Role of Thiol-Disulfide System in Mechanisms of Functional Changes in Neutrophils under Conditions of Oxidative Stress

• Published in: Bulletin of experimental biology and medicine 2010-12, Vol.150 (2), p.198-202
• Main Authors: Stepovaya, E. A, Petina, G. V, Zhavoronok, T. V, Ryazanceva, N. V, Ivanov, V. V, Ageeva, T. S, Tetenev, F. F, Novitsky, V. V
• Format: Article
• Language: English
• Subjects: Adult; Bacterial pneumonia; Biomedical and Life Sciences; Biomedicine; Cell Biology; Community-Acquired Infections - blood; Community-Acquired Infections - metabolism; Ethylmaleimide; Female; Glutathione - metabolism; Humans; Hydrogen Peroxide; Hydroxyl Radical - metabolism; In Vitro Techniques; Interleukin-8 - metabolism; interleukins; Internal Medicine; Laboratory Medicine; Male; Middle Aged; Neutrophils - metabolism; Oxidative stress; Oxidative Stress - physiology; Pathology; Peroxidase - metabolism; Pneumonia; Pneumonia - blood; Pneumonia - metabolism; Protein binding; Protein Disulfide Reductase (Glutathione) - metabolism; thiol-disulfi de system, neutrophils; Thiols; Tumor necrosis factor; Tumor Necrosis Factor-alpha - metabolism
• ISSN: 0007-4888; 1573-8221
• DOI: 10.1007/s10517-010-1104-z

We studied the state of the thiol-disulfide system (contents of reduced and oxidized glutathione, their ratio, and concentrations of protein SH-groups and protein-bound glutathione) and functional properties of neutrophils (production of hydroxyl radicals, IL-8, and TNF-α and myeloperoxidase activity) from healthy donors under conditions of oxidative stress in vitro induced by H₂O₂ in a final concentration of 200 μM and from patients with community-acquired pneumonia. We evaluated the role of reduced and protein-bound glutathione in the regulation of functional state of blood neutrophils from patients with community-acquired pneumonia and during oxidative stress in vitro under conditions cell incubation with N-ethylmaleimide or 1,4-dithioerythritolsulfhydryl, the blocker and protector of sulfhydryl groups, respectively.