PMC:1472690 / 620-1901 JSONTXT

{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T311","span":{"begin":294,"end":298},"obj":"Protein"},{"id":"T312","span":{"begin":384,"end":388},"obj":"Protein"},{"id":"T313","span":{"begin":414,"end":437},"obj":"Protein"},{"id":"T314","span":{"begin":438,"end":440},"obj":"Protein"},{"id":"T315","span":{"begin":542,"end":546},"obj":"Protein"},{"id":"T316","span":{"begin":654,"end":660},"obj":"Protein"},{"id":"T317","span":{"begin":765,"end":771},"obj":"Protein"},{"id":"T318","span":{"begin":857,"end":863},"obj":"Protein"},{"id":"T319","span":{"begin":893,"end":899},"obj":"Protein"},{"id":"T320","span":{"begin":904,"end":908},"obj":"Protein"},{"id":"T321","span":{"begin":947,"end":953},"obj":"Protein"},{"id":"T322","span":{"begin":995,"end":1001},"obj":"Protein"},{"id":"T323","span":{"begin":1049,"end":1054},"obj":"Protein"},{"id":"T324","span":{"begin":1059,"end":1063},"obj":"Protein"},{"id":"T325","span":{"begin":1112,"end":1118},"obj":"Protein"},{"id":"T326","span":{"begin":1127,"end":1132},"obj":"Protein"},{"id":"T327","span":{"begin":1133,"end":1139},"obj":"Protein"},{"id":"T328","span":{"begin":1231,"end":1237},"obj":"Protein"},{"id":"T329","span":{"begin":1247,"end":1251},"obj":"Protein"},{"id":"T330","span":{"begin":1276,"end":1280},"obj":"Protein"},{"id":"T304","span":{"begin":48,"end":67},"obj":"Protein"},{"id":"T305","span":{"begin":72,"end":76},"obj":"Protein"},{"id":"T306","span":{"begin":95,"end":101},"obj":"Protein"},{"id":"T307","span":{"begin":144,"end":149},"obj":"Protein"},{"id":"T308","span":{"begin":151,"end":155},"obj":"Protein"},{"id":"T309","span":{"begin":157,"end":180},"obj":"Protein"},{"id":"T310","span":{"begin":184,"end":196},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"Despite an activation of nuclear factor (NF)κB, NFinterleukin(IL)-6 and NFAT similar to LPS or TSST-1, we observed no significant production of IL-1β, IL-6, tumor necrosis factor α or interferon γ induced by glucan phosphate. Glucan phosphate-treated leukocytes induced a substantial amount of IL-8 (peak at 18 h: 5000 pg/ml), likely due to binding of NFκB to a consensus site in the IL-8 promoter. An increase in IL-1receptor antagonist(RA) production (peak at 24 h: 12000 pg/ml) by glucan phosphate-treated cells positively correlated with IL-8 levels. Glucan phosphate induced significant binding to a known NFIL-6 site and a new NFAT site within the IL-1RA promoter, which was confirmed by inhibition experiments. When applied in combination with either LPS or TSST-1 at the same time points, we detected that glucan phosphate elevated the LPS- and the TSST-1-induced DNA binding of NFκB, NFIL-6 and NFAT, leading to a synergistic increase of IL-1RA. Further, glucan phosphate modulated the TSST-1-induced inflammatory response via reduction of IL-1β and IL-6. As a consequence, glucan phosphate shifted the TSST-1-induced IL-1β/IL-1RA ratio towards an anti-inflammatory phenotype. Subsequently, glucan phosphate decreased the TSST-1-induced, IL-1-dependent production of IL-2."}

