@article{oai:repo.qst.go.jp:00047693,
 author = {Pei, Hailong and Zhang, Jian and Nie, Jing and Ding, Nan and Hu, Wentao and Hua, Junrui and Hirayama, Ryoichi and Furusawa, Yoshiya and Liu, Cuihua and Li, Bingyan and K, Hei Tom and Zhou, Guangming and Ｐｅｉ Ｈａｉｌｏｎｇ and 張 健 and Ｄｉｎｇ Ｎａｎ and 胡 文涛 and 平山 亮一 and 古澤 佳也 and 劉 翠華 and 李 冰燕 and 周 光明},
 issue = {1},
 journal = {Cell cycle (Georgetown, Tex.)},
 month = {Jan},
 note = {Our recent study showed that quiescent G0 cells are more resistant to ionizing radiation than G1 cells; however, the underlying mechanism for this increased radioresistance is unknown. Based on the relatively lower DNA damage induced in G0 cells, we hypothesize that these cells are exposed to less oxidative stress during exposure. As a catalytic subunit of NADPH oxidase, Ras-related C3 botulinum toxin substrate 2 (RAC2) may be involved in the cellular response to ionizing radiation. Here, we show that RAC2 was expressed at low levels in G0 cells but increased substantially in G1 cells. Relative to G1 cells, the total antioxidant capacity in G0 phase cells increased upon exposure to X-ray radiation, whereas the intracellular concentration of ROS and malondialdehyde increased only slightly. The induction of DNA single- and double-stranded breaks in G1 cells by X-ray radiation was inhibited by knockdown of RAC2. P38 MAPK interaction with RAC2 resulted in a decrease of functional RAC2. Increased phosphorylation of P38 MAPK in G0 cells also increased cellular radioresistance; however, excessive production of ROS caused P38 MAPK dephosphorylation. P38 MAPK, phosphorylated P38 MAPK, and RAC2 regulated in mutual feedback and negative feedback regulatory pathways, resulting in the radioresistance of G0 cells.},
 pages = {113--122},
 title = {RAC2-P38 MAPK-dependent NADPH oxidase activity is associated with the resistance of quiescent cells to ionizing radiation.},
 volume = {16},
 year = {2017}
}