Biologically-active unilamellar vesicles from red blood cells

2019 ◽  
Vol 7 (4) ◽  
pp. 1393-1398 ◽  
Author(s):  
Hyun-Sook Jang ◽  
Yoon-Kyoung Cho ◽  
Steve Granick
Keyword(s):  
Membrane Protein ◽  
Red Blood Cells ◽  
Fluorescence Intensity ◽  
Blood Cells ◽  
Cytochalasin B ◽  
Blocking Agent ◽  
Biologically Active ◽  
Unilamellar Vesicles

Methods are described to prepare biologically-active unilamellar vesicles from red blood cells. Whereas glucose enters the GUV causing fluorescence intensity to increase, mediated by the action of the membrane protein GLUT1, control experiments confirm that this fails to be observed in the presence of the blocking agent cytochalasin B.

scholarly journals Alterations in the Properties of Red Blood Cells in Men with Coronary Artery Diseases after Comprehensive Cardiac Rehabilitation

2020 ◽  
Vol 2020 ◽  
pp. 1-9
Author(s):  
Krzysztof Gwozdzinski ◽  
Anna Pieniazek ◽  
Joanna Bernasinska-Slomczewska ◽  
Joanna Brzeszczynska ◽  
Robert Irzmanski ◽  
...  
Keyword(s):  
Coronary Artery ◽  
Membrane Protein ◽  
Cardiac Rehabilitation ◽  
Red Blood Cells ◽  
Membrane Fluidity ◽  
Exercise Test ◽  
Blood Cells ◽  
Reduced Glutathione ◽  
Osmotic Fragility ◽  
Cardiac Intervention

Purpose. Comprehensive cardiac rehabilitation (CCR) is a complex program aimed at improving the health status of patients with coronary artery disease (CAD), especially those who have been subjected to cardiac interventions (PCI and CABG).The aim of this study was to measure the changes in the properties of red blood cells (RBCs) in men with CAD after cardiac intervention and after participation in CCR program. Methods. In this study, we have investigated the influence of the physical training-based CCR program in 12 men with CAD, after PCI or CABG. The characteristics of RBCs including the basic morphology of RBCs, the conformational state of RBC membrane protein and hemoglobin, acetylcholinesterase activity, membrane fluidity, the osmotic fragility, and thiol concentration in membrane and in hemolysate were measured. Ascorbate concentration and reduced glutathione were also determined. The analysis was performed in men, before and after participation in CCR. The properties of RBCs were observed in connection with the exercise test, and parameters were evaluated before, immediately after, and 1 hour after the exercise test. Results. After CCR, a decrease in the mobility of erythrocyte membrane proteins was observed, which was accompanied by a decrease in lipid fluidity. In addition, immediately after the exercise test and 1 hour later, we measured a decrease in thiol level in hemolysate, but not in the plasma membrane. Unexpectedly, an increase in reduced glutathione concentration one hour after the exercise test after completing comprehensive cardiac rehabilitation was observed. Conclusion. CCR in men with CAD after cardiac intervention is connected with decreased membrane fluidity and decreased membrane protein mobility, which indicates that reduction of oxidative changes in these components occurs.

Trans-bilayer phospholipid movements in human red blood cells deficient in the 32kDa Band-7.2b membrane protein, ‘stomatin’

1997 ◽  
Vol 25 (3) ◽  
pp. 492S-492S ◽  
Author(s):  
Mei M. Ho ◽  
Anna Nicolaou ◽  
Annette C. Argent ◽  
Gordon W. Stewart
Keyword(s):  
Membrane Protein ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Human Red Blood Cells

Comparison between Ca2+-induced scrambling of various fluorescently labelled lipid analogues in red blood cells

2002 ◽  
Vol 362 (3) ◽  
pp. 741-747 ◽  
Author(s):  
David W. C. DEKKERS ◽  
Paul COMFURIUS ◽  
Edouard M. BEVERS ◽  
Robert F. A. ZWAAL
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Red Blood Cells ◽  
Phospholipase D ◽  
Blood Cells ◽  
Amino Group ◽  
Flip Flop ◽  
Putative Membrane Protein ◽  
Kinetics Of

Treatment of red blood cells with calcium and ionomycin causes activation of the lipid scramblase, a putative membrane protein catalysing flip-flop of (phospho)lipids. Various fluorescent 1-oleoyl-2-[6(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino] caproyl (C6-NBD) analogues were tested for transbilayer movement across the plasma membrane of red blood cells. Among these phospholipid analogues were phosphatidylgalactose, phosphatidylmaltose and phosphatidylmaltotriose, which were obtained from C6-NBD-phosphatidylcholine by phospholipase D-catalysed transphosphatidylation. The inward movement after the onset of scrambling was monitored by extraction of the non-internalized probe with BSA. We demonstrate that both the amino group and the size of the headgroup determine the kinetics of lipid scrambling, and that lipids with a ceramide backbone migrate much more slowly than glycerophospholipids with the same headgroup.

