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.

Can we be certain that storage duration of transfused red blood cells does not affect patient outcomes?

BMJ ◽  
2019 ◽  
pp. l2320 ◽  
Author(s):  
Marialena Trivella ◽  
Simon J Stanworth ◽  
Susan Brunskill ◽  
Peter Dutton ◽  
Douglas G Altman
Keyword(s):  
Red Blood Cells ◽  
Patient Outcomes ◽  
Blood Cells ◽  
Storage Duration

scholarly journals The Nature of the Hemorrhagic Disorder Accompanying Hemolytic Transfusion Reactions in Man

Blood ◽  
1957 ◽  
Vol 12 (9) ◽  
pp. 834-843 ◽  
Author(s):  
JULIUS R. KREVANS ◽  
DUDLEY P. JACKSON ◽  
C. LOCKARD CONLEY ◽  
ROBERT C. HARTMANN
Keyword(s):  
Red Blood Cells ◽  
Whole Blood ◽  
Blood Cells ◽  
Fibrinolytic Activity ◽  
Hemorrhagic Diathesis ◽  
Intravascular Coagulation ◽  
Transfusion Reactions

Abstract A hemorrhagic diathesis has been observed in 2 patients who received 500 ml. of incompatible whole blood. In both, hypofibrinogenemia, hypoprothrombinemia and thrombocytopenia were observed and there was no evidence of increased fibrinolytic activity. In one, accelerin activity was reduced and there was transient evidence of a low-titered circulating anticoagulant. The most likely explanation for the observed changes is intravascular coagulation in the recipient, presumably initiated by the thromboplastin-like activity of the hemolyzed red blood cells.

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.

scholarly journals Selenium-Epoxy ‘Click’ Reaction and Se-Alkylation—Efficient Access to Organo-Selenium and Selenonium Compounds

Chemistry ◽  
2020 ◽  
Vol 2 (4) ◽  
pp. 827-836
Author(s):  
Taejun Eom ◽  
Anzar Khan
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Ring Opening ◽  
Click Reaction ◽  
Oxirane Ring ◽  
New Class ◽  
Ring Opening Reaction ◽  
Efficient Access ◽  
High Concentrations ◽  
Cationic Materials

This work establishes the ‘click’ nature of the base-catalyzed oxirane ring opening reaction by the selenolate nucleophile. The ‘click’-generated ß-hydroxy selenide can be alkylated to afford cationic selenium species. Hemolytic studies suggest that selenonium cations do not lyse red blood cells even at high concentrations. Overall, these results indicate the future applicability of the developed organo-selenium chemistry in the preparation of a new class of cationic materials based on the seleno-ether motif.

K(86Rb) transport heterogeneity in the low-density fraction of sickle cell anemia red blood cells

1996 ◽  
Vol 271 (4) ◽  
pp. C1111-C1121 ◽  
Author(s):  
Z. Etzion ◽  
V. L. Lew ◽  
R. M. Bookchin
Keyword(s):  
Red Blood Cells ◽  
Sickle Cell ◽  
Sickle Cell Anemia ◽  
Blood Cells ◽  
Highly Nonlinear ◽  
Heterogeneous Expression ◽  
Transport Path ◽  
High Concentrations ◽  
K Transport ◽  
Slow Turnover

Previous studies have suggested ion transport heterogeneity among sickle cell anemia (SS) reticulocytes that could influence their dehydration susceptibility. We examined Ca2(+)-independent K transport in the lowest density (F1), reticulocyte-rich SS cells, measuring the effects of acidification, ouabain, and bumetanide on their unidirectional K(86Rb) fluxes. Unlike those of normal red blood cells and SS discocytes, the SS-F1 K(86Rb) fluxes were highly nonlinear, with large 5-min flux components (previously unobserved) and a more gradual decline over 60 min. Analysis revealed two distinct K pools: a rapid-turnover pool in a small fraction of cells, whose major ouabain-resistant K(86Rb) transport path showed distinctive properties including inhibition by high concentrations of bumetanide (> or = 1 mM) and stimulation at pH 7.0, and another heterogeneous, relatively slow-turnover pool, in most of the F1 cells, whose main ouabain-resistant K(86Rb) path was insensitive to bumetanide but was stimulated at pH 7.0, which is consistent with heterogeneous expression of the acid-sensitive K-Cl cotransport and with both rapid and slower generation of dehydrated SS cells.

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.

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