Inhibitor of Apoptosis Proteins Limit RIP3 Kinase-Dependent Interleukin-1 Activation
Interleukin-1β (IL-1β) is a potent inflammatory cytokine that is usually cleaved and activated by inflammasome-associated caspase-1. To determine whether IL-1β activation is regulated by inhibitor of apoptosis (IAP) proteins, we treated macrophages with an IAP-antagonist “Smac mimetic” compound or g...
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| Veröffentlicht in: | Immunity (Cambridge, Mass.) Mass.), 2012-02, Vol.36 (2), p.215-227 |
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| creator | Vince, James E. Wong, W. Wei-Lynn Gentle, Ian Lawlor, Kate E. Allam, Ramanjaneyulu O'Reilly, Lorraine Mason, Kylie Gross, Olaf Ma, Stephen Guarda, Greta Anderton, Holly Castillo, Rosa Häcker, Georg Silke, John Tschopp, Jürg |
| description | Interleukin-1β (IL-1β) is a potent inflammatory cytokine that is usually cleaved and activated by inflammasome-associated caspase-1. To determine whether IL-1β activation is regulated by inhibitor of apoptosis (IAP) proteins, we treated macrophages with an IAP-antagonist “Smac mimetic” compound or genetically deleted the genes that encode the three IAP family members cIAP1, cIAP2, and XIAP. After Toll-like receptor priming, IAP inhibition triggered cleavage of IL-1β that was mediated not only by the NLRP3-caspase-1 inflammasome, but also by caspase-8 in a caspase-1-independent manner. In the absence of IAPs, rapid and full generation of active IL-1β by the NLRP3-caspase-1 inflammasome, or by caspase-8, required the kinase RIP3 and reactive oxygen species production. These results demonstrate that activation of the cell death-inducing ripoptosome platform and RIP3 can generate bioactive IL-1β and implicate them as additional targets for the treatment of pathological IL-1-driven inflammatory responses.
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► IAP inhibition induces NLRP3 inflammasome-dependent and -independent IL-1 activation ► Genetic deletion of the three IAPs (cIAP1, cIAP2, XIAP) activates IL-1 ► Inflammasome-independent IL-1 maturation is mediated by caspase-8 cleavage ► RIP3 signaling, and not cell death, activates IL-1 |
| doi_str_mv | 10.1016/j.immuni.2012.01.012 |
| format | Article |
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[Display omitted]
► IAP inhibition induces NLRP3 inflammasome-dependent and -independent IL-1 activation ► Genetic deletion of the three IAPs (cIAP1, cIAP2, XIAP) activates IL-1 ► Inflammasome-independent IL-1 maturation is mediated by caspase-8 cleavage ► RIP3 signaling, and not cell death, activates IL-1</description><identifier>ISSN: 1074-7613</identifier><identifier>EISSN: 1097-4180</identifier><identifier>DOI: 10.1016/j.immuni.2012.01.012</identifier><identifier>PMID: 22365665</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Apoptosis ; Baculoviral IAP Repeat-Containing 3 Protein ; Carrier Proteins - agonists ; Carrier Proteins - metabolism ; Caspase 1 - metabolism ; Caspase-1 ; Caspase-8 ; Cell activation ; DIABLO protein ; IAP protein ; Immune system ; Inflammasomes - immunology ; Inflammasomes - metabolism ; Inflammation ; Inhibitor of Apoptosis Proteins - antagonists & inhibitors ; Inhibitor of Apoptosis Proteins - deficiency ; Inhibitor of Apoptosis Proteins - genetics ; Inhibitor of Apoptosis Proteins - metabolism ; Interleukin 1 ; Interleukin-1beta - metabolism ; Macrophages ; Macrophages - cytology ; Macrophages - drug effects ; Macrophages - immunology ; Macrophages - metabolism ; Mammals ; Membranes ; Mice ; Mice, Knockout ; Mitochondrial Proteins - agonists ; Molecular Mimicry ; NLR Family, Pyrin Domain-Containing 3 Protein ; Proteins ; Reactive oxygen species ; Reactive Oxygen Species - metabolism ; Receptor-Interacting Protein Serine-Threonine Kinases - metabolism ; Toll-like receptors ; Ubiquitin-Protein Ligases ; X-Linked Inhibitor of Apoptosis Protein - deficiency ; X-Linked Inhibitor of Apoptosis Protein - genetics ; X-Linked Inhibitor of Apoptosis Protein - metabolism ; XIAP protein</subject><ispartof>Immunity (Cambridge, Mass.), 2012-02, Vol.36 (2), p.215-227</ispartof><rights>2012 Elsevier Inc.