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Sodium-dependent vitamin C transporter-2 mediates vitamin C transport at the cortical nerve terminal.

It has been shown that vitamin C (VC) is transported at synaptic boutons, but how this occurs has not been elucidated. This study investigates the role of the sodium-dependent vitamin C transporter-2 (SVCT2) in transporting VC at the cortical nerve terminal. Immunostaining of cultured mouse superior cervical ganglion cells showed the SVCT2 to be expressed in presynaptic boutons, colocalizing with the vesicular monoamine transporter-2 and the norepinephrine transporter. Immunoblotting of enriched cortical synaptosomes demonstrated that the SVCT2 was enriched in presynaptic fractions, confirming a predominantly presynaptic location. In crude synaptosomes, known inhibitors of SVCT2 inhibited uptake of VC. Furthermore, the kinetic features of VC uptake were consistent with SVCT2-mediated function. VC was also found to efflux from synaptosomes by a mechanism not involving the SVCT2. Indeed, VC efflux was substantially offset by reuptake of VC on the SVCT2. The presence and function of the SVCT2 at the presynaptic nerve terminal suggest that it is the transporter responsible for recovery of VC released into the synaptic cleft.

Pubmed ID: 26366722 RIS Download

Mesh terms: Analysis of Variance | Animals | Animals, Newborn | Ascorbic Acid | Benzofurans | Carbon Isotopes | Cells, Cultured | Cerebral Cortex | Disks Large Homolog 4 Protein | Guanylate Kinases | Imidazoles | Membrane Proteins | Mice | Mice, Inbred C57BL | Neurons | Norepinephrine Plasma Membrane Transport Proteins | Protein Transport | Sodium | Sodium-Coupled Vitamin C Transporters | Superior Cervical Ganglion | Synaptosomes | Vesicular Monoamine Transport Proteins

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Associated grants

  • Agency: NIDDK NIH HHS, Id: T35 DK007383
  • Agency: NIAMS NIH HHS, Id: 5T32 AR059039
  • Agency: NINDS NIH HHS, Id: R01 NS057674
  • Agency: NIAMS NIH HHS, Id: T32 AR059039
  • Agency: NINDS NIH HHS, Id: NS057674

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