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J Biol Chem, Vol. 274, Issue 47, 33183-33185, November 19, 1999

COMMUNICATION
The gamma  Subunit Modulates Na+ and K+ Affinity of the Renal Na,K-ATPase

Elena Arystarkhova, Randall K. Wetzel, Natalya K. Asinovski, and Kathleen J. Sweadner

From the Laboratory of Membrane Biology, Neuroscience Center, Massachusetts General Hospital, Charlestown, Massachusetts 02129

The Na+,K+-ATPase catalyzes the active transport of ions. It has two necessary subunits, alpha  and beta , but in kidney it is also associated with a 7.4-kDa protein, the gamma  subunit. Stable transfection was used to determine the effect of gamma  on Na,K-ATPase properties. When isolated from either kidney or transfected cells, alpha beta gamma had lower affinities for both Na+ and K+ than alpha beta . A post-translational modification of gamma  selectively eliminated the effect on Na+ affinity, suggesting three configurations (alpha beta , alpha beta gamma , and alpha beta gamma *) conferring different stable properties to Na,K-ATPase. In the nephron, segment-specific differences in Na+ affinity have been reported that cannot be explained by the known alpha  and beta  subunit isoforms of Na,K-ATPase. Immunofluorescence was used to detect gamma  in rat renal cortex. Cortical ascending limb and some cortical collecting tubules lacked gamma , correlating with higher Na+ affinities in those segments reported in the literature. Selective expression in different segments of the nephron is consistent with a modulatory role for the gamma  subunit in renal physiology.


Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.



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