Red-cell Adhesion in Trypanosomiasis of Man and other Animals

Parasitology ◽  
1931 ◽  
Vol 23 (3) ◽  
pp. 346-359 ◽  
Author(s):  
James Montague Wallace ◽  
Arthur Wormall
Keyword(s):  
Cell Adhesion ◽  
Guinea Pig ◽  
Blood Cells ◽  
Infected Animal ◽  
Glucose Solution ◽  
Red Cells ◽  
Red Cell ◽  
Good Adhesion ◽  
Destructive Action ◽  
Per Se

1. The red-cell adhesion phenomenon in trypanosomiasis of man and other animals, first described by Duke and Wallace (1930) and shown by these authors to be due to the presence in the blood of the infected animal of a sub-stance (adhesin) which appears during the course of an infection, has been investigated further. Several strains of T. rhodesiense and T. gambiense have been used for this study.2. Red-cell adhesion of this nature has been obtained with the red blood cells of primates only, thus confirming the earlier finding.3. No relationship appears to exist between red-cell adhesion and isohaemagglutination, or other types of haemagglutination. The removal, by absorption, of the α and β isohaemagglutinins from a human adhesin serum of blood group O, or the removal from a monkey adhesin serum of agglutinins for baboon, rabbit and guinea-pig red cells does not lead to the removal of the adhesin.4. Centrifuging, per se, does not destroy to any appreciable extent the power of trypanosomes to adhere to red cells.5. Trypanosomes which have been freed from plasma by centrifuging and subsequent washing with citrate-Ringer-glucose solution give good adhesion with human or monkey red cells when a fresh adhesin serum or plasma is used. Little or no adhesion is obtained with these washed trypanosomes however, if the adhesin serum is very old or if it has been previously filtered through a Berkefeld filter candle or if the adhesin serum or plasma has been heated at 56° C. for 30 minutes.6. From this and other evidence the conclusion is reached that in addition to the red cells, trypanosomes and the adhesin some other factor (designated the “X” factor) is necessary for red-cell adhesion.7. This “X” factor is present in the serum or plasma of humans, monkeys, baboons, rabbits and guinea-pigs and has properties similar to those of complement. It is removed, as is most of the haemolytic complement, when the serum is filtered through a Berkefeld filter, it is destroyed by heating at 56° C. for 30 minutes, and, like haemolytic complement, it is inactivated when the serum is subjected to the action of dilute ammonia for about 1½ hours. Filtration, heating at 56° C. for 30 minutes and dilute ammonia appear to have no significant destructive action on the adhesin.8. The requirements for this red-cell adhesion phenomenon are (a) the red cells of a primate, (b) an adhesin, which is probably an antibody-like sub-stance produced during infection with trypanosomes, (c) trypanosomes of a strain related to that which gave rise to the formation of the adhesin, and (d) a complement-like component (“X” factor) present in the plasma and serum of most, if not all, normal animals.

scholarly journals Genetic differences in red cell osmotic fragility: analysis in allophenic mice

Blood ◽  
1982 ◽  
Vol 59 (5) ◽  
pp. 986-989 ◽  
Author(s):  
MJ Dewey ◽  
JL Brown ◽  
FS Nallaseth
Keyword(s):  
Phenotypic Variation ◽  
Blood Cells ◽  
Osmotic Fragility ◽  
Red Cells ◽  
Fragility Analysis ◽  
Red Cell ◽  
F1 Hybrid ◽  
Osmotic Lysis ◽  
Per Se ◽  
Genetically Determined

Abstract Mice of strain DBA/2J were found to produce red cells considerably more resistant to osmotic lysis than cells from C57BL/6J or the F1 hybrid between the two strains. Such strain-specific differences in osmotic fragility could be the result of genetically determined humoral or other systemic differences that indirectly influence red cell properties. Alternatively, this phenotypic variation might be an inherent property of the erythrocyte themselves and be directly controlled by their genotype. Analysis of red cells from allophenic (mosaic) mice of the strain composition C57BL/6J in equilibrium DBA/2J demonstrated that the latter possibility is the case. In such mice, erythrocytes of the DBA/2J genotype are relatively more resistant to osmotic lysis than are those of the C57BL/6J genotype; partial lysis of allophenic blood at intermediate salt concentrations results in marked enrichment for DBA/2J cells among the survivors. Future experiments designed to determine the mechanism underlying this difference can now focus on the properties of the red blood cells per se with the certainty that this property is inherent to the genotype of each cell.

