Caspase family protein (Caspase)

The caspase family comprises cysteine-dependent aspartate-directed proteolytic enzymes that play central roles in programmed cell death (apoptosis) and inflammation. They are synthesized as inactive zymogens containing prodomains with structural motifs from the death domain superfamily—including CARD and DED domains—which mediate recruitment into signaling complexes. Upon activation by cleavage at specific sites, they form active heterotetramers that execute cellular demolition by cleaving key substrates at C-terminal aspartic acid residues[2]. The family is subdivided into initiator/inflammatory and effector/apoptotic groups based on their function. Dysregulation of individual caspases has been implicated in diseases such as cancer, neurodegeneration, and inflammatory disorders[1][2][3]. Note: For structured data applications or drug discovery purposes, it is recommended to specify an individual member of the caspase family rather than using this general term[2][3].

Other names

CaspasesCysteine-aspartic proteasesICE-like proteases

Mechanisms include inhibition of enzymatic activity to block apoptosis or inflammation; specifics depend on the particular caspase targeted.