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Promotes LPS-inducible Murine SerpinB2 Proximal Promoter Activity\nSince C/EBP-β binds to the SerpinB2 proximal promoter in an LPS-inducible manner both in vitro and in vivo, we wanted to address the question of whether C/EBP-β was an essential factor for driving transcription from the SerpinB2 promoter in cells in response to LPS. The ability of endogenous C/EBP-β to direct transcription from the SerpinB2 proximal promoter was examined by transfection of the pGLmP-539 murine SerpinB2 luciferase reporter construct into Cebpb+/+ and Cebpb−/− MEFs. We found that LPS-stimulated SerpinB2 promoter activity was significantly increased in Cebpb+/+ MEFs and abrogated in Cebpb−/− MEFs (Fig. 8A), indicating that endogenous C/EBP-β is required for LPS-induced SerpinB2 proximal promoter activity.\n10.1371/journal.pone.0057855.g008 Figure 8 C/EBP-β is necessary for SerpinB2 proximal promoter activity.\n(A) The SerpinB2 proximal promoter is significantly activated in LPS-stimulated Cebpb+/+ MEFs and not in Cebpb−/− MEFs. Murine SerpinB2 gene promoter activity measured in Cebpb+/+ and Cebpb−/− MEFs expressing the pGLmP-539 SerpinB2 promoter-luciferase reporter in the presence or absence of LPS (100 ng/mL). Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. The results represent the mean and SEM of at least three independent experiments performed in triplicate. (*, p\u003c0.05, one-way ANOVA)."}

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Promotes LPS-inducible Murine SerpinB2 Proximal Promoter Activity\nSince C/EBP-β binds to the SerpinB2 proximal promoter in an LPS-inducible manner both in vitro and in vivo, we wanted to address the question of whether C/EBP-β was an essential factor for driving transcription from the SerpinB2 promoter in cells in response to LPS. The ability of endogenous C/EBP-β to direct transcription from the SerpinB2 proximal promoter was examined by transfection of the pGLmP-539 murine SerpinB2 luciferase reporter construct into Cebpb+/+ and Cebpb−/− MEFs. We found that LPS-stimulated SerpinB2 promoter activity was significantly increased in Cebpb+/+ MEFs and abrogated in Cebpb−/− MEFs (Fig. 8A), indicating that endogenous C/EBP-β is required for LPS-induced SerpinB2 proximal promoter activity.\n10.1371/journal.pone.0057855.g008 Figure 8 C/EBP-β is necessary for SerpinB2 proximal promoter activity.\n(A) The SerpinB2 proximal promoter is significantly activated in LPS-stimulated Cebpb+/+ MEFs and not in Cebpb−/− MEFs. Murine SerpinB2 gene promoter activity measured in Cebpb+/+ and Cebpb−/− MEFs expressing the pGLmP-539 SerpinB2 promoter-luciferase reporter in the presence or absence of LPS (100 ng/mL). Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. The results represent the mean and SEM of at least three independent experiments performed in triplicate. (*, p\u003c0.05, one-way ANOVA)."}

