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PMID: 10331392 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

A family of mammalian Na+-dependent L-ascorbic acid transporters.

Nature ·Vol. 399 ·No. 6731 ·1999-05-06 ·Pages 70-5

Tsukaguchi H, Tokui T, Mackenzie B, Berger UV, Chen XZ, Wang Y, Brubaker RF, Hediger MA

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.

MeSH Terms
Amino Acid Sequence Animals Ascorbic Acid/metabolism Biological Transport Cloning, Molecular DNA, Complementary Molecular Sequence Data Organic Anion Transporters, Sodium-Dependent Proteins/genetics,isolation & purification,metabolism Rabbits Rats Sequence Homology, Amino Acid Sodium/metabolism Sodium-Coupled Vitamin C Transporters Symporters Tissue Distribution Xenopus
Chemicals
DNA, Complementary Organic Anion Transporters, Sodium-Dependent Proteins Slc23a1 protein, rat Slc23a2 protein, rat Sodium-Coupled Vitamin C Transporters Symporters Sodium Ascorbic Acid
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Tsukaguchi H
Membrane Biology Program, Department of Medicine, Brigham & Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA.
Tokui T
Mackenzie B
Berger U V
Chen X Z
Wang Y
Brubaker R F
Hediger M A
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1999-05-06
Pages
70-5
Language
English
Region
England
NLM ID
0410462
Subset
IM
Databases
GENBANK
AF080452, AF080453, AF118561
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