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NLRP3 inflammasome: from a danger signal sensor to a regulatory node of oxidative stress and inflammatory diseases.

Abderrazak A, Syrovets T, Couchie D, El Hadri K, Friguet B, Simmet T, Rouis M - Redox Biol (2015)

Bottom Line: We have reported mutations in NLRP3 that were found to be associated with certain diseases.In addition, we have reviewed the functional link between NLRP3 inflammasome, the regulator of cellular redox status Trx/TXNIP complex, endoplasmic reticulum stress and the pathogenesis of diseases such as type 2 diabetes.Finally, we have provided data on NLRP3 inflammasome, as a critical regulator involved in the pathogenesis of obesity and cardiovascular diseases.

View Article: PubMed Central - PubMed

Affiliation: Sorbonne Universités, UPMC Univ Paris 06, UMR 8256, Biological Adaptation and Ageing - IBPS, F-75005 Paris, France; CNRS-UMR 8256, F-75005 Paris, France; Inserm U1164, F-75005 Paris, France.

No MeSH data available.


Related in: MedlinePlus

NLRP3 inflammasome assembly. CARD, caspase recruitment domain; LRR, leucine-rich repeat; NACHT/NBD, nucleotide binding domain; PYD, pyrin domain; CAP1, caspase-1.
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f0005: NLRP3 inflammasome assembly. CARD, caspase recruitment domain; LRR, leucine-rich repeat; NACHT/NBD, nucleotide binding domain; PYD, pyrin domain; CAP1, caspase-1.

Mentions: To this end, many studies have contributed very valuable insights. It is known that only stimulated cells activate NLRP3, which has a tripartite structure consisting of a pyrin domain (PYD), a nucleotide-binding domain (NBD) and a leucine-rich-repeat (LRR) domain [9]. Upon activation, NLRP3 associates with the adaptor protein ASC, which comprises a caspase recruitment domain (CARD) and a pyrin domain, that are held together solely by a semi-flexible linker [10] allowing both domains to engage freely with other partners. The NLRP3:ASC complex oligomerizes and binds the enzyme caspase 1, thus forming active inflammasome complexes (NLRP3, ASC, and caspase-1) that produce IL1-β [11] (Fig. 1).


NLRP3 inflammasome: from a danger signal sensor to a regulatory node of oxidative stress and inflammatory diseases.

Abderrazak A, Syrovets T, Couchie D, El Hadri K, Friguet B, Simmet T, Rouis M - Redox Biol (2015)

NLRP3 inflammasome assembly. CARD, caspase recruitment domain; LRR, leucine-rich repeat; NACHT/NBD, nucleotide binding domain; PYD, pyrin domain; CAP1, caspase-1.
© Copyright Policy - CC BY-NC-ND
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4315937&req=5

f0005: NLRP3 inflammasome assembly. CARD, caspase recruitment domain; LRR, leucine-rich repeat; NACHT/NBD, nucleotide binding domain; PYD, pyrin domain; CAP1, caspase-1.
Mentions: To this end, many studies have contributed very valuable insights. It is known that only stimulated cells activate NLRP3, which has a tripartite structure consisting of a pyrin domain (PYD), a nucleotide-binding domain (NBD) and a leucine-rich-repeat (LRR) domain [9]. Upon activation, NLRP3 associates with the adaptor protein ASC, which comprises a caspase recruitment domain (CARD) and a pyrin domain, that are held together solely by a semi-flexible linker [10] allowing both domains to engage freely with other partners. The NLRP3:ASC complex oligomerizes and binds the enzyme caspase 1, thus forming active inflammasome complexes (NLRP3, ASC, and caspase-1) that produce IL1-β [11] (Fig. 1).

Bottom Line: We have reported mutations in NLRP3 that were found to be associated with certain diseases.In addition, we have reviewed the functional link between NLRP3 inflammasome, the regulator of cellular redox status Trx/TXNIP complex, endoplasmic reticulum stress and the pathogenesis of diseases such as type 2 diabetes.Finally, we have provided data on NLRP3 inflammasome, as a critical regulator involved in the pathogenesis of obesity and cardiovascular diseases.

View Article: PubMed Central - PubMed

Affiliation: Sorbonne Universités, UPMC Univ Paris 06, UMR 8256, Biological Adaptation and Ageing - IBPS, F-75005 Paris, France; CNRS-UMR 8256, F-75005 Paris, France; Inserm U1164, F-75005 Paris, France.

No MeSH data available.


Related in: MedlinePlus