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obesity-associated NLRC4 inflammasome activation/ interleukin-1 signalling promotes breast cancer progression in humans and in mouse models
this study shows that human NAIP (show NAIP Proteins)-NLRC4-inflammasome senses the Pseudomonas aeruginosa T3SS inner-rod protein
mRNA expression levels of NLRP1 and NLRC4 were not altered in chronic hepatitis B patients, suggesting that these genes are not responsible for the impaired immune responses against HBV observed in these patients.
The authors describe a novel mutation in NLRC4 in a large pedigree causing an NLRC4-associated, partially anakinra-responsive AID, dominated by cutaneous erythematous nodes and urticarial rash, arthralgias, and late-onset enterocolitis.
Results found that NLRC4 expression increased in for promoting DN progression and demonstrate NLRC4-driven IL-1beta (show IL1B Proteins) production as critical for the progression of DN.
Ubiquitin-tagged NLRC4 could induce cell death and activate caspase-8 (show CASP8 Proteins) independent of Ser (show SIGLEC1 Proteins)(533) phosphorylation. Our
LPS (show IRF6 Proteins) activates the MAPK (show MAPK1 Proteins) pathway in macrophages, thus resulting in the upregulation of NLRC4; however, NLRC4 inhibits IL1beta (show IL1B Proteins) and IL18 (show IL18 Proteins) production, contributing to the anti-inflammatory response.
High expression of NLRP3 (show NLRP3 Proteins), NLRC4, and CASP1 (show CASP1 Proteins) in background non-tumorous liver is significantly correlated with poor prognosis of patients after resection of hepatocellular carcinoma.
association of IL-18 (show IL18 Proteins) levels with a single nucleotide polymorphism in the untranslated exon 2 of the inflammasome component NLRC4
While both contributing to pathogen clearance, NLRP3 (show NLRP3 Proteins) more than NLRC4 contributes to deleterious inflammatory responses in cystic fibrosis (show S100A8 Proteins) and correlates with defective NLRC4-dependent IL-1Ra (show IL1RN Proteins) production.
Specific NLRC4 activation in Mrp8 (show S100A8 Proteins) (+) cells (primarily neutrophil lineage) is sufficient to cause severe inflammatory disease.
data provide evidence that the NLRC4 inflammasome contributes to resistance through regulation of caspase-1 (show CASP1 Proteins), IL-1beta (show IL1B Proteins) and IL-18 (show IL18 Proteins) in a CD11blowLy6Glow population of cells
NLRC4 expression controls melanoma tumor growth.
The interplay between NLRP3 (show NLRP3 Proteins) and NLRC4 reveals an unexpected overlap between what had been considered distinct inflammasome scaffolds.
The activation of NLRC4 by flagellin (show FliC Proteins) downregulated the flagellin (show FliC Proteins)-induced and TLR5 (show TLR5 Proteins)-mediated immune responses against flagellin (show FliC Proteins).
TLR5 (show TLR5 Proteins) but not NLRC4 is required for S. pneumoniae FliC (show FliC Proteins)-induced protection.
Data indicate that NLRC4 activation in Intestinal epithelial cells (IECs) leads to cell expulsion and IL-18 (show IL18 Proteins) release, and implicate Caspase-8 (show CASP8 Proteins) in NLRC4 inflammasome responses in vivo by generation of doubly deficient in Caspase-1 (show CASP1 Proteins) and Caspase-8 (show CASP8 Proteins).
The tick protein sialostatin L2 binds to annexin A2 (show ANXA2 Proteins) and inhibits NLRC4-mediated inflammasome activation.
LPS (show TLR4 Proteins) activates the MAPK (show MAPK1 Proteins) pathway in macrophages, thus resulting in the upregulation of NLRC4; however, NLRC4 inhibits IL1beta (show IL1B Proteins) and IL18 (show IL18 Proteins) production, contributing to the anti-inflammatory response.
In C. elegans, Ced4 binds and activates Ced3, an apoptotic initiator caspase, via caspase-associated recruitment domains (CARDs). Human Ced4 homologs include APAF1 (MIM 602233), NOD1/CARD4 (MIM 605980), and NOD2/CARD15 (MIM 605956). These proteins have at least 1 N-terminal CARD domain followed by a centrally located nucleotide-binding domain (NBD or NACHT) and a C-terminal regulatory domain, found only in mammals, that contains either WD40 repeats or leucine-rich repeats (LRRs). CARD12 is a member of the Ced4 family and can induce apoptosis.
caspase recruitment domain protein 12
, NLR family CARD domain-containing protein 4
, ice protease-activating factor
, NLR family, CARD domain containing 4
, CARD, LRR, and NACHT-containing protein
, ICE-protease activating factor
, NOD-like receptor C4
, caspase recruitment domain family, member 12
, caspase recruitment domain-containing protein 12
, nucleotide-binding oligomerization domain, leucine rich repeat and CARD domain containing 4