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J. Biol. Chem., Vol. 276, Issue 50, 47087-47093, December 14, 2001
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From the Aldosterone controls extracellular volume and
blood pressure by regulating Na+ reabsorption, in
particular by epithelia of the distal nephron. A main regulatory site
of this transcellular transport is the epithelial sodium channel (ENaC)
that mediates luminal Na+ influx. The Na,K-ATPase
(Na+ pump) that coordinately extrudes Na+
across the basolateral membrane is known to be regulated by short term
aldosterone as well. We now show that in the cortical collecting duct
(CCD) from adrenalectomized rats, the increase in Na,K-ATPase activity (approximately 3-fold in 3 h), induced by a single
aldosterone injection, can be fully accounted by the increase in
Na,K-ATPase cell surface expression (+ 497 ± 35%). The short
term aldosterone action was further investigated in cultured mouse
collecting duct principal cells mpkCCDcl4. Within 2 h,
maximal Na,K-ATPase function assessed by Na+ pump current
(Ip) measurements and Na,K-ATPase cell surface
expression were increased by 20-50%. Aldosterone did not modify the
Na+ dependence of the Na+ pumps and induced
transcription- and translation-dependent actions on pump
surface expression and current independently of ENaC-mediated Na+ influx. In summary, short term aldosterone directly
increases the cell surface expression of pre-existing Na+
pumps in kidney CCD target cells. Thus, aldosterone controls Na+ reabsorption in the short term not only by regulating
the apical cell surface expression of ENaC (Loffing, J., Zecevic, M.,
Feraille, E., Kaissling, B., Asher, C., Rossier, B. C., Firestone,
G. L., Pearce, D., and Verrey, F. (2001) Am. J. Physiol. 280, F675-F682) but also by coordinately acting on the
basolateral cell surface expression of the Na,K-ATPase.
Short Term Effect of Aldosterone on Na,K-ATPase Cell Surface
Expression in Kidney Collecting Duct Cells*
§,
,,**, and Institute of Physiology, University of
Zürich, Zürich, CH-8057 Switzerland, the ¶ Division of
Nephrology and Department of Pathology, University of Geneva, CH-1211
Geneva, Switzerland, and INSERM, Unité 478, Faculté
de Médecine Xavier-Bichat,
75870 Paris Cedex 18, France
*
This work was supported by Swiss National Science Foundation
Grants 31-59141.99 (to F. V.) and 31-50830.99 (to E. F.), by the Hartmann-Müller Stiftung in Zürich, and by the Carlos
and Elsie de Reuter Foundation in Geneva.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.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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