scholarly journals Redox Properties of Human Erythrocytes Are Adapted for Vitamin C Recycling

2021 ◽  
Vol 12 ◽  
Author(s):  
Michael Eigenschink ◽  
Danylo Savran ◽  
Christoph P. Zitterer ◽  
Sebastian Granitzer ◽  
Magdalena Fritz ◽  
...  
Keyword(s):  
Vitamin C ◽  
Glucose Transporter ◽  
Homo Sapiens ◽  
Mammalian Species ◽  
Human Erythrocytes ◽  
Radical Scavenger ◽  
Radical Oxygen Species ◽  
Ascorbate Free Radical ◽  
Plasma Membrane Electron Transport ◽  
Membrane Bound

Ascorbic acid (AA; or vitamin C) is an important physiological antioxidant and radical scavenger. Some mammalian species, including homo sapiens, have lost the ability to synthetize AA and depend on its nutritional uptake. Erythrocytes from AA-auxotroph mammals express high amounts of the glucose transporter GLUT1. This isoform enables rapid uptake of glucose as well as dehydroascorbate (DHA), the fully oxidized form of AA. Here, we explored the effects of DHA uptake on the redox metabolism of human erythrocytes. DHA uptake enhanced plasma membrane electron transport (PMET) activity. This process is mediated by DCytb, a membrane bound cytochrome catalyzing extracellular reduction of Fe3+ and ascorbate free radical (AFR), the first oxidized form of AA. DHA uptake also decreased cellular radical oxygen species (ROS) levels. Both effects were massively enhanced in the presence of physiological glucose concentrations. Reduction of DHA to AA largely depleted intracellular glutathione (GSH) and induced the efflux of its oxidized form, GSSG. GSSG efflux could be inhibited by MK-571 (IC50 = 5 μM), indicating involvement of multidrug resistance associated protein (MRP1/4). DHA-dependent GSH depletion and GSSG efflux were completely rescued in the presence of 5 mM glucose and, partially, by 2-deoxy-glucose (2-DG), respectively. These findings indicate that human erythrocytes are physiologically adapted to recycle AA both intracellularly via GLUT1-mediated DHA uptake and reduction and extracellularly via DCytb-mediated AFR reduction. We discuss the possibility that this improved erythrocyte-mediated AA recycling was a prerequisite for the emergence of AA auxotrophy which independently occurred at least twice during mammalian evolution.

The Glut1 and Glut4 glucose transporters are differentially expressed during perinatal and postnatal erythropoiesis

Blood ◽  
2008 ◽  
Vol 112 (12) ◽  
pp. 4729-4738 ◽  
Author(s):  
Amélie Montel-Hagen ◽  
Lionel Blanc ◽  
Myriam Boyer-Clavel ◽  
Chantal Jacquet ◽  
Michel Vidal ◽  
...  
Keyword(s):  
Glucose Transporter ◽  
Mammalian Species ◽  
Expression Patterns ◽  
Erythroid Differentiation ◽  
Human Erythrocytes ◽  
Adult Mice ◽  
Glut1 Expression ◽  
Specific Trait ◽  
Living Organisms ◽  
Glut1 Glucose Transporter

Abstract Glucose is a major source of energy for living organisms, and its transport in vertebrates is a universally conserved property. Of all cell lineages, human erythrocytes express the highest level of the Glut1 glucose transporter with more than 200 000 molecules per cell. However, we recently reported that erythrocyte Glut1 expression is a specific trait of vitamin C–deficient mammalian species, comprising only higher primates, guinea pigs, and fruit bats. Here, we show that in all other tested mammalian species, Glut1 was transiently expressed in erythrocytes during the neonatal period. Glut1 was up-regulated during the erythroblast stage of erythroid differentiation and was present on the vast majority of murine red blood cells (RBCs) at birth. Notably though, Glut1 was not induced in adult mice undergoing anemia-induced erythropoiesis, and under these conditions, the up-regulation of a distinct transporter, Glut4, was responsible for an increased glucose transport. Sp3 and Sp1 transcriptions factors have been proposed to regulate Glut1 transcription, and we find that the concomitant repression of Glut1 and induction of Glut4 was associated with a significantly augmented Sp3/Sp1 ratio. Glucose transporter expression patterns in mice and human erythrocytes are therefore distinct. In mice, there is a postnatal switch from Glut1 to Glut4, with Glut4 further up-regulated under anemic conditions.

scholarly journals Random distribution of the glucose transporter of human erythrocytes in reconstituted liposomes.

1982 ◽  
Vol 257 (18) ◽  
pp. 11100-11105 ◽  
Author(s):  
S Sase ◽  
Y Anraku ◽  
M Nagano ◽  
M Osumi ◽  
M Kasahara
Keyword(s):  
Glucose Transporter ◽  
Random Distribution ◽  
Human Erythrocytes

Characterization of the glucose transporter from human erythrocytes

1978 ◽  
Vol 8 (4) ◽  
pp. 447-453 ◽  
Author(s):  
David C. Sogin ◽  
Peter C. Hinkle
Keyword(s):  
Glucose Transporter ◽  
Human Erythrocytes

scholarly journals Compartmentalization of membrane trafficking, glucose transport, glycolysis, actin, tubulin and the proteasome in the cytoplasmic droplet/Hermes body of epididymal sperm

Open Biology ◽  
2015 ◽  
Vol 5 (8) ◽  
pp. 150080 ◽  
Author(s):  
Catherine E. Au ◽  
Louis Hermo ◽  
Elliot Byrne ◽  
Jeffrey Smirle ◽  
Ali Fazel ◽  
...  
Keyword(s):  
Membrane Trafficking ◽  
Glucose Transporter ◽  
Molecular Level ◽  
Mammalian Species ◽  
Cytoskeletal Proteins ◽  
Epididymal Sperm ◽  
Quantitative Electron Microscopy ◽  
Cytoplasmic Droplet ◽  
Germ Cell Differentiation

