scholarly journals Mechanics for the Adhesion and Aggregation of Red Blood Cells on Chitosan

2018 ◽  
Vol 34 (5) ◽  
pp. 725-732 ◽  
Author(s):  
K. Y. Chen ◽  
T. H. Lin ◽  
C. Y. Yang ◽  
Y. W. Kuo ◽  
U. Lei
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Biomedical Applications ◽  
Adhesion Force ◽  
Layer Structure ◽  
Optical Tweezer ◽  
Wound Dressings ◽  
Zeta Potentials ◽  
Rbc Membrane ◽  
Layer Structures

AbstractHemostasis, a process which causes bleeding to stop, can be enhanced using chitosan; but the detailed mechanism is unclear. Red blood cells (RBCs) adhere to chitosan because of their opposite charges, but the adhesion force is small, 3.83 pN as measured here using an optical tweezer, such that the direct adhesion cannot be the sole cause for hemostasis. However, it was observed in this study that layer structures of aggregated RBCs were formed next to chitosan objects in both static and flowing environments, but not formed next to cotton and rayon yarns. The layer structure is the clue for the initiation of hemostatsis. Through the supporting measurements of zeta potentials of RBCs and pH's using blood-chitosan mixtures, it is proposed here that the formation of the RBC layer structure next to chitosan objects is due to the reduction of repulsive electric double layer force between RBCs, because of the association of H+ deprotonated from chitosan with COO− on RBC membrane, under the DLVO (Derjaguin-Landau-Verwey-Overbeek) theory. The results are beneficial for designing effective chitosan-based wound dressings, and also for general biomedical applications.

scholarly journals Hemoglobin Oxidation in Stored Blood Accelerates Hemolysis and Oxidative Injury to Red Blood Cells

2020 ◽  
Vol 12 (04) ◽  
pp. 244-249
Author(s):  
Ibrahim Mustafa ◽  
Tameem Ali Qaid Hadwan
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Morphological Changes ◽  
Hemoglobin Concentration ◽  
Red Cell Membrane ◽  
Rbc Membrane ◽  
Hemoglobin Oxidation ◽  
Rbc Indices ◽  
Methemoglobin Formation ◽  
Stored Blood

Abstract Introduction Maintaining blood supply is a challenge in blood banks. Red blood cells (RBCs) stored at 4°C experience issues of biochemical changes due to metabolism of cells, leading to changes collectively referred to as “storage lesions.” Oxidation of the red cell membrane, leading to lysis, contributes to these storage lesions. Methods Blood bags with CPD-SAGM stored at 4°C for 28 days were withdrawn aseptically on days 1, 14, and 28. Hematology analyzer was used to investigate RBC indices. Hemoglobin oxidation was studied through spectrophotometric scan of spectral change. RBC lysis was studied with the help of Drabkin's assay, and morphological changes were observed by light and scan electron microscopy. Results RBCs show progressive changes in morphology echinocytes and spherocytes on day 28. There was 0.85% RBC lysis, an approximately 20% decrease in percentage oxyhemoglobin, and a 14% increase in methemoglobin formation, which shows hemoglobin oxidation on day 28. Conclusions Oxidative damage to RBC, with an increase in storage time was observed in the present study. The observed morphological changes to RBC during the course of increased time shows that there is progressive damage to RBC membrane and a decrease in hemoglobin concentration; percentage RBC lysis is probably due to free hemoglobin and iron.

scholarly journals Sensing of red blood cells with decreased membrane deformability by the human spleen

2018 ◽  
Vol 2 (20) ◽  
pp. 2581-2587 ◽  
Author(s):  
Innocent Safeukui ◽  
Pierre A. Buffet ◽  
Guillaume Deplaine ◽  
Sylvie Perrot ◽  
Valentine Brousse ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Ex Vivo ◽  
Volume Ratio ◽  
Red Cells ◽  
Human Spleen ◽  
Rbc Membrane ◽  
Membrane Rigidity ◽  
Cellular Deformability ◽  
Distinct Features

