Irreversible inhibition by acetaldehyde of cholecystokinin-induced amylase secretion from isolated rat pancreatic acini

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

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2859-2863
Number of pages5
JournalBiochemical Pharmacology
Volume34
Issue number16
DOIs
StatePublished - Aug 15 1985
Externally publishedYes

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Acetaldehyde
Cholecystokinin
Amylases
Rats
Cholecystokinin Receptors
Sincalide
Cell membranes
Cell Membrane

ASJC Scopus subject areas

  • Pharmacology

Cite this

Irreversible inhibition by acetaldehyde of cholecystokinin-induced amylase secretion from isolated rat pancreatic acini. / Sankaran, Hariharan; Lewin, Mark B.; Wong, Anny; Deveney, Clifford; Wendland, Michael F.; Leimgruber, Richard M.; Geokas, Michael C.

In: Biochemical Pharmacology, Vol. 34, No. 16, 15.08.1985, p. 2859-2863.

Research output: Contribution to journalArticle

Sankaran, Hariharan ; Lewin, Mark B. ; Wong, Anny ; Deveney, Clifford ; Wendland, Michael F. ; Leimgruber, Richard M. ; Geokas, Michael C. / Irreversible inhibition by acetaldehyde of cholecystokinin-induced amylase secretion from isolated rat pancreatic acini. In: Biochemical Pharmacology. 1985 ; Vol. 34, No. 16. pp. 2859-2863.
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AU - Wendland, Michael F.

AU - Leimgruber, Richard M.

AU - Geokas, Michael C.

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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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