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addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T1167","span":{"begin":1071,"end":1077},"obj":"Protein"},{"id":"T1168","span":{"begin":1202,"end":1206},"obj":"Protein"},{"id":"T1169","span":{"begin":1208,"end":1213},"obj":"Protein"},{"id":"T1170","span":{"begin":1215,"end":1219},"obj":"Protein"},{"id":"T1171","span":{"begin":1221,"end":1225},"obj":"Protein"},{"id":"T1172","span":{"begin":1230,"end":1236},"obj":"Protein"},{"id":"T1173","span":{"begin":1262,"end":1266},"obj":"Protein"},{"id":"T1174","span":{"begin":1268,"end":1272},"obj":"Protein"},{"id":"T1175","span":{"begin":1274,"end":1278},"obj":"Protein"},{"id":"T1176","span":{"begin":1280,"end":1285},"obj":"Protein"},{"id":"T1177","span":{"begin":1287,"end":1292},"obj":"Protein"},{"id":"T1178","span":{"begin":1297,"end":1302},"obj":"Protein"},{"id":"T1179","span":{"begin":1346,"end":1350},"obj":"Protein"},{"id":"T1180","span":{"begin":1420,"end":1424},"obj":"Protein"},{"id":"T1181","span":{"begin":1462,"end":1466},"obj":"Protein"},{"id":"T1182","span":{"begin":1525,"end":1529},"obj":"Protein"},{"id":"T1183","span":{"begin":1600,"end":1606},"obj":"Protein"},{"id":"T1184","span":{"begin":1662,"end":1668},"obj":"Protein"},{"id":"T1185","span":{"begin":1781,"end":1787},"obj":"Protein"},{"id":"T1186","span":{"begin":1976,"end":1982},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T1917","span":{"begin":1600,"end":1606},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T1918","span":{"begin":1662,"end":1668},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T1919","span":{"begin":1781,"end":1787},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T1920","span":{"begin":1976,"end":1982},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T1922","span":{"begin":1221,"end":1225},"obj":"http://www.uniprot.org/uniprot/P10145"},{"id":"T1923","span":{"begin":1420,"end":1424},"obj":"http://www.uniprot.org/uniprot/P10145"},{"id":"T1924","span":{"begin":1071,"end":1077},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T1925","span":{"begin":1208,"end":1213},"obj":"http://www.uniprot.org/uniprot/P01584"},{"id":"T1926","span":{"begin":1268,"end":1272},"obj":"http://www.uniprot.org/uniprot/P60568"},{"id":"T1927","span":{"begin":1274,"end":1278},"obj":"http://www.uniprot.org/uniprot/P05112"},{"id":"T1928","span":{"begin":1280,"end":1285},"obj":"http://www.uniprot.org/uniprot/P22301"},{"id":"T1929","span":{"begin":1287,"end":1292},"obj":"http://www.uniprot.org/uniprot/P29459"},{"id":"T1930","span":{"begin":1287,"end":1292},"obj":"http://www.uniprot.org/uniprot/P29460"},{"id":"T1931","span":{"begin":1814,"end":1818},"obj":"http://www.uniprot.org/uniprot/P17947"},{"id":"T1909","span":{"begin":1202,"end":1206},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T1910","span":{"begin":1346,"end":1350},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T1913","span":{"begin":1215,"end":1219},"obj":"http://www.uniprot.org/uniprot/P05231"},{"id":"T1914","span":{"begin":1525,"end":1529},"obj":"http://www.uniprot.org/uniprot/P05231"},{"id":"T1916","span":{"begin":1230,"end":1236},"obj":"http://www.uniprot.org/uniprot/P18510"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"UBERON-AE","denotations":[{"id":"T1071","span":{"begin":876,"end":881},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"GO-BP","denotations":[{"id":"T1093","span":{"begin":675,"end":683},"obj":"http://purl.obolibrary.org/obo/GO_0007349"},{"id":"T1098","span":{"begin":317,"end":321},"obj":"http://purl.obolibrary.org/obo/GO_0016303"},{"id":"T1099","span":{"begin":819,"end":834},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T1100","span":{"begin":1633,"end":1646},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T1101","span":{"begin":835,"end":845},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T1102","span":{"begin":1170,"end":1189},"obj":"http://purl.obolibrary.org/obo/GO_0001816"},{"id":"T1103","span":{"begin":1727,"end":1739},"obj":"http://purl.obolibrary.org/obo/GO_0032496"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"GO-MF","denotations":[{"id":"T1192","span":{"begin":152,"end":166},"obj":"http://purl.obolibrary.org/obo/GO_0001872"},{"id":"T1193","span":{"begin":441,"end":455},"obj":"http://purl.obolibrary.org/obo/GO_0001872"},{"id":"T1194","span":{"begin":550,"end":564},"obj":"http://purl.obolibrary.org/obo/GO_0001872"},{"id":"T1195","span":{"begin":938,"end":952},"obj":"http://purl.obolibrary.org/obo/GO_0001872"},{"id":"T1199","span":{"begin":1622,"end":1629},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T1200","span":{"begin":1954,"end":1961},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T1204","span":{"begin":1215,"end":1219},"obj":"http://purl.obolibrary.org/obo/GO_0005138"},{"id":"T1205","span":{"begin":1525,"end":1529},"obj":"http://purl.obolibrary.org/obo/GO_0005138"},{"id":"T1207","span":{"begin":1221,"end":1225},"obj":"http://purl.obolibrary.org/obo/GO_0005153"},{"id":"T1208","span":{"begin":1420,"end":1424},"obj":"http://purl.obolibrary.org/obo/GO_0005153"},{"id":"T1209","span":{"begin":317,"end":321},"obj":"http://purl.obolibrary.org/obo/GO_0016303"},{"id":"T1210","span":{"begin":1268,"end":1272},"obj":"http://purl.obolibrary.org/obo/GO_0005134"},{"id":"T1211","span":{"begin":1274,"end":1278},"obj":"http://purl.obolibrary.org/obo/GO_0005136"},{"id":"T1212","span":{"begin":1280,"end":1285},"obj":"http://purl.obolibrary.org/obo/GO_0005141"},{"id":"T1213","span":{"begin":1287,"end":1292},"obj":"http://purl.obolibrary.org/obo/GO_0005143"},{"id":"T1214","span":{"begin":1622,"end":1654},"obj":"http://purl.obolibrary.org/obo/GO_0008134"},{"id":"T1215","span":{"begin":1622,"end":1654},"obj":"http://purl.obolibrary.org/obo/GO_0033613"},{"id":"T1216","span":{"begin":1622,"end":1654},"obj":"http://purl.obolibrary.org/obo/GO_0043425"},{"id":"T1217","span":{"begin":1622,"end":1654},"obj":"http://purl.obolibrary.org/obo/GO_0070491"},{"id":"T1218","span":{"begin":1771,"end":1783},"obj":"http://purl.obolibrary.org/obo/GO_0005135"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"GO-CC","denotations":[{"id":"T1223","span":{"begin":894,"end":899},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"sentences","denotations":[{"id":"T1081","span":{"begin":0,"end":111},"obj":"Sentence"},{"id":"T1082","span":{"begin":112,"end":339},"obj":"Sentence"},{"id":"T1083","span":{"begin":340,"end":495},"obj":"Sentence"},{"id":"T1084","span":{"begin":496,"end":615},"obj":"Sentence"},{"id":"T1085","span":{"begin":616,"end":846},"obj":"Sentence"},{"id":"T1086","span":{"begin":847,"end":1116},"obj":"Sentence"},{"id":"T1087","span":{"begin":1117,"end":1303},"obj":"Sentence"},{"id":"T1088","span":{"begin":1304,"end":1558},"obj":"Sentence"},{"id":"T1089","span":{"begin":1559,"end":1678},"obj":"Sentence"},{"id":"T1090","span":{"begin":1679,"end":1880},"obj":"Sentence"},{"id":"T1091","span":{"begin":1881,"end":1992},"obj":"Sentence"},{"id":"T30","span":{"begin":0,"end":111},"obj":"Sentence"},{"id":"T31","span":{"begin":112,"end":339},"obj":"Sentence"},{"id":"T32","span":{"begin":340,"end":495},"obj":"Sentence"},{"id":"T33","span":{"begin":496,"end":615},"obj":"Sentence"},{"id":"T34","span":{"begin":616,"end":846},"obj":"Sentence"},{"id":"T35","span":{"begin":847,"end":1116},"obj":"Sentence"},{"id":"T36","span":{"begin":1117,"end":1303},"obj":"Sentence"},{"id":"T37","span":{"begin":1304,"end":1558},"obj":"Sentence"},{"id":"T38","span":{"begin":1559,"end":1678},"obj":"Sentence"},{"id":"T39","span":{"begin":1679,"end":1880},"obj":"Sentence"},{"id":"T40","span":{"begin":1881,"end":1992},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"simple1","denotations":[{"id":"T1269","span":{"begin":1071,"end":1077},"obj":"Protein"},{"id":"T1270","span":{"begin":1202,"end":1206},"obj":"Protein"},{"id":"T1271","span":{"begin":1208,"end":1213},"obj":"Protein"},{"id":"T1272","span":{"begin":1215,"end":1219},"obj":"Protein"},{"id":"T1273","span":{"begin":1221,"end":1225},"obj":"Protein"},{"id":"T1274","span":{"begin":1230,"end":1236},"obj":"Protein"},{"id":"T1275","span":{"begin":1262,"end":1266},"obj":"Protein"},{"id":"T1276","span":{"begin":1268,"end":1272},"obj":"Protein"},{"id":"T1277","span":{"begin":1274,"end":1278},"obj":"Protein"},{"id":"T1278","span":{"begin":1280,"end":1285},"obj":"Protein"},{"id":"T1279","span":{"begin":1287,"end":1292},"obj":"Protein"},{"id":"T1280","span":{"begin":1297,"end":1302},"obj":"Protein"},{"id":"T1281","span":{"begin":1346,"end":1350},"obj":"Protein"},{"id":"T1282","span":{"begin":1420,"end":1424},"obj":"Protein"},{"id":"T1283","span":{"begin":1462,"end":1466},"obj":"Protein"},{"id":"T1284","span":{"begin":1525,"end":1529},"obj":"Protein"},{"id":"T1285","span":{"begin":1600,"end":1606},"obj":"Protein"},{"id":"T1286","span":{"begin":1662,"end":1668},"obj":"Protein"},{"id":"T1287","span":{"begin":1781,"end":1787},"obj":"Protein"},{"id":"T1288","span":{"begin":1976,"end":1982},"obj":"Protein"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"BioNLP16_DUT","denotations":[{"id":"T2946","span":{"begin":1071,"end":1077},"obj":"Protein"},{"id":"T2947","span":{"begin":1202,"end":1206},"obj":"Protein"},{"id":"T2948","span":{"begin":1208,"end":1213},"obj":"Protein"},{"id":"T2949","span":{"begin":1215,"end":1219},"obj":"Protein"},{"id":"T2950","span":{"begin":1221,"end":1225},"obj":"Protein"},{"id":"T2951","span":{"begin":1230,"end":1236},"obj":"Protein"},{"id":"T2952","span":{"begin":1262,"end":1266},"obj":"Protein"},{"id":"T2953","span":{"begin":1268,"end":1272},"obj":"Protein"},{"id":"T2954","span":{"begin":1274,"end":1278},"obj":"Protein"},{"id":"T2955","span":{"begin":1280,"end":1285},"obj":"Protein"},{"id":"T2956","span":{"begin":1287,"end":1292},"obj":"Protein"},{"id":"T2957","span":{"begin":1297,"end":1302},"obj":"Protein"},{"id":"T2958","span":{"begin":1346,"end":1350},"obj":"Protein"},{"id":"T2959","span":{"begin":1420,"end":1424},"obj":"Protein"},{"id":"T2960","span":{"begin":1462,"end":1466},"obj":"Protein"},{"id":"T2961","span":{"begin":1525,"end":1529},"obj":"Protein"},{"id":"T2962","span":{"begin":1600,"end":1606},"obj":"Protein"},{"id":"T2963","span":{"begin":1662,"end":1668},"obj":"Protein"},{"id":"T2964","span":{"begin":1781,"end":1787},"obj":"Protein"},{"id":"T2965","span":{"begin":1976,"end":1982},"obj":"Protein"},{"id":"T2974","span":{"begin":1622,"end":1629},"obj":"Binding"}],"relations":[{"id":"R1833","pred":"themeOf","subj":"T2963","obj":"T2974"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"BioNLP16_Messiy","denotations":[{"id":"T1944","span":{"begin":1071,"end":1077},"obj":"Protein"},{"id":"T1945","span":{"begin":1202,"end":1206},"obj":"Protein"},{"id":"T1946","span":{"begin":1208,"end":1213},"obj":"Protein"},{"id":"T1947","span":{"begin":1215,"end":1219},"obj":"Protein"},{"id":"T1948","span":{"begin":1221,"end":1225},"obj":"Protein"},{"id":"T1949","span":{"begin":1230,"end":1236},"obj":"Protein"},{"id":"T1950","span":{"begin":1262,"end":1266},"obj":"Protein"},{"id":"T1951","span":{"begin":1268,"end":1272},"obj":"Protein"},{"id":"T1952","span":{"begin":1274,"end":1278},"obj":"Protein"},{"id":"T1953","span":{"begin":1280,"end":1285},"obj":"Protein"},{"id":"T1954","span":{"begin":1287,"end":1292},"obj":"Protein"},{"id":"T1955","span":{"begin":1297,"end":1302},"obj":"Protein"},{"id":"T1956","span":{"begin":1346,"end":1350},"obj":"Protein"},{"id":"T1957","span":{"begin":1420,"end":1424},"obj":"Protein"},{"id":"T1958","span":{"begin":1462,"end":1466},"obj":"Protein"},{"id":"T1959","span":{"begin":1525,"end":1529},"obj":"Protein"},{"id":"T1960","span":{"begin":1600,"end":1606},"obj":"Protein"},{"id":"T1961","span":{"begin":1662,"end":1668},"obj":"Protein"},{"id":"T1962","span":{"begin":1781,"end":1787},"obj":"Protein"},{"id":"T1963","span":{"begin":1976,"end":1982},"obj":"Protein"},{"id":"T1972","span":{"begin":1622,"end":1629},"obj":"Binding"}],"relations":[{"id":"R1060","pred":"themeOf","subj":"T1961","obj":"T1972"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"DLUT931","denotations":[{"id":"T2042","span":{"begin":1071,"end":1077},"obj":"Protein"},{"id":"T2043","span":{"begin":1202,"end":1206},"obj":"Protein"},{"id":"T2044","span":{"begin":1208,"end":1213},"obj":"Protein"},{"id":"T2045","span":{"begin":1215,"end":1219},"obj":"Protein"},{"id":"T2048","span":{"begin":1262,"end":1266},"obj":"Protein"},{"id":"T2049","span":{"begin":1268,"end":1272},"obj":"Protein"},{"id":"T2050","span":{"begin":1274,"end":1278},"obj":"Protein"},{"id":"T2051","span":{"begin":1280,"end":1285},"obj":"Protein"},{"id":"T2052","span":{"begin":1287,"end":1292},"obj":"Protein"},{"id":"T2053","span":{"begin":1297,"end":1302},"obj":"Protein"},{"id":"T2054","span":{"begin":1346,"end":1350},"obj":"Protein"},{"id":"T2055","span":{"begin":1420,"end":1424},"obj":"Protein"},{"id":"T2056","span":{"begin":1462,"end":1466},"obj":"Protein"},{"id":"T2057","span":{"begin":1525,"end":1529},"obj":"Protein"},{"id":"T2058","span":{"begin":1600,"end":1606},"obj":"Protein"},{"id":"T2059","span":{"begin":1662,"end":1668},"obj":"Protein"},{"id":"T2060","span":{"begin":1781,"end":1787},"obj":"Protein"},{"id":"T2061","span":{"begin":1976,"end":1982},"obj":"Protein"},{"id":"T2070","span":{"begin":1622,"end":1629},"obj":"Binding"},{"id":"T2046","span":{"begin":1221,"end":1225},"obj":"Protein"},{"id":"T2047","span":{"begin":1230,"end":1236},"obj":"Protein"}],"relations":[{"id":"R1086","pred":"themeOf","subj":"T2058","obj":"T2070"},{"id":"R1095","pred":"themeOf","subj":"T2059","obj":"T2070"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"bionlp-st-ge-2016-test-ihmc","denotations":[{"id":"T2879","span