Caspase-11

Caspase‑11 is a murine pro-inflammatory cysteine-aspartate protease that plays a central role in the innate immune system’s response to cytosolic Gram-negative bacterial infection. It acts as an intracellular pattern recognition receptor by directly sensing lipopolysaccharide (LPS) from invading bacteria within the cytoplasm. Upon LPS binding via its N-terminal caspase recruitment domain (CARD), caspase‑11 oligomerizes and auto-processes to become catalytically active. Activated caspase‑11 cleaves gasdermin D, releasing its N-terminal fragment which forms pores in the plasma membrane—this process triggers pyroptosis, an inflammatory form of programmed cell death that helps eliminate infected cells but can also contribute to pathological inflammation such as sepsis if uncontrolled. Caspase‑11 is not constitutively expressed; it requires priming through pathogen or cytokine signaling pathways before it can be activated by LPS. Its function is analogous to human caspases 4 and 5, which mediate similar non-canonical inflammasome responses. While essential for defense against certain pathogens, dysregulated or excessive activation leads to detrimental effects including endotoxic shock due to widespread cell lysis and release of inflammatory mediators.

Other names

Casp4CASP-11Ich3Caspl