scholarly journals Genetic differences in red cell osmotic fragility: analysis in allophenic mice

Blood ◽  
1982 ◽  
Vol 59 (5) ◽  
pp. 986-989
Author(s):  
MJ Dewey ◽  
JL Brown ◽  
FS Nallaseth
Keyword(s):  
Phenotypic Variation ◽  
Blood Cells ◽  
Osmotic Fragility ◽  
Red Cells ◽  
Fragility Analysis ◽  
Red Cell ◽  
F1 Hybrid ◽  
Osmotic Lysis ◽  
Per Se ◽  
Genetically Determined

Mice of strain DBA/2J were found to produce red cells considerably more resistant to osmotic lysis than cells from C57BL/6J or the F1 hybrid between the two strains. Such strain-specific differences in osmotic fragility could be the result of genetically determined humoral or other systemic differences that indirectly influence red cell properties. Alternatively, this phenotypic variation might be an inherent property of the erythrocyte themselves and be directly controlled by their genotype. Analysis of red cells from allophenic (mosaic) mice of the strain composition C57BL/6J in equilibrium DBA/2J demonstrated that the latter possibility is the case. In such mice, erythrocytes of the DBA/2J genotype are relatively more resistant to osmotic lysis than are those of the C57BL/6J genotype; partial lysis of allophenic blood at intermediate salt concentrations results in marked enrichment for DBA/2J cells among the survivors. Future experiments designed to determine the mechanism underlying this difference can now focus on the properties of the red blood cells per se with the certainty that this property is inherent to the genotype of each cell.

Cow red blood cells. II. Stimulation of bovine red cell glycolysis by plasma

1979 ◽  
Vol 236 (5) ◽  
pp. C262-C267 ◽  
Author(s):  
M. J. Seider ◽  
H. D. Kim
Keyword(s):  
Guinea Pig ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Red Cells ◽  
Red Cell ◽  
Cellular Components ◽  
Glycolytic Rate ◽  
Purines And Pyrimidines ◽  
Stimulation Of

Cow red cell glycolysis, which can be stimulated by a variety of purines and pyrimidines, was also found to be elevated by its own plasma. Dialyzed or charcoal-treated plasma could no longer stimulate glycolysis, suggesting that the stimulating factors may be purines or pyrimidines. Determination of purines or pyrimidines in plasma revealed the presence of xanthine (0.31 muM), hypoxanthine (0.60 muM), and adenosine (0.05 muM), as well as unknown compounds. A physiologic level of hypoxanthine, with or without xanthine and adenosine approximating their concentrations in plasma, resulted in the stimulation of cow red cell glycolytic rate by 16% (P less than 0.01). These findings suggest that plasma-borne purines may act on cow red cells in concert with as yet unidentified factors. Moreover, exchanging calf and cow plasmas produced no stimulatory effect on either calf or cow red cell glycolysis, suggesting that a) calf red cells lack some of the cellular components that respond to this stimulator and, b) only cow plasma contains this specific stimulator. In other species, including dog, cat, rabbit, rat, guinea pig, and human, stimulation of glycolysis by plasma was not observed.

scholarly journals ON THE RELATION OF WHITE BLOOD CELLS AND PLATELETS TO VENOM HEMOLYSIS

1956 ◽  
Vol 104 (4) ◽  
pp. 517-523 ◽  
Author(s):  
Joseph C. Turner ◽  
Keyword(s):  
Guinea Pig ◽  
Hemolytic Activity ◽  
Chromatographic Separation ◽  
Blood Cells ◽  
Direct Action ◽  
White Blood Cells ◽  
Substantial Reduction ◽  
Red Cells ◽  
Phospholipase Activity ◽  
Paper Chromatographic Separation

Removal of the white cells and platelets from suspensions of red cells usually produces substantial reduction in the hemolytic activity of venoms. Guinea pig red cells constitute a notable exception and may be lysed by a direct action of venom. White blood cells and platelets appear to contribute to hemolysis by serving as sources of phosphatides for the formation of lysophosphatides. No correlation could be found between phospholipase activity and direct hemolytic activity of venoms. A recently described method (8) of paper chromatographic separation of phospholipides has been used successfully in part of the work.

scholarly journals Normal Functions of the Spleen Relative to Red Blood Cells: A Review

Blood ◽  
1959 ◽  
Vol 14 (4) ◽  
pp. 399-408 ◽  
Author(s):  
WILLIAM H. CROSBY
Keyword(s):  
Cell Surface ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Normal Function ◽  
Red Cells ◽  
Red Cell ◽  
Cell Production ◽  
Normal Functions ◽  
Normal Spleen ◽  
And Storage

