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  • Title: Regulation of a cloned epithelial Na+ channel by its beta- and gamma-subunits.
    Author: Awayda MS, Tousson A, Benos DJ.
    Journal: Am J Physiol; 1997 Dec; 273(6):C1889-99. PubMed ID: 9435494.
    Abstract:
    Using the Xenopus oocyte expression system, we examined the mechanisms by which the beta- and gamma-subunits of an epithelial Na+ channel (ENaC) regulate alpha-subunit channel activity and the mechanisms by which beta-subunit truncations cause ENaC activation. Expression of alpha-ENaC alone produced small amiloride-sensitive currents (-43 +/- 10 nA, n = 7). These currents increased > 30-fold with the coexpression of beta- and gamma-ENaC to -1,476 +/- 254 nA (n = 20). This increase was accompanied by a 3.1- and 2.7-fold increase of membrane fluorescence intensity in the animal and vegetal poles of the oocyte, respectively, with use of an antibody directed against the alpha-subunit of ENaC. Truncation of the last 75 amino acids of the beta-subunit COOH terminus, as found in the original pedigree of individuals with Liddle's syndrome, caused a 4.4-fold (n = 17) increase of the amiloride-sensitive currents compared with wild-type alpha beta gamma-ENaC. This was accompanied by a 35% increase of animal pole membrane fluorescence intensity. Injection of a 30-amino acid peptide with sequence identity to the COOH terminus of the human beta-ENaC significantly reduced the amiloride-sensitive currents by 40-50%. These observations suggest a tonic inhibitory role on the channel's open probability (Po) by the COOH terminus of beta-ENaC. We conclude that the changes of current observed with coexpression of the beta- and gamma-subunits or those observed with beta-subunit truncation are likely the result of changes of channel density in combination with large changes of Po.
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