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The epithelial sodium channel is a multimeric protein formed by three homologous subunits:
, β, and 
; each subunit contains only two transmembrane domains. The level of expression of each of the subunits is markedly different in various Na+ absorbing epithelia raising the possibility that channels with different subunit composition can function in vivo. We have examined the functional properties of channels formed by the association of with β and of with in the Xenopus oocyte expression system using two-microelectrode voltage clamp and patch-clamp techniques. We found that β channels differ from channels in the following functional properties: (a) β channels expressed larger Na+ than Li+ currents (INa+/ILi+ 1.2) whereas channels expressed smaller Na+ than Li+ currents (INa+/ILi+ 0.55); (b) the Michaelis Menten constants (Km) of activation of current by increasing concentrations of external Na+ and Li+ of β channels were larger (Km > 180 mM) than those of channels (Km of 35 and 50 mM, respectively); (c) single channel conductances of β channels (5.1 pS for Na+ and 4.2 pS for Li+) were smaller than those of channels (6.5 pS for Na+ and 10.8 pS for Li+); (d) the half-inhibition constant (Ki) of amiloride was 20-fold larger for β channels than for channels whereas the Ki of guanidinium was equal for both β and . To identify the domains in the channel subunits involved in amiloride binding, we constructed several chimeras that contained the amino terminus of the subunit and the carboxy terminus of the β subunit. A stretch of 15 amino acids, immediately before the second transmembrane domain of the β subunit, was identified as the domain conferring lower amiloride affinity to the β channels. We provide evidence for the existence of two distinct binding sites for the amiloride molecule: one for the guanidium moiety and another for the pyrazine ring. At least two subunits with β or contribute to these binding sites. Finally, we show that the most likely stoichiometry of β and channels is 1:1β and 1:1, respectively.
Key Words: epithelial Na+ channel • amiloride • guanidinium • Xenopus oocyte
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