Abstract
Inflammatory cell death can be mediated by the murine caspase-1 and -11. Genetic and cell biological data point to conflicting conclusions whether these caspases cleave the same substrates or use distinct mechanisms to mediate inflammation and cell death. Peptide screening and biochemical analysis by Gonzales Ramirez et al. now suggest caspase-11 specificity may be determined outside the known substrate motif and identifies substrates cleaved preferentially by caspase-1, providing new opportunities to uniquely target inflammatory caspases.
Highlights
Inflammatory cell death can be mediated by the murine caspase-1 and -11
The inflammatory caspase-1, -4, -5, and -11 are executioners of a lytic form of cell death known as pyroptosis, which is accompanied by release of the potent proinflammatory cytokines interleukin-1 (IL-1)2 and IL-18
Caspases are cysteine proteases that cleave their substrates after an aspartic acid at position 1 (P1), and the P1–P4 amino acids are believed to create a recognition motif that confers both efficacy and a degree of specificity for particular caspases [7, 8]
Summary
Inflammatory cell death can be mediated by the murine caspase-1 and -11. Genetic and cell biological data point to conflicting conclusions whether these caspases cleave the same substrates or use distinct mechanisms to mediate inflammation and cell death. Genetic evidence suggests that these cytokines are not directly cleaved by caspase-11, the two caspases are 53% identical in their catalytic domains and their substrate specificities, based on prior peptide screening, are highly overlapping [4, 5].
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