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even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    bionlp-st-ge-2016-test-proteins

    {"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T12365","span":{"begin":410,"end":414},"obj":"Protein"},{"id":"T12364","span":{"begin":400,"end":405},"obj":"Protein"},{"id":"T12363","span":{"begin":320,"end":326},"obj":"Protein"},{"id":"T12362","span":{"begin":314,"end":319},"obj":"Protein"},{"id":"T12361","span":{"begin":299,"end":305},"obj":"Protein"},{"id":"T12360","span":{"begin":135,"end":141},"obj":"Protein"},{"id":"T12389","span":{"begin":2092,"end":2098},"obj":"Protein"},{"id":"T12388","span":{"begin":1882,"end":1888},"obj":"Protein"},{"id":"T12387","span":{"begin":1581,"end":1587},"obj":"Protein"},{"id":"T12386","span":{"begin":1568,"end":1572},"obj":"Protein"},{"id":"T12385","span":{"begin":1366,"end":1372},"obj":"Protein"},{"id":"T12384","span":{"begin":1283,"end":1287},"obj":"Protein"},{"id":"T12383","span":{"begin":1239,"end":1245},"obj":"Protein"},{"id":"T12382","span":{"begin":1083,"end":1089},"obj":"Protein"},{"id":"T12381","span":{"begin":1030,"end":1036},"obj":"Protein"},{"id":"T12380","span":{"begin":1002,"end":1008},"obj":"Protein"},{"id":"T12379","span":{"begin":894,"end":900},"obj":"Protein"},{"id":"T12378","span":{"begin":879,"end":885},"obj":"Protein"},{"id":"T12377","span":{"begin":803,"end":807},"obj":"Protein"},{"id":"T12376","span":{"begin":754,"end":760},"obj":"Protein"},{"id":"T12375","span":{"begin":708,"end":712},"obj":"Protein"},{"id":"T12374","span":{"begin":700,"end":704},"obj":"Protein"},{"id":"T12373","span":{"begin":693,"end":698},"obj":"Protein"},{"id":"T12372","span":{"begin":687,"end":691},"obj":"Protein"},{"id":"T12371","span":{"begin":656,"end":662},"obj":"Protein"},{"id":"T12370","span":{"begin":647,"end":651},"obj":"Protein"},{"id":"T12369","span":{"begin":594,"end":598},"obj":"Protein"},{"id":"T12368","span":{"begin":583,"end":589},"obj":"Protein"},{"id":"T12367","span":{"begin":551,"end":557},"obj":"Protein"},{"id":"T12366","span":{"begin":474,"end":480},"obj":"Protein"},{"id":"T12405","span":{"begin":3029,"end":3033},"obj":"Protein"},{"id":"T12404","span":{"begin":3014,"end":3018},"obj":"Protein"},{"id":"T12403","span":{"begin":2998,"end":3004},"obj":"Protein"},{"id":"T12402","span":{"begin":2927,"end":2932},"obj":"Protein"},{"id":"T12401","span":{"begin":2853,"end":2859},"obj":"Protein"},{"id":"T12400","span":{"begin":2825,"end":2831},"obj":"Protein"},{"id":"T12399","span":{"begin":2819,"end":2824},"obj":"Protein"},{"id":"T12398","span":{"begin":2785,"end":2789},"obj":"Protein"},{"id":"T12397","span":{"begin":2739,"end":2744},"obj":"Protein"},{"id":"T12396","span":{"begin":2727,"end":2733},"obj":"Protein"},{"id":"T12395","span":{"begin":2636,"end":2642},"obj":"Protein"},{"id":"T12394","span":{"begin":2608,"end":2614},"obj":"Protein"},{"id":"T12393","span":{"begin":2602,"end":2607},"obj":"Protein"},{"id":"T12392","span":{"begin":2486,"end":2492},"obj":"Protein"},{"id":"T12391","span":{"begin":2471,"end":2477},"obj":"Protein"},{"id":"T12390","span":{"begin":2298,"end":2304},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"Potentially even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    bionlp-st-ge-2016-uniprot

