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Articles in PresS, published online ahead of print October 29, 2002
Am J Physiol Renal Physiol, 10.1152/ajprenal.00352.2002
Submitted on October 2, 2002
Accepted on October 22, 2002
1 Department of Internal Medicine, Yale University School of Medicine, New Haven, CT, USA
2 Department of Anatomy and Cell Biology, University of Kansas Medical Center, Kansas City, KS, USA
3 Department of Internal Medicine, Yale University School of Medicine, New Haven, CT, USA; Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT, USA
* To whom correspondence should be addressed. E-mail: peter.aronson{at}yale.edu.
Although NHE3 mediates most Na+-H+ exchange in the proximal tubule, studies of NHE3/NHE2 null mice suggest residual Na+-dependent proton secretion (4). To characterize additional NHE isoforms that might be expressed in the kidney, we identified the partial sequence of a novel NHE. RACE PCR was used to define the 5' and 3' ends, and a cDNA encoding the complete open reading frame was amplified from mouse kidney. The predicted protein of 576 amino acids, which we have named NHE8, has 30-35% amino acid identity to known mammalian isoforms (NHE1-7), but has >50% identity to Drosophila 'NHE1', suggesting it is the mammalian orthologue of this ancient invertebrate isoform. Northern blot of mouse tissues revealed ubiquitous expression. Western blot using anti-NHE8 antibodies demonstrated protein expression in apical membranes purified from rat renal cortex by divalent cation precipitation. In situ hybridization revealed that NHE8 message was present in both cortex and medulla. In the cortex, NHE8 was present in the majority of cortical tubules, consistent with proximal tubule (S1 and S2) localization. In the medulla, NHE8 message was most highly expressed in the proximal tubules (S3) of the outer stripe of the outer medulla. Thus, NHE8 is expressed in the proximal tubule where it may contribute to apical membrane ion transport.
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