We are analyzing https://link.springer.com/article/10.1007/s00018-016-2205-2.

Title:
The intersection of cell death and inflammasome activation | Cellular and Molecular Life Sciences
Description:
Inflammasomes sense cellular danger to activate the cysteine-aspartic protease caspase-1, which processes precursor interleukin-1β (IL-1β) and IL-18 into their mature bioactive fragments. In addition, activated caspase-1 or the related inflammatory caspase, caspase-11, can cleave gasdermin D to induce a lytic cell death, termed pyroptosis. The intertwining of IL-1β activation and cell death is further highlighted by research showing that the extrinsic apoptotic caspase, caspase-8, may, like caspase-1, directly process IL-1β, activate the NLRP3 inflammasome itself, or bind to inflammasome complexes to induce apoptotic cell death. Similarly, RIPK3- and MLKL-dependent necroptotic signaling can activate the NLRP3 inflammasome to drive IL-1β inflammatory responses in vivo. Here, we review the mechanisms by which cell death signaling activates inflammasomes to initiate IL-1β-driven inflammation, and highlight the clinical relevance of these findings to heritable autoinflammatory diseases. We also discuss whether the act of cell death can be separated from IL-1β secretion and evaluate studies suggesting that several cell death regulatory proteins can directly interact with, and modulate the function of, inflammasome and IL-1β containing protein complexes.
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28 years and 1 months (reg. 1997-05-29).

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Keywords {🔍}

pubmed, google, scholar, article, cas, central, inflammasome, cell, activation, caspase, nlrp, immunol, death, nature, nat, apoptosis, doinature, doijimmunol, silke, ilbeta, vince, fitzgerald, chen, signaling, zhang, immunity, sci, wang, inflammasomes, huang, usa, inflammation, secretion, doini, proc, natl, acad, yang, protein, mice, rep, kaiser, mocarski, doipnas, processing, inflammatory, pyroptosis, immune, role, doijcell,

Topics {✒️}

pro-interleukin-1beta protein complexes initiate il-1β-driven inflammation month download article/chapter inflammasome-independent il-1beta production rip1-rip3-drp1 signaling pathway real-time single-cell imaging mavs-induced membrane permeabilization tnf-induced keratinocyte apoptosis mlkl-dependent necroptotic signaling rh domain-interacting protein multi-system autoinflammatory disorder nf-kappab signalling tnf-r1 signaling complex mediates noncanonical il-1beta francisella-infected caspase-1-deficient macrophages rip3-mediated macrophage necrosis calcium-sensing receptor regulates metabolite-sensing receptor gpr43 processes precursor interleukin-1β produce mature il-1beta modulate il-1beta production metabolite-sensing receptors gpr43 microbiota-modulated metabolites shape rip3-dependent cell death pro-interleukin-1beta regulates immune signalling vince & john silke tnf-mediated gene induction cysteine-aspartic protease caspase-1 directly process il-1β full article pdf caspase-1-dependent mitochondrial damage autophagy-mediated secretion il-1beta production shigella-induced apoptosis caspase-1-deficient mice infected cytoplasmic lps recognition interleukin-1beta secretion innate immune receptors caspase-1-dependent pore formation caspase-8-induced il-1 innate immune defense promotes inflammasome activation tlr4-independent endotoxic shock toxin-induced necroptosis il-1beta secretion nf-kappab skin inflammation independently innate immune response adaptor asc acts

Questions {❓}

Lawlor KE, Vince JE (2014) Ambiguities in NLRP3 inflammasome regulation: is there a role for mitochondria?

Schema {🗺️}

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         headline:The intersection of cell death and inflammasome activation
         description:Inflammasomes sense cellular danger to activate the cysteine-aspartic protease caspase-1, which processes precursor interleukin-1β (IL-1β) and IL-18 into their mature bioactive fragments. In addition, activated caspase-1 or the related inflammatory caspase, caspase-11, can cleave gasdermin D to induce a lytic cell death, termed pyroptosis. The intertwining of IL-1β activation and cell death is further highlighted by research showing that the extrinsic apoptotic caspase, caspase-8, may, like caspase-1, directly process IL-1β, activate the NLRP3 inflammasome itself, or bind to inflammasome complexes to induce apoptotic cell death. Similarly, RIPK3- and MLKL-dependent necroptotic signaling can activate the NLRP3 inflammasome to drive IL-1β inflammatory responses in vivo. Here, we review the mechanisms by which cell death signaling activates inflammasomes to initiate IL-1β-driven inflammation, and highlight the clinical relevance of these findings to heritable autoinflammatory diseases. We also discuss whether the act of cell death can be separated from IL-1β secretion and evaluate studies suggesting that several cell death regulatory proteins can directly interact with, and modulate the function of, inflammasome and IL-1β containing protein complexes.
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