Abstract The current paradigm in the pathogenesis of several hemolytic red blood cell disorders is that reduced cellular deformability is a key determinant of splenic sequestration of affected red cells. Three distinct features regulate cellular deformability: membrane deformability, surface area-to-volume ratio (cell sphericity), and cytoplasmic viscosity. By perfusing normal human spleens ex vivo, we had previously showed that red cells with increased sphericity are rapidly sequestered by the spleen. Here, we assessed the retention kinetics of red cells with decreased membrane deformability but without marked shape changes. A controlled decrease in membrane deformability (increased membrane rigidity) was induced by treating normal red cells with increasing concentrations of diamide. Following perfusion, diamide-treated red blood cells (RBCs) were rapidly retained in the spleen with a mean clearance half-time of 5.9 minutes (range, 4.0-13.0). Splenic clearance correlated positively with increased membrane rigidity (r = 0.93; P < .0001). To determine to what extent this increased retention was related to mechanical blockade in the spleen, diamide-treated red cells were filtered through microsphere layers that mimic the mechanical sensing of red cells by the spleen. Diamide-treated red cells were retained in the microsphilters (median, 7.5%; range, 0%-38.6%), although to a lesser extent compared with the spleen (median, 44.1%; range, 7.3%-64.0%; P < .0001). Taken together, these results have implications for understanding the sensitivity of the human spleen to sequester red cells with altered cellular deformability due to various cellular alterations and for explaining clinical heterogeneity of RBC membrane disorders.

scholarly journals Quantitative analysis of three-dimensional morphology and membrane dynamics of red blood cells during temperature elevation

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Keyvan Jaferzadeh ◽  
MinWoo Sim ◽  
NamGon Kim ◽  
InKyu Moon
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Three Dimensional ◽  
Membrane Dynamics ◽  
Mean Corpuscular Hemoglobin ◽  
Rbc Membrane ◽  
Membrane Fluctuations ◽  
Highly Correlated ◽  
3D Profile ◽  
Shape Changes

Abstract The optimal functionality of red blood cells is closely associated with the surrounding environment. This study was undertaken to analyze the changes in membrane profile, mean corpuscular hemoglobin (MCH), and cell membrane fluctuations (CMF) of healthy red blood cells (RBC) at varying temperatures. The temperature was elevated from 17 °C to 41 °C within a duration of less than one hour, and the holograms were recorded by an off-axis configuration. After hologram reconstruction, we extracted single RBCs and evaluated their morphologically related features (projected surface area and sphericity coefficient), MCH, and CMF. We observed that elevating the temperature results in changes in the three-dimensional (3D) profile. Since CMF amplitude is highly correlated to the bending curvature of RBC membrane, temperature-induced shape changes can alter CMF’s map and amplitude; mainly larger fluctuations appear on dimple area at a higher temperature. Regardless of the shape changes, no alterations in MCH were seen with temperature variation.

Hypoxic Vasodilation by Red Blood Cells and Impairment in Vascular Disorders.

Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 1585-1585
Author(s):  
John R. Pawloski ◽  
Timothy J. McMahon ◽  
Greg Ahearne ◽  
Claude A. Piantadosi ◽  
David J. Singel ◽  
...  
Keyword(s):  
Blood Flow ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Vascular Dysfunction ◽  
Aortic Ring ◽  
Efficient Production ◽  
Anion Exchanger 1 ◽  
Rbc Membrane ◽  
Tissue Po2 ◽  
Hypoxic Vasodilation

Abstract Physiological O2 gradients are principal regulators of blood flow in the microcirculation: position-to-position changes in hemoglobin (Hb) O2 saturation are coupled to regulated vasodilation (“hypoxic vasodilation”). The mechanism by which graded changes in O2 content of blood evoke this response has been a great challenge to understand. A new role for red blood cells (RBCs) in hypoxic dilation of blood vessels and inhibition of platelet activation involving release of nitric oxide (NO) bioactivity is described. We show that NO groups can be transferred within hemoglobin (Hb) from hemes to highly-conserved cysteine thiols (β-Cys93) to form bioactive S-nitrosohemoglobin (SNO-Hb), and that efficient production of SNO-Hb requires selective processing of NO within the β-subunits. Bioactive SNO-Hb is localized primarily to the RBC membrane through interaction with Band 3, the transmembrane anion-exchanger 1 protein (AE1). Upon deoxygenation, transfer of the NO group from β-Cys93 of Hb to a cysteine thiol within AE1 serves the RBC vasodilator activity. In this way, O2 binding in Hb modulates the release of NO bioactivity. We further show that RBC NO bioactivity is inversely proportional to pO2 and impaired in disease. In an aortic ring bioassay sparged with variable concentrations of O2, addition of normal human RBCs elicited graded responses from relaxation at tissue pO2 (~3–7 mm Hg, hypoxic vasodilation), to loss of relaxation and progressively greater contractions at pO2’s of 10–63 mm Hg (hyperoxic vasoconstriction). Notably, RBC SNO-Hb levels and hypoxic vasodilation are impaired in several diseases characterized by vascular dysfunction. For example, in RBCs from patients with pulmonary arterial hypertension (PAH), we found decreased (13% of control) SNO-Hb content (assessed by photolysis-chemiluminescence) and impaired O2-dependent vasodilation (bioassay). RBCs from patients with other ischemic disorders have also been examined: RBCs demonstrate a pathogenesis-based impairment in their ability to mediate hypoxic vasodilation by NO. These results confirm the (patho)physiologic importance of RBC NO, and suggest that RBC dysfunction may contribute to impaired blood flow in diseases of the heart, lung and blood.

