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Originally published In Press as doi:10.1074/jbc.C000716200 on December 27, 2000

J. Biol. Chem., Vol. 276, Issue 11, 8358-8363, March 16, 2001
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Cloning, Characterization, and Chromosomal Mapping of a Human Electroneutral Na+-driven Cl-HCO3 Exchanger*

Irina I GrichtchenkoDagger §, Inyeong ChoiDagger , Xiaobo Zhong||, Patricia Bray-Ward||, John M. Russell**, and Walter F. BoronDagger

From the Dagger  Department of Cellular and Molecular Physiology and the || Department of Genetics, Yale University School of Medicine, New Haven, Connecticut 06520 and the ** Department of Biology, Syracuse University, Syracuse, New York 13244

The electroneutral Na+-driven Cl-HCO3 exchanger is a key mechanism for regulating intracellular pH (pHi) in neurons, glia, and other cells. Here we report the cloning, tissue distribution, chromosomal location, and functional characterization of the cDNA of such a transporter (NDCBE1) from human brain (GenBankTM accession number AF069512). NDCBE1, which encodes 1044 amino acids, is 34% identical to the mammalian anion exchanger (AE2); ~50% to the electrogenic Na/HCO3 cotransporter (NBCe1) from salamander, rat, and humans; ~73% to mammalian electroneutral Na/HCO3 cotransporters (NBCn1); 71% to mouse NCBE; and 47% to a Na+-driven anion exchanger (NDAE1) from Drosophila. Northern blot analysis of NDCBE1 shows a robust ~12-kilobase signal in all major regions of human brain and in testis, and weaker signals in kidney and ovary. This human gene (SLC4A8) maps to chromosome 12q13. When expressed in Xenopus oocytes and running in the forward direction, NDCBE1 is electroneutral and mediates increases in both pHi and [Na+]i (monitored with microelectrodes) that require HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> and are blocked by 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS). The pHi increase also requires extracellular Na+. The Na+:HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> stoichiometry is 1:2. Forward-running NDCBE1 mediates a 36Cl efflux that requires extracellular Na+ and HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> and is blocked by DIDS. Running in reverse, NDCBE1 requires extracellular Cl-. Thus, NDCBE1 encodes a human, electroneutral Na+-driven Cl-HCO3 exchanger.

* This work was supported by National Institutes of Health Grant NS18400.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF069512 (for the electroneutral Na+-driven Cl-HCO3 exchanger gene).

The amino acid sequence of this protein can be accessed through NCBI Protein Database under NCBI accession number AAC82380.

§ Supported by the National Kidney Foundation. To whom correspondence should be addressed: Dept. of Cellular and Molecular Physiology, Yale University School of Medicine, 333 Cedar St., New Haven, CT 06520-8026. Tel.: 203-785-5097; Fax: 203-785-4951; E-mail: ira_grich@hotmail.com.

Supported by the American Heart Association.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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