Biglycan: A danger signal that activates the NLRP3 inflammasome via toll-like and P2X receptors
Andrea Babelova,Kristin Moreth,Kristin Moreth,Wasiliki Tsalastra-Greul,Jinyang Zeng-Brouwers,Jinyang Zeng-Brouwers,Oliver Eickelberg,Marian F. Young,Peter Bruckner,Josef Pfeilschifter,Roland M. Schaefer,Hermann Josef Gröne,Liliana Schaefer +12 more
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TLDR
The results provide evidence for direct activation of the NLRP3 inflammasome by biglycan and describe a fundamental paradigm of how tissue stress or injury is monitored by innate immune receptors detecting the release of the extracellular matrix components and turning such a signal into a robust inflammatory response.About:
This article is published in Journal of Biological Chemistry.The article was published on 2009-09-04 and is currently open access. It has received 424 citations till now. The article focuses on the topics: Biglycan & Inflammasome.read more
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Sterile inflammation: sensing and reacting to damage
Grace Y. Chen,Gabriel Núñez +1 more
TL;DR: The triggers and receptor pathways that result in sterile inflammation and its impact on human health are reviewed.
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The NLRP3 inflammasome: molecular activation and regulation to therapeutics
TL;DR: The NLRP3 inflammasome mediates pro-inflammatory responses and pyroptotic cell death and how it is being targeted to treat inflammatory diseases is described.
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Extracellular matrix structure.
TL;DR: The complex ECM structure is emphasized as to provide a better understanding of its dynamic structural and functional multipotency and the implication of the various families of ECM macromolecules in health and disease is presented.
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Proteoglycan form and function: A comprehensive nomenclature of proteoglycans
Renato V. Iozzo,Liliana Schaefer +1 more
TL;DR: The proposed nomenclature encompasses forty-three distinct proteoglycan-encoding genes and many alternatively-spliced variants and is based on three criteria: Cellular and subcellular location, overall gene/protein homology, and the utilization of specific protein modules within their respective protein cores.
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DAMPening Inflammation by Modulating TLR Signalling
Anna M. Piccinini,Kim S. Midwood +1 more
TL;DR: The current knowledge about distinct signalling cascades resulting from self TLR activation is explored and the involvement of endogenous TLR activators in disease is discussed to highlight how specifically targeting DAMPs may yield therapies that do not globally suppress the immune system.
References
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Defective LPS Signaling in C3H/HeJ and C57BL/10ScCr Mice: Mutations in Tlr4 Gene
Alexander Poltorak,Xiaolong He,Irina Smirnova,Mu Ya Liu,Christophe Van Huffel,Xin Du,Dale Birdwell,E. Alejos,M. Silva,Chris Galanos,Marina Freudenberg,Paola Ricciardi-Castagnoli,Betsy Layton,Bruce Beutler +13 more
TL;DR: The mammalian Tlr4 protein has been adapted primarily to subserve the recognition of LPS and presumably transduces the LPS signal across the plasma membrane.
Journal Article
Defective LPS signaling in C3 H/HeJ and C57 BL/10 ScCr mice: Mutations in Tlr4 Gene
Alexander Poltorak,Xiaolong He,Irina Smirnova,Mu Ya Liu,C. Van Huffel,Xin Du,Dale Birdwell,E. Alejos,M. Suva,Chris Galanos,Marina Freudenberg,Paola Ricciardi-Castagnoli,B. Layton,Bruce Beutler +13 more
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Origin and Physiological Roles of Inflammation
TL;DR: This work has shown that tissue stress or malfunction induces an adaptive response that is intermediate between the basal homeostatic state and a classic inflammatory response, which is referred to here as para-inflammation.
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Gout-associated uric acid crystals activate the NALP3 inflammasome
TL;DR: It is shown that MSU and CPPD engage the caspase-1-activating NALP3 (also called cryopyrin) inflammasome, resulting in the production of active interleukin (IL)-1β and IL-18 in mice deficient in the IL-1β receptor.
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Cryopyrin activates the inflammasome in response to toxins and ATP
Sanjeev Mariathasan,David S. Weiss,Kim Newton,Jacqueline McBride,Karen O'Rourke,Meron Roose-Girma,Wyne P. Lee,Yvette Weinrauch,Denise M. Monack,Vishva M. Dixit +9 more
TL;DR: It is shown that cryopyrin-deficient macrophages cannot activate caspase-1 in response to Toll-like receptor agonists plus ATP, the latter activating the P2X7 receptor to decrease intracellular K+ levels.