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Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits

Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits THE amiloride-sensitive epithelial sodium channel constitutes the rate-limiting step for sodium reabsorption in epithelial cells that line the distal part of the renal tubule, the distal colon, the duct of several exocrine glands, and the lung. The activity of this channel is upregulated by vasopressin and aldosterone, hormones involved in the maintenance of sodium balance, blood volume and blood pressure1,2. We have identified the primary structure of the α-subunit of the rat epithelial sodium channel by expression cloning in Xenopus laevis oocytes3. An identical subunit has recently been reported4. Here we identify two other subunits (β and γ) by functional complementation of the α-subunit of the rat epithelial Na+ channel. The ion-selective permeability, the gating properties and the pharmacological profile of the channel formed by coexpressing the three subunits in oocytes are similar to that of the native channel. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits

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References (37)

Publisher
Springer Journals
Copyright
Copyright © 1994 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/367463a0
Publisher site
See Article on Publisher Site

Abstract

THE amiloride-sensitive epithelial sodium channel constitutes the rate-limiting step for sodium reabsorption in epithelial cells that line the distal part of the renal tubule, the distal colon, the duct of several exocrine glands, and the lung. The activity of this channel is upregulated by vasopressin and aldosterone, hormones involved in the maintenance of sodium balance, blood volume and blood pressure1,2. We have identified the primary structure of the α-subunit of the rat epithelial sodium channel by expression cloning in Xenopus laevis oocytes3. An identical subunit has recently been reported4. Here we identify two other subunits (β and γ) by functional complementation of the α-subunit of the rat epithelial Na+ channel. The ion-selective permeability, the gating properties and the pharmacological profile of the channel formed by coexpressing the three subunits in oocytes are similar to that of the native channel.

Journal

NatureSpringer Journals

Published: Feb 3, 1994

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