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The caspase-dependent apoptosis pathway is a regulated cell death pathway in which caspases—cysteine-dependent aspartate-specific proteases—mediate the orderly and energy-dependent execution of cellular demise[1][3][5]. This pathway integrates signals from the intrinsic (mitochondrial) and extrinsic (death receptor) initiation cascades, activating initiator caspases (such as caspase-8 for extrinsic and caspase-9 for intrinsic), which in turn cleave and activate executioner caspases (notably caspase-3, -6, and -7). These effector caspases dismantle the cell by proteolytically degrading key structural and regulatory proteins, leading to the characteristic morphological and biochemical features of apoptosis[4][5]. This pathway is a target of anti-cancer and anti-inflammatory strategies, and its dysfunction is implicated in various diseases including cancer, immune disorders, and neurodegeneration[1][4][5]. However, as a pathway rather than a discrete gene or protein, "caspase-dependent apoptosis pathway" is not itself a canonical molecular target; instead, individual caspases within the pathway (e.g., caspase-3, caspase-8, caspase-9) are direct therapeutic targets[1][3][5]. Therefore, this entry refers to a signaling cascade, not a druggable receptor or protein.
Caspase inhibition, Caspase activation
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