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J Biol Chem, Vol. 274, Issue 33, 23286-23295, August 13, 1999

Association of the Epithelial Sodium Channel with Apx and -Spectrin in A6 Renal Epithelial Cells

Jonathan B. Zuckerman^§, Xiyin Chen, Joely D. Jacobs, Baofeng Hu, Thomas R. Kleyman^§**, and Peter R. Smith

From the Departments of  Medicine and ^** Physiology, University of Pennsylvania and the ^§ Veterans Affairs Medical Center, Philadelphia, Pennsylvania 19104, the  Department of Physiology, MCP-Hahnemann University, Philadelphia, Pennsylvania 19129, and the  Department of Physiology and Biophysics, University of Alabama at Birmingham, Birmingham, Alabama 35294

Recent molecular cloning of the epithelial sodium channel (ENaC) provides the opportunity to identify ENaC-associated proteins that function in regulating its cell surface expression and activity. We have examined whether ENaC is associated with Apx (apical protein Xenopus) and the spectrin-based membrane cytoskeleton in Xenopus A6 renal epithelial cells. We have also addressed whether Apx is required for the expression of amiloride-sensitive Na⁺ currents by cloned ENaC. Sucrose density gradient centrifugation of A6 cell detergent extracts showed co-sedimentation of xENaC, -spectrin, and Apx. Immunoblot analysis of proteins co-immunoprecipitating under high stringency conditions from peak Xenopus ENaC/Apx-containing gradient fractions indicate that ENaC, Apx, and -spectrin are associated in a macromolecular complex. To examine whether Apx is required for the functional expression of ENaC, mENaC cRNAs were coinjected into Xenopus oocytes with Apx sense or antisense oligodeoxynucleotides. The two-electrode voltage clamp technique showed there was a marked reduction in amiloride-sensitive current in oocytes coinjected with antisense oligonucleotides when to compared with oocytes coinjected with sense oligonucleotides. These studies indicate that ENaC is associated in a macromolecular complex with Apx and -spectrin in A6 cells and suggest that Apx is required for the functional expression of ENaC in Xenopus epithelia.

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