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Am J Physiol Cell Physiol 283: C1206-C1218, 2002. First published June 5, 2002; doi:10.1152/ajpcell.00512.2001
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Vol. 283, Issue 4, C1206-C1218, October 2002

AE4 is a DIDS-sensitive Clminus /HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> exchanger in the basolateral membrane of the renal CCD and the SMG duct

Shigeru B. H. Ko1, Xiang Luo1, Henrik Hager2, Alexandra Rojek2, Joo Young Choi1, Christoph Licht3, Makoto Suzuki4, Shmuel Muallem1, Søren Nielsen2, and Kenichi Ishibashi4

1 Department of Physiology and 3 Department of Medicine, Division of Nephrology, University of Texas Southwestern Medical Center, Dallas, Texas 75390; 2 Department of Cell Biology, Institute of Anatomy, University of Aarhus, DK 8000 Denmark; and 4 Department of Pharmacology, Jichi Medical School, Minamikawachi, 329-0498 Tochigi, Japan

The renal cortical collecting duct (CCD) plays an important role in systemic acid-base homeostasis. The beta -intercalated cells secrete most of the HCO<UP><SUB>3</SUB><SUP>−</SUP></UP>, which is mediated by a luminal, DIDS-insensitive, Cl-/HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> exchange. The identity of the luminal exchanger is a matter of debate. Anion exchanger isoform 4 (AE4) cloned from the rabbit kidney was proposed to perform this function (Tsuganezawa H et al. J Biol Chem 276: 8180-8189, 2001). By contrast, it was proposed (Royaux IE et al. Proc Natl Acad Sci USA 98: 4221-4226, 2001) that pendrin accomplishes this function in the mouse CCD. In the present work, we cloned, localized, and characterized the function of the rat AE4. Northern blot and RT-PCR showed high levels of AE4 mRNA in the CCD. Expression in HEK-293 and LLC-PK1 cells showed that AE4 is targeted to the plasma membrane. Measurement of intracellular pH (pHi) revealed that AE4 indeed functions as a Cl-/HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> exchanger. However, AE4 activity was inhibited by DIDS. Immunolocalization revealed species-specific expression of AE4. In the rat and mouse CCD and the mouse SMG duct AE4 was in the basolateral membrane. By contrast, in the rabbit, AE4 was in the luminal and lateral membranes. In both, the rat and rabbit CCD AE4 was in alpha -intercalated cells. Importantly, localization of AE4 was not affected by the systemic acid-base status of the rats. Therefore, we conclude that expression and possibly function of AE4 is species specific. In the rat and mouse AE4 functions as a Cl-/HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> exchanger in the basolateral membrane of alpha -intercalated cells and may participate in HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> absorption. In the rabbit AE4 may contribute to HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> secretion.

anion exchanger isoform 4; 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid; submandibular gland; alpha -intercalated cells; kidney; cortical collecting duct


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