Apoptosis is a major form of cell death characterized by several morphological features that include chromatin condensation and fragmentation, cell membrane blebbing, and formation of apoptotic bodies. These morphological changes occur via a signaling pathway that leads to the recruitment and activation of caspases, a family of cystein-containing, aspartate-specific proteases. Caspases exist as inactive proenzymes in cells and are activated through their processing into subunits in response to apoptotic stimulation. Activated caspases cleave a variety of important cellular proteins, other caspases, and Bcl-2 family members, leading to a commitment to cell death. Caspase-6 (also known as Mch2α) is a 34 kDa protein that has been involved in “effector” caspases (which include caspase-3, -6, and -7) that are cleaved by “initiator” caspases (which include caspase-8 and -9) into active form which then cleave various cellular proteins including lamin A and other caspases.