    bionlp-st-ge-2016-test-proteins

    {"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T15768","span":{"begin":766,"end":774},"obj":"Protein"},{"id":"T15767","span":{"begin":730,"end":737},"obj":"Protein"},{"id":"T15766","span":{"begin":678,"end":683},"obj":"Protein"},{"id":"T15765","span":{"begin":647,"end":652},"obj":"Protein"},{"id":"T15764","span":{"begin":589,"end":597},"obj":"Protein"},{"id":"T15763","span":{"begin":545,"end":550},"obj":"Protein"},{"id":"T15762","span":{"begin":532,"end":537},"obj":"Protein"},{"id":"T15761","span":{"begin":488,"end":516},"obj":"Protein"},{"id":"T15760","span":{"begin":408,"end":416},"obj":"Protein"},{"id":"T15759","span":{"begin":367,"end":374},"obj":"Protein"},{"id":"T15758","span":{"begin":294,"end":302},"obj":"Protein"},{"id":"T15757","span":{"begin":227,"end":234},"obj":"Protein"},{"id":"T15756","span":{"begin":101,"end":109},"obj":"Protein"},{"id":"T15755","span":{"begin":80,"end":87},"obj":"Protein"},{"id":"T15754","span":{"begin":38,"end":46},"obj":"Protein"},{"id":"T15753","span":{"begin":0,"end":7},"obj":"Protein"},{"id":"T26146","span":{"begin":1404,"end":1411},"obj":"Protein"},{"id":"T26145","span":{"begin":1374,"end":1389},"obj":"Protein"},{"id":"T26144","span":{"begin":1343,"end":1353},"obj":"Protein"},{"id":"T26143","span":{"begin":1304,"end":1328},"obj":"Protein"},{"id":"T26142","span":{"begin":1262,"end":1299},"obj":"Protein"},{"id":"T26141","span":{"begin":1132,"end":1169},"obj":"Protein"},{"id":"T26140","span":{"begin":1093,"end":1098},"obj":"Protein"},{"id":"T26139","span":{"begin":1080,"end":1085},"obj":"Protein"},{"id":"T26138","span":{"begin":1036,"end":1044},"obj":"Protein"},{"id":"T26137","span":{"begin":1014,"end":1019},"obj":"Protein"},{"id":"T26136","span":{"begin":989,"end":994},"obj":"Protein"},{"id":"T26135","span":{"begin":917,"end":925},"obj":"Protein"},{"id":"T26134","span":{"begin":872,"end":880},"obj":"Protein"},{"id":"T26133","span":{"begin":847,"end":854},"obj":"Protein"},{"id":"T26152","span":{"begin":1750,"end":1787},"obj":"Protein"},{"id":"T26151","span":{"begin":1691,"end":1723},"obj":"Protein"},{"id":"T26150","span":{"begin":1666,"end":1673},"obj":"Protein"},{"id":"T26149","span":{"begin":1588,"end":1593},"obj":"Protein"},{"id":"T26148","span":{"begin":1560,"end":1568},"obj":"Protein"},{"id":"T26147","span":{"begin":1503,"end":1510},"obj":"Protein"},{"id":"T26158","span":{"begin":2135,"end":2142},"obj":"Protein"},{"id":"T26157","span":{"begin":2057,"end":2069},"obj":"Protein"},{"id":"T26156","span":{"begin":2019,"end":2051},"obj":"Protein"},{"id":"T26155","span":{"begin":1915,"end":1930},"obj":"Protein"},{"id":"T26154","span":{"begin":1862,"end":1872},"obj":"Protein"},{"id":"T26153","span":{"begin":1792,"end":1816},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"C/EBP-β Promotes LPS-inducible Murine SerpinB2 Proximal Promoter Activity\nSince C/EBP-β binds to the SerpinB2 proximal promoter in an LPS-inducible manner both in vitro and in vivo, we wanted to address the question of whether C/EBP-β was an essential factor for driving transcription from the SerpinB2 promoter in cells in response to LPS. The ability of endogenous C/EBP-β to direct transcription from the SerpinB2 proximal promoter was examined by transfection of the pGLmP-539 murine SerpinB2 luciferase reporter construct into Cebpb+/+ and Cebpb−/− MEFs. We found that LPS-stimulated SerpinB2 promoter activity was significantly increased in Cebpb+/+ MEFs and abrogated in Cebpb−/− MEFs (Fig. 8A), indicating that endogenous C/EBP-β is required for LPS-induced SerpinB2 proximal promoter activity.\n10.1371/journal.pone.0057855.g008 Figure 8 C/EBP-β is necessary for SerpinB2 proximal promoter activity.\n(A) The SerpinB2 proximal promoter is significantly activated in LPS-stimulated Cebpb+/+ MEFs and not in Cebpb−/− MEFs. Murine SerpinB2 gene promoter activity measured in Cebpb+/+ and Cebpb−/− MEFs expressing the pGLmP-539 SerpinB2 promoter-luciferase reporter in the presence or absence of LPS (100 ng/mL). Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. The results represent the mean and SEM of at least three independent experiments performed in triplicate. (*, p\u003c0.05, one-way ANOVA)."}

