Red blood cell hemolysis during processing

Sowemimo-Coker, Samuel

doi:10.1053/tmrv.2002.29404

Cited by 313 publications

(327 citation statements)

References 89 publications

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“…Potassium levels increased by 376% (P Ͻ 0.001) and exceeded the maximum level of instrument detection (20 mmol/liter) beyond 3 weeks of RBC storage. Free Hb in the storage medium (indicating RBC hemolysis) increased throughout the 6 weeks but remained below allowable levels, as in previous reports (23,24). Consistent with previous studies of leukodepleted blood, RBC adhesion to endothelial cells (data not shown) and RBC exposure of phosphatidyl serine (Fig.…”

Section: Resultssupporting

confidence: 80%

Evolution of adverse changes in stored RBCs

Bennett‐Guerrero¹,

Veldman²,

Doctor

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

543

556

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Recent studies have underscored questions about the balance of risk and benefit of RBC transfusion. A better understanding of the nature and timing of molecular and functional changes in stored RBCs may provide strategies to improve the balance of benefit and risk of RBC transfusion. We analyzed changes occurring during RBC storage focusing on RBC deformability, RBC-dependent vasoregulatory function, and S-nitrosohemoglobin (SNO-Hb), through which hemoglobin (Hb) O2 desaturation is coupled to regional increases in blood flow in vivo (hypoxic vasodilation). Five hundred ml of blood from each of 15 healthy volunteers was processed into leukofiltered, additive solution 3-exposed RBCs and stored at 1-6°C according to AABB standards. Blood was subjected to 26 assays at 0, 3, 8, 24 and 96 h, and at 1, 2, 3, 4, and 6 weeks. RBC SNO-Hb decreased rapidly (1.2 ؋ 10 ؊4 at 3 h vs. 6.5 ؋ 10 ؊4 (fresh) mol S-nitrosothiol (SNO)/mol Hb tetramer (P ‫؍‬ 0.032, mercuric-displaced photolysis-chemiluminescence assay), and remained low over the 42-day period. The decline was corroborated by using the carbon monoxide-saturated copper-cysteine assay [3.0 ؋ 10 ؊5 at 3 h vs. 9.0 ؋ 10 ؊5 (fresh) mol SNO/mol Hb]. In parallel, vasodilation by stored RBCs was significantly depressed. RBC deformability assayed at a physiological shear stress decreased gradually over the 42-day period (P < 0.001). Time courses vary for several storage-induced defects that might account for recent observations linking blood transfusion with adverse outcomes. Of clinical concern is that SNO levels, and their physiological correlate, RBC-dependent vasodilation, become depressed soon after collection, suggesting that even ''fresh'' blood may have developed adverse biological characteristics.adenosine triphosphate ͉ hemoglobin ͉ nitric oxide ͉ S-nitrosothiols ͉ transfusion

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Section: Resultssupporting

confidence: 80%

Evolution of adverse changes in stored RBCs

Bennett‐Guerrero¹,

Veldman²,

Doctor

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

543

556

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“…It has been postulated that washing removes debris, nonviable cells and unspecified metabolic breakdown products, thereby reducing possible sources of toxicity by removing supernatant hemoglobin, leukocytes and plasma. [9][10][11] Also, when older units of blood are used in massive transfusions, saline washing has been employed in an effort to reduce the risk of hyperkalemia. This latter rationale has been challenged, particularly when applied to less-than-massive volumes of blood transfused, because when small volumes are transfused, the major consideration for the patient is the total amount of K þ transfused and the transfusion rate.…”

Section: Discussionmentioning

confidence: 99%

Increased hemolysis from saline pre-washing RBCs or centrifugal pumps in neonatal ECMO

et al. 2007

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Objectives: Hemolysis is a significant complication of extracorporeal membrane oxygenation (ECMO), with a reported incidence of 12.2%. The aims of this study were (1) to investigate hemolysis caused by saline-washed versus unwashed RBCs, (2) to determine in vitro the effects of saline washing on erythrocyte hemolytic markers and (3) to investigate hemolysis by centrifugal versus roller pumps.Study design: (1) To evaluate the effect of pre-transfusion saline-washing versus non-washing, the peak plasma-free hemoglobin (FHb) and total bilirubin in the first 3 days versus the next 4 days of ECMO were compared (2) Pre-and postsaline-washed RBCs were analyzed for K þ , hemoglobin, mean corpuscular volume, FHb and hemolysis at baseline and after 4 h of storage at 41C. (3) Over 10 000 neonatal ECMO cases were retrospectively reviewed to study the effect of pump type on hemolysis.Results: (1) The washed blood group had significantly more hemolysis within the first 3 days of ECMO. (2) Immediately after saline washing, the K þ and Hb concentrations were significantly decreased compared with unwashed blood, and these differences were maintained after 4 h. The osmotic fragility of washed RBCs after 4 h of storage at 41C was significantly higher than at baseline. (3) Hemolysis was reported more often in the centrifugal than in the roller pump group.Conclusions: (1) Using unwashed RBCs decreased hemolysis within the first 3 days of ECMO. (2) Saline washing, while decreasing the concentration of K þ in the plasma, significantly increases RBC membrane osmotic fragility. (3) Hemolysis is linked to the use of centrifugal pumps.

