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Inactivation of glutathione peroxidase 1 and peroxiredoxin 2 by peroxides in red blood cells

Title
Inactivation of glutathione peroxidase 1 and peroxiredoxin 2 by peroxides in red blood cells
Authors
Cho C.-S.Rhee S.G.
Ewha Authors
이서구
SCOPUS Author ID
이서구scopusscopus
Issue Date
2012
Journal Title
Selenium: Its Molecular Biology and Role in Human Health
Publisher
Springer New York
Indexed
SCOPUS scopus
Abstract
Glutathione peroxidase 1 (GPx1), peroxiredoxin II (Prx II), and catalase are the principal enzymes responsible for peroxide elimination in red blood cells (RBCs). GPx1, which contains a selenocysteine (Sec) residue at its active site, is irreversibly inactivated by its own substrate as the result of the oxidation of selenium atom followed by the conversion of oxidized Sec to dehydroalanine (DHA). Prx II is inactivated when its catalytic cysteine (Cys) is hyperoxidized to cysteine sulfinic acid during catalysis. The hyperoxidation can be reversed by sulfiredoxin. The activity of sulfiredoxin in RBCs is sufficient to counteract the Prx II hyperoxidation that occurs during elimination of H2O2 molecules resulting from hemoglobin (Hb) autoxidation. We developed a blot method for detection of DHA-containing proteins, with the use of which we observed that the amount of DHA-containing GPx1 increases with aging of RBCs as well as in RBCs exposed to H2O2 generated either externally by glucose oxidase or internally as a result of aniline-induced Hb autoxidation. Given that the conversion of Sec to DHA is irreversible and that protein turnover mechanism is lacking in RBCs, the content of DHA-GPx1 in each RBC likely reflects total oxidative stress experienced by the cell during its lifetime. Therefore, DHA-GPx1 in RBCs might be a suitable surrogate marker for evaluation of oxidative stress in the body. © 2012 Springer Science+Business Media, LLC. All rights reserved.
DOI
10.1007/978-1-4614-1025-6_39
ISBN
9781461410256; 146141024X; 9781461410249
Appears in Collections:
일반대학원 > 생명·약학부 > Journal papers
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