Journal
JOURNAL OF IMMUNOLOGY
Volume 187, Issue 5, Pages 2748-2754Publisher
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.1100477
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Funding
- National Institutes of Health [U54 AI57141, P50 HG02360]
- National Institute of General Medical Sciences Public Health Service [T32 G07270]
- Helen Riaboff Whiteley Fellowship
- Poncin and Achievement Rewards for College Scientist fellowships
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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-1b 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. The Journal of Immunology, 2011, 187: 2748-2754.
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