Metabolic dependence of red cell deformability

Weed, Robert I.; LaCelle, Paul L.; Merrill, Edward W.

doi:10.1172/jci106038

Cited by 787 publications

(282 citation statements)

References 38 publications

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“…While the most commonly perceived functions of the RBC are to deliver O 2 and remove CO 2 , these biologically essential tasks could not be accomplished absent the unique deformability of the intact erythrocyte [3,[11][12][13]16]. As shown in Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Cellular deformability is a function of its surface to volume ratio, cytoplasmic viscosity, and membrane viscoelasticity [6][7][8][9][10]. Biological, pharmacological or biochemical changes that affect any of these variables can contribute to loss of cellular deformability and the premature clearance of the RBC via capillary or splenic sequestration, phagocytosis or intravascular lysis [3,[11][12][13][14][15][16]. If sufficient RBC are lost, anemia and tissue hypoxia will result.…”

Section: Introductionmentioning

confidence: 99%

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Microfluidic analysis of cellular deformability of normal and oxidatively damaged red blood cells

et al. 2013

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Microfluidic analysis of blood has potential clinical value for determining normal and abnormal erythrocyte deformability. To determine if a microfluidic device could reliably measure intra-and inter-personal variations of normal and oxidized human red blood cell (RBC), venous blood samples were collected from repeat donors over time. RBC deformability was defined by the cortical tension (pN/mm), as determined from the threshold pressure required to deform RBC through 2-2.5 lm funnel-shaped constrictions. Oxidized RBC were prepared by treatment with phenazine methosulphate (PMS; 50 mM). Analysis of the control and oxidized RBC demonstrated that the microfluidic device could clearly differentiate between normal and mildly oxidized (20.13 6 1.47 versus 27.51 6 3.64 pN/mm) RBC. In vivo murine studies further established that the PMS-mediated loss of deformability correlated with premature clearance. Deformability variation within an individual over three independent samplings (over 21 days) demonstrated minimal changes in the mean pN/mm. Moreover, inter-individual variation in mean control RBC deformability was similarly small (range: 19.37-21.40 pN/mm). In contrast, PMS-oxidized cells demonstrated a greater inter-individual range (range: 25.97-29.90 pN/mm) reflecting the differential oxidant sensitivity of an individual's RBC. Importantly, similar deformability profiles (mean and distribution width; 20.49 6 1.67 pN/mm) were obtained from whole blood via finger prick sampling. These studies demonstrated that a low cost microfluidic device could be used to reproducibly discriminate between normal and oxidized RBC. Advanced microfluidic devices could be of clinical value in analyzing populations for hemoglobinopathies or in evaluating donor RBC products post-storage to assess transfusion suitability. Am. J. Hematol. 88:682-689,

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Microfluidic analysis of cellular deformability of normal and oxidatively damaged red blood cells

et al. 2013

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“…Interestingly, ATP-depletion of RBCs is not fully complete after 16h of incubation in glucosefree medium 17,37 . The effective energy coincides with the thermal energy at high frequency for all conditions, but it increases up to 23kBT at low frequencies for fresh RBCs (ref 27 ).…”

Section: Main Textmentioning

confidence: 99%

“…By comparing membrane fluctuations directly between healthy RBCs and cells depleted of ATP (adenosine triphosphate), recent experiments find a decrease of fluctuations upon ATP-depletion, hence suggesting that an active process may contribute to membrane undulations 6,[14][15][16] . However, the passive mechanical properties of the RBC membrane themselves depend strongly on ATP, as illustrated by the stiffening of the RBC membrane on starvation [17][18][19]6,15 , that correlates with a sudden transition from discocyte to spiculated echinocyte shapes 20,21 . Therefore a direct and compelling explanation for the decrease of fluctuations observed in ATP-depleted cells is the stiffening of the membrane 22,23 rather than the loss of putative active (that is, non-equilibrium) fluctuations.…”

Section: Main Textmentioning

confidence: 99%

Equilibrium physics breakdown reveals the active nature of red blood cell flickering

et al. 2016

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“…In experiments where this was not performed no effect of 4 This is equivalent to approximately 5 X 108 ghosts . The total spectrin/ghost present can be calculated from the known protein content/ghost (5 .7 X 10-10 mg/ghost ; Dodge et al ., 1963 ;Weed et al, 1969) and the known percentage of spectrin (25% of the total protein weight ; Steck et al ., 1971) or ,71µg spectrin per 0 .05 ml packed ghosts . I The appearance of less CIH on ghosts with aggregated CIH sites may be due to a CIH particlepacking problem .…”

Section: Nicorson and Painter Antispectrin Effects On Cih Topographymentioning

confidence: 99%

Anionic Sites of Human Erythrocyte Membranes

Nicolson

Painter

1973

The Journal of Cell Biology

299

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The effects of affinity-purified antispectrin y-globulins on the topographic distribution of anionic residues on human erythrocytes membranes was investigated using collo ida iron hydroxide labeling of mounted, fixed, ghost membranes . Antispectrin -y-globulins were sequestered inside ghosts by hemolysis and the ghosts were incubated for 30 min at 37°C and then fixed with glutaraldehyde . The topographic distribution of colloidal iron hydroxide clusters on ghosts incubated with low (<0 .05 mg/ml) or high (>5-10 mg/ml concentrations of sequestered antispectrin was dispersed, but the distribution at intermediate concentrations (0 .1-5 mg/ml) was highly aggregated . The aggregation of colloidal iron hydroxide binding sites was time and temperature dependent and required the sequestering of cross-linking antibodies (antispectrin Fab could not substitute for y-globulin antibodies) inside the ghosts . Prior glutaraldehyde fixation or fixation at the time of hemolysis in antispectrin solutions prevented the antispectrin-induced colloidal iron site aggregation . The antispectrin reacted exclusively at the inner ghost membrane surface and the colloidal iron hydroxide bound to N-acetylneuraminic acid residues on the outer membrane surface which are overwhelming on the sialoglycoprotein glycophorin . These results were interpreted as evidence for a structural transmembrane linkage between the inner surface peripheral protein spectrin and the integral membrane component glycophorin.

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Metabolic dependence of red cell deformability

Cited by 787 publications

References 38 publications

Microfluidic analysis of cellular deformability of normal and oxidatively damaged red blood cells

Microfluidic analysis of cellular deformability of normal and oxidatively damaged red blood cells

Equilibrium physics breakdown reveals the active nature of red blood cell flickering

Anionic Sites of Human Erythrocyte Membranes

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