Red blood cells ABH and Lewis antigens prevalence in von Willebrand disease patients

2003 ◽  
Vol 1 ◽  
pp. P1684-P1684
Author(s):  
O. Zalepouchina ◽  
N. Mineeva ◽  
L. Papayan ◽  
T. Andreeva ◽  
N. Klimova
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Von Willebrand Disease ◽  
Lewis Antigens ◽  
Von Willebrand

scholarly journals The role of diabetes mellitus on the thrombus composition in patients with acute ischemic stroke

2020 ◽  
Vol 26 (3) ◽  
pp. 329-336 ◽  
Author(s):  
Gengfan Ye ◽  
Qun Gao ◽  
Peng Qi ◽  
Junjie Wang ◽  
Shen Hu ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Ischemic Stroke ◽  
Red Blood Cells ◽  
Acute Ischemic Stroke ◽  
Von Willebrand Factor ◽  
Blood Cells ◽  
Smoking History ◽  
Diabetic Patients ◽  
Von Willebrand ◽  
Willebrand Factor

Purpose Diabetes mellitus indicated poor clinical prognosis for patients with acute ischemic stroke. Furthermore, diabetes mellitus could also impact the hemostatic system, while its influence on the histological composition of thrombus is unclear. Methods Consecutive patients with retrieved clots were included. Histologic staining for thrombus included hematoxylin and eosin, Martius Scarlet Blue, immunohistochemistry for von Willebrand factor. The differences in clot composition were compared according to diabetes mellitus history or hyperglycemia (≥7.8 mmol/L) on admission. Results A total of 52 patients were included; half of them were diagnosed as diabetes mellitus previously. Diabetic patients showed higher serum glucose on admission (8.90 vs. 7.40, p = 0.012). The baseline characteristics (expect smoking history and thrombus location), procedural, and clinical outcomes were similar between diabetic patients and nondiabetic patients. As for histologic composition, thrombus in patients with diagnosed diabetes mellitus had more fibrin (44.2% vs. 28.3%, p = 0.004) and fewer red blood cells (26.0% vs. 42.9%, p = 0.013) and equivalent content of platelets (24.0% vs. 21.5%, p = 0.694) and von Willebrand factor (0.041 vs. 0.031, p = 0.234) than patients without diabetes mellitus. However, there was no statistical difference in the content of red blood cells (41.6% vs. 27.3%, p = 0.105), fibrin (37.6% vs. 34.3%, p = 0.627), platelets (21.2% vs. 24.2%, p = 0.498), and von Willebrand factor (0.038 vs. 0.034, p = 0.284) between patients with or without hyperglycemia on admission. Conclusion Clots in diabetic patients had more fibrin and fewer erythrocyte components compared with patients without diabetes mellitus, while hyperglycemia on admission did not show association with clot composition. Further studies are needed to confirm these results.

