Journal
JOURNAL OF IMMUNOLOGY
Volume 173, Issue 10, Pages 6338-6345Publisher
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.173.10.6338
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Funding
- NIAID NIH HHS [AI 56324] Funding Source: Medline
- NIA NIH HHS [5T32 AG 00252-06] Funding Source: Medline
- NIGMS NIH HHS [GM 61694] Funding Source: Medline
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NAIP CIIA HET-E and TP1 (NACHT) family proteins are involved in sensing intracellfilar pathogens or pathogen-derived molecules, triggering host defense responses resulting in caspase-mediated processing of proinflammatory cytokines and NF-kappaB activation. Caspase-associated recruitment domain, leucine-rich repeat, and NACHT-containing protein (CLAN), also known as ICE protease-activating factor, belongs to a branch of the NACHT family that contains proteins carrying caspase-associated recruitment domains (CARDs) and leucine-rich repeats (LRRs). By using gene transfer and RNA-interference approaches, we demonstrate in this study that CLAN modulates endogenous caspase-1 activation and subsequent IL-1beta secretion from human macrophages after exposure to LPS, peptidoglycan, and pathogenic bacteria. CLAN was also found to mediate a direct antibacterial effect within macrophages after Salmonella infection and to sensitize host cells to Salmonella-induced cell death through a caspase-1-independent mechanism. These results indicate that CLAN contributes to several biological processes central to host defense, suggesting a prominent role for this NACHT family member in innate immunity.
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