Access the full text.
Sign up today, get DeepDyve free for 14 days.
Ping Li, H. Allen, Subhashish Banerjee, S. Franklin, L. Herzog, C. Johnston, J. McDowell, M. Paskind, L. Rodman, J. Salfeld, Elizabeth Towne, D. Tracey, Scott Wardwell, F. Wei, W. Wong, R. Kamen, T. Seshadri (1995)
Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shockCell, 80
K. Hogquist, Michelle Nett, E. Unanue, D. Chaplin (1991)
Interleukin 1 is processed and released during apoptosis.Proceedings of the National Academy of Sciences of the United States of America, 88 19
J. Feldmann, A. Prieur, P. Quartier, P. Berquin, S. Certain, E. Cortis, D. Teillac-Hamel, A. Fischer, G. Basile (2002)
Chronic infantile neurological cutaneous and articular syndrome is caused by mutations in CIAS1, a gene highly expressed in polymorphonuclear cells and chondrocytes.American journal of human genetics, 71 1
Suyue Wang, M. Miura, Yong-Keun Jung, Hong Zhu, En Li, Junying Yuan (1998)
Murine Caspase-11, an ICE-Interacting Protease, Is Essential for the Activation of ICECell, 92
F. Martinon, K. Burns, J. Tschopp (2002)
The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta.Molecular cell, 10 2
Lin Wang, G. Manji, Jill Grenier, Amal Al-garawi, Sarah Merriam, J. Lora, B. Geddes, M. Briskin, P. Distefano, J. Bertin (2002)
PYPAF7, a Novel PYRIN-containing Apaf1-like Protein That Regulates Activation of NF-κB and Caspase-1-dependent Cytokine Processing*The Journal of Biological Chemistry, 277
Laetitia Agostini, F. Martinon, K. Burns, M. McDermott, P. Hawkins, J. Tschopp (2004)
NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder.Immunity, 20 3
W. Schilling, Tanya Wasylyna, G. Dubyak, B. Humphreys, W. Sinkins (1999)
Maitotoxin and P2Z/P2X7purinergic receptor stimulation activate a common cytolytic pore.American journal of physiology. Cell physiology, 277 4
J. Damiano, Ruchi Newman, John Reed (2004)
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 Response1The Journal of Immunology, 173
S. Girardin, I. Boneca, J. Viala, M. Chamaillard, A. Labigne, G. Thomas, D. Philpott, P. Sansonetti (2003)
Nod2 Is a General Sensor of Peptidoglycan through Muramyl Dipeptide (MDP) Detection*The Journal of Biological Chemistry, 278
Koichi Kobayashi, M. Chamaillard, Y. Ogura, O. Henegariu, N. Inohara, G. Núñez, R. Flavell (2005)
Nod2-Dependent Regulation of Innate and Adaptive Immunity in the Intestinal TractScience, 307
J. Ting, B. Davis (2005)
CATERPILLER: a novel gene family important in immunity, cell death, and diseases.Annual review of immunology, 23
S. Mariathasan, K. Newton, D. Monack, D. Vučić, D. French, Wyne Lee, M. Roose-Girma, S. Erickson, V. Dixit (2004)
Differential activation of the inflammasome by caspase-1 adaptors ASC and IpafNature, 430
H. Hoffman, James Mueller, D. Broide, A. Wanderer, R. Kolodner (2001)
Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle–Wells syndromeNature Genetics, 29
P. Verhoef, S. Kertesy, M. Estacion, W. Schilling, G. Dubyak (2004)
Maitotoxin induces biphasic interleukin-1beta secretion and membrane blebbing in murine macrophages.Molecular pharmacology, 66 4
D. Perregaux, C. Gabel (1994)
Interleukin-1 beta 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.The Journal of biological chemistry, 269 21
E. Aganna, F. Martinon, P. Hawkins, J. Ross, D. Swan, D. Booth, H. Lachmann, A. Bybee, Roxanne Gaudet, P. Woo, C. Feighery, F. Cotter, M. Thome, G. Hitman, J. Tschopp, M. McDermott (2002)
Association of mutations in the NALP3/CIAS1/PYPAF1 gene with a broad phenotype including recurrent fever, cold sensitivity, sensorineural deafness, and AA amyloidosis.Arthritis and rheumatism, 46 9
S. Srinivasula, J. Poyet, M. Razmara, P. Datta, Zhijia Zhang, E. Alnemri (2002)
The PYRIN-CARD Protein ASC Is an Activating Adaptor for Caspase-1*The Journal of Biological Chemistry, 277
T. Dowds, J. Masumoto, Li Zhu, N. Inohara, G. Núñez (2004)
Cryopyrin-induced interleukin 1beta secretion in monocytic cells: enhanced activity of disease-associated mutants and requirement for ASC.The Journal of biological chemistry, 279 21
S. Maeda, L. Hsu, Hongjun Liu, L. Bankston, M. Iimura, M. Kagnoff, L. Eckmann, M. Karin (2005)
Nod2 Mutation in Crohn's Disease Potentiates NF-κB Activity and IL-1ß ProcessingScience, 307
F. Martinon, Laetitia Agostini, E. Meylan, J. Tschopp (2004)
Identification of Bacterial Muramyl Dipeptide as Activator of the NALP3/Cryopyrin InflammasomeCurrent Biology, 14
M. McDermott (2002)
Genetic clues to understanding periodic fevers, and possible therapies.Trends in molecular medicine, 8 12
Michael Solle, J. Labasi, D. Perregaux, E. Stam, N. Petrushova, B. Koller, R. Griffiths, C. Gabel (2001)
Altered Cytokine Production in Mice Lacking P2X7Receptors*The Journal of Biological Chemistry, 276
A. Poltorak, Xiaolong He, I. Smirnova, Mu-ya Liu, C. Huffel, Xin Du, D. Birdwell, Erica Alejos, Maria Silva, C. Galanos, M. Freudenberg, P. Ricciardi-Castagnoli, Betsy Layton, B. Beutler (1998)
Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene.Science, 282 5396
Masatatsu Yamamoto, K. Yaginuma, H. Tsutsui, J. Sagara, Xin Guan, E. Seki, K. Yasuda, Masahiro Yamamoto, S. Akira, K. Nakanishi, T. Noda, S. Taniguchi (2004)
ASC is essential for LPS‐induced activation of procaspase‐1 independently of TLR‐associated signal adaptor moleculesGenes to Cells, 9
The inflammasome is a complex of proteins involved in the activation of the innate immune system, an evolutionarily ancient antimicrobial defence found in most multicelled animals. When activated the inflammasome sets in motion a cascade of events that leads to the production of active molecules including interleukins. Three papers in this issue report the identification of endogenous danger signals and bacterial components that activate inflammasomes containing cryopyrin (also known as NALP3). Mariathasan et al. show that cryopyrin activates the inflammasome in response to bacterial toxins and to ATP. Kanneganti et al. show that cryopyrin is activated by bacterial RNA and by the immune response modifiers R837 and R848. And Martinon et al. show that gout-associated uric acid crystals have a similar effect. In sum these results show that cryopyrin has a vital role in host antibacterial defences and may act as a sensor of cellular stress. In addition, this work provides insight into the mechanisms of autoinflammatory disorders in which abnormalities in the innate immune system have been implicated.
Nature – Springer Journals
Published: Jan 11, 2006
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.