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Am J Physiol Cell Physiol 274: C1081-C1089, 1998;
0363-6143/98 $5.00
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Vol. 274, Issue 4, C1081-C1089, April 1998

Cloning and functional studies of splice variants of the alpha -subunit of the amiloride-sensitive Na+ channel

J. Kevin Tucker1, Kaichiro Tamba1, Young-Jae Lee1, Li-Ling Shen1, David G. Warnock1,2,3, and Youngsuk Oh1,4

Departments of 1 Medicine and of 2 Physiology and Biophysics, 3 Nephrology Research and Training Center, and 4 Neurobiology Research Center, University of Alabama, Birmingham, Alabama 35294

The alpha -subunit of the amiloride-sensitive epithelial Na+ channel (alpha ENaC) is critical in forming an ion conductive pore in the membrane. We have identified the wild-type and three splice variants of the human alpha ENaC (halpha ENaC) from the human lung cell line H441, using RT-PCR. These splice variants contain various structures in the extracellular domain, resulting in premature truncation (halpha ENaCx), 19-amino acid deletion (halpha ENaC-19), and 22-amino acid insertion (halpha ENaC+22). Wild-type halpha ENaC and splice variants were functionally characterized in Xenopus oocytes by coexpression with hENaC beta - and gamma -subunits. Unlike wild-type halpha ENaC, undetectable or substantially reduced amiloride-sensitive currents were observed in oocytes expressing these splice variants. Wild-type halpha ENaC was the most abundantly expressed halpha ENaC mRNA species in all tissues in which its expression was detected. These findings indicate that the extracellular domain is important to generate structural and functional diversity of halpha ENaC and that alternative splicing may play a role in regulating hENaC activity.

human epithelial sodium channel alpha -subunit; alternative splicing; lung cell line


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