Peroxiredoxin‐2 as a candidate biomarker to test oxidative stress levels of stored red blood cells under blood bank conditions

Rinalducci, Sara; D’Amici, Gian Maria; Blasi, Barbara; Vaglio, Stefania; Grazzini, Giuliano; Zolla, Lello

doi:10.1111/j.1537-2995.2010.03032.x

Cited by 88 publications

(92 citation statements)

References 57 publications

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“…41 In particular, Rocha et al 42 reported that peroxiredoxin 2 located at the membrane in RBC from patients with hereditary spherocytosis concomitantly with an increase in oxidative stress. As we had previously observed 17 through western blotting studies, and confirmed here by 2-DE ( Figure 1A, Online Supplementary Table S1A), peroxiredoxin-2 relocated progressively at the membrane level from the third week to the end of the storage.…”

supporting

confidence: 58%

“…However, the former hypothesis seems reasonable in the light of recent observations by our group which clearly indicate that membrane peroxiredoxin-2 in RBC that have been stored for a long time is still functional. 17 The likely effect of oxidative stress at the membrane protein level appeared not only to be limited to an increase in carbonyl levels (Online Supplementary Figure S2B), but also to an increase in fragmentation of structural proteins [spectrin alpha and beta chains, band 3 and protein 4.1 isoform 6 -structural constituent of cytoskeleton (GO:0005200)]. Fragments of band 4.1 were found at the membrane already at day 14 ( Figure 1A2).…”

Section: Alterations Of Red Blood Cell Membrane Shape and Vesiculatiomentioning

confidence: 99%

“…[8][9][10] The suspending fluid becomes enriched with free hemoglobin and biologically active lipids, along with large quantities of negatively charged microvesicles. 14,15 Membrane protein fragmentation 16 and accumulation of membrane biomarkers 17,18 have also been reported to correlate with storage duration.…”

Section: Introductionmentioning

confidence: 99%

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Time-course investigation of SAGM-stored leukocyte-filtered red bood cell concentrates: from metabolism to proteomics

D’Alessandro¹,

D’Amici²,

Vaglio³

et al. 2011

Haematologica

179

205

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The online version of this article has a Supplementary Appendix. BackgroundResults from recent, highly debated, retrospective studies raised concerns and prompted considerations about further testing the quality of long stored red blood cells from a biochemical standpoint. Design and MethodsWe performed an integrated mass spectrometry-based metabolomics and proteomics timecourse investigation on SAGM-stored red blood cells. In parallel, structural changes during storage were monitored through scanning electron microscopy. ResultsWe detected increased levels of glycolytic metabolites over the first 2 weeks of storage. From day 14 onwards, we observed a significant consumption of all metabolic species, and diversion towards the oxidative phase of the pentose phosphate pathway. These phenomena coincided with the accumulation of reactive oxygen species and markers of oxidation (protein carbonylation and malondialdehyde accumulation) up to day 28. Proteomics evidenced changes at the membrane protein level from day 14 onwards. Changes included fragmentation of membrane structural proteins (spectrin, band 3, band 4.1), membrane accumulation of hemoglobin, antioxidant enzymes (peroxiredoxin-2) and chaperones. While the integrity of red blood cells did not show major deviations at day 14, at day 21 scanning electron microscope images revealed that 50% of the erythrocytes had severely altered shape. We could correlate the scanning electron microscopy observations with the onset of vesiculation, through a proteomics snapshot of the difference in the membrane proteome at day 0 and day 35. We detected proteins involved in vesicle formation and docking to the membrane, such as SNAP alpha. ConclusionsBiochemical and structural parameters did not show significant alterations in the first 2 weeks of storage, but then declined constantly from day 14 onwards. We highlighted several parallelisms between red blood cells stored for a long time and the red blood cells of patients with hereditary spherocytosis.Key words: red blood cell, storage, mass spectrometry, proteomics, metabolomics. Haematologica 2012;97(1):107-115. doi:10.3324/haematol.2011 Citation: D'Alessandro A, D'Amici GM, Vaglio S, and Zolla L. Time-course investigation of SAGM-stored leukocyte-filtered red blood cell concentrates: from metabolism to proteomics.