":{"begin":290,"end":306},"obj":"Entity"},{"id":"T2880","span":{"begin":1808,"end":1835},"obj":"Entity"},{"id":"T2881","span":{"begin":1268,"end":1272},"obj":"Protein"},{"id":"T2883","span":{"begin":959,"end":965},"obj":"Entity"},{"id":"T2884","span":{"begin":1287,"end":1292},"obj":"Protein"},{"id":"T2885","span":{"begin":1297,"end":1302},"obj":"Protein"},{"id":"T2887","span":{"begin":1662,"end":1668},"obj":"Protein"},{"id":"T2888","span":{"begin":1823,"end":1829},"obj":"Protein"},{"id":"T2889","span":{"begin":1462,"end":1466},"obj":"Protein"},{"id":"T2890","span":{"begin":1326,"end":1330},"obj":"Protein"},{"id":"T2891","span":{"begin":1416,"end":1438},"obj":"Entity"},{"id":"T2892","span":{"begin":1781,"end":1787},"obj":"Protein"},{"id":"T2893","span":{"begin":1808,"end":1812},"obj":"Protein"},{"id":"T2894","span":{"begin":1215,"end":1219},"obj":"Protein"},{"id":"T2895","span":{"begin":317,"end":321},"obj":"Protein"},{"id":"T2896","span":{"begin":1655,"end":1677},"obj":"Entity"},{"id":"T2901","span":{"begin":1274,"end":1278},"obj":"Protein"},{"id":"T2903","span":{"begin":1054,"end":1077},"obj":"Protein"},{"id":"T2904","span":{"begin":1504,"end":1510},"obj":"Protein"},{"id":"T2906","span":{"begin":1392,"end":1410},"obj":"Entity"},{"id":"T2907","span":{"begin":1019,"end":1022},"obj":"Entity"},{"id":"T2909","span":{"begin":1321,"end":1373},"obj":"Entity"},{"id":"T2910","span":{"begin":959,"end":980},"obj":"Entity"},{"id":"T2911","span":{"begin":901,"end":905},"obj":"Entity"},{"id":"T2914","span":{"begin":790,"end":810},"obj":"Protein"},{"id":"T2916","span":{"begin":1440,"end":1487},"obj":"Entity"},{"id":"T2917","span":{"begin":1630,"end":1654},"obj":"Protein"},{"id":"T2919","span":{"begin":1262,"end":1266},"obj":"Protein"},{"id":"T2921","span":{"begin":1521,"end":1543},"obj":"Entity"},{"id":"T2922","span":{"begin":1567,"end":1607},"obj":"Entity"},{"id":"T2923","span":{"begin":1202,"end":1206},"obj":"Protein"},{"id":"T2927","span":{"begin":1608,"end":1677},"obj":"Binding"},{"id":"T2836","span":{"begin":1208,"end":1213},"obj":"Protein"},{"id":"T2837","span":{"begin":717,"end":733},"obj":"Entity"},{"id":"T2838","span":{"begin":865,"end":906},"obj":"Entity"},{"id":"T2839","span":{"begin":1114,"end":1115},"obj":"Entity"},{"id":"T2840","span":{"begin":1492,"end":1515},"obj":"Entity"},{"id":"T2842","span":{"begin":1342,"end":1373},"obj":"Entity"},{"id":"T2844","span":{"begin":1420,"end":1424},"obj":"Protein"},{"id":"T2845","span":{"begin":1458,"end":1482},"obj":"Entity"},{"id":"T2847","span":{"begin":1727,"end":1730},"obj":"Entity"},{"id":"T2849","span":{"begin":1221,"end":1225},"obj":"Protein"},{"id":"T2852","span":{"begin":1777,"end":1836},"obj":"Entity"},{"id":"T2854","span":{"begin":1346,"end":1350},"obj":"Protein"},{"id":"T2859","span":{"begin":1058,"end":1070},"obj":"Protein"},{"id":"T2860","span":{"begin":1280,"end":1285},"obj":"Protein"},{"id":"T2864","span":{"begin":1972,"end":1991},"obj":"Entity"},{"id":"T2865","span":{"begin":1814,"end":1818},"obj":"Protein"},{"id":"T2866","span":{"begin":1230,"end":1236},"obj":"Protein"},{"id":"T2867","span":{"begin":1976,"end":1982},"obj":"Protein"},{"id":"T2869","span":{"begin":309,"end":315},"obj":"Protein"},{"id":"T2872","span":{"begin":262,"end":266},"obj":"Protein"},{"id":"T2874","span":{"begin":1525,"end":1529},"obj":"Protein"},{"id":"T2875","span":{"begin":1597,"end":1606},"obj":"Protein"}],"relations":[{"id":