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

Ying Hao Han, Sun Uk Kim, Tae Ho Kwon, Dong Seok Lee, Hye Lin Ha, Doo Sang Park, Eui Jeon Woo, Sang Hee Lee, Jin Man Kim, Ho Byoung Chae, Sang Yeol Lee, Bo Yeon Kim, Do Young Yoon, Sue Goo Rhee, Eitan Fibach, Dae Yeul Yu

Research output: Contribution to journalArticlepeer-review

58 Scopus citations

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.

Original languageEnglish
Pages (from-to)427-432
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume426
Issue number3
DOIs
StatePublished - 28 Sep 2012

Keywords

  • Heme-oxygenase 1
  • Hemoglobin
  • Peroxiredoxin II
  • Reactive oxygen species
  • Red blood cells

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