Red Blood Cell Membrane Fragments but Not Intact Red Blood Cells Promote Calcium Oxalate Monohydrate Crystal Growth and Aggregation

2010 ◽  
Vol 184 (2) ◽  
pp. 743-749 ◽  
Author(s):  
Somchai Chutipongtanate ◽  
Visith Thongboonkerd
Keyword(s):  
Crystal Growth ◽  
Cell Membrane ◽  
Blood Cell ◽  
Calcium Oxalate ◽  
Red Blood Cells ◽  
Red Blood Cell ◽  
Blood Cells ◽  
Calcium Oxalate Monohydrate ◽  
Red Blood Cell Membrane

scholarly journals Complete Deficiency of Glycophorin A in Red Blood Cells From Mice With Targeted Inactivation of the Band 3 (AE1) Gene

Blood ◽  
1998 ◽  
Vol 91 (6) ◽  
pp. 2146-2151 ◽  
Author(s):  
Hani Hassoun ◽  
Toshihiko Hanada ◽  
Mohini Lutchman ◽  
Kenneth E. Sahr ◽  
Jiri Palek ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Blood Cell ◽  
Red Blood Cells ◽  
Red Blood Cell ◽  
Blood Cells ◽  
Band 3 ◽  
Glycophorin A ◽  
Blood Group Antigens ◽  
Red Blood Cell Membrane ◽  
Anion Transporter

Abstract Glycophorin A is the major transmembrane sialoglycoprotein of red blood cells. It has been shown to contribute to the expression of the MN and Wright blood group antigens, to act as a receptor for the malaria parasite Plasmodium falciparum and Sendai virus, and along with the anion transporter, band 3, may contribute to the mechanical properties of the red blood cell membrane. Several lines of evidence suggest a close interaction between glycophorin A and band 3 during their biosynthesis. Recently, we have generated mice where the band 3 expression was completely eliminated by selective inactivation of the AE1 anion exchanger gene, thus allowing us to study the effect of band 3 on the expression of red blood cell membrane proteins. In this report, we show that the band 3 −/− red blood cells contain protein 4.1, adducin, dematin, p55, and glycophorin C. In contrast, the band 3 −/− red blood cells are completely devoid of glycophorin A (GPA), as assessed by Western blot and immunocytochemistry techniques, whereas the polymerase chain reaction (PCR) confirmed the presence of GPA mRNA. Pulse-label and pulse-chase experiments show that GPA is not incorporated in the membrane and is rapidly degraded in the cytoplasm. Based on these findings and other published evidence, we propose that band 3 plays a chaperone-like role, which is necessary for the recruitment of GPA to the red blood cell plasma membrane.

scholarly journals Complete Deficiency of Glycophorin A in Red Blood Cells From Mice With Targeted Inactivation of the Band 3 (AE1) Gene

Blood ◽  
1998 ◽  
Vol 91 (6) ◽  
pp. 2146-2151 ◽  
Author(s):  
Hani Hassoun ◽  
Toshihiko Hanada ◽  
Mohini Lutchman ◽  
Kenneth E. Sahr ◽  
Jiri Palek ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Blood Cell ◽  
Red Blood Cells ◽  
Red Blood Cell ◽  
Blood Cells ◽  
Band 3 ◽  
Glycophorin A ◽  
Blood Group Antigens ◽  
Red Blood Cell Membrane ◽  
Anion Transporter

