Members of the caspase family of cysteine proteases coordinate the morphological 
and biochemical events that typify apoptosis. However, neutralization of caspase 
activity in mammals fails to block death in response to most proapoptotic 
stimuli. This is because many cell death triggers provoke mitochondrial 
dysfunction upstream of caspase activation as a consequence of BAX/BAK channel 
opening. Although genetic or pharmacological inactivation of caspases fails to 
block cell death in most instances, it does convert the phenotype from apoptosis 
to necrosis. This has important implications for how the immune system responds 
to such cells, as necrotic cells provoke inflammation whereas apoptotic cells 
typically do not. Here, we propose an alternative perspective on 
apoptosis-associated caspase function by suggesting that these proteases are 
activated, not to kill, but to extinguish the proinflammatory properties of 
dying cells. This perspective unifies the mammalian caspase family as either 
positive or negative regulators of inflammation.