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J. Biol. Chem., Vol. 275, Issue 32, 24552-24559, August 11, 2000
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From the Regulation of intra- and extracellular ion
activities (e.g. H+, Cl The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF047468.
Cloning and Characterization of a Na+-driven
Anion Exchanger (NDAE1)
A NEW BICARBONATE TRANSPORTER*
§¶,,
,,, and**
Department of Physiology & Biophysics, the
§ Department of Pharmacology, and the Department of
Genetics, Case Western Reserve University School of Medicine,
Cleveland, Ohio 44106-4970
,
Na+) is key to normal function of the central nervous
system, digestive tract, respiratory tract, and urinary system.
With our cloning of an electrogenic
Na+/HCO3 cotransporter (NBC), we found
that NBC and the anion exchangers form a bicarbonate transporter
superfamily. Functionally three other HCO3
transporters are known: a neutral Na+/
HCO3 cotransporter, a K+/
HCO3 cotransporter, and a
Na+-dependent
Cl-HCO3 exchanger. We report the
cloning and characterization of a Na+-coupled
Cl-HCO3 exchanger and a physiologically
unique bicarbonate transporter superfamily member. This
Drosophila cDNA encodes a 1030-amino acid membrane
protein with both sequence homology and predicted topology similar to
the anion exchangers and NBCs. The mRNA is expressed throughout
Drosophila development and is prominent in the central
nervous system. When expressed in Xenopus oocytes, this
membrane protein mediates the transport of Cl,
Na+, H+, and HCO3 but does
not require HCO3. Transport is blocked by the
stilbene 4,4'-diisothiocyanodihydrostilbene- 2,2'-disulfonates and may
not be strictly electroneutral. Our functional data suggest this
Na+ driven anion
exchanger (NDAE1) is responsible for the
Na+-dependent
Cl-HCO3 exchange activity characterized
in neurons, kidney, and fibroblasts. NDAE1 may be generally important
for fly development, because disruption of this gene is apparently
lethal to the Drosophila larva.
*
This work was supported by the American Heart Association
(to M. F. R.) Howard Hughes Medical Institute grant to Case
Western Reserve University School of Medicine (to M. F. R.) Ireland
Cancer Center ACS-IRG 91-022 (to M. F. R.), and Grant
GM39255 (to P. J. H.).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.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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