Complexity of free radical Metabolism in human Erythrocytes

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Complexity of free radical Metabolism in human Erythrocytes

The auto-oxidation of oxyhaemoglobin to methaemoglobin generating superoxide anion radical (O2.-) represents the main source of free radicals in the erythro-cytes. Hydrogen peroxide is produced by O2.- dismutation or originates from the circulation. Human erythrocytes are also exposed to the prooxidative actions of nitric oxide (NO) from circulation. Free radicals that may induce reactions with direct dangerous consequences to erythrocytes are also preceded by the reaction of O2.- and NO producing peroxynitrite. In physiological settings, erythrocytes show a self-sustaining activity of antioxidative defence (AD) enzymes, such as: superoxide dismutase (SOD, EC 1.11.16), catalase (CAT, EC 1.11.1.6), glutathione peroxidase (GSHPx, EC 1.11.1.9) and glutathione reductase (GR, EC 1.6.4.2), as well as low molecular weight antioxidants: glutathione and vitamins E and C. Their coordinate actions protect the erythrocyte's bio-macromolecules from free radical-mediated damage. Since there is no de novo synthesis of AD enzymes in mature erythrocytes, their defence capacity is limited. Free radicals influence antioxidative enzymes capacities and relative share of particular components in the whole antioxidative system. Therefore, by measuring changes in the activity of individual AD components, as well as their interrelations by statistical canonical discriminant methods, valuable data about the complexity, overall relations and coordinated actions in the AD system in erythrocytes and its relevance for systemic effects can be acquired.

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