Caspase-1

Caspase-1, historically named interleukin-1 beta-converting enzyme (ICE), is the prototypical inflammatory caspase and the central effector of canonical inflammasome signaling. Upon assembly of inflammasome complexes such as NLRP3, NLRC4, or AIM2, the protease is recruited via its CARD domain and activated, after which it processes pro-IL-1β and pro-IL-18 into their mature secreted forms and cleaves gasdermin D to trigger pyroptotic cell death. This places Caspase-1 at the interface of innate immunity and inflammatory pathology: it drives host defense against intracellular pathogens, yet excessive activation underlies sepsis, autoinflammatory syndromes, and metabolic inflammation, sustaining interest in selective Caspase-1 inhibitors.