Cited by 158Vitamin C and Antioxidants ResearchAmino Acid Enzymes and MetabolismDrug Transport and Resistance Mechanisms

The sodium-dependent ascorbic acid transporter family SLC23

Bürzle, Marc, Suzuki, Yoshiro, Ackermann, Daniel, Miyazaki, Hiroki, Maeda, Nobuyo, Clémençon, Benjamin, Burrier, Robert, Hediger, Matthias A.·2013·Molecular Aspects of Medicine

Abstract

Transporters for vitamin C and its oxidized form dehydroascorbic acid (DHA) are crucial to maintain physiological concentrations of this important vitamin that is used in a variety of biochemical processes. The human SLC23 family consists of the Na(+)-dependent vitamin C transporters SVCT1 (encoded by the SLC23A1 gene) and SVCT2 (SLC23A2) as well as an orphan transporter SVCT3 (SLC23A3). Phylogenetically, the SLC23 family belongs to the nucleobase-ascorbate transporter (NAT) family, although no nucleobase transport has yet been demonstrated for the human members of this family. The SVCT1 and SVCT2 transporters are rather specific for ascorbic acid, which is an important antioxidant and plays a crucial role in a many metal-containing enzymes. SVCT1 is expressed predominantly in epithelial tissues such as intestine where it contributes to the supply and maintenance of whole-body ascorbic acid levels. In contrast to various other mammals, humans are not capable of synthesizing ascorbic acid from glucose and therefore the uptake of ascorbic acid from the diet via SVCT1 is essential for maintaining appropriate concentrations of vitamin C in the human body. The expression of SVCT2 is relatively widespread, where it serves to either deliver ascorbic acid to tissues with high demand of the vitamin for enzymatic reactions or to protect metabolically highly active cells or specialized tissues from oxidative stress. The murine Slc23a3 gene encoding the orphan transporter SVCT3 was originally cloned from mouse yolk sac, and subsequent studies showed that it is expressed in the kidney. However, the function of SVCT3 has not been reported and it remains speculative as to whether SVCT3 is a nucleobase transporter.

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Crossref · 10.1016/j.mam.2012.12.002

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Authors
Bürzle, M., Suzuki, Y., Ackermann, D., Miyazaki, H., Maeda, N., Clémençon, B., Burrier, R., & Hediger, M. A.
Affiliations
  • University of Bern (CH)
  • University of North Carolina at Chapel Hill (US)
Corresponding author
Hediger, Matthias A.
Venue
Molecular Aspects of Medicine
Publisher
Elsevier BV
Published
2013-04
Volume
34
Issue
2-3
Pages
436-454
ISSN
0098-2997 (ISSN-L)
OpenAlex
W1976586663
Cited by
158
References
119
Citations by year
2026: 8 · 2025: 9 · 2024: 14 · 2023: 15 · 2022: 15 · 2021: 21 · 2020: 15 · 2019: 8 · 2018: 15 · 2017: 8 · 2016: 8 · 2015: 5 · 2014: 12 · 2013: 5
FWCI
1.13
Type
journal article
Language
en
Open access
closed
Locations
  • Molecular Aspects of Medicine (publishedVersion)
  • PubMed (publishedVersion)
  • BORIS (University Library Bern) (submittedVersion)
Funders
  • Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
  • National Centre of Competence in Research Robotics
  • Universität Bern
  • nccr – on the move
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, SVCT1, SVCT2, ascorbic acid transport, dehydroascorbic acid, vitamin C, oxidative stress, kidney, phylogenetic analysis
MeSH terms
Amino Acid Sequence, Animals, Ascorbic Acid, Cloning, Molecular, Gene Expression Regulation, Multigene Family, Humans, Models, Biological, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Conformation, Species Specificity, Molecular Structure, Sequence Alignment, Mice, Rats, Sodium-Coupled Vitamin C Transporters

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