretagogues

J Clin Invest. 1976 Oct;58(4):891-8. doi: 10.1172/JCI108542.


Bombesin (a tetradecapeptide), the C-terminal nonapeptide of bombesin (bombesin-NP), and litorin (a parent nonapeptide), each stimulated amylase secretion from rat pancreatic fragments. These responses were not affected by atropine. The concentrations that produced half-maximal stumulation of secretion were 0.25 nM for bombesin, 0.30 nM for bombesin-NP, and 0.07 nM for litorin, as compared to 0.12 nM for caerulein and 0.80 muM for the cholinergic agent carbamylcholine. When used at maximal concentrations, bombesin, bombesin-NP, and litorin showed no action on cyclic AMP levels in the presence of 5 mM theophylline. By contrast, caerulein and secretin increased cyclic AMP levels by 27 and 208%, respectively. Bombesin, bombesin-NP, and litorin did not activate adenylate cyclase in a purified pancreatic plasma membrane preparation, whereas caerulein and secretin increased this activity 20 and 16-times, respectively...

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenylyl Cyclases / metabolism*
  • Amylases / metabolism*
  • Animals
  • Bombesin / pharmacology*
  • Calcium / metabolism*
  • Ceruletide / pharmacology
  • Cyclic AMP / metabolism
  • In Vitro Techniques
  • Male
  • Oligopeptides / pharmacology*
  • Pancreas / enzymology
  • Pancreas / metabolism*
  • Peptides / pharmacology*
  • Rats


  • Oligopeptides
  • Peptides
  • litorin
  • Ceruletide
  • Cyclic AMP
  • Amylases
  • Adenylyl Cyclases
  • Bombesin
  • Calcium