Inhibition by mepacrine and amylase secretion from intact and permeabilized rat pancreatic acini.
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.
Grosfils
K
K
Department of General and Human Biochemistry, Free University of Brussels, Belgium.
Gomez
F
F
Dehaye
J P
JP
D000681:Amylases / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002217:Carbachol / Q000494:pharmacology; D002463:Cell Membrane Permeability; D004305:Dose-Response Relationship, Drug; D004533:Egtazic Acid / Q000494:pharmacology; D066298:In Vitro Techniques; D007700:Kinetics; D008297:Male; D010179:Pancreas / Q000166:cytology / Q000187:drug effects / Q000201:enzymology*; D011796:Quinacrine / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D012844:Sincalide / Q000494:pharmacology
D004533:Egtazic Acid; D002217:Carbachol; D000681:Amylases; D011796:Quinacrine; D012844:Sincalide; D002118:Calcium