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J Biol Chem, Vol. 273, Issue 34, 21759-21768, August 21, 1998
From the Departments of a Physiology and h Biology,
Dartmouth Medical School, Hanover, New Hampshire 03755, the
g Department of Physiology, Johns Hopkins University, School of
Medicine, Baltimore, Maryland 21205, and the d Department of
Physiology and Biophysics, University of Alabama at Birmingham,
Birmingham, Alabama 35294
The mechanism by which cAMP stimulates cystic
fibrosis transmembrane conductance regulator (CFTR)-mediated chloride
(Cl
Membrane Trafficking of the Cystic Fibrosis Gene Product, Cystic
Fibrosis Transmembrane Conductance Regulator, Tagged with Green
Fluorescent Protein in Madin-Darby Canine Kidney Cells
) secretion is cell type-specific. By using
Madin-Darby canine kidney (MDCK) type I epithelial cells as a model, we
tested the hypothesis that cAMP stimulates Cl secretion
by stimulating CFTR Cl channel trafficking from an
intracellular pool to the apical plasma membrane. To this end, we
generated a green fluorescent protein (GFP)-CFTR expression vector in
which GFP was linked to the N terminus of CFTR. GFP did not alter CFTR
function in whole cell patch-clamp or planar lipid bilayer experiments.
In stably transfected MDCK type I cells, GFP-CFTR localization was
substratum-dependent. In cells grown on glass coverslips,
GFP-CFTR was polarized to the basolateral membrane, whereas in cells
grown on permeable supports, GFP-CFTR was polarized to the apical
membrane. Quantitative confocal fluorescence microscopy and surface
biotinylation experiments demonstrated that cAMP did not stimulate
detectable GFP-CFTR translocation from an intracellular pool to the
apical membrane or regulate GFP-CFTR endocytosis. Disruption of the
microtubular cytoskeleton with colchicine did not affect
cAMP-stimulated Cl secretion or GFP-CFTR expression in
the apical membrane. We conclude that cAMP stimulates CFTR-mediated
Cl secretion in MDCK type I cells by activating channels
resident in the apical plasma membrane.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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