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Transcriptional activity of paired homeobox Pax6 is enhanced by histone acetyltransferase Tip60 during mouse retina development |
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| Authors: | Chul-Hong Kim Jung-Woong Kim Sang-Min Jang Joo-Hee An Ki-Hyun Song Kyung-Hee Choi |
| Affiliation: | a KRIBB, Daejeon, Republic of Korea b College of Life Science and Technology, Heilongjiang Bayi Agricultural University, Daqing, HeiLongJiang Province, China c Bio/Molecular Informatics Center, Konkuk University, Seoul, Republic of Korea d College of Natural Sciences, Kyungpook National University, Daegu, Republic of Korea e College of Medicine, Chungnam National University, Daejeon, Republic of Korea f Environmental Biotechnology Research Center, Gyeongsang National University, Jinju, Republic of Korea g World Class Institute, KRIBB, Cheongwon, Republic of Korea h Division of Molecular Life Sciences, Ewha Womans University, Seoul, Republic of Korea i Dept. of Hematology, Hadassah University Hospital, Ein-Kerem, Jerusalem, Israel |
| 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. |
| Keywords: | Hemoglobin Red blood cells Peroxiredoxin II Reactive oxygen species Heme-oxygenase 1 |
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