Observed differences in dextran and polyvinylpyrrolidone as rouleaux-inducing agents

1980 ◽  
Vol 58 (3) ◽  
pp. 271-274 ◽  
Author(s):  
Lionel S. Sewchand ◽  
Dieter Bruckschwaiger
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Animal Species ◽  
Critical Concentration ◽  
Rbc Membrane ◽  
Low Concentrations ◽  
High Concentrations ◽  
Induced Aggregation ◽  
Do So

The effectiveness of dextran fractions (Dx-500, Dx-100, Dx-70) and polyvinylpyrrolidone (PVP-360, PVP-40) in inducing aggregation of red blood cells (RBC) was studied in a nonflowing environment. The Dx fractions, at low concentrations, induced aggregation of human RBC but failed to do so at high concentrations (concentrations greater than 70 g/L). The effect was different on RBC from animal species (cat and rabbit); aggregation increased steadily with the Dx concentration and there was no critical concentration beyond which Dx failed to induce aggregation. The PVP was found to be very effective, at all concentrations, in inducing aggregation of RBC from both human and the animal species. These results have a twofold significance: (1) they suggest that Dx and PVP, both neutral polymers, interact differently with the human RBC membrane; and (2) the association of Dx with the human RBC membrane is different from that with cat and rabbit RBC membranes.

scholarly journals Raman Spectroscopic Study of TiO2 Nanoparticles’ Effects on the Hemoglobin State in Individual Red Blood Cells

Materials ◽  
2021 ◽  
Vol 14 (20) ◽  
pp. 5920
Author(s):  
Elena Perevedentseva ◽  
Yu-Chung Lin ◽  
Artashes Karmenyan ◽  
Kuan-Ting Wu ◽  
Andrei Lugovtsov ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Tio2 Nanoparticles ◽  
Blood Cells ◽  
Photothermal Therapy ◽  
Raman Laser ◽  
Medical Application ◽  
Photothermal Effect ◽  
Raman Spectroscopic ◽  
Rbc Membrane ◽  
Raman Spectral

Titanium dioxide (TiO2) is considered to be a nontoxic material and is widely used in a number of everyday products, such as sunscreen. TiO2 nanoparticles (NP) are also considered as prospective agents for photodynamic therapy and drug delivery. These applications require an understanding of the potential effects of TiO2 on the blood system and its components upon administration. In the presented work, we analyze the interaction of TiO2 nanoparticles of different crystal phases (anatase and rutile) with individual rat Red Blood Cells (RBC) and the TiO2 influence on the oxygenation state and functionality of RBC, estimated via analysis of Raman spectra of Hemoglobin (Hb) and their distribution along individual RBC. Raman spectral signals also allow localization of the TiO2 NP on the RBC. No penetration of the NP inside RBC was observed; however, both kinds of TiO2 NP adsorbed on the RBC membrane can affect the Hb state. Mechanisms involving the NP–membrane–Hb interaction, resulting in partial deoxygenation of Hb and TiO2 photothermal effect on Hb under Raman laser excitation, are suggested. The possible influence on the safety of TiO2 use in advanced medical application, especially on the safety and efficiency of photothermal therapy, is discussed.

scholarly journals Normal cations and abnormal membrane lipids in the red blood cells of dogs with familial stomatocytosis-hypertrophic gastritis

Blood ◽  
1994 ◽  
Vol 84 (3) ◽  
pp. 904-909 ◽  
Author(s):  
RJ Slappendel ◽  
W Renooij ◽  
JJ de Bruijne
Keyword(s):  
Lipid Metabolism ◽  
Red Blood Cells ◽  
Acid Content ◽  
Blood Cells ◽  
Membrane Function ◽  
Hypertrophic Gastritis ◽  
Menetrier’S Disease ◽  
Rbc Membrane ◽  
Ménétrier's Disease ◽  
Menetrier's Disease