</rights><rights>Copyright © 2012 Elsevier Inc. All rights reserved.</rights><rights>Copyright Elsevier Limited Feb 24, 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c585t-2abf9a9989c3e172ffcfa8bc92e006250bec095c984a57ca8e4f0e9dce77c6753</citedby><cites>FETCH-LOGICAL-c585t-2abf9a9989c3e172ffcfa8bc92e006250bec095c984a57ca8e4f0e9dce77c6753</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.immuni.2012.01.012$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22365665$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vince, James E.</creatorcontrib><creatorcontrib>Wong, W. Wei-Lynn</creatorcontrib><creatorcontrib>Gentle, Ian</creatorcontrib><creatorcontrib>Lawlor, Kate E.</creatorcontrib><creatorcontrib>Allam, Ramanjaneyulu</creatorcontrib><creatorcontrib>O'Reilly, Lorraine</creatorcontrib><creatorcontrib>Mason, Kylie</creatorcontrib><creatorcontrib>Gross, Olaf</creatorcontrib><creatorcontrib>Ma, Stephen</creatorcontrib><creatorcontrib>Guarda, Greta</creatorcontrib><creatorcontrib>Anderton, Holly</creatorcontrib><creatorcontrib>Castillo, Rosa</creatorcontrib><creatorcontrib>Häcker, Georg</creatorcontrib><creatorcontrib>Silke, John</creatorcontrib><creatorcontrib>Tschopp, Jürg</creatorcontrib><title>Inhibitor of Apoptosis Proteins Limit RIP3 Kinase-Dependent Interleukin-1 Activation</title><title>Immunity (Cambridge, Mass.)</title><addtitle>Immunity</addtitle><description>Interleukin-1β (IL-1β) is a potent inflammatory cytokine that is usually cleaved and activated by inflammasome-associated caspase-1. To determine whether IL-1β activation is regulated by inhibitor of apoptosis (IAP) proteins, we treated macrophages with an IAP-antagonist “Smac mimetic” compound or genetically deleted the genes that encode the three IAP family members cIAP1, cIAP2, and XIAP. After Toll-like receptor priming, IAP inhibition triggered cleavage of IL-1β that was mediated not only by the NLRP3-caspase-1 inflammasome, but also by caspase-8 in a caspase-1-independent manner. In the absence of IAPs, rapid and full generation of active IL-1β by the NLRP3-caspase-1 inflammasome, or by caspase-8, required the kinase RIP3 and reactive oxygen species production. These results demonstrate that activation of the cell death-inducing ripoptosome platform and RIP3 can generate bioactive IL-1β and implicate them as additional targets for the treatment of pathological IL-1-driven inflammatory responses.
[Display omitted]
► IAP inhibition induces NLRP3 inflammasome-dependent and -independent IL-1 activation ► Genetic deletion of the three IAPs (cIAP1, cIAP2, XIAP) activates IL-1 ► Inflammasome-independent IL-1 maturation is mediated by caspase-8 cleavage ► RIP3 signaling, and not cell death, activates IL-1</description><subject>Animals</subject><subject>Apoptosis</subject><subject>Baculoviral IAP Repeat-Containing 3 Protein</subject><subject>Carrier Proteins - agonists</subject><subject>Carrier Proteins - metabolism</subject><subject>Caspase 1 - metabolism</subject><subject>Caspase-1</subject><subject>Caspase-8</subject><subject>Cell activation</subject><subject>DIABLO protein</subject><subject>IAP protein</subject><subject>Immune system</subject><subject>Inflammasomes - immunology</subject><subject>Inflammasomes - metabolism</subject><subject>Inflammation</subject><subject>Inhibitor of Apoptosis Proteins - antagonists & inhibitors</subject><subject>Inhibitor of Apoptosis Proteins - deficiency</subject><subject>Inhibitor of Apoptosis Proteins - genetics</subject><subject>Inhibitor of Apoptosis Proteins - metabolism</subject><subject>Interleukin 1</subject><subject>Interleukin-1beta - metabolism</subject><subject>Macrophages</subject><subject>Macrophages - cytology</subject><subject>Macrophages - drug effects</subject><subject>Macrophages - immunology</subject><subject>Macrophages - metabolism</subject><subject>Mammals</subject><subject>Membranes</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Mitochondrial Proteins - agonists</subject><subject>Molecular Mimicry</subject><subject>NLR Family, Pyrin Domain-Containing 3 Protein</subject><subject>Proteins</subject><subject>Reactive oxygen species</subject><subject>Reactive Oxygen Species - metabolism</subject><subject>Receptor-Interacting Protein Serine-Threonine Kinases - metabolism</subject><subject>Toll-like receptors</subject><subject>Ubiquitin-Protein Ligases</subject><subject>X-Linked Inhibitor of Apoptosis Protein - deficiency</subject><subject>X-Linked Inhibitor of Apoptosis Protein - genetics</subject><subject>X-Linked Inhibitor of Apoptosis Protein - metabolism</subject><subject>XIAP protein</subject><issn>1074-7613</issn><issn>1097-4180</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU9r3DAQxUVoyb_2G4Ri6CG5eCvJkmVdCkvapEsXGkp6FrI8JrNdS64kB_rta7NJDj0EBmYOv3nDvEfIBaMrRln9abfCYZg8rjhlfEXZXPyInDKqVSlYQ98ssxKlqll1Qs5S2lHKhNT0mJxwXtWyruUpud_4B2wxh1iEvliPYcwhYSruYsiAPhVbHDAXPzd3VfEdvU1QfoERfAc-FxufIe5h-o2-ZMXaZXy0GYN_R972dp_g_VM_J79uvt5ffyu3P2431-tt6WQjc8lt22urdaNdBUzxvne9bVqnOVBac0lbcFRLpxthpXK2AdFT0J0DpVytZHVOLg-6Ywx_JkjZDJgc7PfWQ5iS0bzSkmvFZ_LqVZJRzuVsCV3Qj_-huzBFP_9hWC2EqoQSy2lxoFwMKUXozRhxsPHvLGWWfMzOHPIxSz6GsrkW8Q9P4lM7QPey9BzIDHw-ADD79ogQTXII3kGHEVw2XcDXL_wDhZmiLw</recordid><startdate>20120224</startdate><enddate>20120224</enddate><creator>Vince, James E.</creator><creator>Wong, W. Wei-Lynn</creator><creator>Gentle, Ian</creator><creator>Lawlor, Kate E.</creator><creator>Allam, Ramanjaneyulu</creator><creator>O'Reilly, Lorraine</creator><creator>Mason, Kylie</creator><creator>Gross, Olaf</creator><creator>Ma, Stephen</creator><creator>Guarda, Greta</creator><creator>Anderton, Holly</creator><creator>Castillo, Rosa</creator><creator>Häcker, Georg</creator><creator>Silke, John</creator><creator>Tschopp, Jürg</creator><general>Elsevier Inc</general><general>Elsevier Limited</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>NAPCQ</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20120224</creationdate><title>Inhibitor of Apoptosis Proteins Limit RIP3 Kinase-Dependent Interleukin-1 Activation</title><author>Vince, James E. ; Wong, W. Wei-Lynn ; Gentle, Ian ; Lawlor, Kate E. ; Allam, Ramanjaneyulu ; O'Reilly, Lorraine ; Mason, Kylie ; Gross, Olaf ; Ma, Stephen ; Guarda, Greta ; Anderton, Holly ; Castillo, Rosa ; Häcker, Georg ; Silke, John ; Tschopp, Jürg</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c585t-2abf9a9989c3e172ffcfa8bc92e006250bec095c984a57ca8e4f0e9dce77c6753</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Animals</topic><topic>Apoptosis</topic><topic>Baculoviral IAP Repeat-Containing 3 Protein</topic><topic>Carrier Proteins - agonists</topic><topic>Carrier Proteins - metabolism</topic><topic>Caspase 1 - metabolism</topic><topic>Caspase-1</topic><topic>Caspase-8</topic><topic>Cell activation</topic><topic>DIABLO protein</topic><topic>IAP protein</topic><topic>Immune system</topic><topic>Inflammasomes - immunology</topic><topic>Inflammasomes - metabolism</topic><topic>Inflammation</topic><topic>Inhibitor of Apoptosis Proteins - antagonists & inhibitors</topic><topic>Inhibitor of Apoptosis Proteins - deficiency</topic><topic>Inhibitor of Apoptosis Proteins - genetics</topic><topic>Inhibitor of Apoptosis Proteins - metabolism</topic><topic>Interleukin 1</topic><topic>Interleukin-1beta - metabolism</topic><topic>Macrophages</topic><topic>Macrophages - cytology</topic><topic>Macrophages - drug effects</topic><topic>Macrophages - immunology</topic><topic>Macrophages - metabolism</topic><topic>Mammals</topic><topic>Membranes</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Mitochondrial Proteins - agonists</topic><topic>Molecular Mimicry</topic><topic>NLR Family, Pyrin Domain-Containing 3 Protein</topic><topic>Proteins</topic><topic>Reactive oxygen species</topic><topic>Reactive Oxygen Species - metabolism</topic><topic>Receptor-Interacting Protein Serine-Threonine Kinases - metabolism</topic><topic>Toll-like receptors</topic><topic>Ubiquitin-Protein Ligases</topic><topic>X-Linked Inhibitor of Apoptosis Protein - deficiency</topic><topic>X-Linked Inhibitor of Apoptosis Protein - genetics</topic><topic>X-Linked Inhibitor of Apoptosis Protein - metabolism</topic><topic>XIAP protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vince, James E.