Glucose Transporter Isoforms GLUT1 and GLUT3 Transport Dehydroascorbic Acid
Steven C. Rumsey,Oran Kwon,Guo Wei Xu,Charles F. Burant,Ian A. Simpson,Mark Levine,Mark Levine +6 more
TLDR
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.About:
This article is published in Journal of Biological Chemistry.The article was published on 1997-07-25 and is currently open access. It has received 431 citations till now. The article focuses on the topics: Dehydroascorbic acid transport & Glucose Transporter Type 1.read more
Citations
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A family of mammalian Na + -dependent L -ascorbic acid transporters
Hiroyasu Tsukaguchi,Taro Tokui,Bryan Mackenzie,Urs V. Berger,Xing-Zhen Chen,Yangxi Wang,Richard F. Brubaker,Matthias A. Hediger,Matthias A. Hediger +8 more
TL;DR: 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.
Journal ArticleDOI
Supply and demand in cerebral energy metabolism: the role of nutrient transporters
TL;DR: Simulations based on concentrations and kinetic parameters of GLUT1 and −3 in BBB endothelial cells, astrocytes, and neurons, along with the corresponding kinetic properties of the MCTs, have successfully modeled brain glucose and lactate levels as well as lactate transients in response to neuronal stimulation.
Journal ArticleDOI
Reprogramming glucose metabolism in cancer: can it be exploited for cancer therapy?
TL;DR: The possibility of exploiting the reprogrammed glucose metabolism for therapeutic approaches that selectively target cancer cells is discussed, which is mediated by oncogenic drivers and by the undifferentiated character of cancer cells.
Journal ArticleDOI
Vitamin C Function in the Brain: Vital Role of the Ascorbate Transporter (SVCT2)
Fiona E. Harrison,James M. May +1 more
TL;DR: Ascorbate is proposed as a neuromodulator of glutamatergic, dopaminergic, cholinergic, and GABAergic transmission and related behaviors, posited to have potential therapeutic roles against ischemic stroke, Alzheimer's disease, Parkinson’s disease, and Huntington's disease.
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Criteria and recommendations for vitamin C intake.
TL;DR: The tolerable upper intake level, the highest daily level of nutrient intake that does not pose risk or adverse health effects to almost all individuals in the population, is proposed to be less than 1 g of vitamin C daily.
References
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Expression cloning and cDNA sequencing of the Na+/glucose co-transporter
TL;DR: The cloned DNA suggests that the mammalian Na+-driven transporter has no evolutionary relationship to the other sugar transporters, and no homology between the Na+/glucose co-transporter and either the mammalian facilitated glucose carrier or the bacterial sugar transport proteins.
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The glucose transporter family: structure, function and tissue-specific expression.
Gwyn W. Gould,Geoffrey D. Holman +1 more
TL;DR: The facilitative glucose transporters are specific for the D-enantiomer of glucose and are not coupled to any energy-requiring components, such as ATP hydrolysis or a HI gradient.
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The human kidney low affinity Na+/glucose cotransporter SGLT2. Delineation of the major renal reabsorptive mechanism for D-glucose.
TL;DR: The characterization of a previously cloned human kidney cDNA that codes for a protein with 59% identity to the high affinity Na+/glucose cotransporter (SGLT1) is reported, and it is demonstrated that this protein (termed SGLT2) mediates saturable Na(+)-dependent and phlorizin-sensitive transport of D-glugose and alpha-methyl-D-glucopyranoside
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Cloning and characterization of a cDNA encoding the rat brain glucose-transporter protein
TL;DR: Data suggest that a genetically unrelated protein is responsible for hexose transport in normal liver, as mRNA from insulin-responsive and nonresponsive tissues are indistinguishable.
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Fructose transporter in human spermatozoa and small intestine is GLUT5.
TL;DR: The biochemical properties and tissue distribution of GLUT5 are consistent with a physiological role for this protein as a fructose transporter.