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supporting

confidence: 58%

Section: Alterations Of Red Blood Cell Membrane Shape and Vesiculatiomentioning

confidence: 99%

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Time-course investigation of SAGM-stored leukocyte-filtered red bood cell concentrates: from metabolism to proteomics

D’Alessandro¹,

D’Amici²,

Vaglio³

et al. 2011

Haematologica

179

205

View full text Add to dashboard Cite

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“…Estes resultados são corroborados pela literatura que constata que as hemácias, durante o período de estocagem, perdem a resistê ncia à hemólise em meios hipotônicos (RAVAL et al, 2013;ALMIZRAQ et al, 2013). Vários estudos vêm sendo realizados para estabelecer uma correlação entre o aumento da fragilidade osmó tica e o estresse oxidativo (SROUR, et al, 2000;RINALDUCCI et al, 2011;D'ALESSANDRO et al, 2012;GRAZZINI e VAGLIO, 2012). No entanto, o estresse oxidativo relacionado às proteínas, e não aos lipídeos, tem sido apontado como o fator mais crítico para o comportamento reológico, incluindo a fragilidade osmótica e a elasticidade (SROUR, et al, 2000;KRIEBARDIS et al, 2007;HALE et al, 2011, SILVA et al 2017.…”

Section: Fragilidade Osmóticaunclassified

Estudo Da Fragilidade Osmótica E Fosfolípideos Totais Em Concentrados De Hemácias Com Nanoemulsões De Vitamina E

Souza¹,

Silva²,

Filho³

et al. 2018

Blucher Biophysics Proceedings

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“…RBCs undergo a series of biochemical and biomechanical changes, collectively known as the ‘hypothermic storage lesion' (HSL) [9]. Characteristics of the HSL includes RBC membrane remodeling, decreased metabolites such as ATP and 2,3-DPG, loss of intracellular potassium, oxidative injury of protein structures and lipid peroxidation, membrane loss, vesiculation, and ultimately hemolysis [10,11,12]. There are increasing concerns regarding the effect of the HSL on hemorheology, including RBC aggregability, deformability and membrane remodeling, effects that could potentially lead to impairment of the oxygen delivery capacity of transfused blood [13,14,15].…”

Section: Introductionmentioning

confidence: 99%

Differences in Rat and Human Erythrocytes Following Blood Component Manufacturing: The Effect of Additive Solutions

SilveiraCavalcante¹,

Acker²,

Holovati³

2015

Transfus Med Hemother

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Background: Small animal models have been previously used in transfusion medicine studies to evaluate the safety of blood transfusion products. Although there are multiple studies on the effects of blood banking practices on human red blood cells (RBCs), little is known about the effect of blood component manufacturing on the quality of rat RBCs. Methods: Blood from Sprague-Dawley rats and human volunteers (n = 6) was collected in CPD anticoagulant, resuspended in SAGM or AS3, and leukoreduced. In vitro quality was analyzed, including deformability, aggregation, microvesiculation, phosphatidylserine (PS) expression, percent hemolysis, ATP, 2,3-DPG, osmotic fragility, and potassium concentrations. Results: Compared to human RBCs, rat RBCs had decreased deformability, membrane rigidity, aggregability, and microvesiculation after component manufacturing process. Rat RBCs in SAGM showed higher hemolysis compared to human RBCs in SAGM (rat 4.70 ± 0.83% vs. human 0.34 ± 0.07%; p = 0.002). Rat RBCs in AS3 had greater deformability and rigidity than in SAGM. The number of microparticles/µl and the percentage PS expression were lower in rat RBCs in AS3 than in rat RBCs in SAGM. Hemolysis was also significantly lower in AS3 compared to SAGM (2.21 ± 0.68% vs. 0.87 ± 0.39%; p = 0.028). Conclusion: Rat RBCs significantly differ from human RBCs in metabolic and membrane-related aspects. SAGM, which is commonly used for human RBC banking, causes high hemolysis and is not compatible with rat RBCs.

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Peroxiredoxin‐2 as a candidate biomarker to test oxidative stress levels of stored red blood cells under blood bank conditions

Abstract: The detailed analysis of these protein associations to the membrane of aged RBCs allowed Prx2 to be suggested as a potential RBC oxidative stress marker for the sake of developing new approaches in quality assurance of blood components.

Cited by 88 publications

References 57 publications

Time-course investigation of SAGM-stored leukocyte-filtered red bood cell concentrates: from metabolism to proteomics

Time-course investigation of SAGM-stored leukocyte-filtered red bood cell concentrates: from metabolism to proteomics

Estudo Da Fragilidade Osmótica E Fosfolípideos Totais Em Concentrados De Hemácias Com Nanoemulsões De Vitamina E

Differences in Rat and Human Erythrocytes Following Blood Component Manufacturing: The Effect of Additive Solutions

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