Figure 6. ONOO− induces p53 SUMOylation and p53–Bcl-2 binding via PIASy activation. (A and B) HUVECs were transfected with PIASy siRNA (si-PIASy) or control siRNA for 48 h and then stimulated with 100 µM ONOO– for the indicated times. p53 SUMOylation (A) and p53–Bcl-2 binding (B) were determined as described in Materials and methods. (left) PIASy and p53 expressions were detected by Western blotting with appropriate specific antibodies. Densitometric analyses of p53 SUMOylation (A) and p53–Bcl-2 binding (B) were performed as described in Fig. 1. (C) HUVECs were transfected with PIASy or control siRNA for 48 h. After treatment with 100 µM ONOO− for 8 h, apoptotic nuclei were detected by TUNEL staining. Data are expressed as mean percentages ± SD from three independent experiments. *, P < 0.05; **, P < 0.01. Molecular masses are given in kilodaltons. IB, immunoblot. IP, immunoprecipitation.
Figure 6.

ONOO− induces p53 SUMOylation and p53–Bcl-2 binding via PIASy activation. (A and B) HUVECs were transfected with PIASy siRNA (si-PIASy) or control siRNA for 48 h and then stimulated with 100 µM ONOO– for the indicated times. p53 SUMOylation (A) and p53–Bcl-2 binding (B) were determined as described in Materials and methods. (left) PIASy and p53 expressions were detected by Western blotting with appropriate specific antibodies. Densitometric analyses of p53 SUMOylation (A) and p53–Bcl-2 binding (B) were performed as described in Fig. 1. (C) HUVECs were transfected with PIASy or control siRNA for 48 h. After treatment with 100 µM ONOO− for 8 h, apoptotic nuclei were detected by TUNEL staining. Data are expressed as mean percentages ± SD from three independent experiments. *, P < 0.05; **, P < 0.01. Molecular masses are given in kilodaltons. IB, immunoblot. IP, immunoprecipitation.

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