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

Details

Serval ID
serval:BIB_7C59A7C33DB2
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits.
Journal
Nature
Author(s)
Canessa C.M., Schild L., Buell G., Thorens B., Gautschi I., Horisberger J.D., Rossier B.C.
ISSN
0028-0836
Publication state
Published
Issued date
02/1994
Peer-reviewed
Oui
Volume
367
Number
6462
Pages
463-467
Language
english
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 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.
Keywords
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
Create date
24/01/2008 13:37
Last modification date
20/08/2019 15:37
Usage data