Caspase 6

Caspase 6, also known as Apoptotic protease Mch-2, belongs to the peptidase C14A family. It functions as a downstream enzyme in the caspase activation cascade and is responsible for the execution of apoptosis. Its overexpression promotes programmed cell death.

Diseases associated with CASP6 include thoracic cancer and myocardial infarction.  Among its related super-pathways are DR3 Signaling and Apoptosis and the survival FAS signaling cascade.

Cell death via apoptosis is a basic cellular function occurring through the cell death receptor family and their ligands which signal through downstream adaptor molecules and the caspase protease family. Caspases have a precursor form composed of a prodomain, and large and small catalytic subunit, and are activated through a cleavage adjacent to an aspartate to liberate units and allow formation of an a2b2 tetramer. Caspase 3 is a cytoplasmic caspase with two isoforms (one acts as a dominant negative inhibitor), and is involved in the activation cascade for apoptosis 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.