Cloning and functional studies of splice variants of the alpha-subunit of the amiloride-sensitive Na+ channel.
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Tucker JK, Tamba K, Lee YJ, Shen LL, Warnock DG, Oh Y
Cloning and functional studies of splice variants of the alpha-subunit of the amiloride-sensitive Na+ channel.
Am J Physiol. 1998 Apr;274(4 Pt 1):C1081-9.
- PubMed ID
- 9575806 [ View in PubMed]
- Abstract
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 (h alpha 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 (h alpha ENaCx), 19-amino acid deletion (h alpha ENaC-19), and 22-amino acid insertion (h alpha ENaC + 22). Wild-type h alpha ENaC and splice variants were functionally characterized in Xenopus oocytes by coexpression with hENaC beta- and gamma-subunits. Unlike wild-type h alpha ENaC, undetectable or substantially reduced amiloride-sensitive currents were observed in oocytes expressing these splice variants. Wild-type h alpha ENaC was the most abundantly expressed h alpha 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 h alpha ENaC and that alternative splicing may play a role in regulating hENaC activity.