    bionlp-st-ge-2016-uniprot

    {"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T26512","span":{"begin":1862,"end":1872},"obj":"http://www.uniprot.org/uniprot/P08659"},{"id":"T26511","span":{"begin":1768,"end":1778},"obj":"http://www.uniprot.org/uniprot/P08659"},{"id":"T26510","span":{"begin":1343,"end":1353},"obj":"http://www.uniprot.org/uniprot/P08659"},{"id":"T26509","span":{"begin":1280,"end":1290},"obj":"http://www.uniprot.org/uniprot/P08659"},{"id":"T26508","span":{"begin":1150,"end":1160},"obj":"http://www.uniprot.org/uniprot/P08659"},{"id":"T26507","span":{"begin":1750,"end":1758},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T26506","span":{"begin":1560,"end":1568},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T26505","span":{"begin":1262,"end":1270},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T26504","span":{"begin":1132,"end":1140},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T26503","span":{"begin":1036,"end":1044},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T26502","span":{"begin":917,"end":925},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T26501","span":{"begin":872,"end":880},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T26500","span":{"begin":1588,"end":1593},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T26499","span":{"begin":1093,"end":1098},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T26498","span":{"begin":1080,"end":1085},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T26497","span":{"begin":1014,"end":1019},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T26496","span":{"begin":989,"end":994},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T26495","span":{"begin":2019,"end":2026},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T26494","span":{"begin":1691,"end":1698},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T26493","span":{"begin":1666,"end":1673},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T26492","span":{"begin":1503,"end":1510},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T26491","span":{"begin":1404,"end":1411},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T26490","span":{"begin":847,"end":854},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T15962","span":{"begin":497,"end":507},"obj":"http://www.uniprot.org/uniprot/P08659"},{"id":"T15961","span":{"begin":766,"end":774},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T15960","span":{"begin":589,"end":597},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T15959","span":{"begin":488,"end":496},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T15958","span":{"begin":408,"end":416},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T15957","span":{"begin":294,"end":302},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T15956","span":{"begin":101,"end":109},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T15955","span":{"begin":38,"end":46},"obj":"http://www.uniprot.org/uniprot/P05120"},{"id":"T15954","span":{"begin":678,"end":683},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T15953","span":{"begin":647,"end":652},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T15952","span":{"begin":545,"end":550},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T15951","span":{"begin":532,"end":537},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T15950","span":{"begin":367,"end":374},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T15949","span":{"begin":227,"end":234},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T15948","span":{"begin":80,"end":87},"obj":"http://www.uniprot.org/uniprot/P28033"},{"id":"T15947","span":{"begin":0,"end":7},"obj":"http://www.uniprot.org/uniprot/P28033"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"C/EBP-β Promotes LPS-inducible Murine SerpinB2 Proximal Promoter Activity\nSince C/EBP-β binds to the SerpinB2 proximal promoter in an LPS-inducible manner both in vitro and in vivo, we wanted to address the question of whether C/EBP-β was an essential factor for driving transcription from the SerpinB2 promoter in cells in response to LPS. The ability of endogenous C/EBP-β to direct transcription from the SerpinB2 proximal promoter was examined by transfection of the pGLmP-539 murine SerpinB2 luciferase reporter construct into Cebpb+/+ and Cebpb−/− MEFs. We found that LPS-stimulated SerpinB2 promoter activity was significantly increased in Cebpb+/+ MEFs and abrogated in Cebpb−/− MEFs (Fig. 8A), indicating that endogenous C/EBP-β is required for LPS-induced SerpinB2 proximal promoter activity.\n10.1371/journal.pone.0057855.g008 Figure 8 C/EBP-β is necessary for SerpinB2 proximal promoter activity.\n(A) The SerpinB2 proximal promoter is significantly activated in LPS-stimulated Cebpb+/+ MEFs and not in Cebpb−/− MEFs. Murine SerpinB2 gene promoter activity measured in Cebpb+/+ and Cebpb−/− MEFs expressing the pGLmP-539 SerpinB2 promoter-luciferase reporter in the presence or absence of LPS (100 ng/mL). Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. The results represent the mean and SEM of at least three independent experiments performed in triplicate. (*, p\u003c0.05, one-way ANOVA)."}

