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Section of Nephrology, Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut 06520-8029
Mammalian
Na+/H+
exchangers (NHEs) are a family of transport proteins (NHE1-NHE5).
To date, the cellular and subcellular localization of NHE4 has not been
characterized using immunochemical techniques. We purified a fusion
protein containing a portion of rat NHE4 (amino acids 565-675) to
use as immunogen. A monoclonal antibody (11H11) was selected by ELISA.
It reacted specifically with both the fusion protein and to a 60- to
65-kDa polypeptide expressed in NHE4-transfected LAP1 cells. By Western
blot analysis, NHE4 was identified as a 65- to 70-kDa protein that was
expressed most abundantly in stomach and in multiple additional
epithelial and nonepithelial rat tissues including skeletal muscle,
heart, kidney, uterus, and liver. Subcellular localization of NHE4 in
the kidney was evaluated by Western blot analysis of membrane fractions
isolated by Percoll gradient centrifugation. NHE4 was found to
cofractionate with the basolateral markers NHE1 and
Na+-K+-ATPase
rather than the luminal marker 
-glutamyl transferase. In stomach,
NHE4 was detected by immunoperoxidase labeling on the basolateral
membrane of cells at the base of the gastric gland. We conclude that
NHE4 is a 65- to 70-kDa protein with a broad tissue distribution. In
two types of epithelial cells, kidney and stomach, NHE4 is localized to
the basolateral membrane.
sodium/proton exchanger; kidney; stomach
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