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

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.

Subcellular fractionation of stored red blood cells reveals a compartment-based protein carbonylation evolution

2012 ◽  
Vol 76 ◽  
pp. 181-193 ◽  
Author(s):  
Julien Delobel ◽  
Michel Prudent ◽  
Olivier Rubin ◽  
David Crettaz ◽  
Jean-Daniel Tissot ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Subcellular Fractionation ◽  
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

scholarly journals Alterations of membrane protein expression in red blood cells of Alzheimer's disease patients

2015 ◽  
Vol 1 (3) ◽  
pp. 334-338 ◽  
Author(s):  
György Várady ◽  
Edit Szabó ◽  
Ágnes Fehér ◽  
Adrienn Németh ◽  
Boglárka Zámbó ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Membrane Protein ◽  
Protein Expression ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Membrane Protein Expression

scholarly journals A study of membrane protein defects and α hemoglobin chains of red blood cells in human β thalassemia

1989 ◽  
Vol 264 (32) ◽  
pp. 19092-19098
Author(s):  
P Rouyer-Fessard ◽  
M C Garel ◽  
C Domenget ◽  
D Guetarni ◽  
D Bachir ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Red Blood Cells ◽  
Blood Cells

scholarly journals Inhibition of deoxygenation-induced membrane protein dephosphorylation and cell dehydration by phorbol esters and okadaic acid in sickle cells

Blood ◽  
1995 ◽  
Vol 86 (5) ◽  
pp. 1999-2007 ◽  
Author(s):  
H Fathallah ◽  
E Coezy ◽  
RS de Neef ◽  
MD Hardy-Dessources ◽  
F Giraud
Keyword(s):  
Membrane Protein ◽  
Red Blood Cells ◽  
Okadaic Acid ◽  
Blood Cells ◽  
Phorbol Esters ◽  
K Channels ◽  
Sickle Cells ◽  
Ca Pump ◽  
Cell Dehydration ◽  
Protein Dephosphorylation

Deoxygenation (DO) of sickle cell anemia red blood cells (SS cells) induces membrane permeabilization to Ca2+, Na+, and K+ and cell dehydration mostly through the activation of the Ca(2+)-dependent K+ channels. We show that DO of both SS cells and normal red blood cells was accompanied by a nonspecific dephosphorylation of membrane proteins. After treatment with a protein kinase C activator (phorbol myristate acetate) or a phosphoprotein phosphatase inhibitor (okadaic acid), the level of membrane protein phosphorylation in deoxygenated cells was maintained higher or equal, respectively, to that of the oxygenated controls. We found that these drugs in SS cells (1) inhibited by 40% the DO-stimulated net Ca2+ uptake, without affecting the DO-stimulated Ca2+ influx, suggesting that they activated the Ca2+ efflux; (2) slightly increased the DO-induced Na+ uptake and decreased the DO-induced K+ loss; and (3) prevented the DO-induced cell dehydration. Both drugs are known to stimulate both phosphorylation and activity of the Ca pump and of the Na/H antiport. Inhibition of SS cell dehydration might be due to an activation of the Ca pump preventing [Ca2+]i elevation responsible for the stimulation of the K+ channels and/or to an activation of the Na/H exchange resulting in cell water gain.

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