Caspase 11

Caspase-11 is a murine inflammatory caspase that drives the noncanonical inflammasome response to cytosolic lipopolysaccharide (LPS) from Gram-negative bacteria^[1][2]. Mechanistically, activated caspase-11 cleaves gasdermin D (GSDMD), producing an N-terminal fragment that promotes pyroptosis, IL-1β maturation, and lethal LPS responses^[1]. In intestinal epithelial defense, caspase-11 deficiency increases Salmonella Typhimurium epithelial colonization, while human caspase-4 depletion similarly increases bacterial colonization in polarized epithelial monolayers^[3]. In kidney injury models, caspase-11/GSDMD signaling promotes tubular epithelial pyroptosis, urinary IL-18 excretion, renal functional deterioration, and podocyte injury under diabetic or acute injury conditions^[4][5]. Compared with canonical inflammasomes that activate caspase-1 through NLR or PYHIN sensors, caspase-11 and human caspase-4/5 act as noncanonical intracellular LPS sensors^[2][6]. For experimental applications, cardiolipin selectively blocks caspase-4/11-dependent cell death by preventing LPS binding, while maclurin suppresses caspase-11 and GSDMD activation in macrophages and improves acute lethal sepsis outcomes in mice^[7][8].