"R1839","pred":"themeOf","subj":"T2917","obj":"T2927"},{"id":"R1841","pred":"partOf","subj":"T2921","obj":"T2874"},{"id":"R1798","pred":"partOf","subj":"T2842","obj":"T2854"},{"id":"R1802","pred":"partOf","subj":"T2845","obj":"T2889"},{"id":"R1805","pred":"partOf","subj":"T2852","obj":"T2892"},{"id":"R1811","pred":"partOf","subj":"T2864","obj":"T2867"},{"id":"R1829","pred":"partOf","subj":"T2891","obj":"T2844"},{"id":"R1830","pred":"partOf","subj":"T2896","obj":"T2887"},{"id":"R1831","pred":"themeOf","subj":"T2896","obj":"T2927"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

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addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"bionlp-st-ge-2016-test-tees","denotations":[{"id":"T1999","span":{"begin":262,"end":266},"obj":"Protein"},{"id":"T2000","span":{"begin":290,"end":315},"obj":"Protein"},{"id":"T2001","span":{"begin":317,"end":321},"obj":"Protein"},{"id":"T2002","span":{"begin":248,"end":258},"obj":"Negative_regulation"},{"id":"T2003","span":{"begin":1058,"end":1077},"obj":"Protein"},{"id":"T2004","span":{"begin":1202,"end":1206},"obj":"Protein"},{"id":"T2005","span":{"begin":1208,"end":1213},"obj":"Protein"},{"id":"T2006","span":{"begin":1215,"end":1225},"obj":"Protein"},{"id":"T2007","span":{"begin":1230,"end":1236},"obj":"Protein"},{"id":"T2008","span":{"begin":1262,"end":1266},"obj":"Protein"},{"id":"T2009","span":{"begin":1268,"end":1272},"obj":"Protein"},{"id":"T2010","span":{"begin":1274,"end":1278},"obj":"Protein"},{"id":"T2011","span":{"begin":1280,"end":1285},"obj":"Protein"},{"id":"T2012","span":{"begin":1287,"end":1292},"obj":"Protein"},{"id":"T2013","span":{"begin":1297,"end":1302},"obj":"Protein"},{"id":"T2014","span":{"begin":1179,"end":1189},"obj":"Gene_expression"},{"id":"T2015","span":{"begin":1179,"end":1189},"obj":"Gene_expression"},{"id":"T2016","span":{"begin":1326,"end":1336},"obj":"Protein"},{"id":"T2017","span":{"begin":1382,"end":1384},"obj":"Protein"},{"id":"T2018","span":{"begin":1443,"end":1452},"obj":"Protein"},{"id":"T2019","span":{"begin":1462,"end":1475},"obj":"Protein"},{"id":"T2020","span":{"begin":1477,"end":1481},"obj":"Protein"},{"id":"T2021","span":{"begin":1600,"end":1606},"obj":"Protein"},{"id":"T2022","span":{"begin":1662,"end":1677},"obj":"Protein"},{"id":"T2023","span":{"begin":1622,"end":1629},"obj":"Binding"},{"id":"T2024","span":{"begin":1781,"end":1796},"obj":"Protein"},{"id":"T2025","span":{"begin":1808,"end":1812},"obj":"Protein"},{"id":"T2026","span":{"begin":1814,"end":1818},"obj":"Protein"},{"id":"T2027","span":{"begin":1823,"end":1835},"obj":"Protein"},{"id":"T2028","span":{"begin":1750,"end":1755},"obj":"Entity"},{"id":"T2029","span":{"begin":1976,"end":1991},"obj":"Protein"}],"relations":[{"id":"R1070","pred":"themeOf","subj":"T2004","obj":"T2014"},{"id":"R1071","pred":"themeOf","subj":"T2005","obj":"T2015"},{"id":"R1072","pred":"themeOf","subj":"T2022","obj":"T2023"},{"id":"R1083","pred":"partOf","subj":"T2024","obj":"T2028"},{"id":"R1084","pred":"partOf","subj":"T2027","obj":"T2028"},{"id":"R1085","pred":"partOf","subj":"T2025","obj":"T2028"},{"id":"R1069","pred":"themeOf","subj":"T1999","obj":"T2002"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"testone","denotations":[{"id":"T960","span":{"begin":1071,"end":1077},"obj":"Protein"},{"id":"T961","span":{"begin":1202,"end":1206},"obj":"Protein"},{"id":"T962","span":{"begin":