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Am J Physiol Cell Physiol (June 5, 2002). doi:10.1152/ajpcell.00512.2001
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Articles in PresS, published online ahead of print June 5, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00512.2001
Submitted on October 25, 2001
Accepted on May 8, 2002

AE4 is a DIDS-Sensitive Cl-/HCO3- exchanger in the basolateral membrane of the rat and mouse renal CCD and the SMG duct

Shigeru B. H. Ko1, Luo Xiang1, Henrik Hager2, Alexandra Rojek2, Joo Young Choi1, Christoph Licht1, Makoto Suzuki3, Shmuel Muallem1*, Soren Nielsen2, and Kenichi Ishibashi3

1 Department of Physiology, and Department of Medicine, University of Texas Southwestern Medical Center, Dallas, TX, USA
2 Department of Cell Biology, Institute of Anatomy, University of Aarhus, Aarhus, Denmark
3 Department of Pharmacology, Jichi Medical School, Minamikawachi, Tochigi, Japan

* To whom correspondence should be addressed. E-mail: shmuel.muallem{at}utsouthwestern.edu.

The kidney cortical collecting duct (CCD) plays an important role in systemic acid-base homeostasis. The ß-intercalated cells are responsible for most HCO3- secretion, which is mediated by a luminal, DIDS-insensitive, Cl-/HCO3- exchange activity. The identity of the Cl-/HCO3- exchanger in the luminal membrane is a matter of debate. Recently AE4, a new member of the AE anion exchanger family, has been cloned from rabbit kidney and was proposed to function as a DIDS-insensitive Cl-/HCO3- exchanger in the luminal membrane of b-intercalated cells (Tsuganezawa et al, J.Biol.Chem., 276, 8180-8189, 2001). By contrast, Royaux et al (Proc. Natl. Acad. Sci. U S A. 98, 4221-4226, 2001) proposed that pendrin is the luminal Cl-/HCO3- exchanger in the mouse ß-intercalated cells. In the present work, we cloned and characterized the function and localization of the AE4 ortholog from rat kidney. Northern blot analysis of rat tissues and RT-PCR analysis of microdissected nephron segments showed high levels of AE4 mRNA in the kidney, and within the kidney in the CCD. Expression in HEK 293 and LLCPK1 cells showed that AE4 is targeted to the plasma membrane. Measurement of pHi in HEK 293 cells showed that AE4 indeed functions as Cl-/HCO3- exchanger. However, the activity of AE4 was completely inhibited by H2DIDS and DIDS. Immunolocalization in vivo revealed species-specific expression of AE4. In the rat CCD and in the mouse CCD and submandibular gland duct AE4 is expressed in the basolateral membrane. By contrast, in the rabbit AE4 was found in the luminal and lateral membranes. Both in the rat and rabbit CCD AE4 was found in a{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 probably function of AE4 is species-dependent. In the rat and mouse AE4 functions as a Cl-/HCO3- exchanger in the basolateral membrane of {alpha}-intercalated cells and may participate in HCO3- absorption by the CCD. In the rabbit AE4 may contribute to HCO3- secretion.




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