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“…We compared two plasma samples, one with low hemolysis (0.021 g/L hemoglobin (Hgb) and the other high hemolysis (0.182 g/L Hgb). Hemolysis is produced by the lysis of red blood cells and the subsequent release of Hgb resulting in reddish blood plasma (16). Hemolysis can occur in vivo because of disease processes, such as hemolytic anemia (16,36), as well as in vitro because of sample collection or handling errors (15,16).…”

Section: Differential Analysis Of a Synaptic Density Fraction From Homentioning

confidence: 99%

“…Hemolysis is produced by the lysis of red blood cells and the subsequent release of Hgb resulting in reddish blood plasma (16). Hemolysis can occur in vivo because of disease processes, such as hemolytic anemia (16,36), as well as in vitro because of sample collection or handling errors (15,16). Triplicate injections of each sample yielded a total of 3771 peptide identifications (2918 Ϯ 73; CV ϭ 2.51%, across technical replicate injections) with 3088 of these candidates being co-identified between sample sets.…”

Section: Differential Analysis Of a Synaptic Density Fraction From Homentioning

confidence: 99%

Maximizing Peptide Identification Events in Proteomic Workflows Using Data-Dependent Acquisition (DDA)

Bateman

Goulding

Shulman

et al. 2014

Molecular & Cellular Proteomics

101

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Current analytical strategies for collecting proteomic data using data-dependent acquisition (DDA) are limited by the low analytical reproducibility of the method. Proteomic discovery efforts that exploit the benefits of DDA, such as providing peptide sequence information, but that enable improved analytical reproducibility, represent an ideal scenario for maximizing measureable peptide identifications in "shotgun"-type proteomic studies. Therefore, we propose an analytical workflow combining DDA with retention time aligned extracted ion chromatogram (XIC) areas obtained from high mass accuracy MS1 data acquired in parallel. We applied this workflow to the analyses of sample matrixes prepared from mouse blood plasma and brain tissues and observed increases in peptide detection of up to 30.5% due to the comparison of peptide MS1 XIC areas following retention time alignment of co-identified peptides. Furthermore, we show that the approach is quantitative using peptide standards diluted into a complex matrix. These data revealed that peptide MS1 XIC areas provide linear response of over three orders of magnitude down to low femtomole (fmol) levels. These findings argue that augmenting "shotgun" proteomic workflows with retention time alignment of peptide identifications and comparative analyses of corresponding peptide MS1 XIC areas improve the analytical performance of global proteomic discovery methods using DDA. Molecular & Cellular Proteomics 13: 10.1074/ mcp.M112.026500, 329-338, 2014.Label-free methods in mass spectrometry-based proteomics, such as those used in common "shotgun" proteomic studies, provide peptide sequence information as well as relative measurements of peptide abundance (1-3). A common data acquisition strategy is based on data-dependent acquisition (DDA) 1 where the most abundant precursor ions are selected for tandem mass spectrometry (MS/MS) analysis (1-2). DDA attempts to minimize redundant peptide precursor selection and maximize the depth of proteome coverage (2). However, the analytical reproducibility of peptide identifications obtained using DDA-based methods result in Ͻ75% overlap between technical replicates (3-4). Comparisons of peptide identifications between replicate analyses have shown that the rate of new peptide identifications increases sharply following two replicate sample injections and gradually tapers off after approximately five replicate injections (4). This phenomenon is due, in part, to the semirandom sampling of peptides in a DDA experiment (5).Alternate label-free methods focused on measuring the abundance of intact peptide ions, such as the accurate mass and time tag (AMT) approach (6 -8, 42), are aimed at differential analyses of extracted ion chromatogram (XIC) areas integrated from high mass accuracy peptide precursor mass spectra (MS1 spectra) exhibiting discrete chromatographic elution times. This method is particularly powerful for the analysis of post-translationally modified (PTM) peptides as pairing the low abundance of PTM candidates with the variabl...

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Red blood cell hemolysis during processing

Cited by 313 publications

References 89 publications

Evolution of adverse changes in stored RBCs

Evolution of adverse changes in stored RBCs

Increased hemolysis from saline pre-washing RBCs or centrifugal pumps in neonatal ECMO

Maximizing Peptide Identification Events in Proteomic Workflows Using Data-Dependent Acquisition (DDA)

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