Abstract During all the stages of a red cell’s life the normal spleen exerts a normal function. Eight of these functions have been considered: (1) erythropoiesis; (2) an effect upon red cell production; (3) an effect upon maturation of the red cell surface; (4) the reservoir function; (5) the "culling function"; (6) iron turnover and storage; (7) the "pitting function"; (8) destruction of old red cells.

scholarly journals THE AGGLUTINATION OF RED BLOOD CELLS IN THE PRESENCE OF BLOOD SERA

1922 ◽  
Vol 4 (4) ◽  
pp. 403-409 ◽  
Author(s):  
Calvin B. Coulter
Keyword(s):  
Cell Membrane ◽  
Guinea Pig ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Ion Concentration ◽  
Red Cell ◽  
Free Medium ◽  
Optimal Point ◽  
Reaction Characteristic ◽  
Pig Serum

1. The addition of blood serum displaces the optimum for agglutination of red blood cells in a salt-free medium to the reaction characteristic of flocculation of the serum euglobulin. 2. This effect is not due merely to a mechanical entanglement of the cells by the precipitating euglobulin, since at reactions at which the latter is soluble it protects the cells from the agglutination which occurs in its absence. 3. A combination of some sort appears therefore to take place between sheep cells and sheep, rabbit, and guinea pig serum euglobulin, and involves a condensation of the serum protein upon the surface of the red cell. 4. At the optimal point for agglutination of persensitized cells both mid- and end-piece of complement combine with the cells. 5. Agglutination is closely related to an optimal H ion concentration in the suspending fluid, and probably of the cell membrane, and not to a definite reaction in the interior of the cell.

The squeezing of red blood cells through capillaries with near-minimal diameters

1989 ◽  
Vol 203 ◽  
pp. 381-400 ◽  
Author(s):  
D. Halpern ◽  
T. W. Secomb
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Cell Shape ◽  
Numerical Solutions ◽  
Tube Diameter ◽  
Red Cells ◽  
Rheological Parameters ◽  
Red Cell ◽  
Red Cell Membrane ◽  
Intact Cells

An analysis is presented of the mechanics of red blood cells flowing in very narrow tubes. Mammalian red cells are highly flexible, but their deformations satisfy two significant constraints. They must deform at constant volume, because the contents of the cell are incompressible, and also at nearly constant surface area, because the red cell membrane strongly resists dilation. Consequently, there exists a minimal tube diameter below which passage of intact cells is not possible. A cell in a tube with this diameter has its critical shape: a cylinder with hemispherical ends. Here, flow of red cells in tubes with near-minimal diameters is analysed using lubrication theory. When the tube diameter is slightly larger than the minimal value, the cell shape is close to its shape in the critical case. However, the rear end of the cell becomes flattened and then concave with a relatively small further increase in the diameter. The changes in cell shape and the resulting rheological parameters are analysed using matched asymptotic expansions for the high-velocity limit and using numerical solutions. Predictions of rheological parameters are also obtained using the assumption that the cell is effectively rigid with its critical shape, yielding very similar results. A rapid decrease in the apparent viscosity of red cell suspensions with increasing tube diameter is predicted over the range of diameters considered. The red cell velocity is found to exceed the mean bulk velocity by an amount that increases with increasing tube diameter.

Phosphatidylserine (PS)-Positive Erythrocytes Bind to Both Immobilized and Soluble Thrombospondin-1 (TSP-1) Via Its Heparin Binding Domain.

Blood ◽  
2006 ◽  
Vol 108 (11) ◽  
pp. 1568-1568
Author(s):  
Yamaja B.N. Setty ◽  
Suhita Gayen Betal ◽  
Surekha Kulkarni ◽  
Marie J. Stuart
Keyword(s):  
Cell Adhesion ◽  
Binding Domain ◽  
Red Cells ◽  
Binding Motif ◽  
Dependent Manner ◽  
Red Cell ◽  
Heparin Binding ◽  
Cell Binding ◽  
Erythrocyte Adhesion ◽  
Heparin Binding Domain

