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    FEBS Lett. 1999 Nov 5;460(3):480-4.

    Cloning and functional characterization of the human sodium-dependent vitamin C transporters hSVCT1 and hSVCT2.

    Source

    Molecular and Clinical Nutrition Section, Bldg. 10, Rm. 4D52, MSC 1372, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-1372, USA.

    Abstract

    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.

    PMID:
    10556521
    [PubMed - indexed for MEDLINE]

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