Hemoglobin oxidation at functional amino acid residues during routine storage of red blood cells

Transfusion ◽  
2015 ◽  
Vol 56 (2) ◽  
pp. 421-426 ◽  
Author(s):  
Matthew Wither ◽  
Monika Dzieciatkowska ◽  
Travis Nemkov ◽  
Pavel Strop ◽  
Angelo D'Alessandro ◽  
...  
Keyword(s):  
Amino Acid ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Amino Acid Residues ◽  
Hemoglobin Oxidation

scholarly journals Binding of various ovotransferrin fragments to chick-embryo red cells

1989 ◽  
Vol 257 (1) ◽  
pp. 301-304 ◽  
Author(s):  
A Oratore ◽  
G D'Andrea ◽  
K Moreton ◽  
J Williams
Keyword(s):  
Amino Acid ◽  
Chick Embryo ◽  
Red Blood Cells ◽  
Receptor Binding ◽  
Blood Cells ◽  
Tight Binding ◽  
Red Cells ◽  
Transferrin Receptors ◽  
Amino Acid Residues

1. The ability of N- and C-terminal half-molecule fragments of hen ovotransferrin to interact with chick red blood cells (CERBC) has been studied under conditions that allow binding of the transferrin to transferrin receptors to take place, but not the delivery of iron to the cell. Two kinds of half-molecule fragments were used: (a) those which can associate with one another to give a dimer resembling native transferrin and (b) those which cannot associate in this way because they lack a few amino acid residues from their C-terminal ends. 2. Neither N nor C half-molecules alone can bind to the CERBC, but, when both are present, tight binding occurs. 3. Whether or not the half-molecules can associate with one another makes little difference to receptor binding. 4. Given that one of the half-molecules is iron-saturated, the presence or absence of iron in the contralateral half-molecule again makes little difference to receptor binding.

scholarly journals Hemoglobin Oxidation in Stored Blood Accelerates Hemolysis and Oxidative Injury to Red Blood Cells

2020 ◽  
Vol 12 (04) ◽  
pp. 244-249
Author(s):  
Ibrahim Mustafa ◽  
Tameem Ali Qaid Hadwan
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Morphological Changes ◽  
Hemoglobin Concentration ◽  
Red Cell Membrane ◽  
Rbc Membrane ◽  
Hemoglobin Oxidation ◽  
Rbc Indices ◽  
Methemoglobin Formation ◽  
Stored Blood

Abstract Introduction Maintaining blood supply is a challenge in blood banks. Red blood cells (RBCs) stored at 4°C experience issues of biochemical changes due to metabolism of cells, leading to changes collectively referred to as “storage lesions.” Oxidation of the red cell membrane, leading to lysis, contributes to these storage lesions. Methods Blood bags with CPD-SAGM stored at 4°C for 28 days were withdrawn aseptically on days 1, 14, and 28. Hematology analyzer was used to investigate RBC indices. Hemoglobin oxidation was studied through spectrophotometric scan of spectral change. RBC lysis was studied with the help of Drabkin's assay, and morphological changes were observed by light and scan electron microscopy. Results RBCs show progressive changes in morphology echinocytes and spherocytes on day 28. There was 0.85% RBC lysis, an approximately 20% decrease in percentage oxyhemoglobin, and a 14% increase in methemoglobin formation, which shows hemoglobin oxidation on day 28. Conclusions Oxidative damage to RBC, with an increase in storage time was observed in the present study. The observed morphological changes to RBC during the course of increased time shows that there is progressive damage to RBC membrane and a decrease in hemoglobin concentration; percentage RBC lysis is probably due to free hemoglobin and iron.

scholarly journals Antagonists of the system L neutral amino acid transporter (LAT) promote endothelial adhesivity of human red blood cells

2017 ◽  
Vol 117 (07) ◽  
pp. 1402-1411 ◽  
Author(s):  
Laura Beth Mann Dosier ◽  
Vikram J. Premkumar ◽  
Hongmei Zhu ◽  
Izzet Akosman ◽  
Michael F. Wempe ◽  
...  
Keyword(s):  
Amino Acid ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Amino Acid Transporter ◽  
Neutral Amino Acid ◽  
Neutral Amino Acid Transporter ◽  
System L

