Primary Structure and Functional Characteristics of a Mammalian Sodium-coupled High Affinity Dicarboxylate Transporter*

@article{Kekuda1999PrimarySA,
  title={Primary Structure and Functional Characteristics of a Mammalian Sodium-coupled High Affinity Dicarboxylate Transporter*},
  author={Ramesh Kekuda and H Wang and W. Huang and Ana M. Pajor and F. H. Leibach and Lawrence D. Devoe and Puttur D. Prasad and Vadivel Ganapathy},
  journal={The Journal of Biological Chemistry},
  year={1999},
  volume={274},
  pages={3422 - 3429}
}
We have cloned a Na+-dependent, high affinity dicarboxylate transporter (NaDC3) from rat placenta. NaDC3 exhibits 48% identity in amino acid sequence with rat NaDC1, a Na+-dependent, low affinity dicarboxylate transporter. NaDC3-specific mRNA is detectable in kidney, brain, liver, and placenta. When expressed in mammalian cells, NaDC3 mediates Na+-dependent transport of succinate with aK t of 2 μm. The transport function of NaDC3 shows a sigmoidal relationship with regard to Na+concentration… 

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