Egf inhibits secretagogue-induced camp production and amylase secretion by pertussis toxin-sensitive g proteins in pancreatic acini. Stryjek-Kaminska, Danuta, Albrecht Piiper, and Stefan Zeuzem. Medical Department (Dir.: Prof. Dr. W.F. Caspary), University of Frankfurt/Main, 60590 Frankfurt, Germany
APStracts 2:0108G, 1995.
In pancreatic acinar cells the epidermal growth factor (EGF) receptor interacts with both cholera toxin- and pertussis toxin-sensitive G proteins. In the present study isolated rat pancreatic acini were used to investigate the effect of EGF on basal and secretagogue -induced cAMP production and amylase release. EGF increased cAMP production and amylase release in pancreatic acini. However, cAMP accumulation and amylase release elicited by either vasoactive intestinal peptide (VIP) or forskolin was inhibited by EGF (17 nM). EGF inhibited the VIP-induced cAMP production and amylase release with EC50 of 3 and 2 nM, respectively. EGF had no effect on the N6,2'-O-dibutyryladenosine 3',5'-monophosphate (dbcAMP)-stimulated amylase release, suggesting that the inhibitory effect of EGF on the VIP- and forskolin-induced cAMP production is due to inhibition of adenylyl cyclase. Pertussis toxin-pretreatment of the acini led to an increase of the basal, EGF- and VIP-stimulated cAMP accumulation and amylase release, indicating that pertussis toxin-sensitive G proteins exert tonic inhibition of adenylyl cyclase even in the absence of agonist. In pertussis toxin-pretreated acini the inhibitory effect of EGF on the VIP-induced cAMP production and amylase release was abolished. In conclusion these results suggest that EGF inhibits secretagogue-induced cAMP production via activation of pertussis toxin-sensitive G proteins in rat pancreatic acini, whereas EGF -induced cAMP production and amylase release occurs via a pertussis toxin-insensitive pathway.

Received 31 October 1994; accepted in final form 9 May 1995.
APS Manuscript Number G438-4.
Article publication pending Am. J. Physiol. (Gastrointest. Liver
Physiology).
ISSN 1080-4757 Copyright 1995 The American Physiological Society.
Published in APStracts on  8 June 1995.