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Vol. 55, Issue 4, 743-752, April 1999
Department of Pharmacy, Kyoto University Hospital, Faculty of
Medicine, Kyoto University, Sakyo-ku, Kyoto, Japan
We have isolated a cDNA coding a new organic anion transporter, OAT-K2,
expressed specifically in rat kidney. The OAT-K2 cDNA had an open
reading frame encoding a 498-amino acid protein (calculated molecular
mass of 55 kDa) that shows 91% identity with the rat kidney-specific
organic anion transporter, OAT-K1. Reverse transcription-coupled polymerase chain reaction analyses revealed that the OAT-K2 mRNA was expressed predominantly in the proximal convoluted tubules, proximal straight tubules, and cortical collecting ducts. When expressed in Xenopus oocytes, OAT-K2 stimulated the uptake
of hydrophobic organic anions, such as taurocholate, methotrexate, folate, and prostaglandin E2, although its homolog OAT-K1
transported methotrexate and folate, but not taurocholate and
prostaglandin E2. In MDCK cells stably transfected with the
OAT-K1 and OAT-K2 cDNAs, each transporter was localized functionally to
the apical membranes and showed transport activity similar to that in
the oocyte. Moreover, the efflux of preloaded taurocholate was also enhanced across the apical membrane in OAT-K2 transfectant. The taurocholate transport by OAT-K2-expressing cells showed saturability (Km = 10.3 µM). Several organic anions, bile
acids, cardiac glycosides, and steroids had potent inhibitory effects
on the OAT-K2-mediated taurocholate transport in the transfectant.
These findings suggest that the OAT-K2 participates in epithelial
transport of hydrophobic anionic compounds in the kidney.
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