Apoptosis, also called programmed cell death, is an essential process in development and disease. The signaling networks that carry out apoptosis is consists of a series of endoproteases called caspases which are synthesized as inactive zymogens. Caspses are grouped into two classes: initiator caspases and effector caspases. Initiator caspases are activated by the assembly of multi-protein complexes such as the death-inducing signaling complex (DISC) (1). This complex consists of the Fas receptor and the death effector domain containing initiator caspases -8 or -10 (1). Once activated, initiator caspases cleave and activate effector caspases which then go on to cleave various substrates to aid in the destruction of the cell in an organized manner.
Caspase-10 is of particular importance given its role in apoptotic induction and implications in tumorigenesis. Examination of lung and breast carcinoma cell lines using western blotting with caspase-10 antibody revealed absence of caspase-10 in the majority of cell lines (1). Caspase-10 is also thought to be involved in promoting cell survival through the activation of NF-kB (1). NF-kB activation is seen in many tumors and may be yet another way caspase-10 influences tumorigenesis depending on the cellular context. In an investigation involving apoptotic mechanisms in human neutrophils, Goepel et al. used caspase-10 antibodies to examine the individual roles of caspase-10 isoforms (2). Western blotting with the caspase-10 antibody revealed down regulation and cleavage of caspase-10b (2). The group also used caspase-10 antibody to immunoprecipitate caspase-10 from cell lysates and measure its activity using a fluorogenic substrate assay (2). Chae et al. used caspase-10 antibody to examine the composition of protein complexes formed by the protein pyrin (3), a protein that is often mutated in inherited inflammatory disorders (3). Immunoprecipitation experiments identified caspase-1 as a component of these complexes while caspases 2-10 were absent (3).
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