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

Détails

ID Serval
serval:BIB_7C59A7C33DB2
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits.
Périodique
Nature
Auteur(s)
Canessa C.M., Schild L., Buell G., Thorens B., Gautschi I., Horisberger J.D., Rossier B.C.
ISSN
0028-0836
Statut éditorial
Publié
Date de publication
02/1994
Peer-reviewed
Oui
Volume
367
Numéro
6462
Pages
463-467
Langue
anglais
Résumé
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 pressure. We have identified the primary structure of the alpha-subunit of the rat epithelial sodium channel by expression cloning in Xenopus laevis oocytes. An identical subunit has recently been reported. Here we identify two other subunits (beta and gamma) by functional complementation of the alpha-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.
Mots-clé
Amiloride, Amino Acid Sequence, Animals, Cell Line, Cells, Cultured, Epithelium, Ion Channel Gating, Membrane Potentials, Molecular Sequence Data, Oocytes, Permeability, Rats, Recombinant Proteins, Sodium Channels, Xenopus laevis
Pubmed
Web of science
Création de la notice
24/01/2008 13:37
Dernière modification de la notice
03/03/2018 18:37
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