No related experience, interaction of endogenous Bax, Bcl 2 has been significantly reduced by the interaction with INrf2 Flag Bcl 2 erh Ht. This was as expected by a dose–Dependent overexpression INrf2 in Hepa 1 cells, the Bcl stabilized 2 and Bax protein supports deteriorate. Limonin Immunpr zipitation Flag of INrf2 in the same experiment showed a st Rkere INrf2 interaction with Bcl 2, but not Bax. Immunpr zipitation Bcl 2 V5 V5 antique Body showed the interaction of Bcl-2 and Bax with two INrf2. Interestingly, the Erh INrf2 increase interaction with Bcl 2 to a decrease in the interaction between Bcl 2 and Bax. This suggests that Bcl INrf2 decreases 2 2 Bax heterodimerization by degradation of the protein Bcl In the same experiment showed Immunpr Zipitation of Bax interaction with Bcl Bax 2, but not with INrf2, also supported the above conclusions.
Figure 4f shows Zibotentan an increase in INrf2: Bcl 2 interaction leads to the decrease of Bcl 2: Bax interaction. Tert butyl hydroquinone antioxidant treatment destabilizes Bcl 2: INrf2: Cul3 RBX1 complex and hte increased phosphorylation of Bcl 2S70 and stabilization of Bcl second We suspect that antioxidants antagonize INrf2: Nrf2 interaction against INrf2: Bcl interacting second Tats Chlich destabilized antioxidant TBHQ / reduced endogenous INrf2, the born Bcl 2 stabilized entered. Immunpr zipitation INrf2 of Hepa 1 cells with DMSO and t BHQ treated, reduced interaction with INrf2 showed Cul3 RBX1 and Bcl 2 in cells treated with BHQ t were compared to DMSO treated control cells.
Immunopr Zipitation Cul3 or RBX1 interaction showed a more or less Similar with Cul3 RBX1 between t and BHQ DMSOtreated cells. However, the interaction with INrf2 and INrf2 binding protein Bcl 2 is significantly reduced in cells treated with BHQ t, as compared to cells treated with DMSO. In other words, leads to dissociation of the t BHQ treatment Cul3 RBX1: INrf2: Bcl 2 complex, which second in a deterioration of INrf2 and stabilization of Bcl Similar results were also observed with Hepa overexpression of INrf2 and Bcl 2 V5 flag. t BHQ treatment showed a decrease over time in INrf2 and erh hte second Bcl Front and rear Immunpr zipitation And immunoblot analysis revealed decreases the processing time t h BHQ Flag INrf2 and Bcl nts 2 V5 degradation flag INrf2 interaction and stabilization of the Bcl 2 V5.
Interestingly, t BHQ treatment of Hepa-1 cells also increased FITTINGS endogenous Bcl-2 S70 phosphorylation. Immunpr zipitation INrf2 of DMSO and t-BHQ-treated cells showed t BHQdependent News INrf2 Bcl 2, Bax increased every interaction with INrf2 and Hte interaction of Bcl 2 and Bax. These data suggest that the TBHQ Cul3 destabilized RBX1: INrf2: Bcl 2 complex increased the phosphorylation of Bcl ht 2S70, which increased the dissociation of Bcl 2 and Bcl INrf2 hte 2: Bax interaction. INrf2 overexpression and etoposide treatment up-regulated pro-apoptotic marker proteins And f Rdern apoptosis. Hepa 1 cells were transfected and treated INrf2 293 cells with tetracycline overexpressing INrf2. This was followed by the treatment with etoposide. INrf2 overexpression and etoposide treatment increased Bax protein ht by two to three times and a decrease in Bcl 2 in both cell lines. INrf2