The effect of 2,3-DPG on red cell enzymes

1974 ◽  
Vol 30 (2) ◽  
pp. 190-192 ◽  
Author(s):  
E. Beutler ◽  
F. Matsumoto ◽  
E. Guinto
Keyword(s):  
Red Cell ◽  
Blood ◽  
1983 ◽  
Vol 62 (3) ◽  
pp. 602-605
Author(s):  
SF Travis

Red cell enzymes, 2,3-diphosphoglycerate (2,3-DPG) and adenosine triphosphate (ATP), were evaluated in a 23-mo-old boy with juvenile chronic myelocytic leukemia (JCML) at the onset of his illness and 6 mo later during the accelerated phase. The activities of the age-dependent red cell enzymes, hexokinase, aldolase, pyruvate kinase, and glucose-6- phosphate dehydrogenase, were elevated, as were the concentrations of red cell 2,3-DPG and ATP, consistent with a young red cell population metabolizing at an increased glycolytic rate. The activities of the non- age-dependent enzymes, glyceraldehyde-3-phosphate dehydrogenase (G3PD), phosphoglycerate kinase, and enolase, were also increased to levels similar to or greater than those observed in term infants. As the illness progressed, the activity of red cell G3PD increased further, and phosphoglucose isomerase activity increased markedly. These results are consistent with the prior suggestion that JCML represents a reversion to “fetal” erythropoiesis.


Blood ◽  
1983 ◽  
Vol 62 (3) ◽  
pp. 602-605 ◽  
Author(s):  
SF Travis

Abstract Red cell enzymes, 2,3-diphosphoglycerate (2,3-DPG) and adenosine triphosphate (ATP), were evaluated in a 23-mo-old boy with juvenile chronic myelocytic leukemia (JCML) at the onset of his illness and 6 mo later during the accelerated phase. The activities of the age-dependent red cell enzymes, hexokinase, aldolase, pyruvate kinase, and glucose-6- phosphate dehydrogenase, were elevated, as were the concentrations of red cell 2,3-DPG and ATP, consistent with a young red cell population metabolizing at an increased glycolytic rate. The activities of the non- age-dependent enzymes, glyceraldehyde-3-phosphate dehydrogenase (G3PD), phosphoglycerate kinase, and enolase, were also increased to levels similar to or greater than those observed in term infants. As the illness progressed, the activity of red cell G3PD increased further, and phosphoglucose isomerase activity increased markedly. These results are consistent with the prior suggestion that JCML represents a reversion to “fetal” erythropoiesis.


2019 ◽  
Vol 16 (9) ◽  
pp. 834-835
Author(s):  
Petter Järemo ◽  
Alenka Jejcic ◽  
Vesna Jelic ◽  
Tasmin Shahnaz ◽  
Homira Behbahani ◽  
...  

Background: Alzheimer’s Disease (AD) features the accumulation of β-amyloid in erythrocytes. The subsequent red cell damage may well affect their oxygen-carrying capabilities. 2,3- diphosphoglycerate (2,3-DPG) binds to the hemoglobin thereby promoting oxygen release. It is theorized that 2,3-DPG is reduced in AD and that the resulting hypoxia triggers erythropoietin (EPO) release. Methods & Objective: To explore this theory, we analyzed red cell 2,3-DPG content and EPO in AD, mild cognitive impairment, and the control group, subjective cognitive impairment. Results: We studied (i) 2,3-DPG in red cells, and (ii) circulating EPO in AD, and both markers were unaffected by dementia. Disturbances of these oxygen-regulatory pathways do not appear to participate in brain hypoxia in AD.


FEBS Letters ◽  
1973 ◽  
Vol 37 (1) ◽  
pp. 21-22 ◽  
Author(s):  
E. Beutler ◽  
E. Guinto
Keyword(s):  
Red Cell ◽  

1980 ◽  
Vol 93 (4) ◽  
pp. 424-429 ◽  
Author(s):  
J. L. Alvarez-Sala ◽  
M. A. Urbán ◽  
J. J. Sicilia ◽  
A. J. Diaz Fdez ◽  
F. Fdez Mendieta ◽  
...  

Abstract. In 21 hyperthyroid female patients studied on 29 occasions, high levels of red-cell 2,3-diphosphoglycerate (2,3-DPG) have been found (5.75 ± 0.7 mm) which, compared to a euthyroid control group (4.88 ± 0.4 mm), could not be accounted for by differences in haematocrit, haemoglobin or phosphataemia. A significant correlation was found (P < 0.05) between serum thyroid hormones and the 2,3-DPG concentration in the hyperthyroid patients. Eight of these patients were reexamined after treatment and normalization of thyroid function, showed a regression to normal 2,3-DPG values (4.81 ± 0.6 mm) which could not be attributed to variations in haematocrit, haemoglobin or phosphataemia either. We therefore deduce that the shift to the right in the haemoglobin oxygen dissociation curve observed in patients of this type may be due to an increase in the red-cell 2,3-DPG content.


1981 ◽  
Vol 56 (2) ◽  
pp. 139-145 ◽  
Author(s):  
Tatyana M. Karaphet ◽  
Rem I. Sukernik ◽  
Ludmila P. Osipova ◽  
Yuriy B. Simchenko

1982 ◽  
Vol 76 (2) ◽  
pp. 135-142 ◽  
Author(s):  
Syamal Roy ◽  
Shibnath Ghatak ◽  
D. K. Ghosh ◽  
M. M. Rakhit

1984 ◽  
Vol 56 (1) ◽  
pp. 109-116 ◽  
Author(s):  
R. M. Winslow ◽  
M. Samaja ◽  
J. B. West

As part of the American Medical Research Expedition to Everest in 1981, we measured hemoglobin concentration, red cell 2,3-diphosphoglycerate (2,3-DPG), Po2 at which hemoglobin is 50% saturated (P50), and acid-base status in expedition members at various altitudes. All measurements were made in expedition laboratories and, with the exception of samples from the South Col of Mt. Everest (8,050 m), within 2 h of blood collection. In vivo conditions were estimated from direct measurements of arterial blood gases and pH or inferred from base excess and alveolar PCO2. As expected, increased 2,3-DPG was associated with slightly increased P50, when expressed at pH 7.4. Because of respiratory alkalosis, however, the subjects' in vivo P50 at 6,300 m (27.6 Torr) was slightly less than at sea level (28.1 Torr). The estimated in vivo P50 was progressively lower at 8,050 m (24.9 Torr) and on the summit at 8,848 m (19.4 Torr in one subject). Our data suggest that, at extreme altitude, the blood O2 equilibrium curve shifts progressively leftward because of respiratory alkalosis. This left shift protects arterial O2 saturation at extreme altitude.


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.


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