Glucose-6-phosphate dehydrogenase and oxidant sensitivity of erythrocytes of three species of wombats

1996 ◽  
Vol 6 (4) ◽  
pp. 225-231 ◽  
Author(s):  
N. S. Agar ◽  
C. A. Gay ◽  
C. Gallagher ◽  
V. R. Steele ◽  
P. Spencer
Keyword(s):  
Glucose 6 Phosphate Dehydrogenase ◽  
Oxidant Sensitivity

scholarly journals NADPH, not glutathione, status modulates oxidant sensitivity in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes

Blood ◽  
1991 ◽  
Vol 77 (9) ◽  
pp. 2059-2064 ◽  
Author(s):  
MD Scott ◽  
L Zuo ◽  
BH Lubin ◽  
DT Chiu
Keyword(s):  
G6pd Deficiency ◽  
Direct Consequence ◽  
Phenazine Methosulfate ◽  
Effect Analysis ◽  
Hemoglobin Oxidation ◽  
Glutathione Status ◽  
Intracellular Glutathione ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Oxidant Sensitivity ◽  
Generating System

Glucose-6-phosphate dehydrogenase (G6PD) deficiency is characterized by the loss of NADPH and enhanced erythrocyte oxidant sensitivity. Historically, it has been theorized that the elevated oxidant sensitivity of G6PD-deficient erythrocytes arises as the direct consequence of decreased intracellular glutathione (GSH) concentrations. To directly investigate the basis of G6PD deficiency oxidant sensitivity, the effects of altered GSH and NADPH concentrations were examined in normal and G6PD-deficient erythrocytes. The results of this study demonstrated that GSH depletion, by 1-chloro- 2,4-dinitrobenzene (CDNB), had no effect on hemoglobin oxidation in response to hydrogen peroxide (H2O2) generating systems (phenazine methosulfate and menadione bisulfite) in either normal or G6PD- deficient cells. Furthermore, a fourfold to sixfold increase in intracellular GSH concentration also did not protect against H2O2- generating systems in the normal or G6PD-deficient erythrocytes. Conversely, introduction of an NADPH-generating system (purified G6PD) into G6PD-deficient cells resulted in a significant decrease in oxidant sensitivity and an ability to cycle GSH. Further experiments demonstrated that the reduced oxidant sensitivity of the G6PD- reconstituted erythrocytes was not due to the maintenance of GSH levels because CDNB-mediated depletion of GSH did not alter this protective effect. Analysis of these results demonstrated a direct correlation between NADPH, but not GSH, concentration and hemoglobin oxidant sensitivity.

scholarly journals Inhibition of the pentose phosphate shunt by lead: a potential mechanism for hemolysis in lead poisoning

Blood ◽  
1984 ◽  
Vol 63 (3) ◽  
pp. 518-524 ◽  
Author(s):  
NA Lachant ◽  
A Tomoda ◽  
KR Tanaka
Keyword(s):  
Lead Poisoning ◽  
Lead Acetate ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Pentose Phosphate ◽  
Mechanism Of Inhibition ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Oxidant Sensitivity ◽  
Clinical Lead Poisoning ◽  
Pentose Phosphate Shunt

Abstract Recent investigations have disclosed a decrease in pentose phosphate shunt activity in hereditary pyrimidine 5′-nucleotidase deficiency. Clinical lead poisoning is associated with an acquired decrease in pyrimidine 5′-nucleotidase activity. The current investigations were undertaken (1) to determine if pentose shunt activity was decreased in erythrocytes exposed to lead, and (2) to compare the mechanism of inhibition to that seen in hereditary pyrimidine 5′-nucleotidase deficiency. Normal erythrocytes incubated with lead acetate in vitro demonstrated increased Heinz body formation, decreased reduced glutathione, a positive ascorbate cyanide test, and a reversible suppression of pentose shunt activity in the intact erythrocyte. Lead acetate added to normal red cell hemolysates markedly inhibited the activities of glucose-6-phosphate dehydrogenase (G6PD) and phosphofructokinase. The mean Kis of lead for glucose-6-phosphate and nicotinamide adenine dinucleotide phosphate (NADP) for G6PD were 1.5 microM and 2.1 microM, respectively, which is within the range of intraerythrocytic lead concentrations found in clinical lead poisoning. Magnesium enhanced the ability of lead to inhibit G6PD. Thus, the shortened erythrocyte survival in lead poisoning appears to be due, in part, to increased oxidant sensitivity secondary to inhibition of G6PD and the pentose shunt. The mechanism of shunt inhibition is, in part, similar to that seen in hereditary pyrimidine 5′-nucleotidase deficiency.