SummaryThe system L neutral amino acid transporter (LAT; LAT1, LAT2, LAT3, or LAT4) has multiple functions in human biology, including the cellular import of S-nitrosothiols (SNOs), biologically active derivatives of nitric oxide (NO). SNO formation by haemoglobin within red blood cells (RBC) has been studied, but the conduit whereby a SNO leaves the RBC remains unidentified. Here we hypothesised that SNO export by RBCs may also depend on LAT activity, and investigated the role of RBC LAT in modulating SNO-sensitive RBC-endothelial cell (EC) adhesion. We used multiple pharmacologic inhibitors of LAT in vitro and in vivo to test the role of LAT in SNO export from RBCs and in thereby modulating RBC-EC adhesion. Inhibition of human RBC LAT by type-1-specific or nonspecific LAT antagonists increased RBC-endothelial adhesivity in vitro, and LAT inhibitors tended to increase post-transfusion RBC sequestration in the lung and decreased oxygenation in vivo. A LAT1-specific inhibitor attenuated SNO export from RBCs, and we demonstrated LAT1 in RBC membranes and LAT1 mRNA in reticulocytes. The proadhesive effects of inhibiting LAT1 could be overcome by supplemental L-CSNO (S-nitroso-L-cysteine), but not D-CSNO or L-Cys, and suggest a basal anti-adhesive role for stereospecific intercellular SNO transport. This study reveals for the first time a novel role of LAT1 in the export of SNOs from RBCs to prevent their adhesion to ECs. The findings have implications for the mechanisms of intercellular SNO signalling, and for thrombosis, sickle cell disease, and post-storage RBC transfusion, when RBC adhesivity is increased.

The human anion transport protein, band 3, contains a CD36-like binding domain forPlasmodium falciparum-infected erythrocytes

Parasitology ◽  
1996 ◽  
Vol 112 (3) ◽  
pp. 261-267 ◽  
Author(s):  
I. Crandall ◽  
I. W. Sherman
Keyword(s):  
Monoclonal Antibody ◽  
Amino Acid ◽  
Blood Cells ◽  
Synthetic Peptide ◽  
Epitope Mapping ◽  
Protein Band ◽  
Band 3 ◽  
Anion Transport ◽  
Transport Protein ◽  
Amino Acid Residues

SUMMARYEpitope mapping of a murine monoclonal antibody (mAb), 5H12, prepared against livePlasmodium falciparum-intected red blood cells indicated that the epitope consisted of amino acid residues 474–487 of the human anion transport protein, band 3. mAb 5H12 enhanced cytoadherence, but inhibited the CD36-like mediated resetting. A synthetic peptide based on the sequence of the epitope (FSFCETNGLE) blocked both resetting and cytoadherence, suggesting that this amino acid sequence may form the CD36-like receptor. The CD36-like region of band 3 was antigenically distinct from platelet or endothelial CD36.

Binding Analysis of a Novel Peptide to Plasmodium falciparum Knob-Associated Histidine Rich Protein (KAHRP)

2007 ◽  
Vol 1 (1) ◽  
Author(s):  
J. Preston ◽  
L. Zeng ◽  
C. G. Takoudis ◽  
X. Li ◽  
A. Chishti
Keyword(s):  
Plasmodium Falciparum ◽  
Amino Acid ◽  
Red Blood Cells ◽  
Blood Vessels ◽  
Real Time ◽  
Optical Sensor ◽  
Blood Cells ◽  
Specific Binding ◽  
Binding Interaction ◽  
The Real

Knob-associated histidine rich protein (KAHRP) is secreted by Plasmodium falciparum in infected red blood cells. This protein is required for the production of surface protrusions called knobs, which have been shown to be crucial for the adherence of P. falciparum-infected erythrocytes (Pf-IRBC) to the endothelia of small blood vessels. KP-AP, a 10-amino acid (AA) peptide (FITRANDTSK), binds specifically with KAHRP in preliminary studies. KP-AP is expected to disrupt knob formation and prohibit adherence of Pf-IRBC to blood vessels and greatly reduce the pathogenicity of the parasite. This paper describes an investigation into the binding interaction between biotinylated KP-AP (Biotin-AP) and a segment of KAHRP. ELISA and the real-time bio-interaction optical sensor, BIAcore are the methods of detection. The specific binding was confirmed with ELISA and the KD value was estimated to be 1.2 μM. Binding was not detected with BIAcore, most likely due to the reduced flexibility of Biotin-AP while immobilized on the sensor chip.

y+ cationic amino acid transport of arginine in packed red blood cells

2013 ◽  
Vol 179 (1) ◽  
pp. e183-e187 ◽  
Author(s):  
Levi D. Procter ◽  
Cindy F. Meier ◽  
Cameron Hamilton ◽  
Andrew R. Gerughty ◽  
Philip Overall ◽  
...  
Keyword(s):  
Amino Acid ◽  
Red Blood Cells ◽  
Amino Acid Transport ◽  
Blood Cells ◽  
Acid Transport ◽  
Packed Red Blood Cells ◽  
Cationic Amino Acid
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