TY - JOUR
T1 - Effect of ethanol on cholecystokinin-induced enzyme secretion from isolated rat pancreatic acini
AU - Lewin, Mark B.
AU - Sankaran, Hariharan
AU - Deveney, Clifford W.
AU - Wong, Anny
AU - Wendland, Michael F.
AU - Geokas, Michael C.
N1 - Funding Information:
* This work was supported by the Medical Research Service of the Veterans Administration and by Research Grant 1088 from the Council for Tobacca Research-USA, Inc., New York. NY. $ Address for correspondence and reprints: M. B. Lewin, Surgical Service (112), Veterans Administration Medical Center. 4150 Clement St., San Francisco, CA 94121.
PY - 1984/10/15
Y1 - 1984/10/15
N2 - Cholecystokinin octapeptide (CCK8)-stimulated amylase release in isolated rat pancreatic acini was inhibited over 30% by 600 mM ethanol. The configuration of the dose-response curve for CCK8, however, in the presence of ethanol was similar to that of the control. Amylase release elicited by maximal concentrations of CCK8 (300 pM) was inhibited by increasing concentrations of ethanol (0.3 to 1.3 M), and this inhibition was concentration dependent. In addition, the binding of [125I]CCK33 to specific membrane receptors on acini was inhibited by ethanol in a dose-dependent manner. A positive correlation between the inhibitory effects of ethanol on CCK binding and CCK-induced amylase release was observed. Furthermore, these inhibitory effects of ethanol were reversible. Basal amylase release, however, was increased 20-50% by ethanol between the concentrations of 0.3 and 1.3M; higher concentrations caused a leakage of amylase from the acini both in the absence and presence of 300 pMCCK8. This is confirmed by 51Cr release from prelabeled acini which revealed no significant damage to acinar cell membrane between 0.3 and 1.6 M ethanol, but significant damage to acini at higher concentrations. These data suggest that the 600 mM ethanol-induced inhibition of CCK action in acini is due to reversible perturbation of the acinar cell membrane.
AB - Cholecystokinin octapeptide (CCK8)-stimulated amylase release in isolated rat pancreatic acini was inhibited over 30% by 600 mM ethanol. The configuration of the dose-response curve for CCK8, however, in the presence of ethanol was similar to that of the control. Amylase release elicited by maximal concentrations of CCK8 (300 pM) was inhibited by increasing concentrations of ethanol (0.3 to 1.3 M), and this inhibition was concentration dependent. In addition, the binding of [125I]CCK33 to specific membrane receptors on acini was inhibited by ethanol in a dose-dependent manner. A positive correlation between the inhibitory effects of ethanol on CCK binding and CCK-induced amylase release was observed. Furthermore, these inhibitory effects of ethanol were reversible. Basal amylase release, however, was increased 20-50% by ethanol between the concentrations of 0.3 and 1.3M; higher concentrations caused a leakage of amylase from the acini both in the absence and presence of 300 pMCCK8. This is confirmed by 51Cr release from prelabeled acini which revealed no significant damage to acinar cell membrane between 0.3 and 1.6 M ethanol, but significant damage to acini at higher concentrations. These data suggest that the 600 mM ethanol-induced inhibition of CCK action in acini is due to reversible perturbation of the acinar cell membrane.
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U2 - 10.1016/0006-2952(84)90081-9
DO - 10.1016/0006-2952(84)90081-9
M3 - Article
C2 - 6207835
AN - SCOPUS:0021175128
SN - 0006-2952
VL - 33
SP - 3225
EP - 3229
JO - Biochemical Pharmacology
JF - Biochemical Pharmacology
IS - 20
ER -