Loading of Human Red Blood Cells with DNA and RNA

1976 ◽  
Vol 31 (3-4) ◽  
pp. 149-151 ◽  
Author(s):  
Dieter Auer ◽  
Gerhard Brandner
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acids ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Human Erythrocytes ◽  
Viral Dna ◽  
External Concentration ◽  
Dna And Rna ◽  
Human Red Blood Cells ◽  
Hank’S Solution

Abstract Human erythrocytes were suspended in Hank’s solution containing mammalian or viral DNA or RNA. After dialysis at 0 °C first against water and subsequently against Hank’s solution, and a further incubation at 37 °C , the erythrocytes were found to be loaded with the nucleic acids. The nucleic acid trapped in the erythrocytes exhibited up to 35 per cent of the external concentration.

scholarly journals Bat Red Blood Cells express Nucleic Acid Sensing Receptors and bind RNA and DNA

2022 ◽  
Author(s):  
LK Metthew Lam ◽  
Jane Dobkin ◽  
Kaitlyn A. Eckart ◽  
Ian Gereg ◽  
Andrew DiSalvo ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acids ◽  
Red Blood Cells ◽  
Immune Function ◽  
Blood Cells ◽  
Toll Like Receptors ◽  
Cpg Dna ◽  
Human Rbcs ◽  
Insight Into ◽  
Rna And Dna

Red blood cells (RBCs) demonstrate immunomodulatory capabilities through the expression of nucleic acid sensors. Little is known about bat RBCs, and no studies have examined the immune function of bat erythrocytes. Here we show that bat RBCs express the nucleic acid-sensing Toll-like receptors TLR7 and TLR9 and bind the nucleic acid ligands, single-stranded RNA, and CpG DNA. Collectively, these data suggest that, like human RBCs, bat erythrocytes possess immune function and may be reservoirs for nucleic acids. These findings provide unique insight into bat immunity and may uncover potential mechanisms by which virulent pathogens in humans are concealed in bats.

Forssman expression on human erythrocytes: biochemical and genetic evidence of a new histo-blood group system

Blood ◽  
2013 ◽  
Vol 121 (8) ◽  
pp. 1459-1468 ◽  
Author(s):  
Lola Svensson ◽  
Annika K. Hult ◽  
Robert Stamps ◽  
Jonas Ångström ◽  
Susann Teneberg ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Group ◽  
Blood Cells ◽  
Human Erythrocytes ◽  
Blood Group System ◽  
Group System ◽  
Glycolipid Antigen ◽  
Human Red Blood Cells ◽  
Key Points ◽  
Forssman Antigen

Key Points A new histo-blood group system was discovered, based on the identification of Forssman glycolipid antigen on human red blood cells. A newly described polymorphism in the GBGT1 gene activates the encoded enzyme to synthesize Forssman antigen.

scholarly journals Transport of uridine in human red blood cells. Demonstration of a simple carrier-mediated process.

1977 ◽  
Vol 69 (1) ◽  
pp. 75-96 ◽  
Author(s):  
Z I Cabantchik ◽  
H Ginsburg
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Human Erythrocytes ◽  
Kinetic Properties ◽  
Kinetic Description ◽  
Human Red Blood Cells ◽  
Methodological Procedures

The kinetic properties of the mediated transport of uridine in human erythrocytes are investigated. Different methodological procedures are use to acquire a complete kinetic description of the system...

scholarly journals Studies on the Nucleic Acids of the Malaria Parasite, Plasmodium Berghei (Vincke & Lips)

1953 ◽  
Vol 6 (2) ◽  
pp. 234 ◽  
Author(s):  
PR Whitfeld
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acids ◽  
Red Blood Cells ◽  
Plasmodium Berghei ◽  
Acid Content ◽  
Blood Cells ◽  
Malaria Parasite ◽  
Nucleic Acid Content ◽  
Solid Residue ◽  
Parasite Plasmodium

Changes in� the nucleic acid content of the solid residue obtained by haemolysing the blood of mice infected with Plasmodium berghei have been examined. The residue from blood in which 25 per cent. of the red blood cells were parasitized contained 20-25 times as much ribosenucleic acid (RNA) and 12 times as much desoxyribosenucleic acid (DNA) as the residue from uninfected blood.

Passive permeability of human red blood cells to calcium

1986 ◽  
Vol 250 (1) ◽  
pp. C26-C31 ◽  
Author(s):  
M. K. McNamara ◽  
J. S. Wiley
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Human Erythrocytes ◽  
Atp Depletion ◽  
Passive Permeability ◽  
Sodium Potassium ◽  
Human Red Blood Cells ◽  
Order Of Magnitude ◽  
The Difference

Ca2+ influx was measured into human erythrocytes in which efflux was blocked by either introduction of an intracellular Ca2+ chelator, introduction of the Ca2+ chelator followed by ATP depletion, or depletion of the Ca2+ pump cofactors ATP and Mg2+. The Ca2+ influx under all three conditions was 14-20 mumol . 1 cells-1 . h-1, which is an order of magnitude higher than the influx previously reported for cells depleted of either ATP or Mg2+ separately. The difference between the two values was explained by the finding of substantial Ca2+ efflux from the Ca2+-loaded ATP-depleted cells, whereas this efflux was insignificant from cells loaded with quin 2 and then ATP depleted. Under these latter conditions Ca2+ influx estimates the unidirectional permeability to this cation. Studies using this technique showed that Ca2+ influx was the same in media of isotonic sodium, potassium, lithium, choline, or magnesium chlorides. Moreover the dependence of Ca2+ influx on external Ca2+ concentration was well described by the sum of saturable and nonsaturable (linear) components.

