Caspases are key effectors of programmed cell death. They are synthesized as inactive proenzymes which are activated by cleavage at a specific aspartate residue to form two subunits. These subunits are normally linked together by a linker which may be involved in the regulation of the different caspases. Caspase-8 is a key enzyme in the apoptosis pathway. Caspase-8 contains two N-terminal region death effector domains which are removed to activate the enzyme along with cleavage into the two subunits. These subunits then for the active protease which is capable of cleaving caspase-3, -6 and -7. These caspases are then capable of cleaving other cellular substrates such as PARP and DFF, which in turn induce apoptosis.
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