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Originally published In Press as doi:10.1074/jbc.M000954200 on March 27, 2000

J. Biol. Chem., Vol. 275, Issue 22, 16550-16559, June 2, 2000
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Methylation Increases the Open Probability of the Epithelial Sodium Channel in A6 Epithelia*

Andrea BecchettiDagger , Alexandra E. KemendyDagger §, James D. StockandDagger , Sarah Sariban-Sohraby||, and Douglas C. EatonDagger **

From the Dagger  Department of Physiology and the  Center for Cell & Molecular Signaling, Emory University School of Medicine, Atlanta, Georgia 30322 and the || Université Libre de Bruxelles, Laboratoire de Physiologie et Physiopatologie, Bruxelles 1070, Belgium

We used single channel methods on A6 renal cells to study the regulation by methylation reactions of epithelial sodium channels. 3-Deazaadenosine (3-DZA), a methyltransferase blocker, produced a 5-fold decrease in sodium transport and a 6-fold decrease in apical sodium channel activity by decreasing channel open probability (Po). 3-Deazaadenosine also blocked the increase in channel open probability associated with addition of aldosterone. Sodium channel activity in excised "inside-out" patches usually decreased within 1-2 min; in the presence of S-adenosyl-L-methionine (AdoMet), activity persisted for 5-8 min. Sodium channel mean time open (topen) before and after patch excision was higher in the presence of AdoMet than in untreated excised patches but less than topen in cell-attached patches. Sodium channel activity in excised patches exposed to both AdoMet and GTP usually remained stable for more than 10 min, and Po and the number of active channels per patch were close to values in cell-attached patches from untreated cells. These findings suggest that a methylation reaction contributes to the activity of epithelial sodium channels in A6 cells and is directed to some regulatory element closely connected with the channel, whose activity also depends on the presence of intracellular GTP.

* This work was supported by Department of Health and Human Services Grant R01 DK37963 (to D. C. E.) and the Egelston Hospital Children's Research Center.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Performed a portion of this work to partially fulfill doctoral requirements.

** To whom reprint requests should be addressed: Dept. of Physiology, Emory University School of Medicine, 1648 Pierce Dr., N.E., Atlanta, GA 30322.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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