Discovered in 1909 by Retzius and described mainly by morphology, the cytoplasmic droplet of sperm (renamed here the Hermes body) is conserved among all mammalian species but largely undefined at the molecular level. Tandem mass spectrometry of the isolated Hermes body from rat epididymal sperm characterized 1511 proteins, 43 of which were localized to the structure in situ by light microscopy and two by quantitative electron microscopy localization. Glucose transporter 3 (GLUT-3) glycolytic enzymes, selected membrane traffic and cytoskeletal proteins were highly abundant and concentrated in the Hermes body. By electron microscope gold antibody labelling, the Golgi trafficking protein TMED7/p27 localized to unstacked flattened cisternae of the Hermes body, as did GLUT-3, the most abundant protein. Its biogenesis was deduced through the mapping of protein expression for all 43 proteins during male germ cell differentiation in the testis. It is at the terminal step 19 of spermiogenesis that the 43 characteristic proteins accumulated in the nascent Hermes body.

Characterization and identification of the glucose transporter of human erythrocytes

1982 ◽  
Vol 693 (1) ◽  
pp. 253-261 ◽  
Author(s):  
Shin'Ichi Sase ◽  
Kuniaki Takata ◽  
Hiroshi Hirano ◽  
Michihiro Kasahara
Keyword(s):  
Glucose Transporter ◽  
Human Erythrocytes

scholarly journals IN SILICO ANTIMALARIAL TARGET SELECTION CONSERVED IN FOUR PLASMODIUM SPECIES

2020 ◽  
Author(s):  
Oladoja AWofisayo
Keyword(s):  
Comparative Genomics ◽  
Peer Review ◽  
In Silico ◽  
Drug Targets ◽  
Homo Sapiens ◽  
Mammalian Species ◽  
Target Selection ◽  
Plasmodium Species ◽  
Data Bank ◽  
Sequence Motifs

Objectives: The need for new antimalarials drugs and drug targets is pertinent due to the emergence of drug resistant strains of the parasites. Improper target selection has resulted in therapeutic failure. The genomic/post genomic era has made possible the deciphering of the 3D crystal structures of proteins and DNA which are drug targets and are deposited in the protein data bank. Methods: Novel antimalarial targets obtained from evolutionary conserved short sequence motifs are utilised and are essential in transcription processes in the parasite. The motifs TGCATGCA, GTGCAC and GTGCGTGC were curated from experimental work, validated and analysed via phylogenomics genomics and comparative genomics. PlasmoDB blastn was applied to determine their similarity in Plasmodium vivax, knowlesi, Ovale and yoeli. The complete genome of Plasmodium falciparum vivax, knowlesi, Ovale and yoeli was downloaded from the plasmoDB and their positions determined. Results: The targets are essential, conserved in rodent and mammalian species via phylogenomics with percentage identity and similarity greater than 80%, have no similar genes in the same genome and also found to be selective in the parasites vis-à-vis the Homo sapiens via comparative genomics with 0% identity and similarity in the human genome. Conclusion: The targets reveal at the molecular and biochemical level, the vulnerable regions in the parasite while safe in human hence their choices in subsequent rationale drug discovery and design protocols. Peer Review History: Received: 18 July 2020; Revised: 1 October; Accepted: 12 October, Available online: 15 November 2020 UJPR follows the most transparent and toughest ‘Advanced OPEN peer review’ system. The identity of the authors and, reviewers will be known to each other. This transparent process will help to eradicate any possible malicious/purposeful interference by any person (publishing staff, reviewer, editor, author, etc) during peer review. As a result of this unique system, all reviewers will get their due recognition and respect, once their names are published in the papers. We expect that, by publishing peer review reports with published papers, will be helpful to many authors for drafting their article according to the specifications. Auhors will remove any error of their article and they will improve their article(s) according to the previous reports displayed with published article(s). The main purpose of it is ‘to improve the quality of a candidate manuscript’. Our reviewers check the ‘strength and weakness of a manuscript honestly’. There will increase in the perfection, and transparency. Received file Average Peer review marks at initial stage: 5.5/10 Average Peer review marks at publication stage: 7.0/10 Reviewer(s) detail: Dr. Tamer ELHABIBI, ERU University, Egypt, [email protected] Dr. Soroush Sardari, Biotech Pasteur Institute of Iran, Tehran, Iran, [email protected] Comments of reviewer(s): Similar Articles: IN SILICO LIGAND-BASED 2D PHARMACOPHORE GENERATION FOR H+/K+ ATPASE INHIBITORS

scholarly journals Lithium-induced modiphication of the physicochemical state of membrane proteins and lipids in human erythrocytes

2021 ◽  
Vol 66 (3) ◽  
pp. 295-301
Author(s):  
G. P. Zubritskaya ◽  
E. I. Slobozhanina
Keyword(s):  
Lithium Salt ◽  
Test System ◽  
Human Erythrocytes ◽  
Lithium Ions ◽  
Physicochemical State ◽  
A Cell ◽  
Cell Test ◽  
Membrane Bound ◽  
Toxic Concentrations

The effect of various concentrations of lithium sulfate on human erythrocytes in vitro has been studied. It has been shown that the effect of lithium salt in maximum pharmacological and toxic concentrations on cells leads to a modification of the physicochemical state of membrane-bound proteins and lipids. It was found that in human erythrocytes exposed to lithium ions, there is a decrease in the activity of membrane-bound acetylcholinesterase and methgemoglobin reductase, as well as a change in the microviscosity of the lipid bilayer of membranes. The results obtained can be used to create a cell test system for assessing the toxicity of lithium compounds.

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