SLC26A6 and SLC26A7 Anion Exchangers Have a Distinct Distribution in Human Kidney

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Abstract

Background: The anion transporters SLC26A6 (PAT1) and SLC26A7, transporting at least chloride, oxalate, sulfate and bicarbonate, show a distinct expression and function in different mammalian species. They are expressed in kidney, but their exact localization in human kidney has not been studied. We therefore examined SLC26A6 and A7 expression in human kidneys. Methods: The localization of SLC26A6 and A7 in different segments of human nephrons was studied by RT-PCR and immunohistochemistry by comparing to the tubular markers PNRA, CD10, Tamm-Horsfall antigen, high molecular weight cytokeratin, CK7, AQP2 and H<sup>+</sup>V-ATPase. Results: In human kidney, SLC26A6 is expressed in distal segments of proximal tubules, parts of the thin and thick ascending limbs of Henle’s loops, macula densa, distal convoluted tubules and a subpopulation of intercalated cells of collecting ducts. SLC26A7 is expressed in extraglomerular mesangial cells and a subpopulation of intercalated cells of collecting ducts. Conclusion: Our results show that in human kidney SLC26A6 and A7 have a distinct, partially overlapping expression in distal segments of nephrons. The distribution partly differs from that found previously in rodent kidneys.

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Renal vacuolar H+-ATPase.

Dennis Brown, K Finberg, Sylvie Breton … (2004)

Vacuolar H(+)-ATPases are ubiquitous multisubunit complexes mediating the ATP-dependent transport of protons. In addition to their role in acidifying the lumen of various intracellular organelles, vacuolar H(+)-ATPases fulfill special tasks in the kidney. Vacuolar H(+)-ATPases are expressed in the plasma membrane in the kidney almost along the entire length of the nephron with apical and/or basolateral localization patterns. In the proximal tubule, a high number of vacuolar H(+)-ATPases are also found in endosomes, which are acidified by the pump. In addition, vacuolar H(+)-ATPases contribute to proximal tubular bicarbonate reabsorption. The importance in final urinary acidification along the collecting system is highlighted by monogenic defects in two subunits (ATP6V0A4, ATP6V1B1) of the vacuolar H(+)-ATPase in patients with distal renal tubular acidosis. The activity of vacuolar H(+)-ATPases is tightly regulated by a variety of factors such as the acid-base or electrolyte status. This regulation is at least in part mediated by various hormones and protein-protein interactions between regulatory proteins and multiple subunits of the pump.

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Functional characterization of three novel tissue-specific anion exchangers SLC26A7, -A8, and -A9.

Ulpu Saarialho-Kere, Pirjo S. A. Mäkelä, Urho M Kujala … (2002)

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.

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Identification of a chloride-formate exchanger expressed on the brush border membrane of renal proximal tubule cells.

G Giebisch, Robin Thomson, A Mentone … (2001)

A key function of the proximal tubule is retrieval of most of the vast quantities of NaCl and water filtered by the kidney. Physiological studies using brush border vesicles and perfused tubules have indicated that a major fraction of Cl(-) reabsorption across the apical membrane of proximal tubule cells occurs via Cl(-)-formate exchange. The molecular identity of the transporter responsible for renal brush border Cl(-)-formate exchange has yet to be elucidated. As a strategy to identify one or more anion exchangers responsible for mediating Cl(-) reabsorption in the proximal tubule, we screened the expressed sequence tag database for homologs of pendrin, a transporter previously shown to mediate Cl(-)-formate exchange. We now report the cDNA cloning of CFEX, a mouse pendrin homolog with expression in the kidney by Northern analysis. Sequence analysis indicated that CFEX very likely represents the mouse ortholog of human SLC26A6. Immunolocalization studies detected expression of CFEX, but not pendrin, on the brush border membrane of proximal tubule cells. Functional expression studies in Xenopus oocytes demonstrated that CFEX mediates Cl(-)-formate exchange. Taken together, these observations identify CFEX as a prime candidate to mediate Cl(-)-formate exchange in the proximal tubule and thereby to contribute importantly to renal NaCl reabsorption. Given its wide tissue distribution, CFEX also may contribute to transcellular Cl(-) transport in additional epithelia such as the pancreas and contribute to transmembrane Cl(-) transport in nonepithelial tissues such as the heart.

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Journal

Journal ID (publisher-id): NEE

Journal ID (nlm-ta): Nephron Exp Nephrol

Journal ID (doi): 10.1159/issn.1660-2129

Title: Cardiorenal Medicine

Publisher: S. Karger AG

ISSN (Electronic): 1660-2129

Publication date Subscription-year: 2005

Publication date (Print): October 2005

Publication date (Electronic): 15 June 2005

Volume: 101

Issue: 2

Pages: e50-e58

Affiliations

^aDepartment of Medical Genetics, University of Helsinki; ^bDepartment of Urology, Helsinki University Central Hospital, Helsinki; ^cDepartment of Pathology, Helsinki University Central Hospital/Peijas Hospital and HUSLAB, Vantaa; ^dInstitute of Biomedicine, Developmental Biology, University of Helsinki, and HUCH Laboratory Diagnostics, Helsinki University Hospital; ^eDepartment of Pathology, Haartman Institute and Helsinki University Central Hospital, University of Helsinki, Helsinki Finland, and Department of Cellular and Molecular Medicine, University of California at San Diego, La Jolla, Calif., USA; ^fDepartment of Biosciences at Novum, Karolinska Institutet, Stockholm, Sweden

Article

Publisher ID: 86345 Other ID: Nephron Exp Nephrol 2005;101:e50–e58

DOI: 10.1159/000086345

PubMed ID: 15956810

SO-VID: daf55181-72cb-48da-85df-fad4872680af

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SLC26A6 and SLC26A7 Anion Exchangers Have a Distinct Distribution in Human Kidney

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Abstract

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Karger: Nephrology

Most cited references 20

Renal vacuolar H+-ATPase.

Functional characterization of three novel tissue-specific anion exchangers SLC26A7, -A8, and -A9.

Identification of a chloride-formate exchanger expressed on the brush border membrane of renal proximal tubule cells.

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