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Vol. 12, Issue 2, 255-264, February 2001
*Division de Néphrologie, Fondation pour Recherches
Médicales, CH-1211 Genève 4, Switzerland;
Cyclic AMP (cAMP) stimulates the transport of Na+ and
Na,K-ATPase activity in the renal cortical collecting duct (CCD). The aim of this study was to investigate the mechanism whereby cAMP stimulates the Na,K-ATPase activity in microdissected rat CCDs and
cultured mouse mpkCCDc14 collecting duct cells.
db-cAMP (10Service de Néphrologie Pédiatrique,
Hôpital A. Trousseau, F-75571 Paris cedex 12, France;
¶Service de Biologie Cellulaire, Unité de Recherche
Associée 1859, Commissariat à l'Energie Atomique Saclay,
F-91191 Gif sur Yvette, France; §Institut National de la
Santé et de la Recherche Médicale U478, Faculté de
Médecine Xavier Bichat, F-75870 Paris Cedex 18, France; and
Département de Morphologie, Centre Médical
Universitaire, 1211 Genève 4, Switzerland
3 M) stimulated by 2-fold the activity
of Na,K-ATPase from rat CCDs as well as the ouabain-sensitive component
of 86Rb+ uptake by rat CCDs (1.7-fold) and
cultured mouse CCD cells (1.5-fold). Pretreatment of rat CCDs with
saponin increased the total Na,K-ATPase activity without further
stimulation by db-cAMP. Western blotting performed after a
biotinylation procedure revealed that db-cAMP increased the amount of
Na,K-ATPase at the cell surface in both intact rat CCDs (1.7-fold) and
cultured cells (1.3-fold), and that this increase was not related to
changes in Na,K-ATPase internalization. Brefeldin A and low temperature
(20°C) prevented both the db-cAMP-dependent increase in cell surface
expression and activity of Na,K-ATPase in both intact rat CCDs and
cultured cells. Pretreatment with the intracellular Ca2+
chelator
bis-(o-aminophenoxy)-N,N,N',N'-tetraacetic
acid also blunted the increment in cell surface expression and
activity of Na,K-ATPase caused by db-cAMP. In conclusion, these results strongly suggest that the cAMP-dependent stimulation of Na,K-ATPase activity in CCD results from the translocation of active pump units
from an intracellular compartment to the plasma membrane.
These authors contributed equally to this work.
#
Corresponding author. E-mail address:
feraille{at}cmu.unige.ch.
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