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Am J Physiol Renal Physiol 284: F182-F188, 2003. First published September 11, 2002; doi:10.1152/ajprenal.00216.2002
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Vol. 284, Issue 1, F182-F188, January 2003

Epithelial sodium channel activity in detergent-resistant membrane microdomains

Vadim G. Shlyonsky, Frédérique Mies, and Sarah Sariban-Sohraby

Laboratory of Physiology and Physiopathology, Université Libre de Bruxelles, 1070 Brussels, Belgium

The activity of epithelial Na+ selective channels is modulated by various factors, with growing evidence that membrane lipids also participate in the regulation. In the present study, Triton X-100 extracts of whole cells and of apical membrane-enriched preparations from cultured A6 renal epithelial cells were floated on continuous-sucrose-density gradients. Na+ channel protein, probed by immunostaining of Western blots, was detected in the high-density fractions of the gradients (between 18 and 30% sucrose), which contain the detergent-soluble material but also in the lighter, detergent-resistant 16% sucrose fraction. Single amiloride-sensitive Na+ channel activity, recorded after incorporation of reconstituted proteoliposomes into lipid bilayers, was exclusively localized in the 16% sucrose fraction. In accordance with other studies, high- and low-density fractions of sucrose gradients likely represent membrane domains with different lipid contents. However, exposure of the cells to cholesterol-depleting or sphingomyelin-depleting agents did not affect transepithelial Na+ current, single-Na+ channel activity, or the expression of Na+ channel protein. This is the first reconstitution study of native epithelial Na+ channels, which suggests that functional channels are compartmentalized in discrete domains within the plane of the apical cell membrane.

sodium reabsorption; A6 cells; amiloride; lipid bilayers


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