scholarly journals Trypanosoma vivax Adhesion to Red Blood Cells in Experimentally Infected Sheep

2016 ◽  
Vol 2016 ◽  
pp. 1-9 ◽  
Author(s):  
Alpidio A. Boada-Sucre ◽  
Marcello Salvatore Rossi Spadafora ◽  
Lucinda M. Tavares-Marques ◽  
Héctor J. Finol ◽  
Armando Reyna-Bello
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Biologically Active ◽  
Economic Losses ◽  
Cellular Interactions ◽  
Trypanosoma Vivax ◽  
Host Parasite ◽  
Frequent Observation ◽  
Active Substances ◽  
Free Flagellum

Trypanosomosis, a globally occurring parasitic disease, poses as a major obstacle to livestock production in tropical and subtropical regions resulting in tangible economic losses. In Latin America including Venezuela, trypanosomosis of ruminants is mainly caused by Trypanosoma vivax. Biologically active substances produced from trypanosomes, as well as host-trypanosome cellular interactions, contribute to the pathogenesis of anemia in an infection. The aim of this study was to examine with a scanning electron microscope the cellular interactions and alterations in ovine red blood cells (RBC) experimentally infected with T. vivax. Ovine infection resulted in changes of RBC shape as well as the formation of surface holes or vesicles. A frequent observation was the adhesion to the ovine RBC by the trypanosome’s free flagellum, cell body, or attached flagellum in a process mediated by the filopodia emission from the trypanosome surface. The observed RBC alterations are caused by mechanical and biochemical damage from host-parasite interactions occurring in the bloodstream. The altered erythrocytes are prone to mononuclear phagocytic removal contributing to the hematocrit decrease during infection.

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.

GLUT-1 mediation of rapid glucose transport in dolphin (Tursiops truncatus) red blood cells

1998 ◽  
Vol 274 (1) ◽  
pp. R112-R119 ◽  
Author(s):  
James D. Craik ◽  
James D. Young ◽  
Christoper I. Cheeseman
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Tursiops Truncatus ◽  
Glucose Transporter ◽  
Cytochalasin B ◽  
Sodium Dodecyl ◽  
Maximal Velocity ◽  
Cell Water ◽  
Glut 1 ◽  
L Cell

d-Glucose entry into erythrocytes from adult dolphins ( Tursiops truncatus) was rapid, showed saturation at high substrate concentrations, and demonstrated a marked stimulation by intracellular d-glucose. Kinetic parameters were estimated from the concentration dependence of initial rates of tracer entry at 6°C: for zero- trans entry, Michaelis constant ( K m) was 0.78 ± 0.10 mM and maximal velocity ( V max) was 300 ± 9 μmol ⋅ l cell water−1 ⋅ min−1; for equilibrium exchange entry, K m was 17.5 ± 0.6 mM and V maxwas 8,675 ± 96 μmol ⋅ l cell water−1 ⋅ min−1. Glucose entry was inhibited by cytochalasin B, and mass law analysis of reversible,d-glucose-displaceable, cytochalasin B binding gave values of 0.37 ± 0.03 nmol/mg membrane protein for maximal binding and 0.48 ± 0.10 μM for the dissociation constant. Dolphin glucose transporter polypeptides were identified on sodium-dodecyl sulfate-polyacrylamide gel electrophoresis immunoblots [using antibodies that recognized human glucose transporter isoform (GLUT-1)] as two molecular species, apparent relative molecular weights of 53,000 and 47,000. Identity of these polypeptides was confirmed byd-glucose-sensitive photolabeling of membranes with [3H]cytochalasin B. Digestion of both dolphin and human red blood cell membranes with glycopeptidase F led to the generation of a sharp band of relative molecular weight 46,000 derived from GLUT-1. Trypsin treatment of human and dolphin erythrocyte membranes generated fragmentation patterns consistent with similar polypeptide structures for GLUT-1 in human and dolphin red blood cells.

Membrane protein carbonylation in non-leukodepleted CPDA-preserved red blood cells

2006 ◽  
Vol 36 (2) ◽  
pp. 279-282 ◽  
Author(s):  
Anastasios G. Kriebardis ◽  
Marianna H. Antonelou ◽  
Konstantinos E. Stamoulis ◽  
Effrosini Economou-Petersen ◽  
Lukas H. Margaritis ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Protein Carbonylation

Alterations in Membrane Protein and Phosphorylation Pattern in ?-Thalassemic Red Blood Cells

1985 ◽  
Vol 445 (1 Fifth Cooley') ◽  
pp. 81-91 ◽  
Author(s):  
JORGE ERUSALIMSKY ◽  
EILAT SHINAR ◽  
ELIEZER A. RACHMILEWITZ ◽  
YORAM MILNER
Keyword(s):  
Membrane Protein ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Phosphorylation Pattern
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