Inhibition by mepacrine and amylase secretion from intact and permeabilized rat pancreatic acini.
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Grosfils K, Gomez F, Dehaye JP
Inhibition by mepacrine and amylase secretion from intact and permeabilized rat pancreatic acini.
Biochem Biophys Res Commun. 1992 Apr 15;184(1):408-13.
- PubMed ID
- 1373616 [ View in PubMed]
- Abstract
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.
DrugBank Data that Cites this Article
- Drug Enzymes
Drug Enzyme Kind Organism Pharmacological Action Actions Carbamoylcholine Cytosolic phospholipase A2 Protein Humans UnknownInducerDetails