Тип публикации: статья из журнала
Год издания: 2010
Идентификатор DOI: 10.1007/s10517-010-1104-z
Ключевые слова: interleukins, oxidative stress, thiol-disulfi de system, neutrophils, disulfide, glutathione, glutathione disulfide, hydrogen peroxide, hydroxyl radical, interleukin 8, myeloperoxidase, thiol, thiol group, tumor necrosis factor alpha, adult, article, cell stress, clinical article, community acquired pneumonia, controlled study, enzyme activity, female, granulocyte function, human, human cell, in vitro study, male, neutrophil, protein binding, regulatory mechanism, Community-Acquired Infections, Ethylmaleimide, Humans, Interleukin-8, Middle Aged, Neutrophils, Peroxidase, Pneumonia, Protein Disulfide Reductase (Glutathione), Tumor Necrosis Factor-alpha
Аннотация: 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-? and myeloperoxidase activity) from healthy donors under condПоказать полностьюitions of oxidative stress in vitro induced by H 2O 2 in a final concentration of 200 ?M 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. © 2010 Springer Science+Business Media, Inc.
Журнал: Bulletin of Experimental Biology and Medicine
Выпуск журнала: Vol. 150, Is. 2
Номера страниц: 198-202