Protein Kinase C δ-Mediated Processes in Cholecystokinin-8-Stimulated Pancreatic Acini
Autor: | Jingzhen Yuan, Fred S. Gorelick, Jeffrey Wang, Aurelia Lugea, Thomas R. Kolodecik, Joseph R. Reeve, Edwin C. Thrower, Salim Cheriyan, Stephen J. Pandol |
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Rok vydání: | 2009 |
Předmět: |
Male
Indoles Endocrinology Diabetes and Metabolism Immunoblotting Mitogen-activated protein kinase kinase digestive system Article MAP2K7 Maleimides Rats Sprague-Dawley Mice Endocrinology Internal Medicine Acinar cell Animals Benzopyrans c-Raf Enzyme Inhibitors Pancreas Cells Cultured Protein kinase C Cholecystokinin Mice Knockout Dose-Response Relationship Drug Hepatology MAP kinase kinase kinase biology Chemistry Cyclin-dependent kinase 2 NF-kappa B Acetophenones Peptide Fragments Rats Cell biology Mice Inbred C57BL Protein Kinase C-delta Amylases Calcium-Calmodulin-Dependent Protein Kinases Trypsinogen biology.protein |
Zdroj: | Pancreas. 38:930-935 |
ISSN: | 0885-3177 |
Popis: | To define the role of protein kinase C delta (PKC delta) in acinar cell responses to the hormone cholecystokinin-8 (CCK) using isoform-specific inhibitors and a previously unreported genetic deletion model.Pancreatic acinar cells were isolated from (1) rat, and pretreated with a PKC delta-specific inhibitor or (2) PKC delta-deficient and wild type mice. Isolated cells were stimulated with CCK (0.001-100 nmol/L) and cell responses were measured.The PKC delta inhibitor did not affect stimulated amylase secretion from rat pancreatic acinar cells. Cholecystokinin-8 stimulation induced a typical biphasic dose-response curve for amylase secretion in acinar cells isolated from both PKC delta(-/-) and wild type mice, with maximal stimulation at 10-pmol/L CCK. Cholecystokinin-8 (100 nmol/L) induced zymogen and nuclear factor kappaB activation in both PKC delta(-/-) and wild type mice, although it was up to 50% less in PKC delta(-/-).In contrast to previous studies, this study has used specific and complementary approaches to examine PKC delta-mediated acinar cell responses. We could not confirm that it mediates amylase release but corroborated its role in the early stages of acute pancreatitis. |
Databáze: | OpenAIRE |
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