Red Blood Cell Mechanical Stability

BACKGROUND: The effects of temperature on micro-rheological variables have not been completely revealed yet. OBJECTIVE: To investigate micro-rheological effects of heat treatment in human, rat, dog, and porcine blood samples. METHODS: Red blood cell (RBC) - buffer suspensions were prepared and immersed in a 37, 40, and 43°C heat-controlled water bath for 10 minutes. Deformability, as well as mechanical stability of RBCs were measured in ektacytometer. These tests were also examined in whole blood samples at various temperatures, gradually between 37 and 45°C in the ektacytometer. RESULTS: RBC deformability significantly worsened in the samples treated at 40 and 43°C degrees, more expressed in human, porcine, rat, and in smaller degree in canine samples. The way of heating (incubation vs. ektacytometer temperation) and the composition of the sample (RBC-PBS suspension or whole blood) resulted in the different magnitude of RBC deformability deterioration. Heating affected RBC membrane (mechanical) stability, showing controversial alterations. CONCLUSION: Significant changes occur in RBC deformability by increasing temperature, showing inter-species differences. The magnitude of alterations is depending on the way of heating and the composition of the sample. The results may contribute to better understanding the micro-rheological deterioration in hyperthermia or fever.

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Contribution of the band 3-ankyrin interaction to erythrocyte membrane mechanical stability

Blood ◽

10.1182/blood.v77.7.1581.1581 ◽

1991 ◽

Vol 77 (7) ◽

pp. 1581-1586 ◽

Cited By ~ 71

Author(s):

PS Low ◽

BM Willardson ◽

N Mohandas ◽

M Rossi ◽

S Shohet

Keyword(s):

Blood Cell ◽

Red Blood Cell ◽

Mechanical Stability ◽

Membrane Integrity ◽

Membrane Skeleton ◽

Band 3 ◽

Cell Membrane Integrity ◽

The Face ◽

Cell Stability

Abstract In an effort to evaluate the role of the band 3-ankyrin linkage in maintenance of red blood cell membrane integrity, solution conditions were sought that would selectively dissociate the band 3-ankyrin linkage, leaving other membrane skeletal interactions intact. For this purpose erythrocytes were equilibrated overnight in nutrient-containing buffers at a range of elevated pHs and then examined for changes in mechanical stability and membrane skeletal composition. Band 3 was found to be released from interaction with the membrane skeleton over a pH range (8.4 to 9.5) that was observed to dissociate the band 3- ankyrin interaction in vitro. In contrast, all other membrane skeletal associations appeared to remain intact up to pH 9.3, after which they were also seen to dissociate. Whereas hemolysis of mechanically unstressed cells did not begin until approximately pH 9.3, where the membrane skeletons began to disintegrate, enhanced fragmentation of shear stressed membranes was seen to begin near pH 8, where band 3 dissociation was first observed. Furthermore, the shear-induced fragmentation rate was found to reach a maximum at pH 9.4, ie, where band 3 dissociation was essentially complete. Based on these correlations, we hypothesize that the band 3-ankyrin linkage of the membrane skeleton to the lipid bilayer is essential for red blood cell stability in the face of mechanical distortion but not for cellular integrity in the absence of mechanical stress.

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Red blood cell mechanical stability test

Clinical Hemorheology and Microcirculation ◽

10.3233/ch-131689 ◽

2013 ◽

Vol 55 (1) ◽

pp. 55-62 ◽

Cited By ~ 23

Author(s):

Oguz K. Baskurt ◽

Herbert J. Meiselman

Keyword(s):

Blood Cell ◽

Red Blood Cell ◽

Mechanical Stability ◽

Stability Test

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Oxidative red blood cell membrane injury in the pathophysiology of severe mouse beta-thalassemia

Blood ◽

10.1182/blood.v79.4.1064.bloodjournal7941064 ◽

1992 ◽

Vol 79 (4) ◽

pp. 1064-1067 ◽

Cited By ~ 26

Author(s):

R Advani ◽

E Rubin ◽

N Mohandas ◽

SL Schrier

Keyword(s):

