We have isolated rat brain cDNA clones encoding AE2, a homologue of the erythrocyte anion exchanger, band 3 (AE1). Immunocytochemistry and in situ hybridization reveal that, in brain, AE2 expression is restricted to the basolateral membrane of the choroid plexus epithelium. Expression of a full-length mouse AE2 cDNA in COS-7 cells resulted in chloride-and bicarbonate-dependent alterations in intracellular pH, demonstrating that AE2 is a Cl/HCO3 exchanger. Cation replacement studies indicate that AE2-mediated exchange is independent of extracellular sodium. COS-7 cells expressing a mutant rat AE2 cDNA clone that lacks the cytoplasmic NH2-terminal 660 amino acids exhibit identical responses to cation and anion substitution. These results indicate that this domain does not play a significant role in either correct insertion of the transporter into the plasma membrane or anion exchange.
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