Caspase-7 (CMH-1, Mch3, ICE-LAP3) has been identified as a major contributor to the execution of apoptosis . Caspase-7, like caspase-3, is an effector caspase that is responsible for cleaving downstream substrates such as (ADP-ribose) polymerase and PARP. During apoptosis, caspase-7 is activated through proteolytic processsing by upstream caspases at Asp23, Asp198, and Asp206 to produce the mature subunits. Similar to caspases-2 and -3, caspase-7 preferentially cleaves substrates following the recognition sequence DEVD.
Caspase-7 (CMH-1, Mch3, ICE-LAP3) has been identified as a major contributor to the execution of apoptosis . Caspase-7, like caspase-3, is an effector caspase that is responsible for cleaving downstream substrates such as (ADP-ribose) polymerase and PARP. During apoptosis, caspase-7 is activated through proteolytic processsing by upstream caspases at Asp23, Asp198, and Asp206 to produce the mature subunits. Similar to caspases-2 and -3, caspase-7 preferentially cleaves substrates following the recognition sequence DEVD.
This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. The precursor of this caspase is cleaved by caspase 3 and 10. It is activated upon cell death stimuli and induces apoptosis. Alternative splicing results in four transcript variants, encoding three distinct isoforms.
Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp- ; -Gly-217' bond. Overexpression promotes programmed cell death.