A family of mammalian Na+-dependent L-ascorbic acid transporters
Abstract
Vitamin C (L-ascorbic acid) is essential for many enzymatic reactions, in which it serves to maintain prosthetic metal ions in their reduced forms (for example, Fe2+, Cu+), and for scavenging free radicals in order to protect tissues from oxidative damage. The facilitative sugar transporters of the GLUT type can transport the oxidized form of the vitamin, dehydroascorbic acid, but these transporters are unlikely to allow significant physiological amounts of vitamin C to be taken up in the presence of normal glucose concentrations, because the vitamin is present in plasma essentially only in its reduced form. Here we describe the isolation of two L-ascorbic acid transporters, SVCT1 and SVCT2, from rat complementary DNA libraries, as the first step in investigating the importance of L-ascorbic acid transport in regulating the supply and metabolism of vitamin C. We find that SVCT1 and SVCT2 each mediate concentrative, high-affinity L-ascorbic acid transport that is stereospecific and is driven by the Na+ electrochemical gradient. 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.
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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.
“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 [81]
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- Authors
- Tsukaguchi, H., Tokui, T., Mackenzie, B., Berger, U. V., Chen, X.-Z., Wang, Y., Brubaker, R. F., & Hediger, M. A.
- Affiliations
- Brigham and Women's Hospital (US)
- Mayo Clinic (US)
- Corresponding author
- Hediger, Matthias A.
- Venue
- Nature
- Published
- 1999-05
- Volume
- 399
- Issue
- 6731
- Pages
- 70-75
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1517698775
- Cited by
- 882
- References
- 32
- Citations by year
- 2026: 10 · 2025: 18 · 2024: 25 · 2023: 29 · 2022: 19 · 2021: 44 · 2020: 46 · 2019: 26 · 2018: 32 · 2017: 26 · 2016: 22 · 2015: 28 · 2014: 44 · 2013: 50 · 2012: 39
- FWCI
- 27.18
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- 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
- vitamin C, SVCT1, SVCT2, sodium-dependent transport, dehydroascorbic acid, transporter isoforms, tissue distribution, intestinal absorption, tubular reabsorption, eye, oxidative stress
- MeSH terms
- Amino Acid Sequence, Animals, Ascorbic Acid, Biological Transport, Cloning, Molecular, Molecular Sequence Data, Proteins, Rabbits, Sodium, Tissue Distribution, Xenopus, Sequence Homology, Amino Acid, DNA, Complementary, Symporters, Organic Anion Transporters, Sodium-Dependent, Rats, Sodium-Coupled Vitamin C Transporters
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