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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Han YH,Kim SU,Kwon TH,Lee DS,Ha HL,Park DS,Woo EJ,Lee SH,Kim JM,Chae HB,Lee SY,Kim BY,Yoon DY,Rhee SG,Fibach E,Yu DY

doi

10.1016/j.bbrc.2012.08.113

subject

Has Abstract

pub_date

2012-09-28 00:00:00

pages

427-32

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(12)01681-6

journal_volume

426

pub_type

杂志文章

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