Characterization of cAMP-dependent protein kinase activation by CCK in rat pancreas
| Autor: | Steven D. Leach, Jean F. Schaefer, Laurence J. Miller, Christopher R. Marino, Fred S. Gorelick |
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| Rok vydání: | 1993 |
| Předmět: |
Male
medicine.medical_specialty Biophysics Pancreatic acini Biology In Vitro Techniques Adenosine 3′ 5′ cyclic monophosphate Biochemistry Cholecystokinin receptor digestive system Protein kinase Article Rats Sprague-Dawley Enzyme activator Structural Biology Internal medicine 1-Methyl-3-isobutylxanthine CCK receptor Genetics medicine Cyclic AMP Animals Kinase activity Protein kinase A Molecular Biology Pancreas Cholecystokinin digestive oral and skin physiology Biological activity Cell Biology Rats Enzyme Activation Endocrinology Second messenger system Phosphodiesterase inhibitor Signal transduction Protein Kinases hormones hormone substitutes and hormone antagonists |
| Zdroj: | FEBS letters. 316(1) |
| ISSN: | 0014-5793 |
| Popis: | This study reports on the use of a new sensitive assay of cAMP-dependent protein kinase activity to examine the effect of cholecystokinin (CCK) on the cAMP second messenger cascade in rat pancreatic acini. Treatment of acini with both low (pM) and high (nM) concentrations of CCK was associated with an increase in cAMP-dependent protein kinase activity. The increases in kinase activity were detected in the absence of phosphodiesterase inhibition, a condition required to detect a measurable increase in cellular cAMP in these cells. Furthermore, the cAMP cascade was dissociated from the secretory effects of CCK, since the CCK analogue, OPE, mediates enzyme secretion but does not increase cellular cAMP levels or kinase activity. |
| Databáze: | OpenAIRE |
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