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Comp Biochem Physiol A Physiol. 1997 Oct;118(2):193-200.

The amiloride-sensitive Na+ channel: from primary structure to function.

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Institut de Pharmacologie, Mol├ęculaire et Cellulaire, CNRS UPR 411 600, Sophia Antipolis, Valbonne, France.


Three homologous subunits of the amiloride-sensitive Na+ channel, entitled alpha, beta, and gamma, have been cloned either from distal colon of a steroid-treated rat or from human lung. The alpha, beta, and gamma 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 alpha-helices, and by short NH2 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.

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