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Peroxiredoxin II is essential for preventing hemolytic anemia from oxidative stress through maintaining hemoglobin stability

Title
Peroxiredoxin II is essential for preventing hemolytic anemia from oxidative stress through maintaining hemoglobin stability
Authors
Han Y.-H.Kim S.-U.Kwon T.-H.Lee D.-S.Ha H.-L.Park D.-S.Woo E.-J.Lee S.-H.Kim J.-M.Chae H.-B.Lee S.Y.Kim B.Y.Yoon D.Y.Rhee S.G.Fibach E.Yu D.-Y.
Ewha Authors
이서구
SCOPUS Author ID
이서구scopusscopus
Issue Date
2012
Journal Title
Biochemical and Biophysical Research Communications
ISSN
0006-291XJCR Link
Citation
vol. 426, no. 3, pp. 427 - 432
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
The pathophysiology of oxidative hemolytic anemia is closely associated with hemoglobin (Hb) stability; however, the mechanism of how Hb maintains its stability under oxidative stress conditions of red blood cells (RBCs) carrying high levels of oxygen is unknown. Here, we investigated the potential role of peroxiredoxin II (Prx II) in preventing Hb aggregation induced by reactive oxygen species (ROS) using Prx II knockout mice and RBCs of patients with hemolytic anemia. Upon oxidative stress, ROS and Heinz body formation were significantly increased in Prx II knockout RBCs compared to wild-type (WT), which ultimately accelerated the accumulation of hemosiderin and heme-oxygenase 1 in the Prx II knock-out livers. In addition, ROS-dependent Hb aggregation was significantly increased in Prx II knockout RBCs. Interestingly, Prx II interacted with Hb in mouse RBCs, and their interaction, in particular, was severely impaired in RBCs of patients with thalassemia (THAL) and sickle cell anemia (SCA). Hb was bound to the decameric structure of Prx II, by which Hb was protected from oxidative stress. These findings suggest that Prx II plays an important role in preventing hemolytic anemia from oxidative stress by binding to Hb as a decameric structure to stabilize it. © 2012 Elsevier Inc.
DOI
10.1016/j.bbrc.2012.08.113
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일반대학원 > 생명·약학부 > Journal papers
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