Glycophorin A is the major transmembrane sialoglycoprotein of red blood cells. It has been shown to contribute to the expression of the MN and Wright blood group antigens, to act as a receptor for the malaria parasite Plasmodium falciparum and Sendai virus, and along with the anion transporter, band 3, may contribute to the mechanical properties of the red blood cell membrane. Several lines of evidence suggest a close interaction between glycophorin A and band 3 during their biosynthesis. Recently, we have generated mice where the band 3 expression was completely eliminated by selective inactivation of the AE1 anion exchanger gene, thus allowing us to study the effect of band 3 on the expression of red blood cell membrane proteins. In this report, we show that the band 3 −/− red blood cells contain protein 4.1, adducin, dematin, p55, and glycophorin C. In contrast, the band 3 −/− red blood cells are completely devoid of glycophorin A (GPA), as assessed by Western blot and immunocytochemistry techniques, whereas the polymerase chain reaction (PCR) confirmed the presence of GPA mRNA. Pulse-label and pulse-chase experiments show that GPA is not incorporated in the membrane and is rapidly degraded in the cytoplasm. Based on these findings and other published evidence, we propose that band 3 plays a chaperone-like role, which is necessary for the recruitment of GPA to the red blood cell plasma membrane.

Characterization of zebrafish merlot/chablis as non-mammalian vertebrate models for severe congenital anemia due to protein 4.1 deficiency

Development ◽  
2002 ◽  
Vol 129 (18) ◽  
pp. 4359-4370 ◽  
Author(s):  
Ebrahim Shafizadeh ◽  
Barry H. Paw ◽  
Helen Foott ◽  
Eric C. Liao ◽  
Bruce A. Barut ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Blood Cell ◽  
Red Blood Cells ◽  
Cell Morphology ◽  
Red Blood Cell ◽  
Blood Cells ◽  
Membrane Skeleton ◽  
Specific Protein ◽  
Abnormal Cell ◽  
Protein 4.1R

The red blood cell membrane skeleton is an elaborate and organized network of structural proteins that interacts with the lipid bilayer and transmembrane proteins to maintain red blood cell morphology, membrane deformability and mechanical stability. A crucial component of red blood cell membrane skeleton is the erythroid specific protein 4.1R, which anchors the spectrin-actin based cytoskeleton to the plasma membrane. Qualitative and quantitative defects in protein 4.1R result in congenital red cell membrane disorders characterized by reduced cellular deformability and abnormal cell morphology. The zebrafish mutants merlot (mot) and chablis (cha) exhibit severe hemolytic anemia characterized by abnormal cell morphology and increased osmotic fragility. The phenotypic analysis of merlot indicates severe hemolysis of mutant red blood cells, consistent with the observed cardiomegaly, splenomegaly, elevated bilirubin levels and erythroid hyperplasia in the kidneys. The result of electron microscopic analysis demonstrates that mot red blood cells have membrane abnormalities and exhibit a severe loss of cortical membrane organization. Using positional cloning techniques and a candidate gene approach, we demonstrate that merlot and chablis are allelic and encode the zebrafish erythroid specific protein 4.1R. We show that mutant cDNAs from both alleles harbor nonsense point mutations, resulting in premature stop codons. This work presents merlot/chablis as the first characterized non-mammalian vertebrate models of hereditary anemia due to a defect in protein 4.1R integrity.

The Study of RBC Deformation in Capillaries With a Lattice Boltzmann Method for Surfactant Covered Droplets

2009 ◽  
Author(s):  
Hassan Farhat ◽  
Joon Sang Lee
Keyword(s):  
Surface Tension ◽  
Cell Membrane ◽  
Blood Cell ◽  
Red Blood Cells ◽  
Red Blood Cell ◽  
Blood Cells ◽  
Shape Change ◽  
Immiscible Fluids ◽  
Surface Velocity ◽  
Droplet Shape

