Deficient Activity of DPNH-dependent Methemoglobin Diaphorase in Cord Blood Erythrocytes

Ross, Jean D.; Bevan-Pritchard, Stephen

doi:10.1182/blood.v21.1.51.51

Cited by 99 publications

(13 citation statements)

References 26 publications

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“…However, the activity was noticeably lower in the foetal blood and somewhat less in infants, than in the 1Cyear-old and adult samples. These findings are broadly consistent with the assay data given by McDonald (1961)' Ross (1963), Bartos (1966) and Williams (1973) in studies on the diaphorase activity in newborn and adult haemolysates.…”

Section: Spectrophotometrysupporting

confidence: 91%

An interpretation of human diaphorase isozymes in terms of three gene loci DIA₁, DIA₂ and DIA₃

Fisher¹,

Edwards²,

Putt³

et al. 1977

Annals of Human Genetics

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NADH and NADPH diaphorase isozymes have been studied in human tissues. Evidence from rare heterozygotes suggests that the red cell and main tissue forms of NADH diaphorase are products of the same locus DIA1. NADPH-dependent diaphorase appears to be the product of a second locus DIA2. A third locus, DIA3, codes for the polymorphic sperm diaphorase. The products of this locus are also found in foetal tissues including placenta and adult brain and gonads. The products of these three loci may be distinguished by their substrate specificity, thermostability and molecular size.

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Section: Spectrophotometrysupporting

confidence: 91%

An interpretation of human diaphorase isozymes in terms of three gene loci DIA₁, DIA₂ and DIA₃

Fisher¹,

Edwards²,

Putt³

et al. 1977

Annals of Human Genetics

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“…The enzyme exists in two forms, one fraction being tightly bound to the inner face of the red blood cell membrane and a second fraction dissolved in the cytosol (8). Earlier work has examined the difference in methemoglobin reductase activity among species and at different ages (1,26,27,36,43). Typically, these earlier investigators have used alternative substrates such as NADH-ferricyanide and diluted hemolysates in their analyses and have not sought to measure functional activity at body temperature.…”

Section: Discussionmentioning

confidence: 99%

A novel method of measuring reduction of nitrite-induced methemoglobin applied to fetal and adult blood of humans and sheep

Power¹,

Bragg²,

Oshiro³

et al. 2007

Journal of Applied Physiology

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The reaction of nitrite with deoxyhemoglobin results in the production of nitric oxide and methemoglobin, a reaction recently proposed as an important oxygen-sensitive source of vasoactive nitric oxide during hypoxic and anoxic stress, with several animal studies suggesting that nitrite may have therapeutic potential. Accumulation of toxic levels of methemoglobin is suppressed by reductase enzymes present within the erythrocyte. Using a novel method of measuring methemoglobin reductase activity in intact erythrocytes, we compared fetal and adult sheep and human blood. After nitrite-induced production of 20% methemoglobin, the blood was equilibrated with carbon monoxide, which effectively stopped further production. Methemoglobin disappearance was first order in nature with specific rate constants (k x 1,000) of 12.9 +/- 1.3 min(-1) for fetal sheep, 5.88 +/- 0.26 min(-1) for adult sheep, 4.27 +/- 0.34 for adult humans, and 3.30 +/- 0.15 for newborn cord blood, all statistically different from one another. The effects of oxygen tensions, pH, hemolysis, and methylene blue are reported. Studies of temperature dependence indicated an activation energy of 8,620 +/- 1,060 calories/mol (2.06 kJ/mol), appreciably higher than would be characteristic of processes limited by passive membrane diffusion. In conclusion, the novel methodology permits absolute quantification of the reduction of nitrite-induced methemoglobin in whole blood.

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“…Haemoglobin F is more rapidly oxidized than adult haemoglobin A, and it thereby generates greater amounts of free oxygen radicals (15,16). Moreover, the capacity for reduction of methaemoglobin is lower in the neonate (17,18). In experiments with hydrogen peroxide, the intracellular antioxidant defence system of the erythrocyte is usually altered by use of glucose-free media or enzyme inhibitors, or both (19).…”

Section: Discussionmentioning

confidence: 99%

Haemolysis in adult and neonatal erythrocytes caused by autoxidation of lipid emulsion (Intralipid)

Kljuchnikov

Pitkänen

et al. 1993

Acta Paediatrica

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Lipid emulsion (Intralipid) causes free radical-mediated damage to human cells in vitro. Incubation with 0.44% Intralipid for 17 h caused 40.3 +/- 3.8% haemolysis in adult human erythrocytes and 26.5 +/- 8.1% in erythrocytes from term newborns (p = 0.0001). In adult erythrocytes mean corpuscular volume increased 68.7 +/- 8.2% and in newborn erythrocytes 54.8 +/- 10.4% (p = 0.0012). Initial concentrations of reduced glutathione in adult and newborn erythrocytes were 65.1 +/- 2.5 and 62.1 +/- 4.0 mg/dl, respectively (ns); after incubation, glutathione concentrations were 21.0 +/- 4.0 and in 25.7 +/- 5.2 mg/dl in adult and newborn erythrocytes, respectively (p = 0.0004). After incubation the concentrations of thiobarbituric acid reactive material and conjugated dienes in newborn erythrocytes (2.8 +/- 0.2 microM and 0.223 +/- 0.019 OD 233, respectively) were higher than those of adult erythrocytes (2.1 +/- 0.4 microM and 0.138 +/- 0.012 OD 233) (p = 0.0001). In both adult and newborn erythrocytes, the effects of Intralipid were significantly inhibited by 0.6 mM deferroxamine or 8 mM sodium etidronate. Despite higher susceptibility to lipid peroxidation of the cell membrane, newborn erythrocytes are more resistant than adult erythrocytes to free radical-mediated effects such as depletion of intracellular glutathione, cell swelling and haemolysis.

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Deficient Activity of DPNH-dependent Methemoglobin Diaphorase in Cord Blood Erythrocytes

Cited by 99 publications

References 26 publications

An interpretation of human diaphorase isozymes in terms of three gene loci DIA₁, DIA₂ and DIA₃

An interpretation of human diaphorase isozymes in terms of three gene loci DIA₁, DIA₂ and DIA₃

A novel method of measuring reduction of nitrite-induced methemoglobin applied to fetal and adult blood of humans and sheep

Haemolysis in adult and neonatal erythrocytes caused by autoxidation of lipid emulsion (Intralipid)

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Deficient Activity of DPNH-dependent Methemoglobin Diaphorase in Cord Blood Erythrocytes

Cited by 99 publications

References 26 publications

An interpretation of human diaphorase isozymes in terms of three gene loci DIA1, DIA2 and DIA3

An interpretation of human diaphorase isozymes in terms of three gene loci DIA1, DIA2 and DIA3

A novel method of measuring reduction of nitrite-induced methemoglobin applied to fetal and adult blood of humans and sheep

Haemolysis in adult and neonatal erythrocytes caused by autoxidation of lipid emulsion (Intralipid)

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An interpretation of human diaphorase isozymes in terms of three gene loci DIA₁, DIA₂ and DIA₃

An interpretation of human diaphorase isozymes in terms of three gene loci DIA₁, DIA₂ and DIA₃