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

Nature volume 367, pages 463–467 (1994)Cite this article

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.

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Author notes

  1. Bernard C. Rossier: To whom correspondence should be addressed.

Authors and Affiliations

  1. Institut de Pharmacologie et de Toxicologie, Université de Lausanne, Bugnon 27, CH-1005, Lausanne, Switzerland

    Cecilia M. Canessa, Laurent Schild, Bernard Thorens, Ivan Gautschi & Jean-Daniel Horisberger

  2. Glaxo Institute for Molecular Biology, Chemin des Aulx 14, 1228, Plan-les Ouates, Geneva, Switzerland

    Gary Buell

Authors
  1. Cecilia M. Canessa
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  2. Laurent Schild
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  3. Gary Buell
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  4. Bernard Thorens
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  5. Ivan Gautschi
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  6. Jean-Daniel Horisberger
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  7. Bernard C. Rossier
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Canessa, C., Schild, L., Buell, G. et al. Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits. Nature 367, 463–467 (1994). https://doi.org/10.1038/367463a0

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