Islet amyloid polypeptide has no effect on amylase release from rat pancreatic acini stimulated by CCK-8, secretin, carbachol and VIP

Tohoku J Exp Med. 1991 Sep;165(1):41-8. doi: 10.1620/tjem.165.41.

Abstract

Islet amyloid polypeptide (IAPP), a novel peptide recently isolated from the amyloid substance of pancreatic islets, has been localized in normal islet B cell granules, suggesting its physiological action in exocrine pancreatic function. In the present study, the direct effect of IAPP on secretagogue-stimulated pancreatic enzyme secretion was investigated using dispersed rat pancreatic acini. Various concentrations of IAPP (10(-5) -10(-10) M) showed no significant influence on amylase release stimulated either by submaximal doses of CCK-8 (10(-11) M), secretin (0.5 x 10(-6) M) or carbachol (10(-6) M), or by a maximal dose of vasoactive intestinal peptide (10(-8) M). These results may provide negative evidence for a physiological significance of IAPP in rat pancreatic enzyme secretion.

MeSH terms

  • Amylases / metabolism*
  • Amyloid / pharmacology*
  • Animals
  • Carbachol / pharmacology
  • In Vitro Techniques
  • Islet Amyloid Polypeptide
  • Male
  • Pancreas / drug effects*
  • Pancreas / enzymology*
  • Rats
  • Rats, Inbred Strains
  • Secretin / pharmacology
  • Sincalide / pharmacology
  • Vasoactive Intestinal Peptide / pharmacology

Substances

  • Amyloid
  • Islet Amyloid Polypeptide
  • Secretin
  • Vasoactive Intestinal Peptide
  • Carbachol
  • Amylases
  • Sincalide