    GO-BP

    {"project":"GO-BP","denotations":[{"id":"T26178","span":{"begin":1862,"end":1881},"obj":"http://purl.obolibrary.org/obo/GO_0050397"},{"id":"T26177","span":{"begin":1862,"end":1881},"obj":"http://purl.obolibrary.org/obo/GO_0050248"},{"id":"T26176","span":{"begin":1862,"end":1881},"obj":"http://purl.obolibrary.org/obo/GO_0047712"},{"id":"T26175","span":{"begin":1862,"end":1881},"obj":"http://purl.obolibrary.org/obo/GO_0047077"},{"id":"T26174","span":{"begin":1862,"end":1881},"obj":"http://purl.obolibrary.org/obo/GO_0045289"},{"id":"T26173","span":{"begin":1484,"end":1499},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T26172","span":{"begin":1915,"end":1939},"obj":"http://purl.obolibrary.org/obo/GO_0033930"},{"id":"T26171","span":{"begin":1374,"end":1398},"obj":"http://purl.obolibrary.org/obo/GO_0033930"},{"id":"T26170","span":{"begin":1915,"end":1939},"obj":"http://purl.obolibrary.org/obo/GO_0033929"},{"id":"T26169","span":{"begin":1374,"end":1398},"obj":"http://purl.obolibrary.org/obo/GO_0033929"},{"id":"T26168","span":{"begin":1915,"end":1939},"obj":"http://purl.obolibrary.org/obo/GO_0033920"},{"id":"T26167","span":{"begin":1374,"end":1398},"obj":"http://purl.obolibrary.org/obo/GO_0033920"},{"id":"T26166","span":{"begin":1915,"end":1939},"obj":"http://purl.obolibrary.org/obo/GO_1903770"},{"id":"T26165","span":{"begin":1374,"end":1398},"obj":"http://purl.obolibrary.org/obo/GO_1903770"},{"id":"T26164","span":{"begin":1915,"end":1939},"obj":"http://purl.obolibrary.org/obo/GO_1903771"},{"id":"T26163","span":{"begin":1374,"end":1398},"obj":"http://purl.obolibrary.org/obo/GO_1903771"},{"id":"T26162","span":{"begin":1915,"end":1939},"obj":"http://purl.obolibrary.org/obo/GO_0004336"},{"id":"T26161","span":{"begin":1374,"end":1398},"obj":"http://purl.obolibrary.org/obo/GO_0004336"},{"id":"T26160","span":{"begin":1915,"end":1939},"obj":"http://purl.obolibrary.org/obo/GO_0004565"},{"id":"T26159","span":{"begin":1374,"end":1398},"obj":"http://purl.obolibrary.org/obo/GO_0004565"},{"id":"T15771","span":{"begin":324,"end":339},"obj":"http://purl.obolibrary.org/obo/GO_0032496"},{"id":"T15770","span":{"begin":385,"end":398},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T15769","span":{"begin":271,"end":284},"obj":"http://purl.obolibrary.org/obo/GO_0006351"}],"text":"C/EBP-β Promotes LPS-inducible Murine SerpinB2 Proximal Promoter Activity\nSince C/EBP-β binds to the SerpinB2 proximal promoter in an LPS-inducible manner both in vitro and in vivo, we wanted to address the question of whether C/EBP-β was an essential factor for driving transcription from the SerpinB2 promoter in cells in response to LPS. The ability of endogenous C/EBP-β to direct transcription from the SerpinB2 proximal promoter was examined by transfection of the pGLmP-539 murine SerpinB2 luciferase reporter construct into Cebpb+/+ and Cebpb−/− MEFs. We found that LPS-stimulated SerpinB2 promoter activity was significantly increased in Cebpb+/+ MEFs and abrogated in Cebpb−/− MEFs (Fig. 8A), indicating that endogenous C/EBP-β is required for LPS-induced SerpinB2 proximal promoter activity.\n10.1371/journal.pone.0057855.g008 Figure 8 C/EBP-β is necessary for SerpinB2 proximal promoter activity.\n(A) The SerpinB2 proximal promoter is significantly activated in LPS-stimulated Cebpb+/+ MEFs and not in Cebpb−/− MEFs. Murine SerpinB2 gene promoter activity measured in Cebpb+/+ and Cebpb−/− MEFs expressing the pGLmP-539 SerpinB2 promoter-luciferase reporter in the presence or absence of LPS (100 ng/mL). Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. The results represent the mean and SEM of at least three independent experiments performed in triplicate. (*, p\u003c0.05, one-way ANOVA)."}

