Fig. 1.
MRE11 participates in ATM activation following oxidative stress. (A) MRC5SV (normal), MRE11-defective HMfibroSV (HM) and ATLD2SV (ATLD) cells were treated with H2O2 (100 μM) for the indicated times and analysed using the indicated antibodies. (B) U2OS cells were transfected with MRE11 siRNA. After 2 days, these cells were treated with H2O2 (100 μM) for the indicated times and analyzsd using the indicated antibodies. (C) Normal (C2ABR) or ATLD2 (ATLD2ABR) lymphoblastoid cells were γ-ray-irradiated (10 Gy) or treated with 100 μM H2O2. After 1 h, cells were harvested and a kinase activity assay was measured using the immunocomplexes with an anti-ATM antibody. Phosphorylation was detected by western blot analysis using an anti-phospho-p53 antibody. The amount of substrate in the reaction was confirmed using an anti-GST antibody.

MRE11 participates in ATM activation following oxidative stress. (A) MRC5SV (normal), MRE11-defective HMfibroSV (HM) and ATLD2SV (ATLD) cells were treated with H2O2 (100 μM) for the indicated times and analysed using the indicated antibodies. (B) U2OS cells were transfected with MRE11 siRNA. After 2 days, these cells were treated with H2O2 (100 μM) for the indicated times and analyzsd using the indicated antibodies. (C) Normal (C2ABR) or ATLD2 (ATLD2ABR) lymphoblastoid cells were γ-ray-irradiated (10 Gy) or treated with 100 μM H2O2. After 1 h, cells were harvested and a kinase activity assay was measured using the immunocomplexes with an anti-ATM antibody. Phosphorylation was detected by western blot analysis using an anti-phospho-p53 antibody. The amount of substrate in the reaction was confirmed using an anti-GST antibody.

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