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Am J Physiol Cell Physiol (June 8, 2005). doi:10.1152/ajpcell.00295.2004
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Submitted on June 23, 2004
Accepted on June 5, 2005

Functional characterization of a high affinity Na+/dicarboxylate cotransporter found in Xenopus laevis kidney and heart

Naomi Oshiro1 and Ana M Pajor1*

1 Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, TX, USA

* To whom correspondence should be addressed. E-mail: ampajor{at}utmb.edu.

The SLC13 gene family includes sodium-coupled transporters for Citric Acid Cycle intermediates and sulfate. The present study describes the sequence and functional characterization of a SLC13 family member from Xenopus laevis , the high affinity Na+/dicarboxylate cotransporter, xNaDC-3. The cDNA sequence of xNaDC-3 codes for a protein of 602 amino acids that is approximately 70% identical to the sequences of mammalian NaDC-3 orthologs. The message for xNaDC-3 is found in kidney, liver, intestine, and heart. The xNaDC-3 has a high affinity for substrate, including a Km for succinate of 4 µM, and it is inhibited by the NaDC-3 test substrates, 2,3-dimethylsuccinate and adipate. The transport of succinate by xNaDC-3 is dependent on sodium, with sigmoidal activation kinetics, and lithium can partially substitute for sodium. As with other members of the family, xNaDC-3 is electrogenic and exhibits inward substrate-dependent currents in the presence of sodium. However, other electrophysiological properties of xNaDC-3 are unique and involve large leak currents, possibly mediated by anions, that are activated by binding of sodium or lithium to a single site.




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A. M. Pajor and K. M. Randolph
Inhibition of the Na+/Dicarboxylate Cotransporter by Anthranilic Acid Derivatives
Mol. Pharmacol., November 1, 2007; 72(5): 1330 - 1336.
[Abstract] [Full Text] [PDF]




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