The role of intracellular zinc in H2O2-induced oxidative stress in human erythrocytes
| Autor: | A. V. Tamashevski, G. P. Zubritskaya, Yu. M. Harmaza, E. I. Slobozhanina, A. G. Kutko, Yu. S. Kanash |
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| Rok vydání: | 2016 |
| Předmět: |
inorganic chemicals
0301 basic medicine chemistry.chemical_classification 030103 biophysics Chemistry Biophysics Glutathione medicine.disease_cause Esterase 03 medical and health sciences chemistry.chemical_compound Cytosol Biochemistry medicine Thiol Hydrogen peroxide Incubation Intracellular Oxidative stress |
| Zdroj: | Biophysics. 61:950-958 |
| ISSN: | 1555-6654 0006-3509 |
| DOI: | 10.1134/s0006350916060087 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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