Human Red Cell Metabolism and in Vivo Oxygen Affinity of Red Cells during 24 Hours' Exposure to Simulated High Altitude (4500 m)

1973 ◽  
Vol 31 (4) ◽  
pp. 447-452 ◽  
Author(s):  
M. Rörth ◽  
S. F. Nygaard ◽  
H. H. Parving ◽  
V. Hansen ◽  
T. Kalsig
1972 ◽  
Vol 29 (3) ◽  
pp. 321-327 ◽  
Author(s):  
M. Rörth ◽  
Susan F. Nygaard ◽  
H. H. Parving ◽  
V. Hansen ◽  
T. Kalsig

Blood ◽  
1987 ◽  
Vol 70 (5) ◽  
pp. 1389-1393
Author(s):  
E Beutler ◽  
L Forman ◽  
C West

The addition of oxalate to blood stored in Citrate-phosphate-dextrose (CPD) produces a marked improvement in 2,3-diphosphoglycerate (2,3-DPG) preservation; an increase in 2,3-DPG levels can also be documented in short-term incubation studies. Oxalate is a potent in vitro inhibitor of red cell lactate dehydrogenase, monophosphoglycerate mutase, and pyruvate kinase (PK). In the presence of fructose 1,6-diphosphate the latter inhibitory effect is competitive with phospho(enol)pyruvate (PEP). Determination of the levels of intermediate compounds in red cells incubated with oxalate suggest the presence of inhibition at the PK step, indicating that this is the site of oxalate action. Apparent inhibition at the glyceraldehyde phosphate dehydrogenase step is apparently due to an increase in the NADH/NAD ratio. Oxalate had no effect on the in vivo viability of rabbit red cells stored in CPD preservatives for 21 days. Greater understanding of the toxicity of oxalate is required before it can be considered suitable as a component of preservative media, but appreciation of the mechanism by which it affects 2,3-DPG levels may be important in design of other blood additives. Malonate, the 3-carbon dicarboxylic acid analogue of oxalate late did not inhibit pyruvate kinase nor affect 2,3-DPG levels.


Blood ◽  
1987 ◽  
Vol 70 (5) ◽  
pp. 1389-1393 ◽  
Author(s):  
E Beutler ◽  
L Forman ◽  
C West

Abstract The addition of oxalate to blood stored in Citrate-phosphate-dextrose (CPD) produces a marked improvement in 2,3-diphosphoglycerate (2,3-DPG) preservation; an increase in 2,3-DPG levels can also be documented in short-term incubation studies. Oxalate is a potent in vitro inhibitor of red cell lactate dehydrogenase, monophosphoglycerate mutase, and pyruvate kinase (PK). In the presence of fructose 1,6-diphosphate the latter inhibitory effect is competitive with phospho(enol)pyruvate (PEP). Determination of the levels of intermediate compounds in red cells incubated with oxalate suggest the presence of inhibition at the PK step, indicating that this is the site of oxalate action. Apparent inhibition at the glyceraldehyde phosphate dehydrogenase step is apparently due to an increase in the NADH/NAD ratio. Oxalate had no effect on the in vivo viability of rabbit red cells stored in CPD preservatives for 21 days. Greater understanding of the toxicity of oxalate is required before it can be considered suitable as a component of preservative media, but appreciation of the mechanism by which it affects 2,3-DPG levels may be important in design of other blood additives. Malonate, the 3-carbon dicarboxylic acid analogue of oxalate late did not inhibit pyruvate kinase nor affect 2,3-DPG levels.


