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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: A vast interest has created to unravel how NLRP3 becomes activated, since mechanistic insight is the prerequisite for a knowledge-based development of therapeutic intervention strategies that specifically target the NLRP3 triggered IL-1β production.We have reported mutations in NLRP3 that were found to be associated with certain diseases.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: A vast interest has created to unravel how NLRP3 becomes activated, since mechanistic insight is the prerequisite for a knowledge-based development of therapeutic intervention strategies that specifically target the NLRP3 triggered IL-1β production.We have reported mutations in NLRP3 that were found to be associated with certain diseases.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