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Am J Physiol Cell Physiol 281: C624-C632, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 2, C624-C632, August 2001

Characterization and imaging of A6 epithelial cell clones expressing fluorescently labeled ENaC subunits

Bonnie L. Blazer-Yost1, Michael Butterworth2, Amy D. Hartman1, Gretchen E. Parker1, Carla J. Faletti1, Willem J. Els2, and Simon J. Rhodes1

1 Department of Biology, Indiana University-Purdue University Indianapolis, Indianapolis, Indiana 46202; and 2 Department of Anatomy and Cell Biology, University of Cape Town Medical School, Cape Town, South Africa

A6 model renal epithelial cells were stably transfected with enhanced green fluorescent protein (EGFP)-tagged alpha - or beta -subunits of the epithelial Na+ channel (ENaC). Transfected RNA and proteins were both expressed in low abundance, similar to the endogenous levels of ENaC in native cells. In living cells, laser scanning confocal microscopy revealed a predominately subapical distribution of EGFP-labeled subunits, suggesting a readily accessible pool of subunits available to participate in Na+ transport. The basal level of Na+ transport in the clonal lines was enhanced two- to fourfold relative to the parent line. Natriferic responses to insulin or aldosterone were similar in magnitude to the parent line, while forskolin-stimulated Na+ transport was 64% greater than control in both the alpha - and beta -transfected lines. In response to forskolin, EGFP-labeled channel subunits traffic to the apical membrane. These data suggest that channel regulators, not the channel per se, form the rate-limiting step in response to insulin or aldosterone stimulation, while the number of channel subunits is important for basal as well as cAMP-stimulated Na+ transport.

sodium transport; amiloride; aldosterone; insulin; channel trafficking; adenosine 3',5'-cyclic monophosphate, signal transduction; epithelial sodium channel; green fluorescent protein


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