Platelet-Independent Adhesion of Red Blood Cells to Von Willebrand Factor

Blood ◽  
2014 ◽  
Vol 124 (21) ◽  
pp. 2769-2769
Author(s):  
Michel WJ Smeets ◽  
Alexander PJ Vlaar ◽  
Herm Jan M Brinkman ◽  
Jan J Voorberg ◽  
Peter L Hordijk
Keyword(s):  
Endothelial Cells ◽  
Blood Cell ◽  
Red Blood Cells ◽  
Von Willebrand Factor ◽  
Cold Storage ◽  
Blood Cells ◽  
Storage Lesion ◽  
Microparticle Formation ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract Background/Objectives Red blood cell (RBC) transfusion can be lifesaving and is an essential therapy in conditions associated with tissue hypoxia due to anemia. However, recent clinical studies show that both the number of RBCs and the age of RBCs transfused are independent risk factors for an increase in transfusion related morbidity and mortality. It has been suggested that the so called “storage lesion” of RBCs, a reduction of quality of erythrocytes and changes in the erythrocyte concentrate storage medium, is the causal factor. Recently it has been shown that cold storage of erythrocytes induces microparticle formation. These erythrocyte microparticles are pro-coagulant and can cause thrombin formation. Another phenomenon of the storage lesion is the rapid and considerable loss of donor erythrocytes from the circulation of transfused patients. We wondered whether thrombin generated by transfused erythrocyte microparticles could contribute to red blood cell adherence to the vascular endothelium. Cytoadherence of red blood cells could contribute to the loss of circulating transfused red blood cells and vascular obstruction and could explain the observed transfusion associated complications in clinical practice. Methods/Results Employing FACS analysis and a microparticle analyzer we showed that erythrocyte cold storage indeed induces microparticle formation. We confirmed the pro-coagulant properties of these microparticles using a chromogenic substrate specific for thombin and a thrombin-anti-thrombin complex ELISA. To determine whether thrombin could induce adhesion of red blood cells to endothelial cells, we cultured human umbilical vein endothelial cells in micro-perfusion chambers and used live-imaging to define the adherence potential of the erythrocytes to endothelial cells at post-capillary flow rate. Thrombin stimulation of the endothelial cells did increase erythrocyte adhesion to endothelial cells. Moreover, the adhesion of erythrocytes followed a pattern resembling platelets binding to von Willebrand factor (VWF). By using live immunofluoresence imaging we confirmed that the erythrocytes did bind to VWF secreted from endothelial cells. Since erythrocyte-VWF interactions may be mediated by platelets, we used fluorescence cell sorting to remove platelets and erythrocyte-platelet complexes from erythrocyte concentrates. The purified erythrocytes did also bind to VWF secreted by endothelial cells and thereby we confirmed that erythrocytes can bind to VWF in a platelet-independent fashion. We further analyzed the specificity of the erythrocyte-VWF interaction by using different protein coatings in micro-perfusion chambers. Erythrocytes did bind to recombinant high molecular weight VWF multimers. Furthermore, they adhered more potently to VWF when compared to fibrinogen or fibrin but showed little binding to fibronectin, collagen type I, or subendothelial extra-cellular matrix proteins. Conclusion Our results suggest that transfusion of RBCs is able to induce endothelial binding of erythrocytes based on a VWF-erythrocyte interaction. We propose that passive infusion of cold stored erythrocyte derived microparticles promotes thrombin generation which subsequently activates endothelial cells and induces VWF secretion. This results in binding of red blood cells to endothelial cells in a platelet-independent fashion which requires the presence of VWF. Based on our results we hypothesize that binding of erythrocytes to VWF may occlude micro-capillaries thereby contributing to transfusion associated complications. Disclosures No relevant conflicts of interest to declare.

scholarly journals Integrin alpha 4 beta 1 and glycoprotein IV (CD36) are expressed on circulating reticulocytes in sickle cell anemia

Blood ◽  
1993 ◽  
Vol 82 (12) ◽  
pp. 3548-3555 ◽  
Author(s):  
CC Joneckis ◽  
RL Ackley ◽  
EP Orringer ◽  
EA Wayner ◽  
LV Parise
Keyword(s):  
Cell Adhesion ◽  
Red Blood Cells ◽  
Sickle Cell ◽  
Blood Cells ◽  
Plasma Proteins ◽  
Vascular Occlusion ◽  
Vascular Cell Adhesion ◽  
Von Willebrand ◽  
Cell Adhesion Molecule 1 ◽  
Willebrand Factor