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T438","span":{"begin":1112,"end":1118},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T439","span":{"begin":1231,"end":1237},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T440","span":{"begin":184,"end":196},"obj":"http://www.uniprot.org/uniprot/P01579"},{"id":"T441","span":{"begin":294,"end":298},"obj":"http://www.uniprot.org/uniprot/P10145"},{"id":"T442","span":{"begin":384,"end":388},"obj":"http://www.uniprot.org/uniprot/P10145"},{"id":"T443","span":{"begin":542,"end":546},"obj":"http://www.uniprot.org/uniprot/P10145"},{"id":"T444","span":{"begin":654,"end":660},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T445","span":{"begin":947,"end":953},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T446","span":{"begin":1133,"end":1139},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T449","span":{"begin":1276,"end":1280},"obj":"http://www.uniprot.org/uniprot/P60568"},{"id":"T427","span":{"begin":151,"end":155},"obj":"http://www.uniprot.org/uniprot/P05231"},{"id":"T428","span":{"begin":1059,"end":1063},"obj":"http://www.uniprot.org/uniprot/P05231"},{"id":"T430","span":{"begin":144,"end":149},"obj":"http://www.uniprot.org/uniprot/P01584"},{"id":"T431","span":{"begin":1049,"end":1054},"obj":"http://www.uniprot.org/uniprot/P01584"},{"id":"T432","span":{"begin":1127,"end":1132},"obj":"http://www.uniprot.org/uniprot/P01584"},{"id":"T434","span":{"begin":95,"end":101},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T435","span":{"begin":765,"end":771},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T436","span":{"begin":857,"end":863},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T437","span":{"begin":995,"end":1001},"obj":"http://www.uniprot.org/uniprot/P06886"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"Despite an activation of nuclear factor (NF)κB, NFinterleukin(IL)-6 and NFAT similar to LPS or TSST-1, we observed no significant production of IL-1β, IL-6, tumor necrosis factor α or interferon γ induced by glucan phosphate. Glucan phosphate-treated leukocytes induced a substantial amount of IL-8 (peak at 18 h: 5000 pg/ml), likely due to binding of NFκB to a consensus site in the IL-8 promoter. An increase in IL-1receptor antagonist(RA) production (peak at 24 h: 12000 pg/ml) by glucan phosphate-treated cells positively correlated with IL-8 levels. Glucan phosphate induced significant binding to a known NFIL-6 site and a new NFAT site within the IL-1RA promoter, which was confirmed by inhibition experiments. When applied in combination with either LPS or TSST-1 at the same time points, we detected that glucan phosphate elevated the LPS- and the TSST-1-induced DNA binding of NFκB, NFIL-6 and NFAT, leading to a synergistic increase of IL-1RA. Further, glucan phosphate modulated the TSST-1-induced inflammatory response via reduction of IL-1β and IL-6. As a consequence, glucan phosphate shifted the TSST-1-induced IL-1β/IL-1RA ratio towards an anti-inflammatory phenotype. Subsequently, glucan phosphate decreased the TSST-1-induced, IL-1-dependent production of IL-2."}

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{"project":"GO-MF","denotations":[{"id":"T336","span":{"begin":872,"end":883},"obj":"http://purl.obolibrary.org/obo/GO_0003677"},{"id":"T338","span":{"begin":341,"end":348},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T339","span":{"begin":592,"end":599},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T340","span":{"begin":876,"end":883},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T343","span":{"begin":151,"end":155},"obj":"http://purl.obolibrary.org/obo/GO_0005138"},{"id":"T344","span":{"begin":1059,"end":1063},"obj":"http://purl.obolibrary.org/obo/GO_0005138"},{"id":"T346","span":{"begin":1247,"end":1251},"obj":"http://purl.obolibrary.org/obo/GO_0005149"},{"id":"T350","span":{"begin":184,"end":196},"obj":"http://purl.obolibrary.org/obo/GO_0005133"},{"id":"T351","span":{"begin":294,"end":298},"obj":"http://purl.obolibrary.org/obo/GO_0005153"},{"id":"T352","span":{"begin":384,"end":388},"obj":"http://purl.obolibrary.org/obo/GO_0005153"},{"id":"T353","span":{"begin":542,"end":546},"obj":"http://purl.obolibrary.org/obo/GO_0005153"},{"id":"T354","span":{"begin":1276,"end":1280},"obj":"http://purl.obolibrary.org/obo/GO_0005134"}],"text":"Despite an activation of nuclear factor (NF)κB, NFinterleukin(IL)-6 and NFAT similar to LPS or TSST-1, we observed no significant production of IL-1β, IL-6, tumor necrosis factor α or interferon γ induced by glucan phosphate. Glucan phosphate-treated leukocytes induced a substantial amount of IL-8 (peak at 18 h: 5000 pg/ml), likely due to binding of NFκB to a consensus site in the IL-8 promoter. An increase in IL-1receptor antagonist(RA) production (peak at 24 h: 12000 pg/ml) by glucan phosphate-treated cells positively correlated with IL-8 levels. Glucan phosphate induced significant binding to a known NFIL-6 site and a new NFAT site within the IL-1RA promoter, which was confirmed by inhibition experiments. When applied in combination with either LPS or TSST-1 at the same time points, we detected that glucan phosphate elevated the LPS- and the TSST-1-induced DNA binding of NFκB, NFIL-6 and NFAT, leading to a synergistic increase of IL-1RA. Further, glucan phosphate modulated the TSST-1-induced inflammatory response via reduction of IL-1β and IL-6. As a consequence, glucan phosphate shifted the TSST-1-induced IL-1β/IL-1RA ratio towards an anti-inflammatory phenotype. Subsequently, glucan phosphate decreased the TSST-1-induced, IL-1-dependent production of IL-2."}

