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. 2020 May 16;34:101587. doi: 10.1016/j.redox.2020.101587

Fig. 6.

Fig. 6

Peroxynitrite mediated inhibition of PP2A activity is responsible for c-Myc stabilization and phospho-activation. (A and B) Western blot and c-Myc reporter luciferase analyses of U2-OS cells subjected to SNP (6 h) and peroxynitrite (2 h) treatments. Fold change in c-Myc reporter activity was normalized to vehicle control. (C and D) Western blot analyses in U2-OS cells of pS62 c-Myc and total c-Myc in the presence of FeTPPS (100 μM/2 h pre-treatment) and l-NAME (5 mM/1hr pre-treatment) with DDC (100 μM/4 h) treatments. (E) Western blot analyses of U2-OS cells subjected to siRNA (100 nM/24 h) targeted against SOD1 demonstrates elevated c-Myc levels which are subsequently depleted in the presence of FeTPPS (100 μM/6 h). (F and G) Ubiquitination IP assay analysis by Western blot to determine the level of c-Myc ubiquitination in the presence and absence of peroxynitrite (20 μM/2 h) or FeTPPS (100 μM/6 h) treatments. One-way ANOVA was employed for statistical analysis (* = p < 0.05, ** = p < 0.01, **** = p < 0.0001).