Abstract
Extract: Glutathione (GSH) oxidation and hexose monophosphate (HMP) shunt activity were compared in cord and adult erythrocytes (RBC) stressed with hydrogen peroxide (H2O2). In the absence of glucose, GSH (micromoles per milliliter RBC) in cord erythrocytes decreased from 2.52 ± 0.20 (0 hr) to 1.37 ± 0.30 (2 hr) to 0.92 ± 0.22 (4 hr). Adult erythrocytes treated similarly manifested a GSH change from 2.23 ± 0.17 (0 hr) to 1.06 ± 0.24 (2 hr) to 0.59 ± 0.35 (4 hr). The activity of HMP shunt (micromoles CO2/ml RBC/hr) in cord erythrocytes increased from a control rate of 0.081 ± 0.015 to 0.203 ± 0.52 when stressed with hydrogen peroxide. Erythrocytes from adults had a resting rate of 0.062 ± 0.014 that increased to 0.212 ± 0.045 when incubated with H2O2. Sodium ascorbate also was used as a peroxide-generating agent, and resulted in qualitatively similar responses as H2O2 in both GSH oxidation and HMP shunt activity of neonatal and adult erythrocytes.
Speculation: The partial deficiency of GSH-peroxidase in erythrocytes from neonates probably is not functionally significant in the intact cell. More functional studies are necessary to ascertain which of the many differences between erythrocytes from neonates and adults may be related to the increased oxidant sensitivity of these cells. In addition, these data again point out that there is often a poor correlation between isolated enzyme assays and the manner in which an enzyme functions within the intact cell. In the case of hemolytic anemias associated with enzyme abnormalities, more functional cellular tests of specific enzymes would be useful in attempting to correlate altered enzyme activity with cell function and hemolysis.
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Glader, B., Conrad, M. Decreased Glutathione Peroxidase in Neonatal Erthyrocytes: Lack of Relation to Hydrogen Peroxide Metabolism. Pediatr Res 6, 900–904 (1972). https://doi.org/10.1203/00006450-197212000-00008
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DOI: https://doi.org/10.1203/00006450-197212000-00008
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