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1 Physiology and Biophysics, Weill Medical College of Cornell University, New York, New York, United States
* To whom correspondence should be addressed. E-mail: lgpalm{at}med.cornell.edu.
Antibodies directed against subunits of ENaC were used together with electrophysiological measurements in the CCD to investigate the processing of the proteins in rat kidney with changes in Na or K intake. When animals were maintained on a low-Na diet for 7-9 days, the abundance of two forms of the 
subunit, with apparent masses of 85 and 30 kDa, increased. Salt restriction also increased the abundance of the 
subunit and produced an endoglycosidase H (Endo H)-resistant pool of this subunit. The abundance of the 90 kDa form of the 
subunit decreased, while that of a 70 kDa form increased and this peptide also exhibited Endo H-resistant glycosylation. These changes in and subunits were correlated with increases in Na conductance elicited by a 4-hour infusion with aldosterone. Changes in all three subunits were correlated with decreases in Na conductance when Na-deprived animals drank saline for 5 hours. We conclude that ENaC subunits are mainly in an immature form in salt-replete rats. With Na depletion the subunits mature in a process that involves proteolytic cleavage and further glycosylation. Similar changes occurred in and but not subunits when animals were treated with exogenous aldosterone, and in and but not subunits when animals were fed a high-K diet. Changes in the processing and maturation of the channels occur rapidly enough to be involved in the daily regulation of ENaC activity and Na reabsorption by the kidney.
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