Chopping GSDMD: caspase‐8 has joined the team of pyroptosis‐mediating caspases
Inflammatory and apoptotic caspases mediate two distinct forms of cell death: pyroptosis and apoptosis, respectively. Three independent studies have now demonstrated that the “apoptotic” caspase‐8 can cleave gasdermin D (GSDMD) leading to pyroptosis‐like cell death and IL‐1β release in murine macrop...
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description | Inflammatory and apoptotic caspases mediate two distinct forms of cell death: pyroptosis and apoptosis, respectively. Three independent studies have now demonstrated that the “apoptotic” caspase‐8 can cleave gasdermin D (GSDMD) leading to pyroptosis‐like cell death and IL‐1β release in murine macrophages (Orning
et al
, 2018; Sarhan
et al
, 2018; Chen
et al
, 2019). Orning
et al
and Chen/Demarco
et al
also show that the NLRP3 inflammasome is activated downstream of active caspase‐8, but they attribute this inflammasome activation to different pore‐forming proteins, GSDMD and pannexin‐1, respectively (Orning
et al
, 2018; Chen
et al
, 2019).
Graphical Abstract
While caspase‐8 is normally associated with apoptosis, recent studies show that it is also involved in pyroptosis, cleaving gasdermin D to trigger pyroptosis‐like cell death and IL‐1β release in macrophages. |
doi_str_mv | 10.15252/embj.2019102065 |
format | Article |
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et al
, 2018; Sarhan
et al
, 2018; Chen
et al
, 2019). Orning
et al
and Chen/Demarco
et al
also show that the NLRP3 inflammasome is activated downstream of active caspase‐8, but they attribute this inflammasome activation to different pore‐forming proteins, GSDMD and pannexin‐1, respectively (Orning
et al
, 2018; Chen
et al
, 2019).
Graphical Abstract
While caspase‐8 is normally associated with apoptosis, recent studies show that it is also involved in pyroptosis, cleaving gasdermin D to trigger pyroptosis‐like cell death and IL‐1β release in macrophages.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.15252/embj.2019102065</identifier><identifier>PMID: 30988015</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Apoptosis ; Caspase ; Caspase 1 ; Caspase 8 ; Caspases ; Cell death ; Cutting ; EMBO07 ; EMBO19 ; Inflammasomes ; Macrophages ; News & Views ; NLR Family, Pyrin Domain-Containing 3 Protein ; Pyroptosis ; Views</subject><ispartof>The EMBO journal, 2019-05, Vol.38 (10), p.n/a</ispartof><rights>The Author(s) 2019</rights><rights>2019 The Authors</rights><rights>2019 EMBO</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5195-1e2c074b188f3b8a07351056c4a443900323dff623e94617546a2a573d18efa53</citedby><cites>FETCH-LOGICAL-c5195-1e2c074b188f3b8a07351056c4a443900323dff623e94617546a2a573d18efa53</cites><orcidid>0000-0002-2924-0038</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6517822/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6517822/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1416,1432,27922,27923,41118,42187,45572,45573,46407,46831,51574,53789,53791</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.15252/embj.2019102065$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30988015$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gram, Anna M</creatorcontrib><creatorcontrib>Booty, Lee M</creatorcontrib><creatorcontrib>Bryant, Clare E</creatorcontrib><title>Chopping GSDMD: caspase‐8 has joined the team of pyroptosis‐mediating caspases</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Inflammatory and apoptotic caspases mediate two distinct forms of cell death: pyroptosis and apoptosis, respectively. Three independent studies have now demonstrated that the “apoptotic” caspase‐8 can cleave gasdermin D (GSDMD) leading to pyroptosis‐like cell death and IL‐1β release in murine macrophages (Orning
et al
, 2018; Sarhan
et al
, 2018; Chen
et al
, 2019). Orning
et al
and Chen/Demarco
et al
also show that the NLRP3 inflammasome is activated downstream of active caspase‐8, but they attribute this inflammasome activation to different pore‐forming proteins, GSDMD and pannexin‐1, respectively (Orning
et al
, 2018; Chen
et al
, 2019).
