Caspase protease (Caspase (family abbreviation: CASP))

Caspases (cysteine aspartic proteases) are a family of cysteine-dependent, aspartate-directed proteolytic enzymes that play essential roles in apoptosis, inflammation, and various aspects of cell signaling and tissue homeostasis[1][3][7][8]. They are synthesized as inactive precursors (procaspases) and activated by proteolytic cleavage in response to apoptotic or inflammatory signals, leading to a cascade that orchestrates regulated cell death and processing of critical cellular substrates[3][7][8]. Caspases are classified as either apoptotic (initiators such as caspase-8, -9, and -10; effectors such as caspase-3, -6, and -7) or inflammatory (such as caspase-1, -4, -5, and -11), each with distinct but sometimes overlapping roles[5][7]. Aberrant caspase activity has been implicated in a wide spectrum of diseases, including cancer, neurodegeneration, autoimmune disorders, inflammation, and cardiovascular diseases[3][6][5]. Pharmacological targeting of caspases, especially with inhibitors, is a strategy investigated for treating diseases characterized by excessive cell death or inflammation, but broad caspase inhibition carries significant safety risks[5][8].

Other names

Cysteine aspartic proteaseCysteine-dependent aspartate-directed proteaseCaspase familyCASP

Inhibition of proteolytic activity at aspartic acid residues (caspase inhibition) Blockade of apoptotic cascades Inhibition of cytokine maturation