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http://purl.uniprot.org/citations/18250463http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18250463http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18250463http://www.w3.org/2000/01/rdf-schema#comment"High mobility group box 1 protein (HMGB1), originally characterized as a nuclear DNA-binding protein, has also been described to have an extracellular role when it is involved in cellular activation and proinflammatory responses. In this study, FLAG-tagged HMGB1 was inducibly expressed in the presence of culture media with or without added IL-1beta, IFN-gamma, or TNF-alpha. HMGB1 purified from cells grown in culture media alone only minimally increased cytokine production by MH-S macrophages and had no effect on murine neutrophils. In contrast, HMGB1 isolated from cells cultured in the presence of IL-1beta, IFN-gamma, and TNF-alpha had enhanced proinflammatory activity, resulting in increased production of MIP-2 and TNF-alpha by exposed cells. IL-1beta was bound to HMGB1 isolated from cells cultured with this cytokine, and purified HMGB1 incubated with recombinant IL-1beta acquired proinflammatory activity. Addition of anti-IL-1beta Abs or the IL-1 receptor antagonist to cell cultures blocked the proinflammatory activity of HMGB1 purified from IL-1beta-exposed cells, indicating that such activity was dependent on interaction with the IL-1 receptor. These results demonstrate that HMGB1 acquires proinflammatory activity through binding to proinflammatory mediators, such as IL-1beta."xsd:string
http://purl.uniprot.org/citations/18250463http://purl.org/dc/terms/identifier"doi:10.4049/jimmunol.180.4.2531"xsd:string
http://purl.uniprot.org/citations/18250463http://purl.org/dc/terms/identifier"doi:10.4049/jimmunol.180.4.2531"xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/author"Xu Z."xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/author"Xu Z."xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/author"Abraham E."xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/author"Abraham E."xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/author"Sha Y."xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/author"Sha Y."xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/author"Zmijewski J."xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/author"Zmijewski J."xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/name"J. Immunol."xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/name"J. Immunol."xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/pages"2531-2537"xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/pages"2531-2537"xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/title"HMGB1 develops enhanced proinflammatory activity by binding to cytokines."xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/title"HMGB1 develops enhanced proinflammatory activity by binding to cytokines."xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/volume"180"xsd:string
http://purl.uniprot.org/citations/18250463http://purl.uniprot.org/core/volume"180"xsd:string
http://purl.uniprot.org/citations/18250463http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18250463
http://purl.uniprot.org/citations/18250463http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18250463