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. 2003 Jul 7;162(1):59–69. doi: 10.1083/jcb.200302084

Figure 3.

Figure 3.

Caspase 12 functions downstream of the multidomain proapoptotic Bcl-2 family proteins. (A) ER stress–induced caspase 12 cleavage is dependent on Bax and Bak. Immortalized wild-type and bax − / − bak − / − MEFs and NIH3T3 cells were treated with brefeldin A (BFA; 10 μg/ml), thapsigargin (Thap; 2 μM), or tunicamycin (Tuni; 10 μg/ml) for 30 h. Caspase 12 level and processing were examined by immunoblotting of 20 μg of total cellular protein from samples as indicated. An ∼42-kD caspase 12 fragment is indicated by the arrow. Induction of CHOP expression is shown as an indicator of the ER stress response. A nonspecific band (NS) is shown as a loading control. (B) Caspase 12 kills bax − / − bak − / − cells. Wild-type and bax − / − bak − / − MEFs were cotransfected with pEGFP and constructs expressing caspase 3, caspase 9, caspase 12, and t-caspase 12. 24 h after transfection, cells were stained with DAPI, and cell death percentage was determined by the ratio of DAPI-positive to GFP-positive cells.