    {"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T14314","span":{"begin":879,"end":885},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T14313","span":{"begin":754,"end":760},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T14312","span":{"begin":551,"end":557},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T14311","span":{"begin":299,"end":305},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T14310","span":{"begin":135,"end":141},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T14304","span":{"begin":2927,"end":2932},"obj":"http://www.uniprot.org/uniprot/P01584"},{"id":"T14303","span":{"begin":2819,"end":2824},"obj":"http://www.uniprot.org/uniprot/P01584"},{"id":"T14302","span":{"begin":2739,"end":2744},"obj":"http://www.uniprot.org/uniprot/P01584"},{"id":"T14301","span":{"begin":2602,"end":2607},"obj":"http://www.uniprot.org/uniprot/P01584"},{"id":"T14300","span":{"begin":693,"end":698},"obj":"http://www.uniprot.org/uniprot/P01584"},{"id":"T14299","span":{"begin":400,"end":405},"obj":"http://www.uniprot.org/uniprot/P01584"},{"id":"T14298","span":{"begin":314,"end":319},"obj":"http://www.uniprot.org/uniprot/P01584"},{"id":"T14295","span":{"begin":1687,"end":1691},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T14294","span":{"begin":1568,"end":1572},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T14293","span":{"begin":1283,"end":1287},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T14292","span":{"begin":803,"end":807},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T14291","span":{"begin":687,"end":691},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T14275","span":{"begin":2825,"end":2831},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T14274","span":{"begin":2727,"end":2733},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T14273","span":{"begin":2608,"end":2614},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T14272","span":{"begin":2486,"end":2492},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T14271","span":{"begin":1882,"end":1888},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T14270","span":{"begin":1612,"end":1618},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T14269","span":{"begin":1581,"end":1587},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T14268","span":{"begin":1366,"end":1372},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T14267","span":{"begin":1002,"end":1008},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T14266","span":{"begin":894,"end":900},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T14265","span":{"begin":656,"end":662},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T14321","span":{"begin":2636,"end":2642},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T14320","span":{"begin":2471,"end":2477},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T14319","span":{"begin":2298,"end":2304},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T14318","span":{"begin":2092,"end":2098},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T14317","span":{"begin":1239,"end":1245},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T14316","span":{"begin":1083,"end":1089},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T14315","span":{"begin":1030,"end":1036},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T14250","span":{"begin":647,"end":651},"obj":"http://www.uniprot.org/uniprot/P10145"},{"id":"T14264","span":{"begin":474,"end":480},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T14263","span":{"begin":320,"end":326},"obj":"http://www.uniprot.org/uniprot/P18510"},{"id":"T14329","span":{"begin":3029,"end":3033},"obj":"http://www.uniprot.org/uniprot/P60568"},{"id":"T14328","span":{"begin":700,"end":704},"obj":"http://www.uniprot.org/uniprot/P05231"},{"id":"T14327","span":{"begin":410,"end":414},"obj":"http://www.uniprot.org/uniprot/P05231"},{"id":"T14323","span":{"begin":2998,"end":3004},"obj":"http://www.uniprot.org/uniprot/P06886"},{"id":"T14322","span":{"begin":2853,"end":2859},"obj":"http://www.uniprot.org/uniprot/P06886"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"Potentially even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    GO-BP

    {"project":"GO-BP","denotations":[{"id":"T11935","span":{"begin":3029,"end":3044},"obj":"http://purl.obolibrary.org/obo/GO_0032663"},{"id":"T11934","span":{"begin":3029,"end":3044},"obj":"http://purl.obolibrary.org/obo/GO_0032623"},{"id":"T11933","span":{"begin":2453,"end":2463},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T11932","span":{"begin":1314,"end":1324},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T11931","span":{"begin":1208,"end":1218},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T11930","span":{"begin":460,"end":470},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T11929","span":{"begin":386,"end":396},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T11928","span":{"begin":254,"end":266},"obj":"http://purl.obolibrary.org/obo/GO_0006954"},{"id":"T11916","span":{"begin":2551,"end":2564},"obj":"http://purl.obolibrary.org/obo/GO_0006351"}],"text":"Potentially even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    GO-MF

