PMID- 10631088
OWN - NLM
STAT- MEDLINE
DCOM- 20000223
LR  - 20141120
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 267
IP  - 2
DP  - 2000 Jan 19
TI  - Human vitamin C (L-ascorbic acid) transporter SVCT1.
PG  - 488-94
AB  - In human, vitamin C (l-ascorbic acid) is an essential micronutrient required for 
      an array of biological functions including enzymatic reactions and antioxidation.
      We describe here the molecular cloning of a novel human cDNA encoding a vitamin C
      transporter SVCT1. SVCT1 is largely confined to bulk-transporting epithelia
      (e.g., kidney and small intestine) with a putative alternative-splice product
      present in thymus. Applying radiotracer and voltage-clamp approaches in
      cRNA-injected Xenopus oocytes, we found that SVCT1 mediates saturable,
      concentrative, high-affinity l-ascorbic acid transport (K(0.5) = 50-100 microM)
      that is electrogenic and can be inhibited by phloretin. SVCT1 displays exquisite 
      substrate selectivity, greatly favoring l-ascorbic acid over its isomers
      d-isoascorbic acid and dehydroascorbic acid and 2- or 6-substituted analogues,
      whereas glucose and nucleobases are excluded. We have mapped the SLC23A2 gene
      (coding for SVCT1) to human chromosome 5 in band 5q31.2-31.3, within a region
      commonly deleted in malignant myeloid (leukemia) diseases. In addition, we have
      demonstrated that the human SLC23A1 gene product is a related high-affinity
      l-ascorbic acid transporter (SVCT2) that is widely distributed in brain, retina, 
      and a host of endocrine and neuroendocrine tissues. The molecular identification 
      of the human l-ascorbic acid transporters now provides the tools with which to
      investigate their roles in vitamin C metabolism in health and disease.
CI  - Copyright 2000 Academic Press.
FAU - Wang, Y
AU  - Wang Y
AD  - Membrane Biology Program and Renal Division, Department of Pathology, Department 
      of Obstetrics, Gynecology & Reproductive Biology, Brigham & Women's Hospital and 
      Harvard Medical School, Boston, MA 02115, USA.
FAU - Mackenzie, B
AU  - Mackenzie B
FAU - Tsukaguchi, H
AU  - Tsukaguchi H
FAU - Weremowicz, S
AU  - Weremowicz S
FAU - Morton, C C
AU  - Morton CC
FAU - Hediger, M A
AU  - Hediger MA
LA  - eng
GR  - DK46289/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (DNA Primers)
RN  - 0 (DNA, Complementary)
RN  - 0 (Organic Anion Transporters, Sodium-Dependent)
RN  - 0 (Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (SLC23A1 protein, human)
RN  - 0 (SLC23A2 protein, human)
RN  - 0 (Sodium-Coupled Vitamin C Transporters)
RN  - 0 (Symporters)
RN  - PQ6CK8PD0R (Ascorbic Acid)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Ascorbic Acid/*metabolism
MH  - Base Sequence
MH  - Biological Transport, Active
MH  - Chromosome Mapping
MH  - Chromosomes, Human, Pair 5/genetics
MH  - Cloning, Molecular
MH  - DNA Primers/genetics
MH  - DNA, Complementary/genetics
MH  - Female
MH  - Humans
MH  - In Situ Hybridization, Fluorescence
MH  - In Vitro Techniques
MH  - Kinetics
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Oocytes/metabolism
MH  - *Organic Anion Transporters, Sodium-Dependent
MH  - Proteins/chemistry/*genetics/*metabolism
MH  - Recombinant Proteins/chemistry/genetics/metabolism
MH  - Sodium-Coupled Vitamin C Transporters
MH  - *Symporters
MH  - Xenopus laevis
EDAT- 2000/01/13 09:00
MHDA- 2000/02/26 09:00
CRDT- 2000/01/13 09:00
PHST- 2000/01/13 09:00 [pubmed]
PHST- 2000/02/26 09:00 [medline]
PHST- 2000/01/13 09:00 [entrez]
AID - 10.1006/bbrc.1999.1929 [doi]
AID - S0006-291X(99)91929-0 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2000 Jan 19;267(2):488-94. doi:
      10.1006/bbrc.1999.1929.