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J. Biol. Chem., Vol. 277, Issue 50, 48172-48181, December 13, 2002

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Ca²⁺-dependent Protein Kinase-A Modulation of the Plasma Membrane Ca²⁺-ATPase in Parotid Acinar Cells^*

Jason I. E. Bruce, David I. Yule, and Trevor J. Shuttleworth

From the Department of Pharmacology and Physiology, School of Medicine and Dentistry, University of Rochester Medical Center, Rochester New York 14642

Cross-talk between cAMP and [Ca²⁺]_i signaling pathways represents a general feature that defines the specificity of stimulus-response coupling in a variety of cell types including parotid acinar cells. We have reported recently that cAMP potentiates Ca²⁺ release from intracellular stores, primarily because of a protein kinase A-mediated phosphorylation of type II inositol 1,4,5-trisphosphate receptors (Bruce, J. I. E., Shuttleworth, T. J. S., Giovannucci, D. R., and Yule, D. I. (2002) J. Biol. Chem. 277, 1340-1348). The aim of the present study was to evaluate the functional and molecular mechanism whereby cAMP regulates Ca²⁺ clearance pathways in parotid acinar cells. Following an agonist-induced increase in [Ca²⁺]_i the rate of Ca²⁺ clearance, after the removal of the stimulus, was potentiated substantially (~2-fold) by treatment with forskolin. This effect was prevented completely by inhibition of the plasma membrane Ca²⁺-ATPase (PMCA) with La³⁺. PMCA activity, when isolated pharmacologically, was also potentiated (~2-fold) by forskolin. Ca²⁺ uptake into the endoplasmic reticulum of streptolysin-O-permeabilized cells by sarco/endoplasmic reticulum Ca²⁺-ATPase was largely unaffected by treatment with dibutyryl cAMP. Finally, in situ phosphorylation assays demonstrated that PMCA was phosphorylated by treatment with forskolin but only in the presence of carbamylcholine (carbachol). This effect of forskolin was Ca²⁺-dependent, and protein kinase C-independent, as potentiation of PMCA activity and phosphorylation of PMCA by forskolin also occurred when [Ca²⁺]_i was elevated by the sarco/endoplasmic reticulum Ca²⁺-ATPase inhibitor cyclopiazonic acid and was attenuated by pre-incubation with the Ca²⁺ chelator, 1,2-bis(o-aminophenoxy) ethane-N,N,N',N'-tetraacetic acid (BAPTA). The present study demonstrates that elevated cAMP enhances the rate of Ca²⁺ clearance because of a complex modulation of PMCA activity that involves a Ca²⁺-dependent step. Tight regulation of both Ca²⁺ release and Ca²⁺ efflux may represent a general feature of the mechanism whereby cAMP improves the fidelity and specificity of Ca²⁺ signaling.

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