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

Author

Listed:
  • Hiroyasu Tsukaguchi

    (Brigham & Women's Hospital and Harvard Medical School)

  • Taro Tokui

    (Brigham & Women's Hospital and Harvard Medical School
    Sankyo Company Ltd, Analytical and Metabolic Research Laboratories)

  • Bryan Mackenzie

    (Brigham & Women's Hospital and Harvard Medical School)

  • Urs V. Berger

    (Brigham & Women's Hospital and Harvard Medical School)

  • Xing-Zhen Chen

    (Brigham & Women's Hospital and Harvard Medical School)

  • Yangxi Wang

    (Brigham & Women's Hospital and Harvard Medical School)

  • Richard F. Brubaker

    (Mayo Clinic)

  • Matthias A. Hediger

    (Brigham & Women's Hospital and Harvard Medical School
    Harvard Medical School)

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+)1,2, and for scavenging free radicals in order to protect tissues from oxidative damage3. The facilitative sugar transporters of the GLUT type can transport the oxidized form of the vitamin, dehydroascorbic acid4,5,6, 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 form7. 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.

Suggested Citation

  • Hiroyasu Tsukaguchi & Taro Tokui & Bryan Mackenzie & Urs V. Berger & Xing-Zhen Chen & Yangxi Wang & Richard F. Brubaker & Matthias A. Hediger, 1999. "A family of mammalian Na+-dependent L-ascorbic acid transporters," Nature, Nature, vol. 399(6731), pages 70-75, May.
    • Handle: RePEc:nat:nature:v:399:y:1999:i:6731:d:10.1038_19986
    DOI: 10.1038/19986
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    Cited by:

    1. Mingxing Wang & Jin He & Shanshan Li & Qianwen Cai & Kaiming Zhang & Ji She, 2023. "Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter," Nature Communications, Nature, vol. 14(1), pages 1-8, December.
    2. Takaaki A. Kobayashi & Hiroto Shimada & Fumiya K. Sano & Yuzuru Itoh & Sawako Enoki & Yasushi Okada & Tsukasa Kusakizako & Osamu Nureki, 2024. "Dimeric transport mechanism of human vitamin C transporter SVCT1," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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