    GO-MF

    {"project":"GO-MF","denotations":[{"id":"T26193","span":{"begin":1862,"end":1881},"obj":"http://purl.obolibrary.org/obo/GO_0050397"},{"id":"T26192","span":{"begin":1862,"end":1881},"obj":"http://purl.obolibrary.org/obo/GO_0050248"},{"id":"T26191","span":{"begin":1862,"end":1881},"obj":"http://purl.obolibrary.org/obo/GO_0047712"},{"id":"T26190","span":{"begin":1862,"end":1881},"obj":"http://purl.obolibrary.org/obo/GO_0047077"},{"id":"T26189","span":{"begin":1862,"end":1881},"obj":"http://purl.obolibrary.org/obo/GO_0045289"},{"id":"T26188","span":{"begin":1915,"end":1939},"obj":"http://purl.obolibrary.org/obo/GO_0033930"},{"id":"T26187","span":{"begin":1374,"end":1398},"obj":"http://purl.obolibrary.org/obo/GO_0033930"},{"id":"T26181","span":{"begin":1374,"end":1398},"obj":"http://purl.obolibrary.org/obo/GO_0004336"},{"id":"T26180","span":{"begin":1915,"end":1939},"obj":"http://purl.obolibrary.org/obo/GO_0004565"},{"id":"T26179","span":{"begin":1374,"end":1398},"obj":"http://purl.obolibrary.org/obo/GO_0004565"},{"id":"T26186","span":{"begin":1915,"end":1939},"obj":"http://purl.obolibrary.org/obo/GO_0033929"},{"id":"T26185","span":{"begin":1374,"end":1398},"obj":"http://purl.obolibrary.org/obo/GO_0033929"},{"id":"T26184","span":{"begin":1915,"end":1939},"obj":"http://purl.obolibrary.org/obo/GO_0033920"},{"id":"T26183","span":{"begin":1374,"end":1398},"obj":"http://purl.obolibrary.org/obo/GO_0033920"},{"id":"T26182","span":{"begin":1915,"end":1939},"obj":"http://purl.obolibrary.org/obo/GO_0004336"}],"text":"C/EBP-β Promotes LPS-inducible Murine SerpinB2 Proximal Promoter Activity\nSince C/EBP-β binds to the SerpinB2 proximal promoter in an LPS-inducible manner both in vitro and in vivo, we wanted to address the question of whether C/EBP-β was an essential factor for driving transcription from the SerpinB2 promoter in cells in response to LPS. The ability of endogenous C/EBP-β to direct transcription from the SerpinB2 proximal promoter was examined by transfection of the pGLmP-539 murine SerpinB2 luciferase reporter construct into Cebpb+/+ and Cebpb−/− MEFs. We found that LPS-stimulated SerpinB2 promoter activity was significantly increased in Cebpb+/+ MEFs and abrogated in Cebpb−/− MEFs (Fig. 8A), indicating that endogenous C/EBP-β is required for LPS-induced SerpinB2 proximal promoter activity.\n10.1371/journal.pone.0057855.g008 Figure 8 C/EBP-β is necessary for SerpinB2 proximal promoter activity.\n(A) The SerpinB2 proximal promoter is significantly activated in LPS-stimulated Cebpb+/+ MEFs and not in Cebpb−/− MEFs. Murine SerpinB2 gene promoter activity measured in Cebpb+/+ and Cebpb−/− MEFs expressing the pGLmP-539 SerpinB2 promoter-luciferase reporter in the presence or absence of LPS (100 ng/mL). Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. The results represent the mean and SEM of at least three independent experiments performed in triplicate. (*, p\u003c0.05, one-way ANOVA)."}

