Cryopyrin activates the inflammasome in response to toxins and ATP

Nature

Volumn 440, Issue 7081, 2006, Pages 228-232

  Mariathasan, Sanjeev ^a   Weiss, David S ^b   Newton, Kim ^a   McBride, Jacqueline ^a   O'Rourke, Karen ^a   Roose Girma, Meron ^a   Lee, Wyne P ^a   Weinrauch, Yvette ^c   Monack, Denise M ^b   Dixit, Vishva M ^a  

^a GENENTECH INC   (United States)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL CULTURE; DISEASE CONTROL; GENES; PROTEINS;

CASPASE-1; CRYOPYRIN; INFLAMMASOME ACTIVATION;

ADENOSINETRIPHOSPHATE;

ADENOSINE TRIPHOSPHATE; CELL PROTEIN; CRYOPYRIN; CYTOKINE; INFLAMMASOME; INTERLEUKIN 18; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; MAITOTOXIN; NIGERICIN; POTASSIUM ION; PURINE P2X 7 RECEPTOR; PURINE P2X RECEPTOR; TOLL LIKE RECEPTOR; UNCLASSIFIED DRUG;

PROTEIN;

ANIMAL CELL; ARTICLE; AUTOINFLAMMATORY DISEASE; CONTROLLED STUDY; FRANCISELLA TULARENSIS; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; INNATE IMMUNITY; LISTERIA MONOCYTOGENES; MOUSE; MUCKLE WELLS SYNDROME; NONHUMAN; POTASSIUM CELL LEVEL; PRIORITY JOURNAL; SALMONELLA TYPHIMURIUM; STAPHYLOCOCCUS AUREUS;

ANIMALIA; FRANCISELLA TULARENSIS; LISTERIA MONOCYTOGENES; NEGIBACTERIA; POSIBACTERIA; SALMONELLA TYPHIMURIUM; STAPHYLOCOCCUS AUREUS;

EID: 32944470765     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature04515     Document Type: Article

References (25)

1. Mariathasan, S. et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 430, 213-218 (2004).
2. Martinon, F., Burns, K. & Tschopp, J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-β. Mol. Cell 10, 417-426 (2002).
3. Srinivasula, S. M. et al. The PYRIN-CARD protein ASC is an activating adaptor for caspase-1. J. Biol. Chem. 277, 21119-21122 (2002).
4. Wang, L. et al. PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-κB and caspase-1-dependent cytokine processing. J. Biol. Chem. 277, 29874-29880 (2002).
5. Agostini, L. et al. NALP3 forms an IL-1β-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder. Immunity 20, 319-325 (2004).
6. Dowds, T. A., Masumoto, J., Zhu, L., Inohara, N. & Nunez, G. Cryopyrin-induced interleukin 1β secretion in monocytic cells: enhanced activity of disease-associated mutants and requirement for ASC. J. Biol. Chem. 279, 21924-21928 (2004).
7. Ting, J. P. & Davis, B. K. CATERPILLER: a novel gene family important in immunity, cell death, and diseases. Annu. Rev. Immunol. 23, 387-414 (2005).
8. Perregaux, D. & Gabel, C. A. Interleukin-1β maturation and release in response to ATP and nigericin. Evidence that potassium depletion mediated by these agents is a necessary and common feature of their activity. J. Biol. Chem. 269, 15195-15203 (1994).
9. 7 receptors. J. Biol. Chem. 276, 125-132 (2001).
10. Hogquist, K. A., Nett, M. A., Unanue, E. R. & Chaplin, D. D. Interleukin 1 is processed and released during apoptosis. Proc. Natl Acad. Sci. USA 88, 8485-8489 (1991).
11. Yamamoto, M. et al. ASC is essential for LPS-induced activation of procaspase-1 independently of TLR-associated signal adaptor molecules. Genes Cells 9, 1055-1067 (2004).
12. Poltorak, A. et al. Defective LPS signalling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science 282, 2085-2088 (1998).
13. Wang, S. et al. Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE. Cell 92, 501-509 (1998).
14. 7 purinergic receptor stimulation activate a common cytolytic pore. Am. J. Physiol. 277, C766-C776 (1999).
15. Verhoef, P. A., Kertesy, S. B., Estacion, M., Schilling, W. P. & Dubyak, G. R. Maitotoxin induces biphasic interleukin-1β secretion and membrane blebbing in murine macrophages. Mol. Pharmacol. 66, 909-920 (2004).
16. Li, P. et al. Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock. Cell 80, 401-411 (1995).
17. Martinon, F., Agostini, L., Meylan, E. & Tschopp, J. Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome. Curr. Biol. 14, 1929-1934 (2004).
18. Girardin, S. E. et al. Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection. J. Biol. Chem. 278, 8869-8872 (2003).
19. Kobayashi, K. S. et al. Nod2-dependent regulation of innate and adaptive immunity in the intestinal tract. Science 307, 731-734 (2005).
20. Maeda, S. et al. Nod2 mutation in Crohn's disease potentiates NF-κB activity and IL-1beta processing. Science 307, 734-738 (2005).
21. Damiano, J. S., Newman, R. M. & Reed, J. C. Multiple roles of CLAN (caspase-associated recruitment domain, leucine-rich repeat, and NAIP CIIA HET-E, and TP1-containing protein) in the mammalian innate immune response. J. Immunol. 173, 6338-6345 (2004).
22. Hoffman, H. M., Mueller, J. L., Broide, D. H., Wanderer, A. A. & Kolodner, R. D. Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome. Nature Genet. 29, 301-305 (2001).
23. McDermott, M. F. Genetic clues to understanding periodic fevers, and possible therapies. Trends Mol. Med. 8, 550-554 (2002).
24. Feldmann, J. et al. Chronic infantile neurological cutaneous and articular syndrome is caused by mutations in CIAS1, a gene highly expressed in polymorphonuclear cells and chondrocytes. Am. J. Hum. Genet. 71, 198-203 (2002).
25. Aganna, E. et al. Association of mutations in the NALP3/CIAS1/PYPAF1 gene with a broad phenotype including recurrent fever, cold sensitivity, sensorineural deafness, and AA amyloidosis. Arthritis Rheum. 46, 2445-2452 (2002).