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1 Department of Pharmacology
and Toxicology, Kyorin University School of Medicine, Tokyo 181, Japan; 2 Department of
Pharmacology, Catholic University Medical College, Seoul
137-701, Korea; 3 Drug
Metabolism and Pharmacokinetics IV,
We report here the isolation, functional
characterization, tissue distribution, and membrane localization of rat
renal Na+-dicarboxylate
transporter (rNaDC-1). rNaDC-1 consists of 2,245 nucleotides, and the
deduced amino acid sequence showed 73% and 75% identity to rabbit and
human NaDC-1, respectively. When expressed in Xenopus
laevis oocytes, rNaDC-1 mediated sodium-dependent
uptake of di- and tricarboxylates. Substrates of rNaDC-1 evoked inward currents in oocytes expressed with rNaDC-1; succinate,
-ketoglutarate, and glutarate were relatively
high-affinity substrates, and citrate was a low-affinity substrate of
rNaDC-1. The coupling ratio of citrate to charge was determined to be
1:1 at pH 7.4; influx of one positive charge per citrate molecule
suggests a symport of three Na+
with a divalent citrate. Expression of rNaDC-1 mRNA was detected in the
kidney and the small and large intestines. Immunohistochemistry using
polyclonal antibodies raised against the 14 amino acids at the COOH
terminus of rNaDC-1 revealed that rNaDC-1 is localized exclusively in
the luminal membrane of S2 and S3.
sodium-dicarboxylate transporter; membrane localization; electrogenic transport ; citrate; organic anion transport
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