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...

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.

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.

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 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.

Isoenzymes of Phosphoglucomutase from Human Red Blood Cells: Isolation and Kinetic Properties

1989 ◽  
Vol 19 (3) ◽  
pp. 251-271 ◽  
Author(s):  
A. Accorsi ◽  
E. Piatti ◽  
M. P. Piacentini ◽  
S. Gini ◽  
A. Fazi
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Kinetic Properties ◽  
Human Red Blood Cells

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.

MOLECULAR EVENTS ASSOCIATED WITH VIPERA LATIFI VENOM EFFECT ON CONDITION OF HUMAN RED BLOOD CELLS

2016 ◽  
Vol 50 (2 (240)) ◽  
pp. 43-50
Author(s):  
L.A. Ghulikyan ◽  
M. Mohamadvarzi ◽  
G.V. Ghukasyan ◽  
A.V. Kishmairyan ◽  
N.A. Zaqaryan ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Human Erythrocytes ◽  
Human Red Blood Cells ◽  
Molecular Events ◽  
Membrane Structure And Function ◽  
Electrolyte Homeostasis ◽  
The Sixties ◽  
And Function

Viper venom as a hemolytic biochemical “cocktail” of toxins, primarily cause to the systemic alteration of blood cells. In the sixties and seventies, human erythrocytes were extensively studied, but the mechanical and chemical stresses commonly exerted on red blood cells continue to attract interest of scientists for the study of membrane structure and function. Here we monitor the effect of Vipera latifi venom on human erythrocytes ghost membranes using phase contrast microscopy and changes in ATPase activity under snake venom influence in vitro. The ion pumps (Na+, K+)-ATPase and (Ca2+, Mg2+)-ATPase plays a pivotal role in the active transport of certain cations and maintenance of intracellular electrolyte homeostasis. We also describe the action of Vipera latifi venom on the freeradical processes in the membrane of erythrocyte ghosts and changes of activity of superoxide dismutase in course of envenomation.

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