Abstract Phosphatidylserine (PS)-dependent erythrocyte adhesion to both cultured endothelial cells and the components of sub-endothelial matrix appears to be mediated in part via thrombospondin-1 (TSP). While TSP exhibits multiple cell-binding domains, the PS-binding site on TSP has not been identified. Since a cell-binding domain for anionic heparin is located at the amino-terminal domain of TSP, we hypothesized that anionic PS-positive (PS+ve) red cells bind to this domain. In a recent preliminary study, using a flow adhesion system and PS+ve erythrocytes (prepared by treating control AA red cells with A23187), we have demonstrated that heparin inhibited PS+ve erythrocyte adhesion to immobilized TSP in a concentration-dependent manner with 58 to 77% inhibition noted at concentrations between 1 and 50 U/ml (n=9, P<0.001). Other anionic polysaccharides including high molecular weight dextran sulfate and chondroitin sulfate A also inhibited PS+ve erythrocyte adhesion to immobilized TSP with the magnitude of the inhibitory effects comparable to heparin. These results suggested that the heparin-binding domain on TSP may be involved in PS-mediated red cell adhesion to immobilized TSP. We have extended these studies to characterize the PS-binding site on TSP using monoclonal antibodies directed against specific cell-binding domains on the molecule and also using specific TSP peptides. We demonstrate that pre-incubation of immobilized TSP with an antibody directed against the heparin-binding domain on TSP (TSP-Ab9, Lab Vision) blocked PS-mediated red cell adhesion to immobilized TSP (80% inhibition compared to an isotype-matched negative control antibody, n=7, P<0.001), whereas an antibody that recognizes the collagen-binding domain on TSP (TSP-Ab4) did not affect this process. In addition, incubation of PS+ve erythrocytes with a TSP peptide containing the specific heparin-binding motif, KKTRG, inhibited PS-mediated red cell adhesion by 55% (P<0.001, n=6), whereas a peptide lacking the binding motif had no effect. Since protein confirmation of immobilized TSP appears to be different from that of soluble TSP, we next investigated whether soluble TSP, like immobilized TSP, also interacted with PS+ve erythrocytes. Erythrocytes containing 8 to 10% PS+ve cells were incubated in the absence or the presence of increasing concentrations of soluble TSP (0.1 to 10 μg/ml), and then analyzed by flow cytometry for surface bound TSP using both adhesion blocking (TSP-Ab9) and non-blocking (TSP-Ab4) anti-TSP antibodies. We demonstrate that soluble TSP binds to PS+ve erythrocytes in a concentration-dependent manner with 3 to 11% TSP-positive (TSP+ve) red cells measured at soluble TSP concentrations between 1 to 10 μg/ml (n=4). In addition, TSP binding could be detected only with the non-adhesion blocking antibody TSP-Ab4, which recognizes the collagen-binding domain on TSP. The adhesion blocking antibody TSP-Ab9 that interacts with the heparin binding domain, failed to detect any TSP+ve red cells. No TSP+ve erythrocytes were detected when PS-negative control red cells were evaluated in binding assays. In parallel adhesion experiments, soluble TSP inhibited PS+ve erythrocyte adhesion to immobilized TSP at concentrations at which significant TSP binding to erythrocytes occurred (43% and 44% inhibition at 5 and 10 μg of soluble TSP per ml, n=4). These results conclusively demonstrate that PS-positive erythrocytes interact with both immobilized and fluid phase TSP through the heparin-binding domain, and that heparin blocks this interaction.

Endothelial Activation by Sickle Mouse Red Cells and Their Endothelial Adhesion In Vivo is Abolished by Catalase Treatment of Sickle Cells, but Not Quiescent Endothelium, Implying a Role of Heme-Mediated Peroxide Generation in Sickle Cell Adhesion.

Blood ◽  
2009 ◽  
Vol 114 (22) ◽  
pp. 902-902 ◽  
Author(s):  
Dhananjay K. Kaul ◽  
Sandra M. Suzuka ◽  
Mary Fabry
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Blood Cells ◽  
Fold Increase ◽  
Endothelial Activation ◽  
Red Cells ◽  
Time Dependent ◽  
C57bl Mouse ◽  
C57bl Mice

