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Cloning and functional characterization of the human sodium-dependent vitamin C transporters hSVCT1 and hSVCT2
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Two sodium-dependent vitamin C transporters, hSVCT1 and hSVCT2, were cloned from a human kidney cDNA library. hSVCT1 had a 1797 bp open reading frame encoding a 598 amino acid polypeptide. The 1953 bp open reading frame of hSVCT2 encoded a 650 amino acid polypeptide. Using a Xenopus laevis oocyte expression system, both transporters were functionally expressed. By Eadie-Hofstee transformation the apparent K(m) of hSVCT1 for ascorbate was 252.0 microM and of hSVCT2 for ascorbate was 21.3 microM. Both transporters were sodium-dependent and did not transport dehydroascorbic acid. Incubation of oocytes expressing either transporter with phorbol 12-myristate 13-acetate (PMA) inhibited ascorbate transport activity. Availability of the human transporter clones may facilitate new strategies for determining vitamin C intake.
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“The Michaelis constant Km, i.e., the concentration of vitamin C transported by half of the maximal transport velocity, was reported to be in a wide range from 10 to 200 µM, suggesting a large capacity to absorb dietary vitamin C.”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [51]
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“Vitamin C is efficiently and saturably reabsorbed from the urinary tract, and SVCT1 plays an important role, as documented by knockout Slc23a1−/− mice with an 18-fold higher ascorbate excretion [51,80,81].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [51]
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“Vitamin C is taken up by the cells via SVCT2 (SLC23A2, Figure 2C), which is a close analogue of SVCT1 with which it shares 65% sequence homology.”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [51]
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“Its activity is highest at a neutral pH. It drops markedly with increasing acidity [51,52,53,54].”
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Metadata
- Authors
- Daruwala, R., Song, J., Koh, W. S., Rumsey, S. C., & Levine, M.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Levine, Mark
- ORCID
- Levine, Mark
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1999-11
- Volume
- 460
- Issue
- 3
- Pages
- 480-484
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2079405203
- Cited by
- 272
- References
- 19
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 6 · 2023: 10 · 2022: 1 · 2021: 15 · 2020: 10 · 2019: 3 · 2018: 11 · 2017: 6 · 2016: 8 · 2015: 9 · 2014: 6 · 2013: 17 · 2012: 9
- FWCI
- 8.84
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Vitamin C and Antioxidants Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- sodium-dependent vitamin C transporters, ascorbate transport, vitamin C, dehydroascorbic acid, phorbol myristate acetate, transporter inhibition, kidney, oocyte expression, Michaelis constant, vitamin C intake
- MeSH terms
- Amino Acid Sequence, Animals, Ascorbic Acid, Base Sequence, Biological Transport, Carrier Proteins, Cloning, Molecular, Bucladesine, Female, Humans, Molecular Sequence Data, Oocytes, Proteins, Sodium, Tetradecanoylphorbol Acetate, Protein Biosynthesis, Xenopus laevis, Symporters, Organic Anion Transporters, Sodium-Dependent, Sodium-Coupled Vitamin C Transporters
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