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Am J Physiol Cell Physiol 280: C1215-C1223, 2001;
0363-6143/01 $5.00
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Vol. 280, Issue 5, C1215-C1223, May 2001

Cloning and functional characterization of a high-affinity Na+/dicarboxylate cotransporter from mouse brain

Ana M. Pajor, Rama Gangula, and Xiaozhou Yao

Department of Physiology and Biophysics, University of Texas Medical Branch, Galveston, Texas 77555

Neurons contain a high-affinity Na+/dicarboxylate cotransporter for absorption of neurotransmitter precursor substrates, such as alpha -ketoglutarate and malate, which are subsequently metabolized to replenish pools of neurotransmitters, including glutamate. We have isolated the cDNA coding for a high-affinity Na+/dicarboxylate cotransporter from mouse brain, called mNaDC-3. The mRNA coding for mNaDC-3 is found in brain and choroid plexus as well as in kidney and liver. The mNaDC-3 transporter has a broad substrate specificity for dicarboxylates, including succinate, alpha -ketoglutarate, fumarate, malate, and dimethylsuccinate. The transport of citrate is relatively insensitive to pH, but the transport of succinate is inhibited by acidic pH. The Michaelis-Menten constant for succinate in mNaDC-3 is 140 µM in transport assays and 16 µM at -50 mV in two-electrode voltage clamp assays. Transport is dependent on sodium, although lithium can partially substitute for sodium. In conclusion, mNaDC-3 likely codes for the high-affinity Na+/dicarboxylate cotransporter in brain, and it has some unusual electrical properties compared with the other members of the family.

succinate; citrate; sodium; neurotransmitters; Xenopus oocytes


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