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

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. BS Eadie-Hofstee transformation the apparent K-m of hSVCT1 for ascorbate was 252.0 mu M and of hSVCT2 for ascorbate was 21.3 mu M. 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. (C) 1999 Federation of European Biochemical Societies.