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- W2141621785 abstract "Abstract Activation of caspase-1 leads to pyroptosis, a program of cell death characterized by cell lysis and inflammatory cytokine release. Caspase-1 activation triggered by multiple nucleotide-binding oligomerization domain-like receptors (NLRs; NLRC4, NLRP1b, or NLRP3) leads to loss of lysosomes via their fusion with the cell surface, or lysosome exocytosis. Active caspase-1 increased cellular membrane permeability and intracellular calcium levels, which facilitated lysosome exocytosis and release of host antimicrobial factors and microbial products. Lysosome exocytosis has been proposed to mediate secretion of IL-1β and IL-18; however, blocking lysosome exocytosis did not alter cytokine processing or release. These studies indicate two conserved secretion pathways are initiated by caspase-1, lysosome exocytosis, and a parallel pathway resulting in cytokine release, and both enhance the antimicrobial nature of pyroptosis." @default.
- W2141621785 created "2016-06-24" @default.
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- W2141621785 date "2011-09-01" @default.
- W2141621785 modified "2023-10-12" @default.
- W2141621785 title "Coordinated Host Responses during Pyroptosis: Caspase-1–Dependent Lysosome Exocytosis and Inflammatory Cytokine Maturation" @default.
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- W2141621785 doi "https://doi.org/10.4049/jimmunol.1100477" @default.
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