</creatorcontrib><creatorcontrib>Wong, W. 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Wei-Lynn</au><au>Gentle, Ian</au><au>Lawlor, Kate E.</au><au>Allam, Ramanjaneyulu</au><au>O'Reilly, Lorraine</au><au>Mason, Kylie</au><au>Gross, Olaf</au><au>Ma, Stephen</au><au>Guarda, Greta</au><au>Anderton, Holly</au><au>Castillo, Rosa</au><au>Häcker, Georg</au><au>Silke, John</au><au>Tschopp, Jürg</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inhibitor of Apoptosis Proteins Limit RIP3 Kinase-Dependent Interleukin-1 Activation</atitle><jtitle>Immunity (Cambridge, Mass.)</jtitle><addtitle>Immunity</addtitle><date>2012-02-24</date><risdate>2012</risdate><volume>36</volume><issue>2</issue><spage>215</spage><epage>227</epage><pages>215-227</pages><issn>1074-7613</issn><eissn>1097-4180</eissn><abstract>Interleukin-1β (IL-1β) is a potent inflammatory cytokine that is usually cleaved and activated by inflammasome-associated caspase-1. To determine whether IL-1β activation is regulated by inhibitor of apoptosis (IAP) proteins, we treated macrophages with an IAP-antagonist “Smac mimetic” compound or genetically deleted the genes that encode the three IAP family members cIAP1, cIAP2, and XIAP. After Toll-like receptor priming, IAP inhibition triggered cleavage of IL-1β that was mediated not only by the NLRP3-caspase-1 inflammasome, but also by caspase-8 in a caspase-1-independent manner. In the absence of IAPs, rapid and full generation of active IL-1β by the NLRP3-caspase-1 inflammasome, or by caspase-8, required the kinase RIP3 and reactive oxygen species production. These results demonstrate that activation of the cell death-inducing ripoptosome platform and RIP3 can generate bioactive IL-1β and implicate them as additional targets for the treatment of pathological IL-1-driven inflammatory responses.
[Display omitted]
► IAP inhibition induces NLRP3 inflammasome-dependent and -independent IL-1 activation ► Genetic deletion of the three IAPs (cIAP1, cIAP2, XIAP) activates IL-1 ► Inflammasome-independent IL-1 maturation is mediated by caspase-8 cleavage ► RIP3 signaling, and not cell death, activates IL-1</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>22365665</pmid><doi>10.1016/j.immuni.2012.01.012</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; EZB-FREE-00999 freely available EZB journals |
| subjects | Animals Apoptosis Baculoviral IAP Repeat-Containing 3 Protein Carrier Proteins - agonists Carrier Proteins - metabolism Caspase 1 - metabolism Caspase-1 Caspase-8 Cell activation DIABLO protein IAP protein Immune system Inflammasomes - immunology Inflammasomes - metabolism Inflammation Inhibitor of Apoptosis Proteins - antagonists & inhibitors Inhibitor of Apoptosis Proteins - deficiency Inhibitor of Apoptosis Proteins - genetics Inhibitor of Apoptosis Proteins - metabolism Interleukin 1 Interleukin-1beta - metabolism Macrophages Macrophages - cytology Macrophages - drug effects Macrophages - immunology Macrophages - metabolism Mammals Membranes Mice Mice, Knockout Mitochondrial Proteins - agonists Molecular Mimicry NLR Family, Pyrin Domain-Containing 3 Protein Proteins Reactive oxygen species Reactive Oxygen Species - metabolism Receptor-Interacting Protein Serine-Threonine Kinases - metabolism Toll-like receptors Ubiquitin-Protein Ligases X-Linked Inhibitor of Apoptosis Protein - deficiency X-Linked Inhibitor of Apoptosis Protein - genetics X-Linked Inhibitor of Apoptosis Protein - metabolism XIAP protein |
| title | Inhibitor of Apoptosis Proteins Limit RIP3 Kinase-Dependent Interleukin-1 Activation |
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