Caspase-7 is an effector caspase with important roles in mediating cell death signaling. As an effector caspase, caspase-7 is cleaved and activated by initiator caspases such as caspase-1 (1). Like other caspase family proteins, caspase-7 contains a catalytic cysteine residue in its active site. This allows caspase-7 to cleave various substrates, such as PARP, to aid in the degradation and destruction of the cell (2). Mutations in caspase-7 have been found in numerous cancers demonstrating the importance of caspase-7 mediated apoptosis in preventing tumorigenesis (1). Caspase-7 shows some functional redundancy with caspase-3 as both they share a number of the same substrates. However both of these effector caspases have distinct functions during apoptosis. Recent studies have indicated caspase-3 is needed for efficient cell killing and can also block ROS production (3). Caspase-7, on the other hand, is responsible for ROS production and aids in cell detachment during apoptosis (3). These studies made use of cell lines derived from caspase-3/7 knockout mice as well as western blotting with caspase-7 antibodies to measure protein levels. As with other caspases, monitoring the cleavage of procaspase-7 by western blot using caspase-7 antibodies provides an excellent tool to study progression of apoptosis. This approach was utilized by Jin et al. (4). By western blotting using a caspase-7 antibody, the researchers were able to monitor apoptosis induction and identify the role of tumor suppressor genes in cervical cancer (4). Alternatively, caspase-7 antibodies specific to just the cleaved active form can be used to monitor apoptosis by western blot or through immunohistochemistry. This strategy was used by Blanc-Brude et al. in their study of survivin as an upstream regulator of mitochondrial dependent apoptosis (5). Expression of survivin inhibited apoptosis and prevented the production of active caspase-7 as detected with the caspase-7 antibody (5).
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