This study aims at analyzing the shape change of red blood cells in the process of streaming through a capillary smaller than the red blood cell diameter. The characteristics of its shape change and velocity can potentially lead to an indicator of a variety of diseases. We approach this problem with considering red blood cells as surfactant covered droplets. This assumption is justified by the fact that the cell membrane liquefies under high pressure in small capillaries, and this allows the marginalization of the mechanical properties of the membrane. The red blood cell membrane is in fact a macro-colloid containing lipid surfactant. When liquefied, it can be treated as a droplet of immiscible hemoglobin covered with lipid surfactant in plasma surrounding. The merit is to analyze the effect of the flow condition and domain geometry on the surfactant concentration change over the droplet interface, and the effect of this change on the surface tension of the droplet. The distribution of the surfactant is calculated by enforcing conservation of the surfactant mass concentration on the interface, leading to a convection diffusion equation. The equation takes account of the effects of the normal and Marangoni stresses as a boundary condition on the interface between the immiscible fluids. The gradient in the surface tension adversely determines the droplet shape by effecting a local change in the capillary number, and influences its velocity by retarding the local surface velocity. The choice of the Gunstensen model is motivated by its capability of handling incompressible fluids, and the locality of the application of the surface tension. We used the same concept to investigate the dynamic shape change of the RBC while flowing through the microvasculature, and explore the physics of the Fahraeus, and the Fahraeus-Lindqvist effects.

scholarly journals Systemic lupus erythematosus serum deposits C4d on red blood cells, decreases red blood cell membrane deformability, and promotes nitric oxide production

2011 ◽  
Vol 63 (2) ◽  
pp. 503-512 ◽  
Author(s):  
Ionita C. Ghiran ◽  
Mark L. Zeidel ◽  
Sergey S. Shevkoplyas ◽  
Jennie M. Burns ◽  
George C. Tsokos ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Systemic Lupus Erythematosus ◽  
Cell Membrane ◽  
Blood Cell ◽  
Red Blood Cells ◽  
Red Blood Cell ◽  
Lupus Erythematosus ◽  
Blood Cells ◽  
Nitric Oxide Production ◽  
Systemic Lupus

scholarly journals Red Blood Cell Membrane-Camouflaged Tedizolid Phosphate-Loaded PLGA Nanoparticles for Bacterial-Infection Therapy

Pharmaceutics ◽  
2021 ◽  
Vol 13 (1) ◽  
pp. 99
Author(s):  
Xinyi Wu ◽  
Yichen Li ◽  
Faisal Raza ◽  
Xuerui Wang ◽  
Shulei Zhang ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Membrane ◽  
Blood Cell ◽  
Sustained Release ◽  
Delivery System ◽  
Red Blood Cell ◽  
Multiple Drug Resistance ◽  
Plga Nanoparticles ◽  
Multiple Drug ◽  
Red Blood Cell Membrane

Multiple drug resistance (MDR) in bacterial infections is developed with the abuse of antibiotics, posing a severe threat to global health. Tedizolid phosphate (TR-701) is an efficient prodrug of tedizolid (TR-700) against gram-positive bacteria, including methicillin-sensitive staphylococcus aureus (MSSA) and methicillin-resistant staphylococcus aureus (MRSA). Herein, a novel drug delivery system: Red blood cell membrane (RBCM) coated TR-701-loaded polylactic acid-glycolic acid copolymer (PLGA) nanoparticles (RBCM-PLGA-TR-701NPs, RPTR-701Ns) was proposed. The RPTR-701Ns possessed a double-layer core-shell structure with 192.50 ± 5.85 nm in size, an average encapsulation efficiency of 36.63% and a 48 h-sustained release in vitro. Superior bio-compatibility was confirmed with red blood cells (RBCs) and HEK 293 cells. Due to the RBCM coating, RPTR-701Ns on one hand significantly reduced phagocytosis by RAW 264.7 cells as compared to PTR-701Ns, showing an immune escape effect. On the other hand, RPTR-701Ns had an advanced exotoxins neutralization ability, which helped reduce the damage of MRSA exotoxins to RBCs by 17.13%. Furthermore, excellent in vivo bacteria elimination and promoted wound healing were observed of RPTR-701Ns with a MRSA-infected mice model without causing toxicity. In summary, the novel delivery system provides a synergistic antibacterial treatment of both sustained release and bacterial toxins absorption, facilitating the incorporation of TR-701 into modern nanotechnology.

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