1208,"end":1213},"obj":"Protein"},{"id":"T963","span":{"begin":1215,"end":1219},"obj":"Protein"},{"id":"T964","span":{"begin":1221,"end":1225},"obj":"Protein"},{"id":"T965","span":{"begin":1230,"end":1236},"obj":"Protein"},{"id":"T966","span":{"begin":1262,"end":1266},"obj":"Protein"},{"id":"T967","span":{"begin":1268,"end":1272},"obj":"Protein"},{"id":"T968","span":{"begin":1274,"end":1278},"obj":"Protein"},{"id":"T969","span":{"begin":1280,"end":1285},"obj":"Protein"},{"id":"T970","span":{"begin":1287,"end":1292},"obj":"Protein"},{"id":"T971","span":{"begin":1297,"end":1302},"obj":"Protein"},{"id":"T972","span":{"begin":1346,"end":1350},"obj":"Protein"},{"id":"T973","span":{"begin":1420,"end":1424},"obj":"Protein"},{"id":"T974","span":{"begin":1462,"end":1466},"obj":"Protein"},{"id":"T975","span":{"begin":1525,"end":1529},"obj":"Protein"},{"id":"T976","span":{"begin":1600,"end":1606},"obj":"Protein"},{"id":"T977","span":{"begin":1662,"end":1668},"obj":"Protein"},{"id":"T978","span":{"begin":1781,"end":1787},"obj":"Protein"},{"id":"T979","span":{"begin":1976,"end":1982},"obj":"Protein"},{"id":"T988","span":{"begin":539,"end":546},"obj":"Regulation"},{"id":"T989","span":{"begin":1425,"end":1433},"obj":"Entity"},{"id":"T990","span":{"begin":1448,"end":1452},"obj":"Entity"},{"id":"T991","span":{"begin":1622,"end":1629},"obj":"Binding"},{"id":"T992","span":{"begin":1669,"end":1677},"obj":"Entity"}],"relations":[{"id":"R363","pred":"themeOf","subj":"T976","obj":"T991"},{"id":"R368","pred":"partOf","subj":"T989","obj":"T973"},{"id":"R369","pred":"themeOf","subj":"T992","obj":"T991"},{"id":"R370","pred":"partOf","subj":"T992","obj":"T977"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}

{"project":"test3","denotations":[{"id":"T1005","span":{"begin":1071,"end":1077},"obj":"Protein"},{"id":"T1006","span":{"begin":1202,"end":1206},"obj":"Protein"},{"id":"T1007","span":{"begin":1208,"end":1213},"obj":"Protein"},{"id":"T1008","span":{"begin":1215,"end":1219},"obj":"Protein"},{"id":"T1009","span":{"begin":1221,"end":1225},"obj":"Protein"},{"id":"T1010","span":{"begin":1230,"end":1236},"obj":"Protein"},{"id":"T1011","span":{"begin":1262,"end":1266},"obj":"Protein"},{"id":"T1012","span":{"begin":1268,"end":1272},"obj":"Protein"},{"id":"T1013","span":{"begin":1274,"end":1278},"obj":"Protein"},{"id":"T1014","span":{"begin":1280,"end":1285},"obj":"Protein"},{"id":"T1015","span":{"begin":1287,"end":1292},"obj":"Protein"},{"id":"T1016","span":{"begin":1297,"end":1302},"obj":"Protein"},{"id":"T1017","span":{"begin":1346,"end":1350},"obj":"Protein"},{"id":"T1018","span":{"begin":1420,"end":1424},"obj":"Protein"},{"id":"T1019","span":{"begin":1462,"end":1466},"obj":"Protein"},{"id":"T1020","span":{"begin":1525,"end":1529},"obj":"Protein"},{"id":"T1021","span":{"begin":1600,"end":1606},"obj":"Protein"},{"id":"T1022","span":{"begin":1662,"end":1668},"obj":"Protein"},{"id":"T1023","span":{"begin":1781,"end":1787},"obj":"Protein"},{"id":"T1024","span":{"begin":1976,"end":1982},"obj":"Protein"},{"id":"T1046","span":{"begin":539,"end":546},"obj":"Regulation"},{"id":"T1047","span":{"begin":1071,"end":1077},"obj":"Protein"},{"id":"T1048","span":{"begin":1142,"end":1148},"obj":"Regulation"},{"id":"T1049","span":{"begin":1202,"end":1206},"obj":"Protein"},{"id":"T1050","span":{"begin":1208,"end":1213},"obj":"Protein"},{"id":"T1051","span":{"begin":1215,"end":1219},"obj":"Protein