scholarly journals The Wrb antigen, a receptor for Plasmodium falciparum malaria, is located on a helical region of the major membrane sialoglycoprotein of human red blood cells

1983 ◽  
Vol 209 (1) ◽  
pp. 273-276 ◽  
Author(s):  
K Ridgwell ◽  
M J Tanner ◽  
D J Anstee
Keyword(s):  
Plasmodium Falciparum ◽  
Monoclonal Antibodies ◽  
Red Blood Cells ◽  
Falciparum Malaria ◽  
Blood Cells ◽  
Plasmodium Falciparum Malaria ◽  
Human Erythrocytes ◽  
Glycophorin A ◽  
Human Red Blood Cells ◽  
Helical Region

1. Immunoprecipitation of periodate/NaB3H4-labelled human erythrocytes using anti-Wrightb (Wrb) monoclonal antibodies showed that these antibodies specifically react with the major erythrocyte sialoglycoprotein alpha (glycophorin A). 2. Similar experiments on erythrocytes from the only known individual lacking the Wrb antigen but with otherwise normal sialoglycoproteins did not result in the immunoprecipitation of any sialoglycoprotein. 3. We suggest that the Wrb antigen is located on an alpha-helical region between residues 55 and 70 of sialoglycoprotein alpha.

scholarly journals Activity profile of the CA125 antigen towards human red blood cells

2010 ◽  
Vol 62 (2) ◽  
pp. 271-280 ◽  
Author(s):  
N. Mitic ◽  
Miroslava Jankovic
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
High Serum ◽  
Human Erythrocytes ◽  
Serum Concentrations ◽  
Activity Profile ◽  
Human Red Blood Cells ◽  
Erythrocyte Adhesion ◽  
Insight Into

Starting from the mucin nature of the CA125 antigen and conditions associated with high serum concentrations, this study is an attempt to gain insight into its activity profile towards human erythrocytes. Carcinomaassociated and pregnancy-associated CA125 antigens were tested in agglutination/aggregation, adhesion and hemolysis assays. The results obtained indicated that CA125 antigens increased agglutination/aggregation and inhibited erythrocyte adhesion, but differed in their effective concentrations. Galectin-1 slightly modulated the effects observed. CA125 antigens had no effect on hemolysis. The activity profile of the CA125 antigen towards erythrocytes may have biomedical consequences in different microenvironments in relevant physiological and pathophysiological conditions.

scholarly journals Accurate and precise quantification of Cu,Zn-SOD in human red blood cells using species-specific double and triple IDMS

2016 ◽  
Vol 31 (9) ◽  
pp. 1922-1928 ◽  
Author(s):  
Julia Gleitzmann ◽  
Andrea Raab ◽  
Dirk Schulze ◽  
Hermann Wätzig ◽  
Jörg Feldmann ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Red Blood Cells ◽  
Isotope Dilution ◽  
Blood Cells ◽  
Isotope Dilution Mass Spectrometry ◽  
Human Erythrocytes ◽  
Human Red Blood Cells ◽  
Precise Quantification ◽  
Species Specific

Species-specific double and triple isotope dilution mass spectrometry (IDMS) was applied for the precise quantification of Cu,Zn-SOD in human erythrocytes.

scholarly journals Release of choline by phospholipase D and a related phosphoric diester hydrolase in human erythrocytes. 1H spin-echo n.m.r. studies

1992 ◽  
Vol 284 (1) ◽  
pp. 61-65 ◽  
Author(s):  
H Selle ◽  
B E Chapman ◽  
P W Kuchel
Keyword(s):  
Red Blood Cells ◽  
Phospholipase D ◽  
Calcium Ions ◽  
Blood Cells ◽  
Spin Echo ◽  
Enzymic Activity ◽  
Human Erythrocytes ◽  
Human Red Blood Cells ◽  
Phosphate Ions

A previously detected phosphatidylcholine-specific phospholipase D from lysates of human red blood cells has been further characterized by 1H spin-echo n.m.r. spectroscopy. A second choline-releasing enzymic activity was observed after addition of glycerophosphocholine. Both of these phosphoric diester hydrolase activities were activated to different extents by different concentrations of calcium ions. Differences between the two activities were also observed on inhibition by barium and phosphate ions. These distinct, choline-yielding, reactions which occur in the cytoplasm of red blood cells may be involved in the regulation of the levels of membrane phosphatidylcholine.

scholarly journals FUSION OF INTACT HUMAN ERYTHROCYTES AND ERYTHROCYTE GHOSTS

1974 ◽  
Vol 63 (1) ◽  
pp. 1-11 ◽  
Author(s):  
Hava Peretz ◽  
Zivia Toister ◽  
Yehudith Laster ◽  
Abraham Loyter
Keyword(s):  
Red Blood Cells ◽  
Clostridium Perfringens ◽  
Human Erythrocyte ◽  
Blood Cells ◽  
Sendai Virus ◽  
Iodoacetic Acid ◽  
Human Erythrocytes ◽  
Erythrocyte Ghosts ◽  
Human Red Blood Cells ◽  
Bivalent Cations

Sendai virus is able to induce the fusion of human erythrocytes. Bivalent cations or ATP are not essential for polyerythrocyte formation. High fusion indices were obtained when Sendai virus was added to cells incubated in the presence of both EDTA and iodoacetic acid. Human erythrocyte ghosts prepared by gradual hemolysis still retain the potential to undergo virus-induced fusion. Fusion of human red blood cells without the addition of viruses was obtained by incubation of erythrocytes at pH 10.5 in the presence of Ca++ (40 mM) or by addition of phospholipase C Clostridium perfringens preparations to cells previously agglutinated or polylysine.

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