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J. Biol. Chem., Vol. 277, Issue 16, 14246-14254, April 19, 2002
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From the A second distinct family of anion exchangers,
SLC26, in addition to the classical SLC4 (or anion exchanger) family,
has recently been delineated. Particular interest in this gene family
is stimulated by the fact that the SLC26A2, SLC26A3,
and SLC26A4 genes have been recognized as the disease genes
mutated in diastrophic dysplasia, congenital chloride diarrhea, and
Pendred syndrome, respectively. We report the expansion of the
SLC26 gene family by characterizing three novel
tissue-specific members, named SLC26A7, SLC26A8, and SLC26A9, on chromosomes 8, 6, and 1, respectively. The
SLC26A7-A9 proteins are structurally very similar at the amino acid
level to the previous family members and show tissue-specific
expression in kidney, testis, and lung, respectively. More detailed
characterization by immunohistochemistry and/or in situ hybridization
localized SLC26A7 to distal segments of nephrons, SLC26A8 to developing spermatocytes, and SLC26A9 to the lumenal side of the bronchiolar and
alveolar epithelium of lung. Expression of SLC26A7-A9 proteins in
Xenopus oocytes demonstrated chloride, sulfate, and oxalate transport activity, suggesting that they encode functional anion exchangers. The functional characterization of the novel
tissue-specific members may provide new insights to anion transport
physiology in different parts of body.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF331521, AF331522, and AF331525.
Functional Characterization of Three Novel Tissue-specific Anion
Exchangers SLC26A7, -A8, and -A9*
,,,,
, and**
Department of Medical Genetics, Biomedicum
Helsinki and Helsinki University Central Hospital, P. O. Box 63 (Haartmaninkatu 8), 00014 University of Helsinki, Helsinki, the
§ Department of Pathology, Haartman Institute and Helsinki
University Central Hospital, P. O. Box 21, 00014 University of
Helsinki, Finland, ¶ Department of Dermatology, Helsinki
University Central Hospital, 00029 Helsinki, Finland,
School of Biomedical Sciences, Department of Physiology and
Pharmacology, University of Queensland, Brisbane,
Queensland 4072, Australia, and ** Karolinska Institute,
Department of Biosciences at Novum, and Clinical Research Centre,
14157 Huddinge, Sweden
*
This study was supported by the Academy of Finland, Duodecim
Foundation, Ella and Georg Ehrnrooth Foundation, Finska
Läkaresällskapet, Sigrid Juselius Foundation, Foundation
for Pediatric Research, Ulla Hjelt Fund, HUCH research funds, the
National Health and Medical Research Council of Australia (to D. M.),
the Wihuri Foundation, Oskar Öflund Foundation, and Research and
Science Foundation of Farmos.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.
To whom correspondence should be addressed: Karolinska
Institute, Dept. of Biosciences at Novum, 14157 Huddinge, Sweden. Tel.: 358-50-5319123; Fax: 46-8-7745538; E-mail:
juha.kere@biosci.ki.se.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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