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. Author manuscript; available in PMC: 2012 Jan 3.

Published in final edited form as: Gene Ther. 2010 Feb 25;17(4):550–559. doi: 10.1038/gt.2010.5

DLD1 cells were grown in 6-well plates overnight and then treated with the agents as indicated for 12, 18, 24 and 48 h. Cells were lyzed and subject to Western blot analysis as described in Materials and Methods. The cells were treated with, lane 1: mock-treated; lane 2: Ox; lane 3: vJS6; lane 4: vvTRAIL; lane 5: Ox + vJS6; lane 6: Ox + vvTRAIL; and lane 7: etoposide (100 μM) (positive control). (A). The regulation of representative anti-apoptotic and pro-apoptotic proteins in cancer cells under various treatments. The anti-PARP antibody was against the cleaved form of PARP. (B). Kinetics of cleaved PARP. The antibody mainly recognizes the cleaved form of PARP. The time points were 12, 18 24 and 48 h. (C). Kinetics of cleaved caspase-8.

DLD1 cells were grown in 6-well plates overnight and then treated with the agents as indicated for 12, 18, 24 and 48 h. Cells were lyzed and subject to Western blot analysis as described in Materials and Methods. The cells were treated with, lane 1: mock-treated; lane 2: Ox; lane 3: vJS6; lane 4: vvTRAIL; lane 5: Ox + vJS6; lane 6: Ox + vvTRAIL; and lane 7: etoposide (100 μM) (positive control). (A). The regulation of representative anti-apoptotic and pro-apoptotic proteins in cancer cells under various treatments. The anti-PARP antibody was against the cleaved form of PARP. (B). Kinetics of cleaved PARP. The antibody mainly recognizes the cleaved form of PARP. The time points were 12, 18 24 and 48 h. (C). Kinetics of cleaved caspase-8.