    {"project":"GO-MF","denotations":[{"id":"T12571","span":{"begin":3029,"end":3033},"obj":"http://purl.obolibrary.org/obo/GO_0005134"},{"id":"T12570","span":{"begin":3014,"end":3018},"obj":"http://purl.obolibrary.org/obo/GO_0005149"},{"id":"T12569","span":{"begin":2785,"end":2789},"obj":"http://purl.obolibrary.org/obo/GO_0005149"},{"id":"T12567","span":{"begin":700,"end":704},"obj":"http://purl.obolibrary.org/obo/GO_0005138"},{"id":"T12566","span":{"begin":410,"end":414},"obj":"http://purl.obolibrary.org/obo/GO_0005138"},{"id":"T12561","span":{"begin":647,"end":651},"obj":"http://purl.obolibrary.org/obo/GO_0005153"},{"id":"T12547","span":{"begin":2313,"end":2320},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12546","span":{"begin":2107,"end":2114},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12545","span":{"begin":1748,"end":1755},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12544","span":{"begin":1542,"end":1549},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12543","span":{"begin":1259,"end":1266},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12542","span":{"begin":1098,"end":1105},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12541","span":{"begin":1054,"end":1061},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12540","span":{"begin":769,"end":776},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12539","span":{"begin":566,"end":573},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Potentially even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    GO-CC

    {"project":"GO-CC","denotations":[{"id":"T12574","span":{"begin":3060,"end":3065},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Potentially even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    sentences

    {"project":"sentences","denotations":[{"id":"T11885","span":{"begin":2975,"end":3093},"obj":"Sentence"},{"id":"T11884","span":{"begin":2799,"end":2974},"obj":"Sentence"},{"id":"T11883","span":{"begin":2653,"end":2798},"obj":"Sentence"},{"id":"T11882","span":{"begin":2505,"end":2652},"obj":"Sentence"},{"id":"T11881","span":{"begin":2269,"end":2504},"obj":"Sentence"},{"id":"T11880","span":{"begin":2150,"end":2268},"obj":"Sentence"},{"id":"T11879","span":{"begin":1931,"end":2149},"obj":"Sentence"},{"id":"T11878","span":{"begin":1765,"end":1930},"obj":"Sentence"},{"id":"T11877","span":{"begin":1383,"end":1764},"obj":"Sentence"},{"id":"T11876","span":{"begin":1167,"end":1382},"obj":"Sentence"},{"id":"T11875","span":{"begin":961,"end":1166},"obj":"Sentence"},{"id":"T11874","span":{"begin":723,"end":960},"obj":"Sentence"},{"id":"T11873","span":{"begin":482,"end":722},"obj":"Sentence"},{"id":"T11872","span":{"begin":276,"end":481},"obj":"Sentence"},{"id":"T11871","span":{"begin":0,"end":275},"obj":"Sentence"},{"id":"T201","span":{"begin":0,"end":275},"obj":"Sentence"},{"id":"T202","span":{"begin":276,"end":481},"obj":"Sentence"},{"id":"T203","span":{"begin":482,"end":722},"obj":"Sentence"},{"id":"T204","span":{"begin":723,"end":960},"obj":"Sentence"},{"id":"T205","span":{"begin":961,"end":1166},"obj":"Sentence"},{"id":"T206","span":{"begin":1167,"end":1382},"obj":"Sentence"},{"id":"T207","span":{"begin":1383,"end":1764},"obj":"Sentence"},{"id":"T208","span":{"begin":1765,"end":1930},"obj":"Sentence"},{"id":"T209","span":{"begin":1931,"end":2149},"obj":"Sentence"},{"id":"T210","span":{"begin":2150,"end":2268},"obj":"Sentence"},{"id":"T211","span":{"begin":2269,"end":2504},"obj":"Sentence"},{"id":"T212","span":{"begin":2505,"end":2652},"obj":"Sentence"},{"id":"T213","span":{"begin":2653,"end":2798},"obj":"Sentence"},{"id":"T214","span":{"begin":2799,"end":2974},"obj":"Sentence"},{"id":"T215","span":{"begin":2975,"end":3093},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Potentially even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    simple1

