The role of intracellular zinc in H2O2-induced oxidative stress in human erythrocytes

详细

In vitro exposure of human erythrocytes to H₂O₂ at concentrations of 30–1000 μM resulted in a dose-dependent increase of the intracellular levels of Zn²⁺ and inhibition of the cytosolic esterase activity, which is a major marker of erythrocyte viability. The observed effect depended on the concentration of H₂O₂ and the duration of exposure of the cells to this compound. An inverse relationship between the changes in the intracellular level of labile zinc ions and esterase activity in the cells exposed to hydrogen peroxide was detected; this was indicative of the role of Zn²⁺ in the programmed death of red blood cells. The combined action of hydrogen peroxide and N',N'-tetrakis-(2-pyridyl-methyl)-ethylenediamine, an intracellular zinc ion chelator, has been found to eliminate the cytotoxic effect of H₂O₂, whereas the addition of Zn²⁺ to the erythrocyte incubation medium enhanced the effects of hydrogen peroxide. The reduction of the concentration of non-protein thiol groups due to a decrease of the level of reduced glutathione was shown to contribute to the release of Zn²⁺ from the intracellular binding sites during oxidative stress induced by H₂O₂ in human erythrocytes.