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The Amiloride-Sensitive Na + Channel: From Primary Structure to Function

Three homologous subunits of the amiloride-sensitive Na + channel, entitled α, β, and γ, have been cloned either from distal colon of a steroid-treated rat or from human lung. The α, β, and γ subunits have similarities with degenerins, a family of proteins found in the mechanosensory neurons of the...

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Published in:Comparative biochemistry and physiology. A, Comparative physiology Comparative physiology, 1997-10, Vol.118 (2), p.193-200
Main Authors: Voilley, Nicolas, Galibert, Anne, Bassilana, Frédéric, Renard, Stéphane, Lingueglia, Eric, Coscoy, Sylvie, Champigny, Guy, Hofman, Paul, Lazdunski, Michel, Barbry, Pascal
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Language:English
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Summary:Three homologous subunits of the amiloride-sensitive Na + channel, entitled α, β, and γ, have been cloned either from distal colon of a steroid-treated rat or from human lung. The α, β, and γ subunits have similarities with degenerins, a family of proteins found in the mechanosensory neurons of the nematode Caenorhabditis elegans. All these proteins are characterized by the presence of a large extracellular domain, located between two transmembrane α-helices, and by short NH 2 and COOH terminal cytoplasmic segments. They constitute the first members of a new gene super-family of ionic channels. The epithelial Na + channel is specifically expressed at the apical membrane of Na +-reabsorbing epithelial cells. Its activity is controlled by several distinct hormones, especially by corticosteroids. These hormones act either transcriptionally (such as aldosterone in distal colon, or glucocorticoids in lung) and/or post-transcriptionally (such as aldosterone in kidney). Recent works have provided new insights in the function of that important osmoregulatory system.
ISSN:0300-9629
1096-4940
1879-1115
DOI:10.1016/S0300-9629(97)00066-2