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Immunolocalization of AE2 Anion Exchanger in Rat and Mouse Epididymis¹

^a Renal Unit and Program in Membrane Biology, Massachusetts General Hospital, Charlestown, Massachusetts 02129 ^b Molecular Medicine and Renal Units, Beth Israel Deaconess Medical Center, Boston, Massachusetts 02215 ^c Division of Hematology, The Children's Hospital, Boston, Massachusetts 02215 ^d Departments of Medicine, Cell Biology, ^e and Pediatrics, ^f Harvard Medical School, Boston, Massachusetts 02215 ^g The Jackson Laboratories, Bar Harbor, Maine 04609

A low-bicarbonate concentration and an acidic pH in the luminal fluid of the epididymis and vas deferens are important for sperm maturation. These factors help maintain mature sperm in an immotile but viable state during storage in the cauda epididymidis and vas deferens. Two proton extrusion mechanisms, an Na⁺/H⁺ exchanger and an H⁺ATPase, have been proposed to be involved in this luminal acidification process. The Na⁺/H⁺ exchanger has not yet been localized in situ, but we have reported that H⁺ATPase is expressed on the apical membrane of apical (or narrow) and clear cells of the epididymis. These cells are enriched in carbonic anhydrase II, indicating the involvement of bicarbonate in the acidification process and suggesting that the epididymis is a site of bicarbonate reabsorption. Previous unsuccessful attempts to localize the Cl/HCO₃ anion exchanger AE1 in rat epididymis did not investigate other anion exchanger (AE) isoforms. In this report, we used a recently described SDS antigen unmasking treatment to localize the Cl/HCO₃ exchanger AE2 in rat and mouse epididymis. AE2 is highly expressed in the initial segment, intermediate zone, and caput epididymidis, where it is located on the basolateral membrane of epithelial cells. The cauda epididymidis and vas deferens also contain basolateral AE2, but in lower amounts. The identity of the AE2 protein was further confirmed by the observation that basolateral AE2 expression was unaltered in the epididymis of AE1-knockout mice. Basolateral AE2 may participate in bicarbonate reabsorption and luminal acidification, and/or may be involved in intracellular pH homeostasis of epithelial cells of the male reproductive tract.

¹ S.B. was supported by NIH Grant DK 38452, by a grant from the National Kidney Foundation, and by a Claflin Distinguished Scholar Award from the Massachusetts General Hospital. L.J.J. is a Ph.D. scholar from the August Krogh Institute, The University of Copenhagen, and was partially supported by grant 11-0971 from the Danish Natural Science Research Council. S.L.A. was supported by NIH grants DK43495 and DK34854 (Harvard Digestive Diseases Center), and an Established Investigator Award of the American Heart Association.

² Correspondence: Sylvie Breton, Renal Unit and Program in Membrane Biology, Massachusetts General Hospital East, 149 13th Street, Charlestown, MA 02129. FAX: 617 726 5669; sbreton{at}receptor.mgh.harvard.edu

³ L.J. Jensen and A.K. Stuart-Tilley share the first author position.

⁴ Current address: Zoophysiological Laboratory, August Krogh Institute, 13 Universitetsparken, DK-2100, Kbh. O, Denmark.

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