    {"project":"simple1","denotations":[{"id":"T12784","span":{"begin":3029,"end":3033},"obj":"Protein"},{"id":"T12783","span":{"begin":3014,"end":3018},"obj":"Protein"},{"id":"T12782","span":{"begin":2998,"end":3004},"obj":"Protein"},{"id":"T12781","span":{"begin":2927,"end":2932},"obj":"Protein"},{"id":"T12780","span":{"begin":2853,"end":2859},"obj":"Protein"},{"id":"T12779","span":{"begin":2825,"end":2831},"obj":"Protein"},{"id":"T12778","span":{"begin":2819,"end":2824},"obj":"Protein"},{"id":"T12777","span":{"begin":2785,"end":2789},"obj":"Protein"},{"id":"T12776","span":{"begin":2739,"end":2744},"obj":"Protein"},{"id":"T12775","span":{"begin":2727,"end":2733},"obj":"Protein"},{"id":"T12774","span":{"begin":2636,"end":2642},"obj":"Protein"},{"id":"T12773","span":{"begin":2608,"end":2614},"obj":"Protein"},{"id":"T12772","span":{"begin":2602,"end":2607},"obj":"Protein"},{"id":"T12771","span":{"begin":2486,"end":2492},"obj":"Protein"},{"id":"T12770","span":{"begin":2471,"end":2477},"obj":"Protein"},{"id":"T12769","span":{"begin":2298,"end":2304},"obj":"Protein"},{"id":"T12768","span":{"begin":2092,"end":2098},"obj":"Protein"},{"id":"T12767","span":{"begin":1882,"end":1888},"obj":"Protein"},{"id":"T12766","span":{"begin":1581,"end":1587},"obj":"Protein"},{"id":"T12765","span":{"begin":1568,"end":1572},"obj":"Protein"},{"id":"T12764","span":{"begin":1366,"end":1372},"obj":"Protein"},{"id":"T12763","span":{"begin":1283,"end":1287},"obj":"Protein"},{"id":"T12762","span":{"begin":1239,"end":1245},"obj":"Protein"},{"id":"T12761","span":{"begin":1083,"end":1089},"obj":"Protein"},{"id":"T12760","span":{"begin":1030,"end":1036},"obj":"Protein"},{"id":"T12759","span":{"begin":1002,"end":1008},"obj":"Protein"},{"id":"T12758","span":{"begin":894,"end":900},"obj":"Protein"},{"id":"T12757","span":{"begin":879,"end":885},"obj":"Protein"},{"id":"T12756","span":{"begin":803,"end":807},"obj":"Protein"},{"id":"T12755","span":{"begin":754,"end":760},"obj":"Protein"},{"id":"T12754","span":{"begin":708,"end":712},"obj":"Protein"},{"id":"T12753","span":{"begin":700,"end":704},"obj":"Protein"},{"id":"T12752","span":{"begin":693,"end":698},"obj":"Protein"},{"id":"T12751","span":{"begin":687,"end":691},"obj":"Protein"},{"id":"T12750","span":{"begin":656,"end":662},"obj":"Protein"},{"id":"T12749","span":{"begin":647,"end":651},"obj":"Protein"},{"id":"T12748","span":{"begin":594,"end":598},"obj":"Protein"},{"id":"T12747","span":{"begin":583,"end":589},"obj":"Protein"},{"id":"T12746","span":{"begin":551,"end":557},"obj":"Protein"},{"id":"T12745","span":{"begin":474,"end":480},"obj":"Protein"},{"id":"T12744","span":{"begin":410,"end":414},"obj":"Protein"},{"id":"T12743","span":{"begin":400,"end":405},"obj":"Protein"},{"id":"T12742","span":{"begin":320,"end":326},"obj":"Protein"},{"id":"T12741","span":{"begin":314,"end":319},"obj":"Protein"},{"id":"T12740","span":{"begin":299,"end":305},"obj":"Protein"},{"id":"T12739","span":{"begin":135,"end":141},"obj":"Protein"}],"text":"Potentially even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    BioNLP16_DUT

    {"project":"BioNLP16_DUT","denotations":[{"id":"T16580","span":{"begin":320,"end":326},"obj":"Protein"},{"id":"T16579","span":{"begin":314,"end":319},"obj":"Protein"},{"id":"T16578","span":{"begin":299,"end":305},"obj":"Protein"},{"id":"T16577","span":{"begin":135,"end":141},"obj":"Protein"},{"id":"T16681","span":{"begin":3019,"end":3028},"obj":"Positive_regulation"},{"id":"T16680","span":{"begin":3005,"end":3012},"obj":"Positive_regulation"},{"id":"T16679","span":{"begin":2986,"end":2993},"obj":"Negative_regulation"},{"id":"T16678","span":{"begin":3034,"end":3044},"obj":"Gene_expression"},{"id":"T16677","span":{"begin":2717,"end":2723},"obj":"Negative_regulation"},{"id":"T16676","span":{"begin":2586,"end":2594},"obj":"Negative_regulation"},{"id":"T16675","span":{"begin":2478,"end":2485},"obj":"Positive_regulation"},{"id":"T16674","span":{"begin":2493,"end":2503},"obj":"Gene_expression"},{"id":"T16673","span":{"begin":2450,"end":2463},"obj":"Positive_regulation"},{"id":"T16672","span":{"begin":1311,"end":1324},"obj":"Positive_regulation"},{"id":"T16671","span":{"begin":860,"end":871},"obj":"Positive_regulation"},{"id":"T16670","span":{"begin":901,"end":911},"obj":"Gene_expression"},{"id":"T16669","span":{"begin":886,"end":893},"obj":"Positive_regulation"},{"id":"T16668","span":{"begin":566,"end":573},"obj":"Binding"},{"id":"T16667","span":{"begin":558,"end":565},"obj":"Positive_regulation"},{"id":"T16666","span":{"begin":457,"end":470},"obj":"Positive_regulation"},{"id":"T16665","span":{"begin":381,"end":396},"obj":"Negative_regulation"},{"id":"T16664","span":{"begin":306,"end":313},"obj":"Positive_regulation"},{"id":"T16620","span":{"begin":3014,"end":3018},"obj":"Protein"},{"id":"T16622","span":{"begin":2998,"end":3004},"obj":"Protein"},{"id":"T16621","span":{"begin":3029,"end":3033},"obj":"Protein"},{"id":"T16619","span":{"begin":2927,"end":2932},"obj":"Protein"},{"id":"T16618","span":{"begin":2853,"end":2859},"obj":"Protein"},{"id":"T16617","span":{"begin":2825,"end":2831},"obj":"Protein"},{"id":"T16616","span":{"begin":2819,"end":2824},"obj":"Protein"},{"id":"T16615","span":{"begin":2785,"end":2789},"obj":"Protein"},{"id":"T16614","span":{"begin":2739,"end":2744},"obj":"Protein"},{"id":"T16613","span":{"begin":2727,"end":2733},"obj":"Protein"},{"id":"T16612","span":{"begin":2636,"end":2642},"obj":"Protein"},{"id":"T16611","span":{"begin":2608,"end":2614},"obj":"Protein"},{"id":"T16610","span":{"begin":2602,"end":2607},"obj":"Protein"},{"id":"T16609","span":{"begin":2486,"end":2492},"obj":"Protein"},{"id":"T16608","span":{"begin":2471,"end":2477},"obj":"Protein"},{"id":"T16607","span":{"begin":2298,"end":2304},"obj":"Protein"},{"id":"T16606","span":{"begin":2092,"end":2098},"obj":"Protein"},{"id":"T16605","span":{"begin":1882,"end":1888},"obj":"Protein"},{"id":"T16604","span":{"begin":1581,"end":1587},"obj":"Protein"},{"id":"T16603","span":{"begin":1568,"end":1572},"obj":"Protein"},{"id":"T16602","span":{"begin":1366,"end":1372},"obj":"Protein"},{"id":"T16601","span":{"begin":1283,"end":1287},"obj":"Protein"},{"id":"T16600","span":{"begin":1239,"end":1245},"obj":"Protein"},{"id":"T16599","span":{"begin":1083,"end":1089},"obj":"Protein"},{"id":"T16598","span":{"begin":1030,"end":1036},"obj":"Protein"},{"id":"T16597","span":{"begin":1002,"end":1008},"obj":"Protein"},{"id":"T16596","span":{"begin":894,"end":900},"obj":"Protein"},{"id":"T16595","span":{"begin":879,"end":885},"obj":"Protein"},{"id":"T16594","span":{"begin":803,"end":807},"obj":"Protein"},{"id":"T16593","span":{"begin":754,"end":760},"obj":"Protein"},{"id":"T16592","span":{"begin":708,"end":712},"obj":"Protein"},{"id":"T16591","span":{"begin":700,"end":704},"obj":"Protein"},{"id":"T16590","span":{"begin":693,"end":698},"obj":"Protein"},{"id":"T16589","span":{"begin":687,"end":691},"obj":"Protein"},{"id":"T16588","span":{"begin":656,"end":662},"obj":"Protein"},{"id":"T16587","span":{"begin":647,"end":651},"obj":"Protein"},{"id":"T16586","span":{"begin":594,"end":598},"obj":"Protein"},{"id":"T16585","span":{"begin":583,"end":589},"obj":"Protein"},{"id":"T16584","span":{"begin":551,"end":557},"obj":"Protein"},{"id":"T16583","span":{"begin":474,"end":480},"obj":"Protein"},{"id":"T16582","span":{"begin":410,"end":414},"obj":"Protein"},{"id":"T16581","span":{"begin":400,"end":405},"obj":"Protein"}],"relations":[{"id":"R11357","pred":"themeOf","subj":"T16581","obj":"T16665"},{"id":"R11386","pred":"themeOf","subj":"T16582","obj":"T16665"},{"id":"R11391","pred":"themeOf","subj":"T16583","obj":"T16666"},{"id":"R11394","pred":"causeOf","subj":"T16578","obj":"T16664"},{"id":"R11395","pred":"themeOf","subj":"T16584","obj":"T16667"},{"id":"R11396","pred":"themeOf","subj":"T16579","obj":"T16664"},{"id":"R11397","pred":"themeOf","subj":"T16585","obj":"T16668"},{"id":"R11398","pred":"themeOf","subj":"T16586","obj":"T16668"},{"id":"R11399","pred":"themeOf","subj":"T16587","obj":"T16668"},{"id":"R11400","pred":"themeOf","subj":"T16678","obj":"T16681"},{"id":"R1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even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    BioNLP16_Messiy

