TY - JOUR
T1 - Irreversible inhibition by acetaldehyde of cholecystokinin-induced amylase secretion from isolated rat pancreatic acini
AU - Sankaran, Hariharan
AU - Lewin, Mark B.
AU - Wong, Anny
AU - Deveney, Clifford W.
AU - Wendland, Michael F.
AU - Leimgruber, Richard M.
AU - Geokas, Michael C.
N1 - Funding Information:
* Supported by a grant from the Medical Research Service, Veterans Administration. t Address all correspondence to: H. Sankaran, Ph.D., Surgical Service (112)) VA Medical Center, 4150 Clement St., San Francisco, CA 94121. $ Present address: Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco, CA 94143.
PY - 1985/8/15
Y1 - 1985/8/15
N2 - Acetaldehyde inhibited both amylase secretion induced by maximal concentrations (300 pM) of cholecystokinin octapeptide and the binding of radioiodinated cholecystokinin to receptors on isolated rat pancreatic acini. This inhibition was concentration dependent (10 mM to 1M for amylase secretion and 100 mM to 1M for binding). However, a correlation between the two inhibitory effects could not be obtained. Furthermore, the inhibitory effects were not reversible. Acetaldehyde did not alter the basal amylase secretion between 6 and 45 mM concentrations. However, 60, 100 and 300 mM acetaldehyde significantly decreased basal amylase secretion; no significant change in amylase secretion was observed at 600 mM and 1M. Higher concentrations of acetaldehyde produced a 2- to 10-fold increase in basal amylase secretion. 51Cr release from prelabeled acini revealed no significant cell membrane damage between 10 and 600 mM acetaldehyde. These data suggest that acetaldehyde inhibition of cholecystokinin-induced amylase secretion is intracellularly mediated.
AB - Acetaldehyde inhibited both amylase secretion induced by maximal concentrations (300 pM) of cholecystokinin octapeptide and the binding of radioiodinated cholecystokinin to receptors on isolated rat pancreatic acini. This inhibition was concentration dependent (10 mM to 1M for amylase secretion and 100 mM to 1M for binding). However, a correlation between the two inhibitory effects could not be obtained. Furthermore, the inhibitory effects were not reversible. Acetaldehyde did not alter the basal amylase secretion between 6 and 45 mM concentrations. However, 60, 100 and 300 mM acetaldehyde significantly decreased basal amylase secretion; no significant change in amylase secretion was observed at 600 mM and 1M. Higher concentrations of acetaldehyde produced a 2- to 10-fold increase in basal amylase secretion. 51Cr release from prelabeled acini revealed no significant cell membrane damage between 10 and 600 mM acetaldehyde. These data suggest that acetaldehyde inhibition of cholecystokinin-induced amylase secretion is intracellularly mediated.
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U2 - 10.1016/0006-2952(85)90007-3
DO - 10.1016/0006-2952(85)90007-3
M3 - Article
C2 - 2411269
AN - SCOPUS:0022391531
SN - 0006-2952
VL - 34
SP - 2859
EP - 2863
JO - Biochemical Pharmacology
JF - Biochemical Pharmacology
IS - 16
ER -