Functional expression and subcellular localization of an anion exchanger cloned from choroid plexus.
Author(s) -
A E Lindsey,
Karin Schneider,
Donna M. Simmons,
Roland Baron,
Byong Sop Lee,
Ron R. Kopito
Publication year - 1990
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.87.14.5278
Subject(s) - choroid plexus , band 3 , complementary dna , extracellular , immunocytochemistry , microbiology and biotechnology , intracellular ph , intracellular , cytoplasm , chemistry , in situ hybridization , biochemistry , biology , gene expression , membrane protein , membrane , gene , central nervous system , endocrinology
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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