Graphical Abstract
While caspase‐8 is normally associated with apoptosis, recent studies show that it is also involved in pyroptosis, cleaving gasdermin D to trigger pyroptosis‐like cell death and IL‐1β release in macrophages.</description><subject>Apoptosis</subject><subject>Caspase</subject><subject>Caspase 1</subject><subject>Caspase 8</subject><subject>Caspases</subject><subject>Cell death</subject><subject>Cutting</subject><subject>EMBO07</subject><subject>EMBO19</subject><subject>Inflammasomes</subject><subject>Macrophages</subject><subject>News & Views</subject><subject>NLR Family, Pyrin Domain-Containing 3 Protein</subject><subject>Pyroptosis</subject><subject>Views</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtvEzEUhS0Eomlhz6oaiQ2bKff6MfZUVSVIH4BaIfFYW87EkziaGQ_2pFV2_Qn8Rn5JHRJaWgmxugt_59xzfQh5hXCAggr61raTxQEFLBEoFOIJGSEvIKcgxVMyAlpgzlGVO2Q3xgUACCXxOdlhUCoFKEbky3ju-951s-z868nlyWFWmdibaH_d_FTZ3MRs4V1np9kwt9lgTZv5OutXwfeDjy4mqrVTZ4a1wVYZX5BntWmifbmde-T72em38Yf84vP5x_G7i7wSWIocLa1A8gkqVbOJMiCZQBBFxQ3nrARglE3ruqDMlrxAKXhhqBGSTVHZ2gi2R443vv1yklJUthuCaXQfXGvCSnvj9MOXzs31zF_pQqBUlCaDN1uD4H8sbRx062Jlm8Z01i-jpjT9KgMh17teP0IXfhm6dF6iKC-BlxITBRuqCj7GYOu7MAj6d2F6XZi-LyxJ9v8-4k7wp6EEHG2Aa9fY1X8N9enl-08P_HEjj0nZzWy4D_7PTLeMe7M8</recordid><startdate>20190515</startdate><enddate>20190515</enddate><creator>Gram, Anna M</creator><creator>Booty, Lee M</creator><creator>Bryant, Clare E</creator><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>John Wiley and Sons Inc</general><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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-2924-0038</orcidid></search><sort><creationdate>20190515</creationdate><title>Chopping GSDMD: caspase‐8 has joined the team of pyroptosis‐mediating caspases</title><author>Gram, Anna M ; Booty, Lee M ; Bryant, Clare E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5195-1e2c074b188f3b8a07351056c4a443900323dff623e94617546a2a573d18efa53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Apoptosis</topic><topic>Caspase</topic><topic>Caspase 1</topic><topic>Caspase 8</topic><topic>Caspases</topic><topic>Cell death</topic><topic>Cutting</topic><topic>EMBO07</topic><topic>EMBO19</topic><topic>Inflammasomes</topic><topic>Macrophages</topic><topic>News & Views</topic><topic>NLR Family, Pyrin Domain-Containing 3 Protein</topic><topic>Pyroptosis</topic><topic>Views</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gram, Anna M</creatorcontrib><creatorcontrib>Booty, Lee M</creatorcontrib><creatorcontrib>Bryant, Clare E</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Gram, Anna M</au><au>Booty, Lee M</au><au>Bryant, Clare E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chopping GSDMD: caspase‐8 has joined the team of pyroptosis‐mediating caspases</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2019-05-15</date><risdate>2019</risdate><volume>38</volume><issue>10</issue><epage>n/a</epage><issn>0261-4189</issn><eissn>1460-2075</eissn><abstract>Inflammatory and apoptotic caspases mediate two distinct forms of cell death: pyroptosis and apoptosis, respectively. Three independent studies have now demonstrated that the “apoptotic” caspase‐8 can cleave gasdermin D (GSDMD) leading to pyroptosis‐like cell death and IL‐1β release in murine macrophages (Orning
et al
, 2018; Sarhan
et al
, 2018; Chen
et al
, 2019). Orning
et al
and Chen/Demarco
et al
also show that the NLRP3 inflammasome is activated downstream of active caspase‐8, but they attribute this inflammasome activation to different pore‐forming proteins, GSDMD and pannexin‐1, respectively (Orning
et al
, 2018; Chen
et al
, 2019).
Graphical Abstract
While caspase‐8 is normally associated with apoptosis, recent studies show that it is also involved in pyroptosis, cleaving gasdermin D to trigger pyroptosis‐like cell death and IL‐1β release in macrophages.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>30988015</pmid><doi>10.15252/embj.2019102065</doi><tpages>3</tpages><orcidid>https://orcid.org/0000-0002-2924-0038</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Apoptosis Caspase Caspase 1 Caspase 8 Caspases Cell death Cutting EMBO07 EMBO19 Inflammasomes Macrophages News & Views NLR Family, Pyrin Domain-Containing 3 Protein Pyroptosis Views |
title | Chopping GSDMD: caspase‐8 has joined the team of pyroptosis‐mediating caspases |
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