Am J Physiol Cell Physiol AJP: Cell Physiology
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Am J Physiol Cell Physiol 278: C865-C872, 2000;
0363-6143/00 $5.00
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Vol. 278, Issue 5, C865-C872, May 2000

Inhibition of phosphatidylinositol 3-kinase does not alter forskolin-stimulated Clminus secretion by T84 cells

Jeffrey L. Dickson, Tracy D. Conner, and Tom W. Ecay

Department of Physiology, James H. Quillen College of Medicine, East Tennessee State University, Johnson City, Tennessee 37614

Wortmannin is a potent inhibitor of phosphatidylinositol 3-kinase (PI3K) and membrane trafficking in many cells. To test the hypothesis that cystic fibrosis transmembrane conductance regulator (CFTR) traffics into and out of the plasma membrane during cAMP-stimulated epithelial Cl- secretion, we have studied the effects of wortmannin on forskolin-stimulated Cl- secretion by the human colonic cell line T84. At the PI3K inhibitory concentration of 100 nM, wortmannin did not affect significantly forskolin-stimulated Cl- secretion measured as short-circuit current (ISC). However, 500 nM wortmannin significantly inhibited forskolin-stimulated ISC. cAMP activation of apical membrane CFTR Cl- channels in alpha -toxin-permeabilized monolayers was not reduced by 500 nM wortmannin, suggesting that inhibition of other transporters accounts for the observed reduction in T84 Cl- secretion. Forskolin inhibits apical endocytosis of horseradish peroxidase (HRP), but wortmannin did not alter forskolin inhibition of apical HRP endocytosis. In the absence of forskolin, wortmannin stimulated HRP endocytosis significantly. We conclude that, in T84 cells, apical fluid phase endocytosis is not dependent on PI3K activity and that CFTR does not recycle through a PI3K-dependent and wortmannin-sensitive membrane compartment.

wortmannin; epithelia; short-circuit current; cystic fibrosis transmembrane conductance regulator; endocytosis


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