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Localization of Sodium Bicarbonate Cotransporter (NBC) Protein and Messenger Ribonucleic Acid in Rat Epididymis¹

^a Renal Unit and Program in Membrane Biology, Massachusetts General Hospital, ^b Department of Pathology, Harvard Medical School, Charlestown, Massachusetts 02129 ^c Renal Division, Brigham and Women's Hospital, Boston, Massachusetts 02115 ^d Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06520

An acidic environment is important for sperm maturation in the epididymis and also helps to maintain mature sperm in an immotile state during storage in this organ. Both an Na⁺/H⁺ exchanger and an H⁺ATPase have been implicated in this process. The H⁺ATPase is concentrated in specialized apical (and/or narrow) and clear cells of the epididymis, while the Na⁺/H⁺ exchanger has not yet been localized in situ. As in other proton-secreting epithelia, bicarbonate transport occurs in the epididymis, where it is implicated in luminal acidification. In this study we used an antibody raised against a fusion protein (maltose-binding protein: MBP-NBC-5) from the C-terminus of the recently cloned rat kidney Na⁺/HCO₃^- cotransporter (NBC) to localize this protein in the epididymis and vas deferens of the rat. The distribution of the respective mRNA was mapped by in situ hybridization. NBC message was strongly expressed in the initial segment and the intermediate zone of the epididymis, and the NBC-5 antibody gave a strong basolateral staining in both principal cells and apical/narrow cells in this region. Western blotting revealed a single band at about 160 kDa in the epididymis. The intensity of staining as well as mRNA levels decreased in the cauda epididymidis and in the vas deferens, where only weak staining was seen. Basolateral NBC may function in parallel with apical proton secretion to regulate luminal acidification and/or bicarbonate reabsorption in the excurrent duct system.

¹ This work was supported by NIH Grant DK 38452 (S.B. and D.B.). S.B. was partially supported by a grant from the National Kidney Foundation and by a Claflin Distinguished Scholar Award from the Massachusetts General Hospital. B.M.S. was supported by a "Forschungsstipendium" from the Deutsche Forschungsgemeinschaft (DFG). L.J.J. is a Ph.D.-scholar from the August Krogh Institute and was partially supported by grant 11-0971 from the Danish Natural Science Research Council.

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

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