Abstract Abstract 902 Multiple adhesion molecules, expressed on sickle red blood cells (SS RBCs) and activated endothelium, have been implicated in SS RBC adhesion to vascular endothelium. Moreover, intrinsic differences among heterogeneous SS RBC subpopulations, involving differences in red cell adhesion molecules and cell deformability, may contribute to their adhesive and obstructive properties and lead to postcapillary obstruction. However, the role of SS RBCs in endothelium activation and adhesion has not been evaluated despite the insightful studies of Hebbel and coworkers (JCI, 1982) demonstrating that SS RBCs generate excessive amounts of reactive oxygen species due to the presence of unstable hemoglobin S (HbS) and autoxidation of iron in heme. RBCs from transgenic-knockout sickle (BERK) mice similarly show a pronounced increase in heme degradation (Nagababu et. al. Blood Cells Mol Dis, 2008). We hypothesize that hypoxic conditions in venules (oxygen tension,∼30 mm Hg) will accelerate autoxidation of RBC membrane-bound HbS and release H2O2 that will be transferred to adjoining endothelium resulting in its activation (i.e., up-regulation of endothelial adhesion molecules) and SS RBC adhesion. To test the hypothesis that HbS-containing red cells from BERK mice will result in activation of quiescent endothelium in normal mice, we infused FITC (fluorescein isothiocynate)-labeled BERK red cells into congenic C57BL mice. BERK mice, expressing exclusively human βS- and α-globins, have been extensively backcrossed onto C57BL background. Intravital observations were made in the cremaster muscle microcirculatory bed. A single bolus of 150 μl of FITC-labeled BERK RBCs (Hct 30%) was infused into the recipient C57BL mouse via the jugular vein over a period of 5 min to avoid any shear related platelet aggregation. Infusion of FITC-labeled control (C57BL) mouse RBCs into C57BL recipient mice resulted in rare or no RBC adhesion, suggesting that there was no activating effect on endothelium. In contrast, infusion of BERK mouse RBCs into C57BL mice resulted in time-dependent increase in adhesion to venular endothelium. Adhesion became discernable after 3 minutes and showed a 3-5 fold increase after 5-min compared with the number of adherent RBCs at 3 min (P<0.01). Next, we investigated if the infusion of BERK mouse RBCs would induce increased endothelial oxidants. To this end, the cremaster preparation was suffused for 15 min with 123 dihydrorhodamine (DHR), a H2O2-sensitive probe (10 μl/L), followed by a bolus infusion of BERK mouse RBCs, and time-dependent changes in DHR fluorescence intensity were monitored in venules, the sites of adhesion. Infusion of BERK mouse RBCs, but not C57BL RBCs, resulted in time-dependent increase in the fluorescence intensity (ΔI) in venular endothelium, with almost 5-fold increase in DHR intensity after 5 min of BERK RBC infusion (P<0.001) compared with ΔI at 1 min. When infusion of catalase (900 U/mouse) into recipient C57BL mice was followed 30 min later by a bolus of FITC-labeled BERK mouse RBCs, BERK RBC adhesion and pronounced DHR fluorescence in endothelium were observed, demonstrating that intravascular infusion of catalase had little effect on oxidant generation by BERK mouse RBCs. In contrast, infusion of BERK RBCs pre-treated with catalase (100 U in 0.2 ml RBC suspension, 9-fold less catalase per mouse) to quench RBC generated H2O2 inhibited endothelial DHR fluorescence and BERK RBC adhesion. These results strongly suggest an obligatory role of heme-mediated peroxide generation by SS RBC in endothelial activation and SS RBC adhesion, and support the notion that heme-mediated oxidant generation may play a vital role in endothelial dysfunction in sickle cell disease. Disclosures: No relevant conflicts of interest to declare.

scholarly journals Macrophages and iron trafficking at the birth and death of red cells

Blood ◽  
2015 ◽  
Vol 125 (19) ◽  
pp. 2893-2897 ◽  
Author(s):  
Tamara Korolnek ◽  
Iqbal Hamza
Keyword(s):  
Growth Factors ◽  
Blood Cells ◽  
Iron Homeostasis ◽  
Critical Role ◽  
The Body ◽  
Red Cells ◽  
Physical Contact ◽  
Red Cell ◽  
Iron Trafficking ◽  
Intimate Association

Abstract Macrophages play a critical role in iron homeostasis via their intimate association with developing and dying red cells. Central nurse macrophages promote erythropoiesis in the erythroblastic island niche. These macrophages make physical contact with erythroblasts, enabling signaling and the transfer of growth factors and possibly nutrients to the cells in their care. Human mature red cells have a lifespan of 120 days before they become senescent and again come into contact with macrophages. Phagocytosis of red blood cells is the main source of iron flux in the body, because heme must be recycled from approximately 270 billion hemoglobin molecules in each red cell, and roughly 2 million senescent red cells are recycled each second. Here we will review pathways for iron trafficking found at the macrophage-erythroid axis, with a focus on possible roles for the transport of heme in toto.

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