Oxidants and regulation of K+-Cl−cotransport in equine red blood cells

2000 ◽  
Vol 279 (4) ◽  
pp. C981-C989 ◽  
Author(s):  
M. C. Muzyamba ◽  
P. F. Speake ◽  
J. S. Gibson
Keyword(s):  
Carbon Monoxide ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Prolonged Exposure ◽  
Reduced Glutathione ◽  
Low Concentrations ◽  
High Concentrations

The effect of oxidants on K+-Cl−cotransport (KCC) was investigated in equine red blood cells. Carbon monoxide mimicked O2. The substituted benzaldehyde, 12C79 (5 mM), markedly increased O2affinity. In N2, however, O2saturation was low (<10%) but KCC remained active. Nitrite (NO2−) oxidized heme to methemoglobin (metHb). High concentrations of NO2−(1 and 5 mM vs. 0.5 mM) increased KCC activity above control levels; it became O2independent but remained sensitive to other stimuli. 1-Chloro-2,4-dinitrobenzene (1–3 mM) depleted reduced glutathione (GSH). Prolonged exposure (60–120 min, 1 mM) or high concentrations (3 mM) stimulated an O2-independent KCC activity; short exposures and low concentrations (30 min, 0.5 or 1 mM) did not. The effect of these manipulations was correlated with changes in GSH and metHb concentrations. An oxy conformation of Hb was necessary for KCC activation. An increase in its activity over the level found in oxygenated control cells required both accumulation of metHb and depletion of GSH. Findings are relevant to understanding the physiology and pathology of regulation of KCC.

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 Detection of acyl-CoA-binding protein in human red blood cells and investigation of its role in membrane phospholipid renewal

1995 ◽  
Vol 306 (3) ◽  
pp. 793-799 ◽  
Author(s):  
H Fyrst ◽  
J Knudsen ◽  
M A Schott ◽  
B H Lubin ◽  
F A Kuypers
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Human Liver ◽  
Plasma Membranes ◽  
Binding Protein ◽  
Human Red Blood Cells ◽  
Low Concentrations ◽  
Membrane Bound ◽  
High Concentrations

Acyl-CoA-binding protein (ACBP) has been identified in a number of tissues and shown to affect the intracellular distribution and utilization of acyl-CoA. We have detected ACBP in the cytosol but not the membrane of human red blood cells and, using an e.l.i.s.a. with antibodies prepared against human liver ACBP, found that its concentration was 0.5 microM. To investigate the role of ACBP in human red blood cells, we added purified human liver ACBP and radiolabelled acyl-CoA to isolated membranes from these cells. ACBP prevented high concentrations of acyl-CoA from binding to the membrane but could not keep the acyl-CoA in the aqueous phase at low concentrations. This suggested the presence of a pool in the membrane with a binding affinity for acyl-CoA that was greater than that of ACBP for acyl-CoA. In the presence of lysophospholipid, this membrane-bound pool of acyl-CoA was rapidly used as a substrate by acyl-CoA:lysophospholipid acyltransferase (LAT) to generate phospholipid from lysophospholipid. We also found that ACBP-bound acyl-CoA was preferred over free acyl-CoA as a substrate by LAT. These results are the first documentation that human red blood cells contain ACBP and that this protein can affect the utilization of acyl-CoA in plasma membranes of these cells. The interactions between acyl-CoA, ACBP and the membrane suggest that there are several pools of acyl-CoA in the human red blood cell and that ACBP may have a role in regulating their distribution and fate.

Activation by N-ethylmaleimide of a latent K+-Cl- flux in human red blood cells

1984 ◽  
Vol 246 (5) ◽  
pp. C385-C390 ◽  
Author(s):  
P. K. Lauf ◽  
N. C. Adragna ◽  
R. P. Garay
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Sulfhydryl Group ◽  
Maximum Velocity ◽  
Coupled Transport ◽  
Human Red Blood Cells ◽  
Low Concentrations ◽  
Reactive Groups ◽  
High Concentrations ◽  
K Transport

Twenty to fifty percent of the ouabain-insensitive Na+ and K+ fluxes in human red blood cells are mediated by Cl(-) -dependent coupled transport (cotransport). In this paper we report on the effect of the sulfhydryl group reagent N-ethylmaleimide (NEM) on Cl(-) -dependent ouabain-insensitive Na+ and K+ fluxes in human red blood cells. We found that NEM altered Na+ -K+ cotransport and activated a latent Cl(-) -dependent K+ transport mode normally apparently silent. This conclusion was based on the following observations. 1) At low concentrations (0.25 mM) NEM abolished the bumetanide-sensitive Na+ efflux and had no effect, even at a 10-fold higher concentration, on the bumetanide-sensitive K+ efflux. 2) At concentrations above 0.1 mM, NEM stimulated Cl(-) -dependent K+ efflux that was only partially inhibited by high concentrations of bumetanide or furosemide. In experiments using Rb+ as a K+ analogue, NEM activated Rb+ influx by stimulating the maximum velocity and lowering the apparent external cation affinity. The data suggest the presence of chemically reactive groups in human red blood cells for both Cl(-) -dependent K+ transport activated by NEM and Cl(-) -dependent coupled Na+-K+ movements.