"},{"id":"T1052","span":{"begin":1221,"end":1225},"obj":"Protein"},{"id":"T1053","span":{"begin":1230,"end":1236},"obj":"Protein"},{"id":"T1054","span":{"begin":1262,"end":1266},"obj":"Protein"},{"id":"T1055","span":{"begin":1268,"end":1272},"obj":"Protein"},{"id":"T1056","span":{"begin":1274,"end":1278},"obj":"Protein"},{"id":"T1057","span":{"begin":1280,"end":1285},"obj":"Protein"},{"id":"T1058","span":{"begin":1287,"end":1292},"obj":"Protein"},{"id":"T1059","span":{"begin":1297,"end":1302},"obj":"Protein"},{"id":"T1060","span":{"begin":1346,"end":1350},"obj":"Protein"},{"id":"T1061","span":{"begin":1420,"end":1424},"obj":"Protein"},{"id":"T1062","span":{"begin":1462,"end":1466},"obj":"Protein"},{"id":"T1063","span":{"begin":1525,"end":1529},"obj":"Protein"},{"id":"T1064","span":{"begin":1600,"end":1606},"obj":"Protein"},{"id":"T1065","span":{"begin":1622,"end":1629},"obj":"Binding"},{"id":"T1066","span":{"begin":1662,"end":1668},"obj":"Protein"},{"id":"T1067","span":{"begin":1669,"end":1677},"obj":"Entity"},{"id":"T1068","span":{"begin":1781,"end":1787},"obj":"Protein"},{"id":"T1069","span":{"begin":1954,"end":1961},"obj":"Binding"},{"id":"T1070","span":{"begin":1976,"end":1982},"obj":"Protein"}],"relations":[{"id":"R388","pred":"themeOf","subj":"T1067","obj":"T1065"},{"id":"R389","pred":"partOf","subj":"T1067","obj":"T1066"},{"id":"R390","pred":"themeOf","subj":"T1070","obj":"T1069"}],"text":"In addition, β-1→3-D-glucans seem to be able to modify the response to pro-inflammatory stimuli or even sepsis. In a murine polymicrobial sepsis model, β-1→3-D-glucan [20] treatment resulted in decreased septic morbidity and mortality mediated via inhibition of NFκB and stimulation of the phosphoinositide-3-kinase (PI3K) pathway [21,22]. These and other animal studies [23,24] as well as a clinical trial [25] support a protective role of β-1→3-D-glucan in certain pro-inflammatory conditions. The mechanisms underlying these beneficial effects of β-1→3-D-glucan are only partially resolved, especially in humans. Thus, the aim of this study was to elucidate molecular and cellular mechanisms of β-1→3-D-glucans on human leukocytes in pro-inflammatory conditions with special emphasis on the cytokine profile and its transcriptional regulation. For this purpose, peripheral blood mononuclear cells (PBMC) were exposed to a well-defined β-1→3-D-glucan, i.e. glucan phosphate (GP) [20,26], alone or simultaneously with LPS from gram-negative bacteria or the superantigen TSST-1 from gram-positive bacteria over 48 h. Because of the potential effect of β-1→3-D-glucan on cytokine production [12,16-19], TNFα, IL-1β, IL-6, IL-8 and IL-1RA were measured as well as IFNγ, IL-2, IL-4, IL-10, IL-12 and TGFβ1. Correspondingly, four NFκB sites from the TNFα promoter (κ consensus, κ1, κ2, κ3) [27], a κ consensus site from the IL-8 promoter [28], an NFAT site from the IFNγ promoter (ATP2) [29] and a consensus NFIL-6 site from the IL-6 promoter [13] were examined. Because of the anti-inflammatory role of IL-1RA, we focused on binding of transcription factors to the IL-1RA promoter. An inhibitory element and three positive-acting LPS-response elements (LRE-1, LRE-2 and LRE-3) in the IL-1RA promoter, including NFκB, PU.1 and NFIL-6 sites, have been characterized previously [30-33]. Using computational analysis for homology search [34], we looked for new binding motifs in the IL-1RA promoter."}