Inhibition of the pentose phosphate shunt by lead: a potential mechanism for hemolysis in lead poisoning

Blood ◽  
1984 ◽  
Vol 63 (3) ◽  
pp. 518-524
Author(s):  
NA Lachant ◽  
A Tomoda ◽  
KR Tanaka
Keyword(s):  
Lead Poisoning ◽  
Lead Acetate ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Pentose Phosphate ◽  
Mechanism Of Inhibition ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Oxidant Sensitivity ◽  
Clinical Lead Poisoning ◽  
Pentose Phosphate Shunt

Recent investigations have disclosed a decrease in pentose phosphate shunt activity in hereditary pyrimidine 5′-nucleotidase deficiency. Clinical lead poisoning is associated with an acquired decrease in pyrimidine 5′-nucleotidase activity. The current investigations were undertaken (1) to determine if pentose shunt activity was decreased in erythrocytes exposed to lead, and (2) to compare the mechanism of inhibition to that seen in hereditary pyrimidine 5′-nucleotidase deficiency. Normal erythrocytes incubated with lead acetate in vitro demonstrated increased Heinz body formation, decreased reduced glutathione, a positive ascorbate cyanide test, and a reversible suppression of pentose shunt activity in the intact erythrocyte. Lead acetate added to normal red cell hemolysates markedly inhibited the activities of glucose-6-phosphate dehydrogenase (G6PD) and phosphofructokinase. The mean Kis of lead for glucose-6-phosphate and nicotinamide adenine dinucleotide phosphate (NADP) for G6PD were 1.5 microM and 2.1 microM, respectively, which is within the range of intraerythrocytic lead concentrations found in clinical lead poisoning. Magnesium enhanced the ability of lead to inhibit G6PD. Thus, the shortened erythrocyte survival in lead poisoning appears to be due, in part, to increased oxidant sensitivity secondary to inhibition of G6PD and the pentose shunt. The mechanism of shunt inhibition is, in part, similar to that seen in hereditary pyrimidine 5′-nucleotidase deficiency.

scholarly journals NADPH, not glutathione, status modulates oxidant sensitivity in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes

Blood ◽  
1991 ◽  
Vol 77 (9) ◽  
pp. 2059-2064 ◽  
Author(s):  
MD Scott ◽  
L Zuo ◽  
BH Lubin ◽  
DT Chiu
Keyword(s):  
G6pd Deficiency ◽  
Direct Consequence ◽  
Phenazine Methosulfate ◽  
Effect Analysis ◽  
Hemoglobin Oxidation ◽  
Glutathione Status ◽  
Intracellular Glutathione ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Oxidant Sensitivity ◽  
Generating System

Abstract Glucose-6-phosphate dehydrogenase (G6PD) deficiency is characterized by the loss of NADPH and enhanced erythrocyte oxidant sensitivity. Historically, it has been theorized that the elevated oxidant sensitivity of G6PD-deficient erythrocytes arises as the direct consequence of decreased intracellular glutathione (GSH) concentrations. To directly investigate the basis of G6PD deficiency oxidant sensitivity, the effects of altered GSH and NADPH concentrations were examined in normal and G6PD-deficient erythrocytes. The results of this study demonstrated that GSH depletion, by 1-chloro- 2,4-dinitrobenzene (CDNB), had no effect on hemoglobin oxidation in response to hydrogen peroxide (H2O2) generating systems (phenazine methosulfate and menadione bisulfite) in either normal or G6PD- deficient cells. Furthermore, a fourfold to sixfold increase in intracellular GSH concentration also did not protect against H2O2- generating systems in the normal or G6PD-deficient erythrocytes. Conversely, introduction of an NADPH-generating system (purified G6PD) into G6PD-deficient cells resulted in a significant decrease in oxidant sensitivity and an ability to cycle GSH. Further experiments demonstrated that the reduced oxidant sensitivity of the G6PD- reconstituted erythrocytes was not due to the maintenance of GSH levels because CDNB-mediated depletion of GSH did not alter this protective effect. Analysis of these results demonstrated a direct correlation between NADPH, but not GSH, concentration and hemoglobin oxidant sensitivity.

EFFECTS OF DEHYDROEPIANDROSTERONE AND ITS CONJUGATES UPON HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE

1969 ◽  
Vol 61 (1_Suppl) ◽  
pp. S46
Author(s):  
Georg W. Oertel ◽  
Peter Menzel ◽  
Ilse Rebelein
Keyword(s):  
Glucose 6 Phosphate Dehydrogenase

ACUTE ENZYME HISTOCHEMICAL CHANGES IN THE ZONA GLOMERULOSA OF THE RAT ADRENAL CORTEX

1968 ◽  
Vol 59 (3) ◽  
pp. 508-518
Author(s):  
J. D. Elema ◽  
M. J. Hardonk ◽  
Joh, Koudstaal ◽  
A. Arends
Keyword(s):  
Peritoneal Dialysis ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Adrenal Cortex ◽  
Isocitrate Dehydrogenase ◽  
Hydroxysteroid Dehydrogenase ◽  
Zona Glomerulosa ◽  
Acute Changes ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Histochemical Changes

ABSTRACT Acute changes in glucose-6-phosphate dehydrogenase and isocitrate dehydrogenase activity in the zona glomerulosa of the rat adrenal cortex were induced by peritoneal dialysis with 5 % glucose. Although less clear, the activity of 3β-ol-hydroxysteroid dehydrogenase also seemed to increase as well. No changes were seen in the activity of succinate dehydrogenase. Dialysis with 0.9 % NaCl had no effect on any of the enzymes investigated. The possible significance of these observations is discussed.

Glucose-6-Phosphate Dehydrogenase Deficiency in an Old Woman

2020 ◽  
Vol 6 (3) ◽  
Author(s):  
Briantais Antoine ◽  
Froidefond Margaux ◽  
Seguier Julie ◽  
Swiader Laure ◽  
Durand Jean Marc
Keyword(s):  
Dehydrogenase Deficiency ◽  
Glucose 6 Phosphate Dehydrogenase
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