Effect of ethanol on cholecystokinin-induced enzyme secretion from isolated rat pancreatic acini

Mark B. Lewin, Hariharan Sankaran, Clifford Deveney, Anny Wong, Michael F. Wendland, Michael C. Geokas

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)3225-3229
Number of pages5
JournalBiochemical Pharmacology
Volume33
Issue number20
DOIs
StatePublished - Oct 15 1984
Externally publishedYes

Fingerprint

Cholecystokinin
Rats
Ethanol
Amylases
Enzymes
Acinar Cells
Cell membranes
Cell Membrane
Sincalide
Membranes

ASJC Scopus subject areas

  • Pharmacology

Cite this

Effect of ethanol on cholecystokinin-induced enzyme secretion from isolated rat pancreatic acini. / Lewin, Mark B.; Sankaran, Hariharan; Deveney, Clifford; Wong, Anny; Wendland, Michael F.; Geokas, Michael C.

In: Biochemical Pharmacology, Vol. 33, No. 20, 15.10.1984, p. 3225-3229.

Research output: Contribution to journalArticle

Lewin, Mark B. ; Sankaran, Hariharan ; Deveney, Clifford ; Wong, Anny ; Wendland, Michael F. ; Geokas, Michael C. / Effect of ethanol on cholecystokinin-induced enzyme secretion from isolated rat pancreatic acini. In: Biochemical Pharmacology. 1984 ; Vol. 33, No. 20. pp. 3225-3229.
@article{8ff44ca2942c4db1a45a26204288c267,
title = "Effect of ethanol on cholecystokinin-induced enzyme secretion from isolated rat pancreatic acini",
abstract = "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.",
author = "Lewin, {Mark B.} and Hariharan Sankaran and Clifford Deveney and Anny Wong and Wendland, {Michael F.} and Geokas, {Michael C.}",
year = "1984",
month = "10",
day = "15",
doi = "10.1016/0006-2952(84)90081-9",
language = "English (US)",
volume = "33",
pages = "3225--3229",
journal = "Biochemical Pharmacology",
issn = "0006-2952",
publisher = "Elsevier Inc.",
number = "20",

}

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

AU - Wong, Anny

AU - Wendland, Michael F.

AU - Geokas, Michael C.

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.

UR - http://www.scopus.com/inward/record.url?scp=0021175128&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021175128&partnerID=8YFLogxK

U2 - 10.1016/0006-2952(84)90081-9

DO - 10.1016/0006-2952(84)90081-9

M3 - Article

VL - 33

SP - 3225

EP - 3229

JO - Biochemical Pharmacology

JF - Biochemical Pharmacology

SN - 0006-2952

IS - 20

ER -