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Gene Review

Nlrp3  -  NLR family, pyrin domain containing 3

Mus musculus

Synonyms: AGTAVPRL, AII/AVP, Cias1, Cold autoinflammatory syndrome 1 protein homolog, Cryopyrin, ...
 
 
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Disease relevance of Nlrp3

 

High impact information on Nlrp3

  • Here, we demonstrate the effect of NALP3 deficiency on caspase-1 function [1].
  • An in vitro culture of Plasmodium falciparum (isolate FCUP-1/RSA) was arrested in the trophozoite stage with alpha-difluoromethylornithine (DFMO), followed by sorbitol treatment to liberate intracellular parasites from infected erythrocytes [4].
  • The spatiotemporal expression pattern of the FGF10 and FGFR2 genes in human embryos and the reported phenotypes of knockout mice for these genes spurred us to examine their coding sequences in our two cases of MWS [5].
  • Therefore, cryopyrin is essential for inflammasome activation in response to signalling pathways triggered specifically by ATP, nigericin, maitotoxin, S. aureus or L. monocytogenes [6].
  • In contrast, secretion of tumour-necrosis factor-alpha and IL-6, as well as activation of NF-kappaB and mitogen-activated protein kinases (MAPKs) were unaffected by cryopyrin deficiency [7].
 

Associations of Nlrp3 with chemical compounds

  • Gout-associated uric acid crystals activate the NALP3 inflammasome [8].
 

Regulatory relationships of Nlrp3

  • Furthermore, we show that Toll-like receptors and cryopyrin control the secretion of IL-1beta and IL-18 through different intracellular pathways [7].
 

Other interactions of Nlrp3

  • Activating mutations in cryopyrin are associated with familial cold autoinflammatory syndrome, Muckle-Wells syndrome and neonatal onset multisystem inflammatory disease, diseases that are characterized by excessive production of IL-1beta [6].
  • These results provide evidence for cytosolic delivery and sensing of bacterial molecules as a unifying model for caspase-1 activation and position pannexin-1 as a mechanistic link between bacterial stimuli and the cryopyrin inflammasome [9].

References

  1. Critical role for NALP3/CIAS1/Cryopyrin in innate and adaptive immunity through its regulation of caspase-1. Sutterwala, F.S., Ogura, Y., Szczepanik, M., Lara-Tejero, M., Lichtenberger, G.S., Grant, E.P., Bertin, J., Coyle, A.J., Galán, J.E., Askenase, P.W., Flavell, R.A. Immunity (2006) [Pubmed]
  2. IL-1 beta breaks tolerance through expansion of CD25+ effector T cells. O'Sullivan, B.J., Thomas, H.E., Pai, S., Santamaria, P., Iwakura, Y., Steptoe, R.J., Kay, T.W., Thomas, R. J. Immunol. (2006) [Pubmed]
  3. Induction of PYPAF1 during in vitro maturation of mouse mast cells. Kikuchi-Yanoshita, R., Taketomi, Y., Koga, K., Sugiki, T., Atsumi, Y., Saito, T., Ishii, S., Hisada, M., Suzuki-Nishimura, T., Uchida, M.K., Moon, T.C., Chang, H.W., Sawada, M., Inagaki, N., Nagai, H., Murakami, M., Kudo, I. J. Biochem. (2003) [Pubmed]
  4. Plasmodium falciparum: isolation of intact and erythrocyte-free trophozoites from sorbitol lysates. Hoppe, H.C., Coetzee, J., Louw, A.I. Parasitology (1992) [Pubmed]
  5. Matthew-Wood syndrome: Report of two new cases supporting autosomal recessive inheritance and exclusion of FGF10 and FGFR2. Martinovic-Bouriel, J., Bernabé-Dupont, C., Golzio, C., Grattagliano-Bessières, B., Malan, V., Bonnière, M., Esculpavit, C., Fallet-Bianco, C., Mirlesse, V., Le Bidois, J., Aubry, M.C., Vekemans, M., Morichon, N., Etchevers, H., Attié-Bitach, T., Encha-Razavi, F., Benachi, A. Am. J. Med. Genet. A (2007) [Pubmed]
  6. Cryopyrin activates the inflammasome in response to toxins and ATP. Mariathasan, S., Weiss, D.S., Newton, K., McBride, J., O'Rourke, K., Roose-Girma, M., Lee, W.P., Weinrauch, Y., Monack, D.M., Dixit, V.M. Nature (2006) [Pubmed]
  7. Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3. Kanneganti, T.D., Ozören, N., Body-Malapel, M., Amer, A., Park, J.H., Franchi, L., Whitfield, J., Barchet, W., Colonna, M., Vandenabeele, P., Bertin, J., Coyle, A., Grant, E.P., Akira, S., Núñez, G. Nature (2006) [Pubmed]
  8. Gout-associated uric acid crystals activate the NALP3 inflammasome. Martinon, F., Pétrilli, V., Mayor, A., Tardivel, A., Tschopp, J. Nature (2006) [Pubmed]
  9. Pannexin-1-mediated recognition of bacterial molecules activates the cryopyrin inflammasome independent of Toll-like receptor signaling. Kanneganti, T.D., Lamkanfi, M., Kim, Y.G., Chen, G., Park, J.H., Franchi, L., Vandenabeele, P., Núñez, G. Immunity (2007) [Pubmed]
 
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