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Am J Physiol Lung Cell Mol Physiol 282: L12-L25, 2002;
1040-0605/02 $5.00
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Vol. 282, Issue 1, L12-L25, January 2002

A2 adenosine receptors regulate CFTR through PKA and PLA2

B. R. Cobb1,2, F. Ruiz3, C. M. King2, J. Fortenberry2, H. Greer2, T. Kovacs2, E. J. Sorscher2,4, and J. P. Clancy2,5

Departments of 1 Human Genetics, 4 Medicine, and 5 Pediatrics, University of Alabama at Birmingham, Birmingham 35233; 2 Gregory Fleming James Cystic Fibrosis Research Center, University of Alabama at Birmingham, Birmingham, Alabama 35294; and 3 Department of Pediatrics, University of Mississippi, Jackson, Mississippi 39216

We investigated adenosine (Ado) activation of the cystic fibrosis transmembrane conductance regulator (CFTR) in vitro and in vivo. A2B Ado receptors were identified in Calu-3, IB-3-1, COS-7, and primary human airway cells. Ado elevated cAMP in Calu-3, IB-3-1, and COS-7 cells and activated protein kinase A-dependent halide efflux in Calu-3 cells. Ado promoted arachidonic acid release from Calu-3 cells, and phospholipase A2 (PLA2) inhibition blocked Ado-activated halide efflux in Calu-3 and COS-7 cells expressing CFTR. Forskolin- and beta 2-adrenergic receptor-stimulated efflux were not affected by the same treatment. Cytoplasmic PLA2 (cPLA2) was identified in Calu-3, IB-3-1, and COS-7 cells, but cPLA2 inhibition did not affect Ado-stimulated cAMP concentrations. In cftr(+) and cftr(-/-) mice, Ado stimulated nasal Cl- secretion that was CFTR dependent and sensitive to A2 receptor and PLA2 blockade. In COS-7 cells transiently expressing Delta F508 CFTR, Ado activated halide efflux. Ado also activated G551D CFTR-dependent halide efflux when combined with arachidonic acid and phosphodiesterase inhibition. In conclusion, PLA2 and protein kinase A both contribute to A2 receptor activation of CFTR, and components of this signaling pathway can augment wild-type and mutant CFTR activity.

cystic fibrosis transmembrane conductance regulator; airway epithelia; Calu-3 cells; chloride secretion; nasal potential difference; protein kinase A; phospholipase A2


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