Caspase 10

Caspase-3 is one of the most important players in apoptosis signaling. It is synthesized as an inactive 32 kDa pro-enzyme and upon direct activation by Caspase-8, -9 or -10, it gets processed into its active forms, the p17-20 and p10-12 subunits. The latter are responsible for the cleavage of PARP (poly ADP-ribose polymerase), actin and SREBP, which are associated with apoptosis [1].

Survivin is an anti-apoptotic protein which is the smallest protein within a large family of proteins including X-linked IAP, c-IAP1 and 2, IAP-like protein-2, melanoma IAP, NAIP, and Livin. Survivin is responsible for a wide range of basic cellular functions that include the cell cycle regulation, fetal development, cell migration, and tumor progression.

Fas is a member of the tumor necrosis factor (TNF)-receptor superfamily and plays a key role in the physiological regulation of programmed cell death. This receptor contains a death domain which enables the formation of a signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10. The auto-proteolytic processing of these complexed caspases triggers a downstream cascade that leads to membrane-mediated apoptosis.

Caspase 7 (also known as CASP7, Mch3, ICE-LAP3, CMH-1) is a member of caspase family of cysteine proteases. It is an apoptosis-related cystein peptidase encoded by the CASP7 gene in humans. CASP7 homologous sequences have been identified in nearly all mammals. Similar to Caspase 3, Caspase-7 is an effector caspase and plays a key role in apoptotic execution.

Apoptosis is one of the best-characterized phenomena in cellular and molecular biology. Not only is it essential for successful development, but its deregulation also leads to a number of human diseases, most notably cancer.

The caspases are a group of cysteine protease enzymes essential to apoptosis, inflammation and necrosis. Caspase 3 has been identified as one of the key mediators of apoptosis.