1990 ◽  
Vol 152 (1) ◽  
pp. 149-166 ◽  
Author(s):  
FRANK B. JENSEN

Red cell function was studied in carp by a combination of in vivo and in vitro experiments with nitrite as the perturbing agent. In vivo accumulation of nitrite caused a marked increase in the red cell methaemoglobin content, and reduced the mean cellular volume. The oxygen affinity of unoxidized haemoglobin was strongly decreased, partly as result of the elevated concentration of cellular nucleoside triphosphates and haemoglobin associated with red cell shrinkage. Red cell pH was unchanged compared to controls, but reduced when referred to constant extracellular pH and O2 saturation. The mean cellular K+ content decreased, reflecting a K+ loss from the red cells during their shrinkage. This K+ loss contributed significantly to the large plasma hyperkalaemia during nitrite exposure. In vitro experiments revealed that nitrite influx into deoxygenated red cells was much larger than into oxygenated red cells. Nitrite permeation of the red cell membrane was not inhibited by DIDS and did not change extracellular pH. Methaemoglobin (MetHb) formation was more pronounced in deoxygenated blood than in oxygenated blood, but quasi-steady states were reached, reflecting a balance between nitrite-induced MetHb formation and the action of MetHb reductase. Red cells incubated in the oxygenated state released K+, whereas a net K+ uptake occurred in deoxygenated cells. Nitrite did not change the K+ loss from oxygenated cells, but shifted the K+ uptake in deoxygenated cells to a pronounced K+ release by the time high MetHb levels were reached. Both types of red cell K+ release were inhibited by DIDS and appeared to occur via a route involving Band 3. The data are consistent with the hypothesis that a significant DIDS-sensitive K+ efflux from the red cells occurs whenever a large fraction of the haemoglobin molecules assumes an R-like quaternary structure.


PEDIATRICS ◽  
1965 ◽  
Vol 36 (1) ◽  
pp. 104-112
Author(s):  
Frank A. Oski ◽  
J. Lawrence Naiman

The erythrocytes of premature infants, term infants, and adults were studied with respect to ATP levels, ATP stability, glucose consumption, glutathione stability, and the tendency to develop morphologic abnormalities during short periods of incubation. The erythrocytes of both the premature and term infants had higher ATP levels and glucose consumption, greater ATP and glutathione instability, and more marked morphologic abnormalities than the adult red cells. The erythrocytes of the premature infants showed the greatest degrees of abnormality. It is suggested that the premature infant at birth possesses a metabolic profile in his erythrocytes which results in ATP instability.


Blood ◽  
1986 ◽  
Vol 67 (5) ◽  
pp. 1210-1214 ◽  
Author(s):  
NA Noble ◽  
G Rothstein

Abstract The genetic locus designated Dpg has two alleles in outbred Long-Evans rats. Genotype at this locus affects quantities of red cell 2,3- diphosphoglycerate (DPG) and adenosine triphosphate, as well as activities of two important glycolytic enzymes: phosphofructokinase and pyruvate kinase. Intravascular red cell survival is shortened in low- DPG animals. In order to get closer to the specific action of this locus, we addressed the question of whether the Dpg gene acts through intracorpuscular or extracorpuscular factors. Bone marrow transplantation after total body irradiation and 51Cr red cell survival after cross transfusion were the methods used. Because the animals that were used differed in hemoglobin phenotype, donor and recipient cells could be quantified in cross-transplanted animals. Phenotypic markers of Dpg genotype were measured in animals 40 to 50 days after transplantation. Values for these markers correlated highly with the percentage of donor and recipient cells present. In vivo survival of low-DPG red cells was significantly shorter than that of high-DPG cells (P less than .05), regardless of the genotype of the recipient. From the present studies, we conclude that the action of the Dpg gene is exerted by an intracorpuscular factor.


Author(s):  
Melissa Heidy Wongsari ◽  
Rachmawati Muhiddin ◽  
Mansyur Arif

The main source of energy for red cell metabolism is glucose via glycolytic pathway. Red cells metabolism slows down during storage at 2–6OC. Biochemical changes during storage are called storage lesions, i.e. decreased pH, glucose, and ATP, lactic acid accumulation, and loss of red cells function. Samples taken from the tip of PRC bags in CPDA-1 of the same code are divided into four sections, and stored in the blood bank refrigerator at 2–6OC. Glucose level is measured using ABX Pentra 400 (Horiba, Japan) on storage day 3 as a control, day 7, day 14, and day 21. Glucose levels during storage decreased significantly between day 3, and day 7 (p < 0.001), between day 7, and day 14 (p < 0.001), and between day 14, and 21 (p < 0.001). Glucose levels of Packed Red Cells (PRC) decrease during storage. Glycolysis occurs during storage although metabolism slows down.


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