Titre
Functional analyses of a N-terminal splice variant of the alpha subunit of the epithelial sodium channel
Type
article
Institution
UNIL/CHUV/Unisanté + institutions partenaires
Périodique
Auteur(s)
Chraibi, A.
Auteure/Auteur
Verdumo, C.
Auteure/Auteur
Mérillat, A. M.
Auteure/Auteur
Rossier, B. C.
Auteure/Auteur
Horisberger, J. D.
Auteure/Auteur
Hummler, E.
Auteure/Auteur
Liens vers les personnes
Liens vers les unités
ISSN
1015-8987
Statut éditorial
Publié
Date de publication
2001
Volume
11
Numéro
3
Première page
115
Dernière page/numéro d’article
22
Notes
Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.
Résumé
The amiloride-sensitive epithelial sodium channel (ENaC) is the limiting step for sodium absorption in epithelial cells of the distal nephron, distal colon, airways and excretory ducts of several glands. In vivo and in vitro studies showed that the alpha subunit of ENaC is necessary for the expression of functional channels. Using RT-PCR strategy, a novel N-terminal splice variant has been identified which deletes 49 amino acids in the N-terminal region of the mouse alphaENaC subunit. In oocytes expressing the alphaENaC splice variant, together with beta and gammaENaC subunits, amiloride-sensitive currents were less than 20% of values obtained with the wild type ENaC. The single channel conductance and the ionic selectivity were similar and there was only a minor decrease in the level of expression of the protein at the oocyte surface. These findings indicate that the deleted sequence in the N-terminal part of the mouse and rat alphaENaC subunit might play a role in the regulation of the activity of expressed ENaC channels.
Sujets
PID Serval
serval:BIB_9C9D14B997FE
PMID
Date de création
2008-01-24T11:38:40.982Z
Date de création dans IRIS
2025-05-21T03:50:36Z