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J. Biol. Chem., Vol. 265, Issue 14, 7799-7803, May, 1990
C Barlet-Bas, C Khadouri, S Marsy and A Doucet
Besides its role in the control of the rate of functioning of each Na-K-
ATPase unit (as a substrate of the enzyme), the intracellular sodium
concentration also regulates the number of active Na-K-ATPase units, as
previously described in cultured cells. To evaluate such a possibility in
kidney epithelial cells, the intracellular concentration of sodium in rat
cortical collecting tubules (CCT) maintained in vitro was altered by the
use of the sodium ionophore nystatin. When CCT were preincubated for 2-3 h
at 37 degrees C in the presence of nystatin, the enzymatic activity of
Na-K-ATPase was markedly stimulated as compared to tubules preincubated
without nystatin or in the presence of the ionophore but in the absence of
extracellular sodium. Although nystatin increased both Na-K-ATPase activity
and [3H]ouabain specific binding in CCT, its action was independent of de
novo synthesis of the pump since neither actinomycin D nor cycloheximide
abolished it. It is suggested that increasing the sodium concentration in
CCT cells induces the recruitment of a latent pool of Na-K-ATPase units.
The size of this latent pool of enzyme is under the control of
corticosteroids as it is markedly decreased in CCT from adrenalectomized
rats.
Enhanced intracellular sodium concentration in kidney cells recruits a latent pool of Na-K-ATPase whose size is modulated by corticosteroids
Laboratoire de Physiologie Cellulaire, College de France, Centre National de la Recherche Scientifique, Paris.
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