Risk of red cell exposure to the water anomaly upon blood unit cold-storage

Blood transfusion, is not only transferring the blood cells to the recipient, but also transferring other components such as: glucose,lactate, and potassium. When the blood is stored, many alterations occur in its cmponents, particularly a decrease of adenosine5-triphosphate (ATP) and pH, hemolysis, and an increase of potassium levels as well. One of the transfusion complications that should beavoided is hyperkalemia due to the accumulation of potassium that leaks during the storage. However, hyperkalemia related to transfusiondepends not only on the potassium level in the blood unit, but also on its volume and the rate of its blood administration as well. Theaim of this study was to know the potassium levels in stored Packed Red Cell (PRC). A cohort study was done from May–July 2010. Theresearchers used 48 samples from 16 PRCs derived from 16 donors. The samples were drawn from the of PRC hose’s plasma that had beensealed. The potassium levels were measured on the first day, 10th day, and 20th day of the blood collection. The mean potassium levelon the first day was 3.79 mmol/L, 10th day was 12.22 mmol/L and 20th day was 19.77 mmol/L. Comparison of the potassium levelsbetween the first and 10th day, between first and 20th day, and between 10th and 20th day showed a significant difference (p=0.00). Theincrease of potassium levels in the PRC coincide with the storagetime.

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Serial Assessment of Biochemical Parameters of Red Cell in the Blood Unit Segments Kept At 4

Haematology International Journal ◽

10.23880/hij-16000149 ◽

2019 ◽

Vol 3 (3) ◽

Author(s):

Deva Japa Ajith

Keyword(s):

Biochemical Parameters ◽

Red Cell ◽

Blood Unit

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Increased calcium permeability of cold-stored erythrocytes

Blood ◽

10.1182/blood.v60.1.92.92 ◽

1982 ◽

Vol 60 (1) ◽

pp. 92-98 ◽

Cited By ~ 27

Author(s):

JS Wiley ◽

KE McCulloch ◽

DS Bowden

Keyword(s):

Cold Storage ◽

Calcium Content ◽

Ionized Calcium ◽

Red Cell ◽

Total Calcium ◽

Atp Concentration ◽

Significant Change ◽

Calcium Permeability ◽

Passive Influx ◽

In Cells

Abstract The calcium, sodium, and magnesium permeability of erythrocytes from blood stored at 4 degrees C in various anticoagulant media has been studied and compared to that of fresh erythrocytes. Passive influx of CA2+ was measured at 37 degrees C in cells pretreated to abolish Ca2+ pumping and was up to fivefold greater for cold-stored erythrocytes than for fresh cells. The Ca2+ leakiness developed gradually after day 2 and reached a maximum by day 7 of cold storage in ACD, CPD, CPD- adenine, or heparin anticoagulants. The total calcium content of cold- stored erythrocytes in ACD was not significantly different from that of fresh erythrocytes. However, when cold-stored erythrocytes were reincubated at 37 degrees C in media containing 1.5 mM ionized calcium and substrates to regenerate ATP, a net gain of Ca2+ occurred that was greater for stored than for fresh erythrocytes. Cold storage of blood for up to 6 wk in any anticoagulant did not alter either sodium or magnesium permeability. Red cell ATP was also measured and fell steadily during cold storage in ACD or CPD, but more increase in Ca2+ permeability preceded any significant change in red cell ATP, it is likely that a selective calcium leak develops independently of the fall in ATP concentration that occurs on cold storage.

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Increased calcium permeability of cold-stored erythrocytes

Blood ◽

10.1182/blood.v60.1.92.bloodjournal60192 ◽

1982 ◽

Vol 60 (1) ◽

pp. 92-98 ◽

Cited By ~ 1

Author(s):

JS Wiley ◽

KE McCulloch ◽

DS Bowden

Keyword(s):

