sincalide and carbobenzoxyglycylphenylalanine-amide

sincalide has been researched along with carbobenzoxyglycylphenylalanine-amide* in 1 studies

Other Studies

1 other study(ies) available for sincalide and carbobenzoxyglycylphenylalanine-amide

ArticleYear
Metalloendopeptidase inhibitors and stimulus-secretion coupling in the mouse exocrine pancreas.
    Pancreas, 1990, Volume: 5, Issue:5

    Inhibitors of metalloendopeptidases interfere with events involving Ca2(+)-dependent membrane fusion in a number of cell types. The divalent ion chelating agent 1,10-phenanthroline inhibited pancreatic amylase secretion stimulated by carbachol, cholecystokinin-octapeptide (CCK-8), or bombesin, but detailed studies indicated that this is unlikely to be a result of inhibition of metalloendopeptidase activity. The binding of [3H]N-methylscopolamine to pancreatic acini was reduced by 1,10-phenanthroline and this would explain the marked inhibition of carbachol-induced amylase secretion by the chelating agent. CCK-8-stimulated hydrolysis of phosphatidylinositol-4,5-bisphosphate was reduced by 1,10-phenanthroline while the binding of CCK-8 to acini was not affected. This inhibition of hydrolysis would explain the inhibition of CCK-8- and bombesin-induced amylase secretion. The metalloendopeptidase substrate carbobenzoxyglycylphenylalanylamide did not affect bombesin-stimulated amylase secretion. Amylase secretion evoked by treating pancreatic acini with the ionophore A23187 or dibutyryl-cyclic AMP was not reduced by 1,10-phenanthroline, indicating a lack of involvement of metalloendopeptidases in the process of exocytosis in this cell type.

    Topics: Amylases; Animals; Bombesin; Bucladesine; Calcimycin; Carbachol; Dipeptides; Metalloendopeptidases; Mice; N-Methylscopolamine; Pancreas; Phenanthrolines; Phosphatidylinositol 4,5-Diphosphate; Phosphatidylinositols; Receptors, Muscarinic; Scopolamine Derivatives; Sincalide

1990