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http://purl.uniprot.org/citations/20802146http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20802146http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20802146http://www.w3.org/2000/01/rdf-schema#comment"Endotoxin administration recapitulates many of the host responses to sepsis. Inhibitors of the cysteine protease caspase 1 have long been sought as a therapeutic because mice lacking caspase 1 are resistant to LPS-induced endotoxic shock. According to current thinking, caspase 1-mediated shock requires the proinflammatory caspase 1 substrates IL-1β and IL-18. We show, however, that mice lacking both IL-1β and IL-18 are normally susceptible to LPS-induced splenocyte apoptosis and endotoxic shock. This finding indicates the existence of another caspase 1-dependent mediator of endotoxemia. Reduced serum high mobility group box 1 (HMGB1) levels in caspase 1-deficient mice correlated with their resistance to LPS. A critical role for HMGB1 in endotoxemia was confirmed when mice deficient for IL-1β and IL-18 were protected from a lethal dose of LPS by pretreatment with HMGB1-neutralizing Abs. We found that HMGB1 secretion from LPS-primed macrophages required the inflammasome components apoptotic speck protein containing a caspase activation and recruitment domain (ASC), caspase 1 and Nalp3, whereas HMGB1 secretion from macrophages infected in vitro with Salmonella typhimurium was dependent on caspase 1 and Ipaf. Thus, HMGB1 secretion, which is critical for endotoxemia, occurs downstream of inflammasome assembly and caspase 1 activation."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.org/dc/terms/identifier"doi:10.4049/jimmunol.1000803"xsd:string
http://purl.uniprot.org/citations/20802146http://purl.org/dc/terms/identifier"doi:10.4049/jimmunol.1000803"xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Sarkar A."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Sarkar A."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Kanneganti T.D."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Kanneganti T.D."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Dixit V.M."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Dixit V.M."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Tracey K.J."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Tracey K.J."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Lamkanfi M."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Lamkanfi M."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Wewers M.D."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Wewers M.D."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Vande Walle L."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Vande Walle L."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Amer A.O."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Amer A.O."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Vitari A.C."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/author"Vitari A.C."xsd:string
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20802146http://purl.uniprot.org/core/date"2010"xsd:gYear