Caspase enzyme family (Caspases)

The Caspase enzyme family comprises a group of cysteine proteases essential for regulated cell death (apoptosis and pyroptosis), inflammation, and cellular differentiation[1][3][4][6]. Caspases are divided into initiator, executioner, and inflammatory caspases based on their protein domain structure and biological function[3][4]. Initiator caspases (e.g., caspase-2, -8, -9, -10) activate effector or executioner caspases (e.g., caspase-3, -6, -7) which cleave specific cellular substrates to execute apoptosis[1][4][6]. Inflammatory caspases (e.g., caspase-1, -4, -5) control immune responses by processing pro-inflammatory cytokines and mediating pyroptosis[1][3][4]. Caspases are widely recognized as critical therapeutic targets in diseases marked by dysregulated apoptosis or inflammation, such as cancer, neurodegeneration, and inflammatory disorders[1][3][6]. Drugs targeting these enzymes often act as inhibitors to suppress inappropriate cell death or inflammatory signaling[6]. Caspase activation, especially caspase-3 and caspase-1, is frequently measured as a biomarker for apoptosis and inflammasome activity, respectively[3][4].

Other names

Cysteine-aspartic proteasesCysteine-dependent aspartate-directed proteases

- Inhibition of caspase activity to prevent excessive apoptosis or inflammation - Activation (in some research, as a cancer therapy concept)