scholarly journals Interaction of Mercury with Human Erythrocytes

1962 ◽  
Vol 45 (3) ◽  
pp. 395-410 ◽  
Author(s):  
R. Weed ◽  
J. Eber ◽  
A. Rothstein
Keyword(s):  
Red Blood Cells ◽  
Glucose Uptake ◽  
Binding Sites ◽  
Blood Cells ◽  
Reduced Glutathione ◽  
Osmotic Fragility ◽  
Red Cells ◽  
Sulfhydryl Groups ◽  
Low Concentrations ◽  
Binding Curves

The binding of mercury to red blood cells was measured in terms of Hg203 uptake and desorption. The significant features of the binding are: (a) rapid achievement of equilibrium (3 to 5 minutes); (b) release of a Hg-complexing material from the red cells themselves which distorts the binding curves at low concentrations of metal (2.5 x 10-7 to 5.0 x 10-6 M); (c) prevention of binding by cysteine, glutathione, penicillamine, and EDTA but not by imidazole or histidine; (d) binding of mercury in amounts up to 7 times the reduced glutathione concentration of the cells before combination with glutathione itself; (e) binding primarily to sulfhydryl groups of hemoglobin and to a small number of stromal sulfhydryl groups, but also to other non-sulfhydryl cellular ligands after saturation of the sulfhydryl groups. Associated with the binding is inhibition of glucose uptake, induction of loss of K+, and decrease in osmotic fragility. These effects increase over the range of concentrations (1 x 10-17 to 1 x 10-15 moles of Hg/RBC) well below those that result in saturation of the cellular binding sites; above 1 x 10-15 moles/RBC, the effects decrease as the cells become saturated.

scholarly journals Quantitative Recovery of 14C-labeled Carbon Monoxide (14CO) From Viable Heme-labeled Red Blood Cells in the Rat

Blood ◽  
1972 ◽  
Vol 40 (2) ◽  
pp. 257-260 ◽  
Author(s):  
Stephen A. Landaw
Keyword(s):  
Carbon Monoxide ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Quantitative Recovery

Abstract Long-term recovery of 14C-labeled carbon monoxide (14CO) from labeled, transfused red blood cells (RBC) was studied in buffalo rats. Donor RBC (labeled with 14C-2-glycine) were transfused into host rats, and the 14CO formed from degradation of labeled hemoglobin heme was collected over the next 110+ days. The heme-equivalent 14CO recovery in 13 animals averaged 102.1 ± 2.1% (mean ± SE) of activity in hemoglobin heme of donor RBC. This confirms that heme of circulating RBC destroyed by random hemolysis and senescence is quantitatively converted to CO.

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.

Effects of cadmium and zinc on calcium uptake in human red blood cells

1984 ◽  
Vol 247 (3) ◽  
pp. C143-C149 ◽  
Author(s):  
G. A. Plishker
Keyword(s):  
Red Blood Cells ◽  
Disulfide Bond ◽  
Blood Cells ◽  
Calcium Uptake ◽  
Sodium Potassium ◽  
Human Red Blood Cells ◽  
Low Concentrations ◽  
Influx Pathways ◽  
Extracellular Sodium ◽  
Passive Influx

Cadmium and zinc increased the accumulation of calcium in human red blood cells by increasing passive influx without enhancing the permeability to other ions. The effect of cadmium and zinc appeared specific to these metals, because barium, magnesium, cobalt, strontium, manganese, and nickel had no effect. Changes in calcium uptake by extracellular sodium, potassium, and pH were not altered by zinc and cadmium. Inhibition of calcium uptake by quinine, oligomycin, and iodoacetate was not affected by cadmium or zinc. These results suggest that cadmium and zinc increase calcium movement through normal influx pathways. Cadmium and zinc acted synergistically apparently by different mechanisms. Zinc and cadmium differentially affected calcium uptake in different extracellular calcium concentrations. The cadmium effect was increased by low concentrations of 2-mercaptoethanol and above pH 8.0, while the zinc effect was less sensitive to these factors. These findings suggest that the cadmium effect involves a disulfide bond between cysteinyl residues and the zinc effect involves a different site.

Immunoregulatory Effects of Stored Red Blood Cells

Hematology ◽  
2011 ◽  
Vol 2011 (1) ◽  
pp. 466-469 ◽  
Author(s):  
Karina Yazdanbakhsh ◽  
Weili Bao ◽  
Hui Zhong
Keyword(s):  
Red Blood Cells ◽  
Patient Outcomes ◽  
Clinical Studies ◽  
Blood Cells ◽  
Immunomodulatory Effects ◽  
Tissue Microenvironment ◽  
High Concentrations ◽  
Transfusion Reactions ◽  
Immunoregulatory Mechanisms

Abstract Some clinical studies have identified potential adverse patient outcomes associated with RBC storage length. This may in part be due to the release of potentially hazardous bioactive products that accumulate during storage and are delivered at high concentrations during transfusion. In this situation, a proinflammatory tissue microenvironment may be established that can alter immunoregulatory mechanisms. This review highlights some of the potential immunomodulatory effects of stored RBCs that may be responsible for adverse transfusion reactions.

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