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Gene Review

SLC23A2  -  solute carrier family 23 (ascorbic acid...

Homo sapiens

Synonyms: KIAA0238, NBTL1, Na(+)/L-ascorbic acid transporter 2, Nucleobase transporter-like 1 protein, SLC23A1, ...
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Disease relevance of SLC23A2


High impact information on SLC23A2

  • Despite their close sequence homology and similar functions, the two isoforms of the transporter are discretely distributed: SVCT1 is mainly confined to epithelial systems (intestine, kidney, liver), whereas SVCT2 serves a host of metabolically active cells and specialized tissues in the brain, eye and other organs [2].
  • We hypothesized that the Maillard reaction, which leads browning and aroma development during the baking of foods, would occur between the lens proteins and the highly reactive oxidation products of vitamin C. To test this hypothesis, we engineered a mouse that selectively overexpresses the human vitamin C transporter SVCT2 in the lens [3].
  • PCR analysis of cDNA isolated from melanocytes capable of transporting AA revealed a predominance of the full-length isoform, while HL-60 cells, which express SVCT2 at the mRNA level and were incapable of transporting AA, showed a predominance of the short isoform [4].
  • As a prerequisite for investigating 6-bromo-6-deoxy-L-ascorbic acid transported by SVCTs, SVCT2 transport activity in oocytes was enhanced 14-fold by construction and use of a vector that added a fixed poly(A) tail to the 3' end of cRNA [5].
  • Analysis by real time quantitative PCR revealed that the post-confluent differentiation of CaCo-2 cells was accompanied by a marked increase (4-fold) in the steady-state level of SVCT1 mRNA, without changes in SVCT2 mRNA levels [6].

Chemical compound and disease context of SLC23A2

  • Incubation of cells with 6-deoxy-6-fluoro-ascorbic (F-ASA), i.e. a probe specific for the sodium-dependent Vitamin C uptake (SVCT2), revealed a 10-fold uptake suppression into mouse 17EM15 relative to human HLE-B3 and JAR choriocarcinoma cells (a control), that could be overcome by overexpressing hSVCT2 using two different promoter constructs [7].

Biological context of SLC23A2

  • A search for common variants in SLC23A2, using current bioinformatic tools and direct resequencing of control populations, failed to identify common single nucleotide polymorphisms [8].
  • The1797-bp cDNA sequence (open reading frame) of the SLC23A2 gene was derived from a compact genomic sequence of 7966 bp [translation initiation codon (ATG) to poly A tail], which is divided into 14 exons [8].
  • We characterized the genomic structures of SLC23A1 and SLC23A2, determined the extent of genetic variation and linkage disequilibrium across each gene, analyzed nucleotide diversity to estimate the effect of selective pressure, and compared sequence variation across species [9].
  • Our analysis, combined with previous in vitro and in vivo studies, suggests that non-synonymous variation appears to be tolerated in SLC23A1 but not SLC23A2, and that this may be a consequence of different selective pressures following past gene duplication of the sodium-dependent vitamin C transporters [9].
  • Functional analysis of two regulatory regions of the human Na+ -dependent vitamin C transporter 2, SLC23A2, in human vascular smooth muscle cells [10].

Anatomical context of SLC23A2


Associations of SLC23A2 with chemical compounds

  • Characterization of the genomic structure of the human vitamin C transporter SVCT1 (SLC23A2) [8].
  • Exposure to the chemical oxidant tert-butylhydroperoxide (TBH) up-regulated SVCT2 gene expression in HLE-B3 cells [15].
  • Finally, hippocampal cultures from SVCT2-deficient mice showed increased susceptibility to oxidative damage and N-methyl-D-aspartate-induced excitotoxicity [16].
  • In the absence of SVCT2, hippocampal neurons exhibited stunted neurite outgrowth, less glutamate receptor clustering, and reduced spontaneous neuronal activity [16].

