Erythrocyte Glut1 Triggers Dehydroascorbic Acid Uptake in Mammals Unable to Synthesize Vitamin C

  title={Erythrocyte Glut1 Triggers Dehydroascorbic Acid Uptake in Mammals Unable to Synthesize Vitamin C},
  author={Am{\'e}lie Montel-Hagen and Sandrina Kinet and Nicolas Manel and C{\'e}dric Mongellaz and Rainer Prohaska and Jean-Luc Battini and Jean Delaunay and Marc Sitbon and Naomi Taylor},

Figures from this paper

Erythroid glucose transporters
Recent research has shown that erythrocyte expression of GLUT-type transporters varies between mammalian species and that their functions in this context can differ, and data are identified that identify new arrangements ofGLUT members in red cell metabolism.
The Glut1 and Glut4 glucose transporters are differentially expressed during perinatal and postnatal erythropoiesis.
It is shown that in all other tested mammalian species, Glut1 was transiently expressed in erythrocytes during the neonatal period, and Glut4 was associated with a significantly augmented Sp3/Sp1 ratio, and glucose transporter expression patterns in mice and human ery Throcytes are therefore distinct.
Redox Properties of Human Erythrocytes Are Adapted for Vitamin C Recycling
The findings indicate that human erythrocytes are physiologically adapted to recycle AA both intracellularly through GLUT1-mediated DHA uptake and reduction and extracellularly via DCytb-mediated AFR reduction.
Human erythrocytes transport dehydroascorbic acid and sugars using the same transporter complex.
DHA and 3-OMG bind at mutually exclusive sites at exo- and endofacial surfaces of GLUT1 and are transported via the sameGLUT1 complex, indicating that DHA and 2-O-methylglucose is a transported, nonmetabolizable sugar.
Response: Species Diversity in GLUT Expression and Function
GLUT-1 content and interaction with stomatin in red blood cells from species without vitamin C biosynthesis and their relevance for diabetes mellitus type 1
The altered regulation of GLUT-1 in the erythrocyte membrane in the case of diabetes can be reconsidered to prevent vitamin C recycling in plasma and to prevent degradation and loss of dehydroascorbate in times of high oxidative stress.
Mitochondrial GLUT10 facilitates dehydroascorbic acid import and protects cells against oxidative stress: mechanistic insight into arterial tortuosity syndrome.
It is demonstrated that GLUT10 facilitates transport of l-dehydroascorbic acid (DHA), the oxidized form of vitamin C, into mitochondria, and also increases cellular uptake of DHA, which protects cells against oxidative stress, which in turn protects cells from oxidative injury.
Glut-1 explains the evolutionary advantage of the loss of endogenous vitamin C-synthesis
It is proposed that the transport of vitamin C increases an intracellular electron pool, which transfers electrons from intrace cellular ascorbate to extracellular substances like ascorbyl free radical or DHA, resulting in 100-fold smaller daily requirement of this essential redox sensitive micronutrient.
Vitamin C transporters
In humans, the maintenance of a low daily requirement of vitamin C is attained through an efficient system for the recycling of the vitamin involving the two families of vitaminC transporters.
Comparative kinetic analysis of ascorbate (Vitamin-C) recycling dehydroascorbate reductases from plant and human
It is demonstrated that DHAR from stress adapted pearl millet Pennisetum glaucum (PgDHAR) shows the highest turnover rate whereas HsCLIC1, 3, and 4 reduce DHA, albeit at lower rates, corroborate with the levels of reactive oxygen species H2O2 encountered in their respective intracellular environment.


Dehydroascorbic acid transport by GLUT4 in Xenopus oocytes and isolated rat adipocytes.
It is indicated that the insulin-sensitive transporter GLUT4 transports DHA in both rat adipocytes and Xenopus oocytes, and Alterations of this mechanism in diabetes could have clinical implications for ascorbate utilization.
Glucose-Independent Transport of Dehydroascorbic Acid in Human Erythrocytes 1
  • J. Bianchi, R. C. Rose
  • Biology
    Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine
  • 1986
It is confirmed that dehydroascorbic acid may be a ligand of the hexose transport system under certain experimental conditions and suggested that this previously undescribed sugar-independent transporter is the physiologically important route of DHA uptake in erythrocytes.
Glucose Transporter Isoforms GLUT1 and GLUT3 Transport Dehydroascorbic Acid*
GLUT1 and GLUT3 isoforms are the specific glucose transporter isoforms which mediate DHA transport and subsequent accumulation of AA according to Xenopus laevis oocyte expression system studies.
A family of mammalian Na+-dependent L-ascorbic acid transporters
It is found that SVCT1 and SVCT2 each mediate concentrative, high-affinity L-ascorbic acid transport that is stereospecific and is driven by the Na+ electrochemical gradient.
Ascorbate function and metabolism in the human erythrocyte.
  • J. M. May
  • Biology, Physics
    Frontiers in bioscience : a journal and virtual library
  • 1998
The ability of erythrocytes to recycle asCorbate, coupled with the ability of ascorbate to protect alpha-tocopherol in the cell membrane and in lipoproteins, provides a potentially important mechanism for preventing lipid peroxidative damage in areas of inflammation in the vascular bed, such as those involved with atherosclerosis.
Mechanisms of ascorbic acid recycling in human erythrocytes.
Human erythrocyte sugar transport is incompatible with available carrier models.
It is suggested that GLUT1-mediated sugar transport in all cells is an intrinsically symmetric process but that intracellular sugar complexation in human red cells prevents accurate determination of transport rates.
Facilitative glucose transporters.
This review summarizes recent advances concerning the structure, function, and regulation of the Glut proteins.
Association of stomatin (band 7.2b) with Glut1 glucose transporter.
Stomatin is closely associated with Glut1 in the plasma membrane and that overexpression of stomatin results in a depression in the basal rate of glucose transport.
GLUT-1 deficiency syndrome caused by haploinsufficiency of the blood-brain barrier hexose carrier
Two distinct classes of mutations are reported as the molecular basis for the functional defect of glucose transport: hemizygos-ity of GLUT1 and nonsense mutations resulting in truncation of the GLUT-1 protein.