Abstract The abnormal adherence of red blood cells, especially circulating reticulocytes (erythrocyte precursors), to the endothelium is believed to contribute to vascular occlusion observed in patients with sickle cell disease. Although several plasma proteins including von Willebrand factor and fibronectin have been proposed to mediate this adhesion, the mechanism of sickle cell adhesion to the endothelium remains unknown. Using flow cytometry, we screened sickle red blood cells with monoclonal antibodies (MoAbs) against known adhesion receptors and detected integrin subunits alpha 4 and beta 1 and the nonintegrin glycoprotein IV on reticulocytes but not on erythrocytes. No reactivity was detected against integrin subunits alpha 2, alpha 3, alpha 5, alpha 6, alpha v, beta 2, beta 3, integrin alpha IIb beta 3, or the nonintegrin glycoprotein Ib. Immunoprecipitation of reticulocytes with either alpha 4- or beta 1-specific antibodies identified the alpha 4 beta 1 complex (alpha 4(70) and alpha 4(80) forms), a receptor for fibronectin and vascular cell adhesion molecule-1. An antibody against glycoprotein IV, a receptor reported to bind thrombospondin and collagen, immunoprecipitated an 88-kD protein consistent with its reported M(r). MoAbs against alpha 4 and glycoprotein IV bound to an average of 4,600 and 17,500 sites per reticulocyte, respectively. Identification of alpha 4 beta 1 and glycoprotein IV on reticulocytes suggests both plasma-dependent and independent mechanisms of reticulocyte adhesion to endothelium and exposed extracellular matrix.

scholarly journals Weibel Palade Bodies: Unique Secretory Organelles of Endothelial Cells that Control Blood Vessel Homeostasis

2021 ◽  
Vol 9 ◽  
Author(s):  
Johannes Naß ◽  
Julian Terglane ◽  
Volker Gerke
Keyword(s):  
Endothelial Cells ◽  
Blood Flow ◽  
Plasma Membrane ◽  
Blood Vessel ◽  
Blood Cells ◽  
Secretory Granules ◽  
Von Willebrand Disease ◽  
Rab Proteins ◽  
Membrane Tethering ◽  
Von Willebrand

Vascular endothelial cells produce and release compounds regulating vascular tone, blood vessel growth and differentiation, plasma composition, coagulation and fibrinolysis, and also engage in interactions with blood cells thereby controlling hemostasis and acute inflammatory reactions. These interactions have to be tightly regulated to guarantee smooth blood flow in normal physiology, but also allow specific and often local responses to blood vessel injury and infectious or inflammatory insults. To cope with these challenges, endothelial cells have the remarkable capability of rapidly changing their surface properties from non-adhesive (supporting unrestricted blood flow) to adhesive (capturing circulating blood cells). This is brought about by the evoked secretion of major adhesion receptors for platelets (von-Willebrand factor, VWF) and leukocytes (P-selectin) which are stored in a ready-to-be-used form in specialized secretory granules, the Weibel-Palade bodies (WPB). WPB are unique, lysosome related organelles that form at the trans-Golgi network and further mature by receiving material from the endolysosomal system. Failure to produce correctly matured VWF and release it through regulated WPB exocytosis results in pathologies, most importantly von-Willebrand disease, the most common inherited blood clotting disorder. The biogenesis of WPB, their intracellular motility and their fusion with the plasma membrane are regulated by a complex interplay of proteins and lipids, involving Rab proteins and their effectors, cytoskeletal components as well as membrane tethering and fusion machineries. This review will discuss aspects of WPB biogenesis, trafficking and exocytosis focussing on recent findings describing factors contributing to WPB maturation, WPB-actin interactions and WPB-plasma membrane tethering and fusion.

scholarly journals Characterization of the ‘White’ Appearing Clots that Cause Acute Ischemic Stroke