{"project":"GO-CC","denotations":[{"id":"T357","span":{"begin":509,"end":514},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Despite an activation of nuclear factor (NF)κB, NFinterleukin(IL)-6 and NFAT similar to LPS or TSST-1, we observed no significant production of IL-1β, IL-6, tumor necrosis factor α or interferon γ induced by glucan phosphate. Glucan phosphate-treated leukocytes induced a substantial amount of IL-8 (peak at 18 h: 5000 pg/ml), likely due to binding of NFκB to a consensus site in the IL-8 promoter. An increase in IL-1receptor antagonist(RA) production (peak at 24 h: 12000 pg/ml) by glucan phosphate-treated cells positively correlated with IL-8 levels. Glucan phosphate induced significant binding to a known NFIL-6 site and a new NFAT site within the IL-1RA promoter, which was confirmed by inhibition experiments. When applied in combination with either LPS or TSST-1 at the same time points, we detected that glucan phosphate elevated the LPS- and the TSST-1-induced DNA binding of NFκB, NFIL-6 and NFAT, leading to a synergistic increase of IL-1RA. Further, glucan phosphate modulated the TSST-1-induced inflammatory response via reduction of IL-1β and IL-6. As a consequence, glucan phosphate shifted the TSST-1-induced IL-1β/IL-1RA ratio towards an anti-inflammatory phenotype. Subsequently, glucan phosphate decreased the TSST-1-induced, IL-1-dependent production of IL-2."}

{"project":"sentences","denotations":[{"id":"T193","span":{"begin":0,"end":225},"obj":"Sentence"},{"id":"T194","span":{"begin":226,"end":313},"obj":"Sentence"},{"id":"T195","span":{"begin":314,"end":398},"obj":"Sentence"},{"id":"T196","span":{"begin":399,"end":467},"obj":"Sentence"},{"id":"T197","span":{"begin":468,"end":554},"obj":"Sentence"},{"id":"T198","span":{"begin":555,"end":717},"obj":"Sentence"},{"id":"T199","span":{"begin":718,"end":954},"obj":"Sentence"},{"id":"T200","span":{"begin":955,"end":1064},"obj":"Sentence"},{"id":"T201","span":{"begin":1065,"end":1185},"obj":"Sentence"},{"id":"T202","span":{"begin":1186,"end":1281},"obj":"Sentence"},{"id":"T7","span":{"begin":0,"end":225},"obj":"Sentence"},{"id":"T8","span":{"begin":226,"end":313},"obj":"Sentence"},{"id":"T9","span":{"begin":314,"end":398},"obj":"Sentence"},{"id":"T10","span":{"begin":399,"end":467},"obj":"Sentence"},{"id":"T11","span":{"begin":468,"end":554},"obj":"Sentence"},{"id":"T12","span":{"begin":555,"end":717},"obj":"Sentence"},{"id":"T13","span":{"begin":718,"end":954},"obj":"Sentence"},{"id":"T14","span":{"begin":955,"end":1064},"obj":"Sentence"},{"id":"T15","span":{"begin":1065,"end":1185},"obj":"Sentence"},{"id":"T16","span":{"begin":1186,"end":1281},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Despite an activation of nuclear factor (NF)κB, NFinterleukin(IL)-6 and NFAT similar to LPS or TSST-1, we observed no significant production of IL-1β, IL-6, tumor necrosis factor α or interferon γ induced by glucan phosphate. Glucan phosphate-treated leukocytes induced a substantial amount of IL-8 (peak at 18 h: 5000 pg/ml), likely due to binding of NFκB to a consensus site in the IL-8 promoter. An increase in IL-1receptor antagonist(RA) production (peak at 24 h: 12000 pg/ml) by glucan phosphate-treated cells positively correlated with IL-8 levels. Glucan phosphate induced significant binding to a known NFIL-6 site and a new NFAT site within the IL-1RA promoter, which was confirmed by inhibition experiments. When applied in combination with either LPS or TSST-1 at the same time points, we detected that glucan phosphate elevated the LPS- and the TSST-1-induced DNA binding of NFκB, NFIL-6 and NFAT, leading to a synergistic increase of IL-1RA. Further, glucan phosphate modulated the TSST-1-induced inflammatory response via reduction of IL-1β and IL-6. As a consequence, glucan phosphate shifted the TSST-1-induced IL-1β/IL-1RA ratio towards an anti-inflammatory phenotype. Subsequently, glucan phosphate decreased the TSST-1-induced, IL-1-dependent production of IL-2."}

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an activation of nuclear factor (NF)κB, NFinterleukin(IL)-6 and NFAT similar to LPS or TSST-1, we observed no significant production of IL-1β, IL-6, tumor necrosis factor α or interferon γ induced by glucan phosphate. Glucan phosphate-treated leukocytes induced a substantial amount of IL-8 (peak at 18 h: 5000 pg/ml), likely due to binding of NFκB to a consensus site in the IL-8 promoter. An increase in IL-1receptor antagonist(RA) production (peak at 24 h: 12000 pg/ml) by glucan phosphate-treated cells positively correlated with IL-8 levels. Glucan phosphate induced significant binding to a known NFIL-6 site and a new NFAT site within the IL-1RA promoter, which was confirmed by inhibition experiments. When applied in combination with either LPS or TSST-1 at the same time points, we detected that glucan phosphate elevated the LPS- and the TSST-1-induced DNA binding of NFκB, NFIL-6 and NFAT, leading to a synergistic increase of IL-1RA. Further, glucan phosphate modulated the TSST-1-induced inflammatory response via reduction of IL-1β and IL-6. As a consequence, glucan phosphate shifted the TSST-1-induced IL-1β/IL-1RA ratio towards an anti-inflammatory phenotype. 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