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Regulation of phosphatidylinositol 4-kinase activity in rat pancreatic acini

BR Conway, M Withiam-Leitch and RP Rubin

Department of Pharmacology and Therapeutics, State University of New York, Buffalo 14214.

Previous data showed that carbachol (CCh) elicits a concentration- dependent increase in phosphatidylinositol (PtdIns) 4-kinase activity in homogenates derived from agonist-stimulated pancreatic acini. In the present study CCh elicited a time-dependent increase in PtdIns 4-kinase activity, which was blocked by n-methylscopolamine and mimicked by muscarine. A membrane-associated PtdIns 4-kinase activity was identified that displayed maximal activity in the pH range of 5.5-8.5. The zymogen granule fraction possessed relatively high specific enzyme activity, which was sensitive to CCh stimulation. The enzyme had apparent Km values for PtdIns and ATP of 4 and 60 microM, respectively. CCh caused no discernible change in the Km for either PtdIns or ATP but increased Vmax. Dioctanoylglycerol and oleoyl acetylglycerol augmented PtdIns 4-kinase activity, which was blocked by staurosporine, thus suggesting a possible role for protein kinase C in the regulation of PtdIns 4-kinase. These collective findings demonstrate a muscarinic receptor-mediated regulation of PtdIns 4-kinase activity in exocrine pancreas, involving a protein kinase C-dependent process.

Volume 43, Issue 2, pp. 286-292, 02/01/1993
Copyright © 1993 by American Society for Pharmacology and Experimental Therapeutics




This article has been cited by other articles:


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G. B. Willars, S. R. Nahorski, and R. A. J. Challiss
Differential Regulation of Muscarinic Acetylcholine Receptor-sensitive Polyphosphoinositide Pools and Consequences for Signaling in Human Neuroblastoma Cells
J. Biol. Chem., February 27, 1998; 273(9): 5037 - 5046.
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Copyright © 1993 by the American Society for Pharmacology and Experimental Therapeutics