SLC23A2
From Wikipedia, the free encyclopedia
Solute carrier family 23 (nucleobase transporters), member 2, also known as SLC23A2, is a human gene.[1]
The absorption of vitamin C into the body and its distribution to organs requires two sodium-dependent vitamin C transporters. This gene encodes one of the two required transporters and the encoded protein accounts for tissue-specific uptake of vitamin C. Previously, this gene had an official symbol of SLC23A1.[1]
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[edit] Further reading
- Liang WJ, Johnson D, Jarvis SM (2001). "Vitamin C transport systems of mammalian cells.". Mol. Membr. Biol. 18 (1): 87–95. PMID 11396616.
- Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.". DNA Res. 9 (3): 99–106. PMID 12168954.
- Nagase T, Seki N, Ishikawa K, et al. (1997). "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain.". DNA Res. 3 (5): 321–9, 341–54. PMID 9039502.
- Faaland CA, Race JE, Ricken G, et al. (1998). "Molecular characterization of two novel transporters from human and mouse kidney and from LLC-PK1 cells reveals a novel conserved family that is homologous to bacterial and Aspergillus nucleobase transporters.". Biochim. Biophys. Acta 1442 (2-3): 353–60. PMID 9804989.
- Tsukaguchi H, Tokui T, Mackenzie B, et al. (1999). "A family of mammalian Na+-dependent L-ascorbic acid transporters.". Nature 399 (6731): 70–5. doi: . PMID 10331392.
- Hogue DL, Ling V (1999). "A human nucleobase transporter-like cDNA (SLC23A1): member of a transporter family conserved from bacteria to mammals.". Genomics 59 (1): 18–23. doi: . PMID 10395795.
- Rajan DP, Huang W, Dutta B, et al. (1999). "Human placental sodium-dependent vitamin C transporter (SVCT2): molecular cloning and transport function.". Biochem. Biophys. Res. Commun. 262 (3): 762–8. doi: . PMID 10471399.
- Daruwala R, Song J, Koh WS, et al. (1999). "Cloning and functional characterization of the human sodium-dependent vitamin C transporters hSVCT1 and hSVCT2.". FEBS Lett. 460 (3): 480–4. PMID 10556521.
- Breton S, Wiederhold T, Marshansky V, et al. (2000). "The B1 subunit of the H+ATPase is a PDZ domain-binding protein. Colocalization with NHE-RF in renal B-intercalated cells.". J. Biol. Chem. 275 (24): 18219–24. doi: . PMID 10748165.
- Holliday LS, Lu M, Lee BS, et al. (2000). "The amino-terminal domain of the B subunit of vacuolar H+-ATPase contains a filamentous actin binding site.". J. Biol. Chem. 275 (41): 32331–7. doi: . PMID 10915794.
- Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi: . PMID 11780052.
- Hediger MA (2002). "New view at C.". Nat. Med. 8 (5): 445–6. doi: . PMID 11984580.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi: . PMID 12477932.
- Fischer H, Schwarzer C, Illek B (2004). "Vitamin C controls the cystic fibrosis transmembrane conductance regulator chloride channel.". Proc. Natl. Acad. Sci. U.S.A. 101 (10): 3691–6. doi: . PMID 14993613.
- Lutsenko EA, Carcamo JM, Golde DW (2004). "A human sodium-dependent vitamin C transporter 2 isoform acts as a dominant-negative inhibitor of ascorbic acid transport.". Mol. Cell. Biol. 24 (8): 3150–6. PMID 15060139.
- Seno T, Inoue N, Matsui K, et al. (2004). "Functional expression of sodium-dependent vitamin C transporter 2 in human endothelial cells.". J. Vasc. Res. 41 (4): 345–51. doi: . PMID 15340249.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi: . PMID 15489334.
- McNulty AL, Vail TP, Kraus VB (2005). "Chondrocyte transport and concentration of ascorbic acid is mediated by SVCT2.". Biochim. Biophys. Acta 1712 (2): 212–21. doi: . PMID 15921655.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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