2020 ◽  
Author(s):  
Oana Madalina Mereuta ◽  
Seán Fitzgerald ◽  
Rosanna Rossi ◽  
Andrew Douglas ◽  
Abhay Pandit ◽  
...  
Keyword(s):  
Ischemic Stroke ◽  
Red Blood Cells ◽  
Acute Ischemic Stroke ◽  
Blood Cells ◽  
White Blood Cells ◽  
Fatty Acid Binding ◽  
Blue Stain ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract Background: Most clots retrieved from patients with acute ischemic stroke are ‘red’ in color and are predominantly composed of red blood cells and fibrin. ‘White’ clots represent a less common entity and their histological composition is largely unknown.The aim of this study was to investigate the composition, imaging and procedural characteristics of ‘white’ clots retrieved by mechanical thrombectomy.Materials and Methods:Nineteen ‘white’ thrombi selected by visual inspection from 293 cases were collected as part of the multi-institutional RESTORE registry. Non-contrast computed tomography (NCCT), histological and immunohistochemical analyses were performed. Components were quantified using Orbit Image Analysis.Results:Quantification of Martius Scarlett Blue stain identified platelets/other as the major component in ‘white’ clots’ (63%) followed by fibrin (26%), red blood cells (7%) and white blood cells (4%). ‘White’ clots presented significantly more platelets/other and less red blood cells compared to the ‘red’ clots which showed a mean of 23% and 44%, respectively. The mean platelet (CD42b) content in ‘white’ clots was 43%; von Willebrand Factor (vWF) mean expression was 38%.Collagen and calcification were associated in one case. Fatty acid binding protein 4 was expressed in two cases.‘White’ clots were also significantly smaller (9.5 versus 12 mm) and less hyperdense (52 versus 61 Hounsfield Units) on NCCT compared to the other cases.Conclusions:‘White’ clots represented 6% of our cohort and are platelet and vWF-rich. Calcification, collagen and adipocytes were found occasionally. ‘White’ clots differ from other clots in composition, size and density on NCCT.

Mathematical models for shear-induced blood damage based on vortex platform

2021 ◽  
pp. 039139882110035
Author(s):  
Xu Mei ◽  
Min Zhong ◽  
Wanning Ge ◽  
Liudi Zhang
Keyword(s):  
Molecular Weight ◽  
Shear Stress ◽  
Red Blood Cells ◽  
Exposure Time ◽  
Blood Cells ◽  
Ventricular Assist ◽  
Blood Damage ◽  
Weight Analysis ◽  
Von Willebrand

Non-physiological shear stress in Ventricular Assist Device (VAD) is considered to be an important trigger of blood damage, which has become the biggest shackle for clinical application. The researches on blood damage in literature were limited to qualitative but did not make much quantitative analysis. The purpose of this study was to investigate the quantitative influence of two flow-dependent parameters: shear stress (rotational speed) and exposure time on the shear-induced damage of red blood cells and von Willebrand Factor (vWF). A vortex blood-shearing platform was constructed to conduct in vitro experiments. Free hemoglobin assay and vWF molecular weight analysis were then performed on the sheared blood samples. MATLAB was used for regression fitting of original experimental data. The quantitative correlations between the hemolysis index, the degradation of high molecular weight vWF and the two flow-dependent parameters were found both following the power law model. The mathematic models indicated that the sensitivity of blood damage on red blood cells and vWF to exposure time was both greater than that of shear stress. Besides, the damage of vWF was more serious than that of red blood cells at the same flow condition. The models could be used to predict blood damage in blood-contacting medical devices, especially for the slow even stagnant blood flow regions in VAD, thus may provide useful guidance for VAD development and improvement. It also indicated that the vortex platform can be used to study the law of blood damage for the simple structure and easy operation.

scholarly journals Integrin alpha 4 beta 1 and glycoprotein IV (CD36) are expressed on circulating reticulocytes in sickle cell anemia

Blood ◽  
1993 ◽  
Vol 82 (12) ◽  
pp. 3548-3555 ◽  
Author(s):  
CC Joneckis ◽  
RL Ackley ◽  
EP Orringer ◽  
EA Wayner ◽  
LV Parise
Keyword(s):  
Cell Adhesion ◽  
Red Blood Cells ◽  
Sickle Cell ◽  
Blood Cells ◽  
Plasma Proteins ◽  
Vascular Occlusion ◽  
Vascular Cell Adhesion ◽  
Von Willebrand ◽  
Cell Adhesion Molecule 1 ◽  
Willebrand Factor

