Prostaglandin e analogue inhibition of pancreatic enzyme secretion

Karl A. Zucker, Anton J. Bilchik, Irvin M. Modlin, Thomas E. Adrian

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


The effect of native prostaglandins and their methylated analogues on pancreatic enzyme secretion remains unclear, with previous studies reporting inconsistent results. To determine whether the E series prostaglandins directly influence pancreatic secretion, we studied the effect of rioprostil, a prostaglandin Ej analogue, and 16,16-dimethyl prostaglandin E2 (DMPGE2), a prostaglandin E2 analogue, on enzyme release from dispersed guinea pig pancreatic acini. Basal amylase release (4.3 ± 0.6% of total acinar content) was not altered by either analogue (10-10-10-5M). A 50% inhibition of maximal cholecystokinin stimulation (10-9M; 28.8 ± 1.2%) was seen with rioprostil (10-7M; 14.6 ± 1.3%) and DMPGE2(10“6 M; 15.9 ± 0.7%) (both p < 0.005). Prostaglandin inhibition of carbachol-stimulated amylase was less pronounced. The most effective inhibitory dosage with maximal carbachol (10-5M; 30.2 ± 1.9%) was 10-6M for both rioprostil (19.2 ± 1.6%) and DMPGE2(22.4 ± 1.7%) (both p < 0.005). Incubation of acini with A23187, phorbol ester, and l-oleoyl-2-acetyl-glycerol resulted in a dose-dependent increase in amylase release that was not altered by maximal concentrations of either prostaglandin analogue. Our results indicate that rioprostil and DMPGE2 can directly inhibit pancreatic acinar secretion. This effect appears to occur before activation of the inositol phospholipid system.

Original languageEnglish
Pages (from-to)708-714
Number of pages7
Issue number6
Publication statusPublished - Dec 1989
Externally publishedYes


  • Inositol phospholipids
  • Pancreatic acini
  • Prostaglandins

ASJC Scopus subject areas

  • Internal Medicine
  • Endocrinology, Diabetes and Metabolism
  • Hepatology
  • Endocrinology


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