Examination of the red blood cells (RBCs) of eight dogs with familial stomatocytosis-hypertrophic gastritis (FS-HG), a multiorgan disease associated with hemolytic anemia, hereditary stomatocytosis (HSt), and hypertrophic gastritis resembling Menetrier's disease in man, showed abnormal osmotic fragility, normal mean corpuscular volume, slightly increased cell water, and normal cation content and cation fluxes. Cholesterol was decreased in RBC and increased in plasma. In both RBCs and plasma, total phospholipid (PL) was normal, phosphatidylcholine (PC) decreased, and sphingomyelin increased. The palmitic acid content of PC was increased, and the stearic acid content of PC was decreased. Sodium dodecyl sulfate electrophoresis of RBC membrane proteins was normal. These findings have not been described previously in HSt. They suggest that in FS-HG, abnormal composition of the PL in RBCs secondary to abnormal PL in plasma causes defective membrane function and stomatocytic shape-change. This conclusion was supported by a shortened half-life of 51Cr-labeled RBCs from normal dogs after transfusion in dogs with FS-HG. It was concluded (1) that not all hereditary forms of stomatocytosis are necessarily associated with an intrinsic structural defect of the RBC membrane, but that the change in shape of RBC may also be induced by abnormal composition of the plasma; (2) that stomatocytosis may be caused by loss of membrane surface area rather than by the increased cation uptake such as has been shown in some human kindreds with HSt, (3) that FS-HG is a disorder of lipid metabolism, and by consequence, (4) that abnormal lipid metabolism might be involved in the pathogenesis of Menetrier's disease.

scholarly journals Isolation and characterization of an age-related antigen present on senescent human red blood cells

Blood ◽  
1981 ◽  
Vol 58 (2) ◽  
pp. 341-349
Author(s):  
EM Alderman ◽  
HH Fudenberg ◽  
RE Lovins
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Double Immunodiffusion ◽  
Specific Density ◽  
Human Red Blood Cells ◽  
Rbc Membrane ◽  
Isolation And Characterization ◽  
Age Related ◽  
Membrane Bound

Autologous membrane-bound IgG was isolated from a subpopulation of human red blood cells (RBC) with specific density greater than 1.110, by affinity chromatography of purified RBC membrane glycoprotein preparations using immobilized wheat germ agglutinin and immobilized anti-human immunoglobulin (Ig) as immunoabsorbents. The Ig-containing population thus obtained, when further separated by chromatography on Sephadex G-200 in the presence of chaotropic agents, yielded four peaks (Ia, Ib, II, and III). Double immunodiffusion revealed the presence of Ig in the first three peaks (IgM in peak Ia, IgA in Ib, and IgG in II) but not in peak III. Peak III was precipitated by the Ig-containing peaks (Ia, Ib, and II) in immunodiffusion assays, suggesting that the antigenic membrane determinants responsible for the binding of autologous Ig to senescent human RBC were contained in this peak (III). Peaks Ia, Ib and II precipitate purified asialoglycophorin; peak III was reactive with purified autoantibodies directed against asialoglycophorin. These results suggest that an age-related antigenic determinant(s) present on senescent human RBC is exposed by desialylation of the major sialoglycoprotein component of the RBC membrane.

Deoxygenation-induced alterations in sickle cell membrane cholesterol exchange

1995 ◽  
Vol 269 (5) ◽  
pp. C1105-C1111 ◽  
Author(s):  
J. Kavecansky ◽  
F. Schroeder ◽  
C. H. Joiner
Keyword(s):  
Cell Membrane ◽  
Red Blood Cells ◽  
Sickle Cell ◽  
Blood Cells ◽  
Total Sterol ◽  
Membrane Cholesterol ◽  
Unilamellar Vesicles ◽  
Rbc Membrane ◽  
Spicule Formation ◽  
Small Unilamellar Vesicles

Changes in a membrane sterol exchange of sickle red blood cells (SS RBC) induced by deoxygenation were studied using the fluorescent cholesterol analogue dehydroergosterol (DHE). DHE uptake by SS RBC membrane was measured by the incubation of SS RBC with small unilamellar vesicles (SUV) containing DHE. Deoxygenation of SS RBC, but not normal RBC, increased the rate of DHE uptake. DHE membrane content after 5 h of incubation with SUV in the cell-to-SUV ratio of 1:1 (mol lipid) was 16.25 +/- 0.94 and 12.22 +/- 0.85% of total sterol for deoxygenated and oxygenated cells, respectively. Membrane spicules isolated from these deoxygenated SS RBC had three-fold higher DHE content, suggesting that the increased sterol exchange was localized to spicules. When isolated spicules were incubated with DHE-SUV directly, 91 +/- 3% of membrane sterol was rapidly exchanged, in contrast to intact RBC, in which a maximum of 33% of sterol could be exchanged. The results suggest that spicule formation in SS RBC alters membrane cholesterol structure, such that a domain of cholesterol that is normally nonexchangeable becomes readily exchangeable with exogenous sterol.