The abnormal adherence of red blood cells, especially circulating reticulocytes (erythrocyte precursors), to the endothelium is believed to contribute to vascular occlusion observed in patients with sickle cell disease. Although several plasma proteins including von Willebrand factor and fibronectin have been proposed to mediate this adhesion, the mechanism of sickle cell adhesion to the endothelium remains unknown. Using flow cytometry, we screened sickle red blood cells with monoclonal antibodies (MoAbs) against known adhesion receptors and detected integrin subunits alpha 4 and beta 1 and the nonintegrin glycoprotein IV on reticulocytes but not on erythrocytes. No reactivity was detected against integrin subunits alpha 2, alpha 3, alpha 5, alpha 6, alpha v, beta 2, beta 3, integrin alpha IIb beta 3, or the nonintegrin glycoprotein Ib. Immunoprecipitation of reticulocytes with either alpha 4- or beta 1-specific antibodies identified the alpha 4 beta 1 complex (alpha 4(70) and alpha 4(80) forms), a receptor for fibronectin and vascular cell adhesion molecule-1. An antibody against glycoprotein IV, a receptor reported to bind thrombospondin and collagen, immunoprecipitated an 88-kD protein consistent with its reported M(r). MoAbs against alpha 4 and glycoprotein IV bound to an average of 4,600 and 17,500 sites per reticulocyte, respectively. Identification of alpha 4 beta 1 and glycoprotein IV on reticulocytes suggests both plasma-dependent and independent mechanisms of reticulocyte adhesion to endothelium and exposed extracellular matrix.

Hemoglobin crystals of the red blood cells in the human renal cortex: electron microscopic observations of the renal lithiasis

1978 ◽  
Vol 36 (2) ◽  
pp. 480-481
Author(s):  
Kosuke Ueda ◽  
Hiroto Washida ◽  
Nakazo Watari
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Renal Cortex ◽  
Uranyl Acetate ◽  
Osmic Acid ◽  
Renal Lithiasis ◽  
Electron Microscopic ◽  
Hemoglobin C ◽  
First Case ◽  
Ultrathin Sections

IntroductionHemoglobin crystals in the red blood cells were electronmicroscopically reported by Fawcett in the cat myocardium. In the human, Lessin revealed crystal-containing cells in the periphral blood of hemoglobin C disease patients. We found the hemoglobin crystals and its agglutination in the erythrocytes in the renal cortex of the human renal lithiasis, and these patients had no hematological abnormalities or other diseases out of the renal lithiasis. Hemoglobin crystals in the human erythrocytes were confirmed to be the first case in the kidney.Material and MethodsTen cases of the human renal biopsies were performed on the operations of the seven pyelolithotomies and three ureterolithotomies. The each specimens were primarily fixed in cacodylate buffered 3. 0% glutaraldehyde and post fixed in osmic acid, dehydrated in graded concentrations of ethanol, and then embedded in Epon 812. Ultrathin sections, cut on LKB microtome, were doubly stained with uranyl acetate and lead citrate.

Densitometric Identification of Primitive Erythroblasts After Reaction With Diaminobenzidine

1973 ◽  
Vol 31 ◽  
pp. 328-329
Author(s):  
John A. Trotter
Keyword(s):  
Red Blood Cells ◽  
Analytical Method ◽  
Blood Cells ◽  
Guinea Pigs ◽  
Specific Protein ◽  
Visual Examination ◽  
Hemoglobin Synthesis ◽  
Peroxidatic Activity ◽  
Small Density

Hemoglobin is the specific protein of red blood cells. Those cells in which hemoglobin synthesis is initiated are the earliest cells that can presently be considered to be committed to erythropoiesis. In order to identify such early cells electron microscopically, we have made use of the peroxidatic activity of hemoglobin by reacting the marrow of erythropoietically stimulated guinea pigs with diaminobenzidine (DAB). The reaction product appeared as a diffuse and amorphous electron opacity throughout the cytoplasm of reactive cells. The detection of small density increases of such a diffuse nature required an analytical method more sensitive and reliable than the visual examination of micrographs. A procedure was therefore devised for the evaluation of micrographs (negatives) with a densitometer (Weston Photographic Analyzer).

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