Figure 6. Pax3 positively regulates Bcl-2 and Bcl-xL expression. (A) Pax3, Bcl-2, and Bcl-xL gene expression were compared between wild-type myoblasts infected with a retrovirus vector expressing Pax3 (Ect-Pax3) and a control empty vector or MyoD−/− myoblasts transfected with siRNA for Pax3 and a control siRNA (Cont) by RT-PCR. (B) Pax3, Bcl-2, and Bcl-xL protein expression were compared between wild-type myoblasts infected with a retrovirus vector expressing Pax3 and a control empty vector or MyoD−/− myoblasts transfected with siRNA for Pax3 and a control siRNA by Western blotting. (A and B) β-Actin was monitored as a loading control. (C and D) Relative Pax3, Bcl-2, and Bcl-xL protein expression levels shown in B normalized by β-actin expression were compared by Western blotting. (E) Luc activity was assessed after transfection with Bcl-2– or Bcl-xL–Luc reporter genes into wild-type or MyoD−/− myoblasts. Luc activity was also assessed after transfection with Bcl-2– or Bcl-xL–Luc reporter genes and the Pax3 expression vector or control empty vector into wild-type myoblasts. (F) Under differentiation conditions from day 0 to 3 or after UV exposure or treatment with thapsigargin (Thap) for 1 d, cell death was compared between wild-type myoblasts infected with a retrovirus vector expressing Pax3 and a control empty vector. (G) After UV exposure or treatment with thapsigargin for 1 d, caspase-3 activity was compared between wild-type and MyoD−/− myoblasts infected with a retrovirus vector expressing Pax3 and a control empty vector or transfected with siRNA for Pax3 and a control siRNA. *, P < 0.05; **, P < 0.01. Error bars indicate SEM.
Figure 6.

Pax3 positively regulates Bcl-2 and Bcl-xL expression. (A) Pax3, Bcl-2, and Bcl-xL gene expression were compared between wild-type myoblasts infected with a retrovirus vector expressing Pax3 (Ect-Pax3) and a control empty vector or MyoD−/− myoblasts transfected with siRNA for Pax3 and a control siRNA (Cont) by RT-PCR. (B) Pax3, Bcl-2, and Bcl-xL protein expression were compared between wild-type myoblasts infected with a retrovirus vector expressing Pax3 and a control empty vector or MyoD−/− myoblasts transfected with siRNA for Pax3 and a control siRNA by Western blotting. (A and B) β-Actin was monitored as a loading control. (C and D) Relative Pax3, Bcl-2, and Bcl-xL protein expression levels shown in B normalized by β-actin expression were compared by Western blotting. (E) Luc activity was assessed after transfection with Bcl-2– or Bcl-xL–Luc reporter genes into wild-type or MyoD−/− myoblasts. Luc activity was also assessed after transfection with Bcl-2– or Bcl-xL–Luc reporter genes and the Pax3 expression vector or control empty vector into wild-type myoblasts. (F) Under differentiation conditions from day 0 to 3 or after UV exposure or treatment with thapsigargin (Thap) for 1 d, cell death was compared between wild-type myoblasts infected with a retrovirus vector expressing Pax3 and a control empty vector. (G) After UV exposure or treatment with thapsigargin for 1 d, caspase-3 activity was compared between wild-type and MyoD−/− myoblasts infected with a retrovirus vector expressing Pax3 and a control empty vector or transfected with siRNA for Pax3 and a control siRNA. *, P < 0.05; **, P < 0.01. Error bars indicate SEM.

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