L-Asparaginase Loaded Red Blood Cells: From Prescription to Injection

Blood ◽  
2011 ◽  
Vol 118 (21) ◽  
pp. 4252-4252 ◽  
Author(s):  
Jerome Bailly ◽  
Veronique Sezanne ◽  
Yann Godfrin
Keyword(s):  
Side Effects ◽  
Red Blood Cells ◽  
Medicinal Product ◽  
Safety Profile ◽  
Blood Cells ◽  
Blood Bank ◽  
Blood Type ◽  
Rbc Membrane ◽  
Preservative Solution ◽  
Qualified Person

Abstract Abstract 4252 L-asparaginase has been a mainstay of acute lymphoblastic leukemia (ALL) treatment since decades and its efficacy has been demonstrated in a broad range of patient's profiles. However its use is hampered by frequent and/or significant toxicities. L-asparaginase loaded in homologous red blood cells (GRASPA®) is a new pharmaceutical formulation of the enzyme. This cell-based medicinal product allows a better safety profile and an improvement of the pharmacokinetics and pharmacodynamics of the enzyme. As demonstrated by several teams performing different technologies of entrapment (Alpar-HO, 1985; Updike-SJ, 1985; Naqi-A 1988; Kravtzoff-R, 1996; Kwon-YM, 2010; Domenech-C, 2010), L-asparaginase remains active entrapped inside the red blood cell (RBC), while asparagine is constently and actively “pumped” through the membrane of the red cells thanks to N+ channel system. Thus, L-asparaginase loaded RBCs act as “cellular bioreactors”. Indeed, plasmatic asparagine diffuses through the RBC membrane to the intra cellular compartment where it is cleaved by the entrapped L-asparaginase. Thanks to the RBC membrane, the enzyme is protected from body reaction thus reducing the side effects. L-asparaginase loaded red blood cells is a cell-based medicinal product for personalized medicine. The physician prescribes the drug, then the hospital orders the product to the company. The patient weight, the ABO blood type and a valid irregular antibody screening (IAS) have to be joined with this order. The qualified person on the manufacturing site, orders immediately to a blood bank a leukocytes reduced packed RBC unit compatible with the patient. The product is manufactured under cGMP using a 3-hours automated process: (1) a washing step removes the preservative solution from the packed RBC, (2) L-asparaginase is mixed to the RBC washed suspension, (3) the mixture is dialyzed against a hypotonic solution and resealed, (4) a final washing step allows to purify the product, finally (5) the preservative solution is added. According to the prescribed dosage (IU/Kg), the volume of GRASPA® is adjusted in the final product PVC bag. Indeed, the product release specifications are constant and reproducible from batch to batch such as the corpuscular concentration of L-asparaginase (117±19, IU/ml), extracellular hemoglobin (0.11±0.03 g/dL), osmotic fragility (<3.5 g/L of NaCl), extracellular L-asparaginase (0.4±0.2 IU/ml ie <1% of the total activity). Based on these specifications, the qualified person releases the product and ships it (kept at 2–8°C) to the prescriber, meaning the delay between order and delivery is less than 2 days. Currently a 72h shelf-life for the final product is considered. The traceability system assures the linkage between the blood bank and patient's hospital. The manufacturing Key Peformance Indicators:GMP batches manufactured since 01/04/09:148Delivery Rate (since Apr. 2009)Clinical Batches delivered on time100 %Conformance rateGMP batches released (since Apr. 2009)94 %Conformance rate6 last months (since feb. 2011)100 % To date, 135 batches of GRAPSA® were administered to 71 patients enrolled in 3 clinical trials. In ALL patients, hypersensitive reaction, coagulation disorders, hepatic disorders are significantly reduced. The dose of 150IU/kg is currently used in a phase II/III pivotal trial in children and adults with ALL relapse. The dose of 100 IU/kg is optimal (efficacy/tolerance) in newly diagnosed patients over 55yo. Indeed this frail subpopulation of patients can difficultly receive current forms of L-asparaginase due to the known side effects. A phase I clinical trial in pancreatic carcinoma confirmed the good safety profile (also at 150IU/kg) of this form of L-asparaginase even in solid tumors, offering new perspectives in patients where asparagine synthetase in tumor cells is down. Disclosures: Bailly: ERYTECH Pharma: Employment. Sezanne:ERYTECH Pharma: Employment. Godfrin:ERYTECH Pharma: Employment, Equity Ownership, Membership on an entity's Board of Directors or advisory committees.

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