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Apoptosis-associated speck-like protein containing CARD forms specks but does not activate caspase-1 in the absence of NLRP3 during macrophage swelling

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dc.contributor.authorCompan, Vincent
dc.contributor.authorMartín-Sánchez, Fátima
dc.contributor.authorBaroja-Mazo, Alberto
dc.contributor.authorLópez-Castejón, Gloria
dc.contributor.authorGomez, Ana I.
dc.contributor.authorVerkhratsky, Alexei
dc.contributor.authorBrough, David
dc.contributor.authorPelegrin Vivancos, Pablo
dc.contributor.departmentBioquímica y Biología Molecular B e Inmunología
dc.date.accessioned2024-01-25T09:46:36Z
dc.date.available2024-01-25T09:46:36Z
dc.date.issued2015
dc.description©2015. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/ This document is the Submitted version of a Published Work that appeared in final form in The Journal of Immunology. To access the final edited and published work see https://doi.org/10.4049/jimmunol.1301676es
dc.description.abstractApoptosis-associated speck-like protein containing a CARD (ASC) is a key adaptor molecule required for inflammatory processes. ASC acts by bridging NLRP proteins, such as NLRP3, with pro-caspase-1 within the inflammasome complex that subsequently results in the activation of caspase-1 and the secretion of interleukin (IL)-1b and IL-18. In response to bacterial infection, ASC also forms specks by self-oligomerization to activate caspase-1 and induce pyroptosis. Hitherto the role of these specks in NLRP3 inflammasome activation in response to danger signals is largely unexplored. Here we report that under hypotonic conditions, ASC formed specks independently of NLRP3 that did not activate caspase-1. These specks were not associated with pyroptosis and were controlled by Transient Receptor Potential Vanilloid 2 channel mediated signaling. However, interaction with NLRP3 enhanced ASC speck formation leading to fully functional inflammasomes and caspase-1 activation. This study reveals that the ASC speck could present different oligomerization assemblies and represents an essential step in the activation of functional NLRP3 inflammasomes.es
dc.formatapplication/pdfes
dc.format.extent51es
dc.identifier.citationThe Journal of Immunology, volumen 194, nº 3, año 2015, páginas 1261-1273
dc.identifier.doi10.4049/jimmunol.1301676
dc.identifier.issn1550-6606
dc.identifier.issn0022-1767
dc.identifier.urihttp://hdl.handle.net/10201/137759
dc.languageenges
dc.publisherThe American Association of Immunologists, Inc.es
dc.relationPN I+D+I 2008-2011-Instituto Salud Carlos III-FEDER (EMER07/049 y PI09/0120), Fundación Séneca (11922/PI/09), and European Research Council (ERC-2013-CoG 614578), Wellcome Trust.es
dc.relation.publisherversionhttps://journals.aai.org/jimmunol/article/194/3/1261/108974/Apoptosis-Associated-Speck-like-Protein-Containinges
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectMacrófagoses
dc.subjectCitocinases
dc.subjectInflamaciónes
dc.subjectVolumen celulares
dc.subjectInflamasomaes
dc.subject.otherCDU::6 - Ciencias aplicadases
dc.titleApoptosis-associated speck-like protein containing CARD forms specks but does not activate caspase-1 in the absence of NLRP3 during macrophage swellinges
dc.title.alternativeASC speck formation during cell swellinges
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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