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Redox state is a widely used term for the description of redox phenomena in biological systems. The regulating mechanisms responsible for maintaining the redox state are not yet fully known. But it was shown that changes in the redox state might lead to a cascade of intracellular events, beneficial or deleterious to the cell. There are several methods for the description of the intracellular redox state. These methods are based on using measured intracellular concentrations of reduced and oxidized glutathione in the Nernst equation. However, glutathione is not always a basic redox component in biological fluids, organelles, cells or tissues. As a result, changes in the intracellular redox state are not always accompanied by considerable changes of glutathione concentration. In this work it was proposed to use the concept of effective reduction potential for the quantitative characteristic of the intracellular redox state. The effective reduction potential was substantiated on the basis of a thermodynamic description. A new equation for the calculation of the effective reduction potential was derived. This equation summarizes the contribution of different oxidizing and reducing agents in the formation of an effective redox potential. The theoretical estimation of the effective reduction potential values for the different biological fluids and cells was carried out with the use of a method developed.

Myeloperoxidase (MPO) is an oxidant-producing enzyme that can also regulate cellular functions via its nonenzymatic effects. Mature active MPO isolated from normal human neutrophils is a 145 kDa homodimer, which consists of 2 identical protomers, connected by a single disulfide bond. By binding to CD11b/CD18 integrin, dimeric MPO induces neutrophil activation and adhesion augmenting leukocyte accumulation at sites of inflammation. This study was performed to compare the potency of dimeric and monomeric MPO to elicit selected neutrophil responses. Monomeric MPO (hemi-MPO) was obtained by treating the dimeric MPO by reductive alkylation. Analysis of the crucial signal transducer, intracellular Ca, showed that dimeric MPO induces Ca mobilization from the intracellular calcium stores of neutrophils and influx of extracellular Ca whereas the effect of monomeric MPO on Ca increase in neutrophils was less. It was also shown that monomeric MPO was less efficient than dimeric MPO at inducing actin cytoskeleton reorganization, cell survival, and neutrophil degranulation. Furthermore, we have detected monomeric MPO in the blood plasma of patients with acute inflammation. Our data suggest that the decomposition of dimeric MPO into monomers can serve as a regulatory mechanism that controls MPO-dependent activation of neutrophils and reduces the proinflammatory effects of MPO.

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We performed a comparative analysis of functional activity of neutrophils in patients with type 2 diabetes mellitus with and without symptoms of CHD. Enhanced H2O2 production by neutrophils in response to N-formyl-Met-Leu-Phe (fMLP) was found in patients with type 2 diabetes mellitus. In patients with type 2 diabetes mellitus associated with CHD, fMLP-induced release of myeloperoxidase from azurophilic granules of neutrophils was reduced and plasma myeloperoxidase level was elevated. Increased peroxidase activity of myeloperoxidase, reduced plasma catalase activity, and increased levels of TBA-reactive lipid peroxidation products and oxidized glutathione were detected in patients of both groups. Since myeloperoxidase is an important neutrophilic mediator of oxidative stress, its increased activity in the blood can be an additional marker of oxidative stress and cardiovascular risk in patients with diabetes mellitus.