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J Biol Chem, Vol. 274, Issue 29, 20191-20196, July 16, 1999
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.
Expression Cloning and Characterization of a Novel
Sodium-Dicarboxylate Cotransporter from Winter Flounder Kidney
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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