Reversible acetaldehyde inhibition of A23187-stimulated amylase secretion from isolated rat pancreatic acini
- 20 May 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 184 (2) , 259-262
- https://doi.org/10.1016/0014-5793(85)80618-9
Abstract
The Ca2+ ionophore, A23187, stimulated amylase secretion from isolated rat pancreatic acini in a dosedependent manner with a maximal effect at 6 μM. Acetaldehyde, a metabolite of ethanol, caused a reduction in the magnitude of ionophore-stimulated secretion with no evidence of competitive inhibition. Furthermore, 6 μM ionophore-stimulated amylase secretion was dose-dependently inhibited by acetaldehyde. This inhibitory effect of acetaldehyde, however, was reversible on washing and reincubating acetaldehyde-treated acini. These results suggest that acetaldehyde reversibly inhibits intracellular components mediating stimulated secretion and this inhibition requires a continuous chemical interaction between acetaldehyde and intracellular component(s) regulating stimulated enzyme secretionKeywords
This publication has 6 references indexed in Scilit:
- Effect of ethanol on cholecystokinin-induced enzyme secretion from isolated rat pancreatic aciniBiochemical Pharmacology, 1984
- Effect of ionophore A23187 on cytosolic Ca2+ and enzyme secretionAmerican Journal of Physiology-Cell Physiology, 1982
- Preparation and application of Procion Yellow Starch for amylase assayClinica Chimica Acta; International Journal of Clinical Chemistry, 1980
- Regulation of Pancreatic Exocrine Function In Vitro: Initial Steps in the Actions of SecretagoguesAnnual Review of Physiology, 1979
- Control of pancreatic enzyme secretion: A critique on the role of calciumLife Sciences, 1978
- Cellular cyclic nucleotides and enzyme secretion in the pancreatic acinar cell.Proceedings of the National Academy of Sciences, 1976