Abstract
Innate immune responses are tightly regulated by various pathways to control infections and maintain homeostasis. One of these pathways, the inflammasome pathway, activates a family of cysteine proteases called inflammatory caspases. They orchestrate an immune response by cleaving specific cellular substrates. Canonical inflammasomes activate caspase-1, whereas non-canonical inflammasomes activate caspase-4 and -5 in humans and caspase-11 in mice. Caspases are highly specific enzymes that select their substrates through diverse mechanisms. During inflammation, caspase activity is responsible for the secretion of inflammatory cytokines and the execution of a form of lytic and inflammatory cell death called pyroptosis. This review aims to bring together our current knowledge of the biochemical processes behind inflammatory caspase activation, substrate specificity, and substrate signalling.
Highlights
Proteases are central enzymes that mediate numerous signalling roles to ensure cellular functions and organismal homeostasis [1]
Inflammatory caspases are a caspase subset activated by cellular platforms called inflammasomes [6,7,8]
Our understanding of the biochemistry and the cellular processes governed by inflammatory caspases is limited
Summary
Proteases are central enzymes that mediate numerous signalling roles to ensure cellular functions and organismal homeostasis [1]. Inflammatory caspases are a caspase subset activated by cellular platforms called inflammasomes [6,7,8]. A classification system for caspases was developed, dividing each caspase into two main groups in accordance with their function, structure, and activation mechanism (Table 1).
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