    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even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    DLUT931

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Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    bionlp-st-ge-2016-test-ihmc

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even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    bionlp-st-ge-2016-spacy-parsed

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even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    bionlp-st-ge-2016-test-tees

    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Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    testone

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even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}

    test3

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even more relevant than the specific cytokine panel induced by GP, we found that, in the presence of other stimuli (LPS or TSST-1), GP ameliorated their pro-inflammatory immune reactions, similar to the effects in murine models of sepsis and inflammation [21-24]. Mainly, GP altered the TSST-1-induced IL-1β/IL-1RA ratio from a pro- to an anti-inflammatory profile via down-regulation of IL-1β and IL-6, at the same time there was a synergistic up-regulation of IL-1RA. In part, this change may be caused by GP-mediated modulations of the TSST-1 induced binding of NFκB, NFIL-6 and NFAT to known and up to now unknown sites within the IL-8 and IL-1RA promoter instead of the TNFα, IL-1β, IL-6 or IFNγ promoter. Accordingly, we found that the TSST-1-induced binding of NFκB to sites from the TNFα promoter negatively correlated with the GP-mediated enhancement of the TSST-1-induced IL-1RA production (r = -0.88; p \u003c 0.01; data not shown in detail). Of the four examined NFκB sites from the IL-1RA promoter, mostly the TSST-1- and LPS-induced binding to the NFκB3 and the TSST-1-induced binding to the new NFκB consensus site seemed to be increased by GP. So, while we observed a GP-mediated down-regulation of the LPS- and the TSST-1-induced NFκB binding to sites of the TNFα promoter, there was an up-regulation to NFκB3 and NFκB consensus sites of the IL-1RA promoter. These seemingly contradictory data could be explained by differences in either NFκB subunits or conserved nucleotides (#1, 2, 3, 10) within the decameric NFκB binding motif between the TNFα and the IL-1RA promoter (for NFκB3 the IL-1RA motif contains a T on position 10 instead of the conserved C in the TNFα motif, see Table 1), probably leading to differences in binding [41,42]. Despite the location of the new NFκB consensus site (-266 and -280) in the inhibitory element (-250 and -294) of the IL-1RA promoter [30], we observed no inhibition. On the other side, we found an inhibitory NFκB2/3 site (-288 and -302) towards the end of the inhibitory element, demonstrating down-regulations of the LPS- and TSST-1-induced binding, which could not be altered by GP. In our opinion, this site may therefore represent at least a part of the previoulsy described inhibitory element [30]. The GP-modulated increase in TSST-1-induced binding to the new NFκB3 and NFκB consensus site, the NFIL-6 site [32] as well as to the novel NFATP2/3 site may explain the synergistic up-regulation of the TSST-1-induced IL-1RA production. We think that this GP-modulated activation of transcription was reflected by the decrease of the IL-1β/IL-1RA ratio following GP + TSST-1 (Fig. 6). In this context, it has been postulated that in vitro a 100fold excess of IL-1RA over IL-1β might control the biological effects of IL-1 [46,47]. Since, in fact, the IL-1β/IL-1RA ratio following GP + TSST-1 is partially less than 0.01, it is not unreasonable to assume that IL-1β bioactivity is inactivated in our system. Indeed, GP reduced the TSST-1-induced, IL-1-dependent IL-2 production of murine EL-4 cells (data not shown in detail)."}