Other interactions of SLC23A2


Analytical, diagnostic and therapeutic context of SLC23A2


  1. Human placental sodium-dependent vitamin C transporter (SVCT2): molecular cloning and transport function. Rajan, D.P., Huang, W., Dutta, B., Devoe, L.D., Leibach, F.H., Ganapathy, V., Prasad, P.D. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  2. A family of mammalian Na+-dependent L-ascorbic acid transporters. Tsukaguchi, H., Tokui, T., Mackenzie, B., Berger, U.V., Chen, X.Z., Wang, Y., Brubaker, R.F., Hediger, M.A. Nature (1999) [Pubmed]
  3. Vitamin C mediates chemical aging of lens crystallins by the Maillard reaction in a humanized mouse model. Fan, X., Reneker, L.W., Obrenovich, M.E., Strauch, C., Cheng, R., Jarvis, S.M., Ortwerth, B.J., Monnier, V.M. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  4. A human sodium-dependent vitamin C transporter 2 isoform acts as a dominant-negative inhibitor of ascorbic acid transport. Lutsenko, E.A., Carcamo, J.M., Golde, D.W. Mol. Cell. Biol. (2004) [Pubmed]
  5. 6-Bromo-6-deoxy-L-ascorbic acid: an ascorbate analog specific for Na+-dependent vitamin C transporter but not glucose transporter pathways. Corpe, C.P., Lee, J.H., Kwon, O., Eck, P., Narayanan, J., Kirk, K.L., Levine, M. J. Biol. Chem. (2005) [Pubmed]
  6. Up-regulation and polarized expression of the sodium-ascorbic acid transporter SVCT1 in post-confluent differentiated CaCo-2 cells. Maulén, N.P., Henríquez, E.A., Kempe, S., Cárcamo, J.G., Schmid-Kotsas, A., Bachem, M., Grünert, A., Bustamante, M.E., Nualart, F., Vera, J.C. J. Biol. Chem. (2003) [Pubmed]
  7. Relative suppression of the sodium-dependent Vitamin C transport in mouse versus human lens epithelial cells. Obrenovich, M.E., Fan, X., Satake, M., Jarvis, S.M., Reneker, L., Reddan, J.R., Monnier, V.M. Mol. Cell. Biochem. (2006) [Pubmed]
  8. Characterization of the genomic structure of the human vitamin C transporter SVCT1 (SLC23A2). Erichsen, H.C., Eck, P., Levine, M., Chanock, S. J. Nutr. (2001) [Pubmed]
  9. Comparison of the genomic structure and variation in the two human sodium-dependent vitamin C transporters, SLC23A1 and SLC23A2. Eck, P., Erichsen, H.C., Taylor, J.G., Yeager, M., Hughes, A.L., Levine, M., Chanock, S. Hum. Genet. (2004) [Pubmed]
  10. Functional analysis of two regulatory regions of the human Na+ -dependent vitamin C transporter 2, SLC23A2, in human vascular smooth muscle cells. Rubin, S.A., Dey, S., Reidling, J.C. Biochim. Biophys. Acta (2005) [Pubmed]
  11. Functional expression of sodium-dependent vitamin C transporter 2 in human endothelial cells. Seno, T., Inoue, N., Matsui, K., Ejiri, J., Hirata, K., Kawashima, S., Yokoyama, M. J. Vasc. Res. (2004) [Pubmed]
  12. A human nucleobase transporter-like cDNA (SLC23A1): member of a transporter family conserved from bacteria to mammals. Hogue, D.L., Ling, V. Genomics (1999) [Pubmed]
  13. Expression and characterization of vitamin C transporter in the human trophoblast cell line HTR-8/SVneo: effect of steroids, flavonoids and NSAIDs. Biondi, C., Pavan, B., Dalpiaz, A., Medici, S., Lunghi, L., Vesce, F. Mol. Hum. Reprod. (2007) [Pubmed]
  14. Chondrocyte transport and concentration of ascorbic acid is mediated by SVCT2. McNulty, A.L., Vail, T.P., Kraus, V.B. Biochim. Biophys. Acta (2005) [Pubmed]
  15. Vitamin C transport in human lens epithelial cells: evidence for the presence of SVCT2. Kannan, R., Stolz, A., Ji, Q., Prasad, P.D., Ganapathy, V. Exp. Eye Res. (2001) [Pubmed]
  16. Ascorbate transport by primary cultured neurons and its role in neuronal function and protection against excitotoxicity. Qiu, S., Li, L., Weeber, E.J., May, J.M. J. Neurosci. Res. (2007) [Pubmed]
  17. Regulation of the human vitamin C transporters expressed in COS-1 cells by protein kinase C [corrected]. Liang, W.J., Johnson, D., Ma, L.S., Jarvis, S.M., Wei-Jun, L. Am. J. Physiol., Cell Physiol. (2002) [Pubmed]
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