Inhibition by mepacrine of amylase secretion from intact and permeabilized rat pancreatic acini

Grosfils, Katrina; Gomez, Françoise; Dehaye, Jean-Paul

doi:doi/10.1016/0006-291X(92)91208-8

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Inhibition by mepacrine of amylase secretion from intact and permeabilized rat pancreatic acini

par Grosfils, Katrina

;Gomez, Françoise

;Dehaye, Jean-Paul

Référence Biochemical and biophysical research communications, 184, 1, page (408-413)
Publication Publié, 1992-04

Article révisé par les pairs

Résumé :

In intact rat pancreatic acini, the phospholipase A2 inhibitor mepacrine did not affect basal amylase release but dose-dependently inhibited the carbachol (IC50 65 microM) and CCK-8 (IC50 210 microM)-stimulated amylase release. In permeabilized acini, mepacrine shifted the dose-response curve for calcium to the right by a factor 2 and inhibited the release of amylase stimulated by GTPrS. From these results we conclude that carbachol, CCK-8 and GTPrS probably activate a phospholipase A2 closely coupled to exocytosis.

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