Transgenic Mice ◽

Blood Cell ◽

Transgenic Mouse ◽

Red Blood Cell ◽

Mechanical Stability ◽

Clinical Status ◽

Beta Thalassemia ◽

Membrane Injury ◽

Protein 4.1 ◽

Alpha Globin

In severe human beta-thalassemia, the pathophysiology relates to accumulation of excess alpha-globin chains at the membrane. One hypothesis is that membrane-associated alpha-globin by virtue of it's iron or hemichromes produces oxidation of adjacent membrane proteins. The availability of a mouse model of severe beta-thalassemia, as well as a transgenic (thalassemic-sickle) mouse that expresses 12% of human beta s-chain, has allowed us to study the effect of graded accumulation of alpha-chains at the red blood cell (RBC) membrane on the clinical status of the animal and on the material properties of its RBCs. Proteins from control, beta-thalassemic, and transgenic mouse RBC membranes were analyzed for evidence of oxidation, as measured by thiol- disulfide exchange chromatography, which detects intramolecular sulfhydryl oxidation. Ratios of oxidized globin to protein 7 were calculated and increased amounts were seen in thalassemic mice as compared with control mice and transgenic mice. Furthermore, there were increased amounts of thiol-free protein 4.1 in the thalassemic mice, compared with very small amounts in the control mice and intermediate amounts in the transgenic mice. Membrane mechanical stability as assessed by ektacytometry showed that the thalassemic mouse RBCs were markedly unstable. Transgenic mouse RBCs showed intermediate levels of membrane instability compared with the controls. We propose that this oxidized globin, in conjunction with oxidized protein 4.1, accounts (at least in part) for membrane instability. A 12% increase in beta s- globin chain synthesis (by decreasing excess globin available) confers considerable protection against both oxidative damage and the consequent membrane instability.

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Oxidative red blood cell membrane injury in the pathophysiology of severe mouse beta-thalassemia

Blood ◽

10.1182/blood.v79.4.1064.1064 ◽

1992 ◽

Vol 79 (4) ◽

pp. 1064-1067 ◽

Cited By ~ 1

Author(s):

R Advani ◽

E Rubin ◽

N Mohandas ◽

SL Schrier

Keyword(s):

Transgenic Mice ◽

Blood Cell ◽

Transgenic Mouse ◽

Red Blood Cell ◽

Mechanical Stability ◽

Clinical Status ◽

Beta Thalassemia ◽

Membrane Injury ◽

Protein 4.1 ◽

Alpha Globin

Abstract In severe human beta-thalassemia, the pathophysiology relates to accumulation of excess alpha-globin chains at the membrane. One hypothesis is that membrane-associated alpha-globin by virtue of it's iron or hemichromes produces oxidation of adjacent membrane proteins. The availability of a mouse model of severe beta-thalassemia, as well as a transgenic (thalassemic-sickle) mouse that expresses 12% of human beta s-chain, has allowed us to study the effect of graded accumulation of alpha-chains at the red blood cell (RBC) membrane on the clinical status of the animal and on the material properties of its RBCs. Proteins from control, beta-thalassemic, and transgenic mouse RBC membranes were analyzed for evidence of oxidation, as measured by thiol- disulfide exchange chromatography, which detects intramolecular sulfhydryl oxidation. Ratios of oxidized globin to protein 7 were calculated and increased amounts were seen in thalassemic mice as compared with control mice and transgenic mice. Furthermore, there were increased amounts of thiol-free protein 4.1 in the thalassemic mice, compared with very small amounts in the control mice and intermediate amounts in the transgenic mice. Membrane mechanical stability as assessed by ektacytometry showed that the thalassemic mouse RBCs were markedly unstable. Transgenic mouse RBCs showed intermediate levels of membrane instability compared with the controls. We propose that this oxidized globin, in conjunction with oxidized protein 4.1, accounts (at least in part) for membrane instability. A 12% increase in beta s- globin chain synthesis (by decreasing excess globin available) confers considerable protection against both oxidative damage and the consequent membrane instability.

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Contribution of the band 3-ankyrin interaction to erythrocyte membrane mechanical stability

Blood ◽

10.1182/blood.v77.7.1581.bloodjournal7771581 ◽

1991 ◽

Vol 77 (7) ◽

pp. 1581-1586 ◽

Cited By ~ 1

Author(s):

PS Low ◽

BM Willardson ◽

N Mohandas ◽

M Rossi ◽

S Shohet

Keyword(s):

Blood Cell ◽

Red Blood Cell ◽

Mechanical Stability ◽

Membrane Integrity ◽

Membrane Skeleton ◽

Band 3 ◽

Cell Membrane Integrity ◽

The Face ◽

Cell Stability

In an effort to evaluate the role of the band 3-ankyrin linkage in maintenance of red blood cell membrane integrity, solution conditions were sought that would selectively dissociate the band 3-ankyrin linkage, leaving other membrane skeletal interactions intact. For this purpose erythrocytes were equilibrated overnight in nutrient-containing buffers at a range of elevated pHs and then examined for changes in mechanical stability and membrane skeletal composition. Band 3 was found to be released from interaction with the membrane skeleton over a pH range (8.4 to 9.5) that was observed to dissociate the band 3- ankyrin interaction in vitro. In contrast, all other membrane skeletal associations appeared to remain intact up to pH 9.3, after which they were also seen to dissociate. Whereas hemolysis of mechanically unstressed cells did not begin until approximately pH 9.3, where the membrane skeletons began to disintegrate, enhanced fragmentation of shear stressed membranes was seen to begin near pH 8, where band 3 dissociation was first observed. Furthermore, the shear-induced fragmentation rate was found to reach a maximum at pH 9.4, ie, where band 3 dissociation was essentially complete. Based on these correlations, we hypothesize that the band 3-ankyrin linkage of the membrane skeleton to the lipid bilayer is essential for red blood cell stability in the face of mechanical distortion but not for cellular integrity in the absence of mechanical stress.

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