Cold Storage ◽

Calcium Content ◽

Ionized Calcium ◽

Red Cell ◽

Total Calcium ◽

Atp Concentration ◽

Significant Change ◽

Calcium Permeability ◽

Passive Influx ◽

In Cells

The calcium, sodium, and magnesium permeability of erythrocytes from blood stored at 4 degrees C in various anticoagulant media has been studied and compared to that of fresh erythrocytes. Passive influx of CA2+ was measured at 37 degrees C in cells pretreated to abolish Ca2+ pumping and was up to fivefold greater for cold-stored erythrocytes than for fresh cells. The Ca2+ leakiness developed gradually after day 2 and reached a maximum by day 7 of cold storage in ACD, CPD, CPD- adenine, or heparin anticoagulants. The total calcium content of cold- stored erythrocytes in ACD was not significantly different from that of fresh erythrocytes. However, when cold-stored erythrocytes were reincubated at 37 degrees C in media containing 1.5 mM ionized calcium and substrates to regenerate ATP, a net gain of Ca2+ occurred that was greater for stored than for fresh erythrocytes. Cold storage of blood for up to 6 wk in any anticoagulant did not alter either sodium or magnesium permeability. Red cell ATP was also measured and fell steadily during cold storage in ACD or CPD, but more increase in Ca2+ permeability preceded any significant change in red cell ATP, it is likely that a selective calcium leak develops independently of the fall in ATP concentration that occurs on cold storage.

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The orientation of sickle hemoglobin fibers within fascicles

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100104066 ◽

1988 ◽

Vol 46 ◽

pp. 400-401

Author(s):

Christopher A. Miller ◽

Bridget Carragher ◽

William A. McDade ◽

Robert Josephs

Keyword(s):

Sickle Cell ◽

Sickle Cell Anemia ◽

Relative Orientation ◽

Unit Cell ◽

Red Cell ◽

High Ph ◽

Sickle Hemoglobin ◽

Polar Crystal ◽

Helical Configuration

Highly ordered bundles of deoxyhemoglobin S (HbS) fibers, termed fascicles, are intermediates in the high pH crystallization pathway of HbS. These fibers consist of 7 Wishner-Love double strands in a helical configuration. Since each double strand has a polarity, the odd number of double strands in the fiber imparts a net polarity to the structure. HbS crystals have a unit cell containing two double strands, one of each polarity, resulting in a net polarity of zero. Therefore a rearrangement of the double strands must occur to form a non-polar crystal from the polar fibers. To determine the role of fascicles as an intermediate in the crystallization pathway it is important to understand the relative orientation of fibers within fascicles. Furthermore, an understanding of fascicle structure may have implications for the design of potential sickling inhibitors, since it is bundles of fibers which cause the red cell distortion responsible for the vaso-occlusive complications characteristic of sickle cell anemia.

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Erythrophagocytosis in the Liver in Hemolytic Anemias

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100100664 ◽

1968 ◽

Vol 26 ◽

pp. 184-185

Author(s):

O. T. Minick ◽

E. Orfei ◽

F. Volini ◽

G. Kent

Keyword(s):

Acid Phosphatase ◽

Oxidative Damage ◽

Phosphatase Activity ◽

Kupffer Cells ◽

Acid Phosphatase Activity ◽

Common Type ◽

Red Cell ◽

Cell Fragments ◽

Reticulo Endothelial System ◽

Important Site

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).

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Structural integrity after cold storage of human epidermal model in hypothermosol: A correlative ultrastructural and fluorescent assay

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100169080 ◽

1994 ◽

Vol 52 ◽

pp. 270-271

Author(s):

Henry H. Eichelberger ◽

John G. Baust ◽

Robert G. Van Buskirk

Keyword(s):

Cold Storage ◽

Structural Integrity ◽

Culture Media ◽

Cell Structure ◽

Natural State ◽

Sodium Cacodylate ◽

Ruthenium Tetroxide ◽

Cacodylate Buffer ◽

Before And After

For research in cell differentiation and in vitro toxicology it is essential to provide a natural state of cell structure as a benchmark for interpreting results. Hypothermosol (Cryomedical Sciences, Rockville, MD) has proven useful in insuring the viability of synthetic human epidermis during cold-storage and in maintaining the epidermis’ ability to continue to differentiate following warming.Human epidermal equivalent, EpiDerm (MatTek Corporation, Ashland, MA) consisting of fully differentiated stratified human epidermal cells were grown on a microporous membrane. EpiDerm samples were fixed before and after cold-storage (4°C) for 5 days in Hypothermosol or skin culture media (MatTek Corporation) and allowed to recover for 7 days at 37°C. EpiDerm samples were fixed 1 hour in 2.5% glutaraldehyde in sodium cacodylate buffer (pH 7.2). A secondary fixation with 0.2% ruthenium tetroxide (Polysciences, Inc., Warrington, PA) in sodium cacodylate was carried out for 3 hours at 4°C. Other samples were similarly fixed, but with 1% Osmium tetroxide in place of ruthenium tetroxide. Samples were dehydrated through a graded acetone series, infiltrated with Spurrs resin (Polysciences Inc.) and polymerized at 70°C.

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