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J Biol Chem, Vol. 274, Issue 29, 20191-20196, July 16, 1999

Expression Cloning and Characterization of a Novel Sodium-Dicarboxylate Cotransporter from Winter Flounder Kidney

Jürgen Steffgen, Birgitta C. Burckhardt§, Christoph Langenberg, Lars Kühne§, Gerhard A. Müller, Gerhard Burckhardt§, and Natascha A. Wolff§

From the Abteilung Nephrologie und Rheumatologie, Georg-August-Universität Göttingen, Robert-Koch-Strasse 40, D-37075 Göttingen, Germany and the § Abteilung Vegetative Physiologie und Pathophysiologie, Georg-August-Universität Göttingen, Humboldtallee 23, D-37073 Göttingen, Germany

A cDNA coding for a Na+-dicarboxylate cotransporter, fNaDC-3, from winter flounder (Pseudopleuronectes americanus) kidney was isolated by functional expression in Xenopus laevis oocytes. The fNaDC-3 cDNA is 2384 nucleotides long and encodes a protein of 601 amino acids with a calculated molecular mass of 66.4 kDa. Secondary structure analysis predicts at least eight membrane-spanning domains. Transport of succinate by fNaDC-3 was sodium-dependent, could be inhibited by lithium, and evoked an inward current. The apparent affinity constant (Km) of fNaDC-3 for succinate of 30 µM resembles that of Na+-dicarboxylate transport in the basolateral membrane of mammalian renal proximal tubules. The substrates specific for the basolateral transporter, 2,3-dimethylsuccinate and cis-aconitate, not only inhibited succinate uptake but also evoked inward currents, proving that they are transported by fNaDC-3. Succinate transport via fNaDC-3 decreased by lowering pH, as did citrate transport, although much more moderately. These characteristics suggest that fNaDC-3 is a new type of Na+-dicarboxylate transporter that most likely corresponds to the Na+-dicarboxylate cotransporter in the basolateral membrane of mammalian renal proximal tubules.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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