    GO-CC

    {"project":"GO-CC","denotations":[{"id":"T15772","span":{"begin":315,"end":320},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"C/EBP-β Promotes LPS-inducible Murine SerpinB2 Proximal Promoter Activity\nSince C/EBP-β binds to the SerpinB2 proximal promoter in an LPS-inducible manner both in vitro and in vivo, we wanted to address the question of whether C/EBP-β was an essential factor for driving transcription from the SerpinB2 promoter in cells in response to LPS. The ability of endogenous C/EBP-β to direct transcription from the SerpinB2 proximal promoter was examined by transfection of the pGLmP-539 murine SerpinB2 luciferase reporter construct into Cebpb+/+ and Cebpb−/− MEFs. We found that LPS-stimulated SerpinB2 promoter activity was significantly increased in Cebpb+/+ MEFs and abrogated in Cebpb−/− MEFs (Fig. 8A), indicating that endogenous C/EBP-β is required for LPS-induced SerpinB2 proximal promoter activity.\n10.1371/journal.pone.0057855.g008 Figure 8 C/EBP-β is necessary for SerpinB2 proximal promoter activity.\n(A) The SerpinB2 proximal promoter is significantly activated in LPS-stimulated Cebpb+/+ MEFs and not in Cebpb−/− MEFs. Murine SerpinB2 gene promoter activity measured in Cebpb+/+ and Cebpb−/− MEFs expressing the pGLmP-539 SerpinB2 promoter-luciferase reporter in the presence or absence of LPS (100 ng/mL). Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. The results represent the mean and SEM of at least three independent experiments performed in triplicate. (*, p\u003c0.05, one-way ANOVA)."}

    sentences

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    simple1

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The ability of endogenous C/EBP-β to direct transcription from the SerpinB2 proximal promoter was examined by transfection of the pGLmP-539 murine SerpinB2 luciferase reporter construct into Cebpb+/+ and Cebpb−/− MEFs. We found that LPS-stimulated SerpinB2 promoter activity was significantly increased in Cebpb+/+ MEFs and abrogated in Cebpb−/− MEFs (Fig. 8A), indicating that endogenous C/EBP-β is required for LPS-induced SerpinB2 proximal promoter activity.\n10.1371/journal.pone.0057855.g008 Figure 8 C/EBP-β is necessary for SerpinB2 proximal promoter activity.\n(A) The SerpinB2 proximal promoter is significantly activated in LPS-stimulated Cebpb+/+ MEFs and not in Cebpb−/− MEFs. Murine SerpinB2 gene promoter activity measured in Cebpb+/+ and Cebpb−/− MEFs expressing the pGLmP-539 SerpinB2 promoter-luciferase reporter in the presence or absence of LPS (100 ng/mL). Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. The results represent the mean and SEM of at least three independent experiments performed in triplicate. (*, p\u003c0.05, one-way ANOVA)."}

    BioNLP16_DUT

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Promotes LPS-inducible Murine SerpinB2 Proximal Promoter Activity\nSince C/EBP-β binds to the SerpinB2 proximal promoter in an LPS-inducible manner both in vitro and in vivo, we wanted to address the question of whether C/EBP-β was an essential factor for driving transcription from the SerpinB2 promoter in cells in response to LPS. The ability of endogenous C/EBP-β to direct transcription from the SerpinB2 proximal promoter was examined by transfection of the pGLmP-539 murine SerpinB2 luciferase reporter construct into Cebpb+/+ and Cebpb−/− MEFs. We found that LPS-stimulated SerpinB2 promoter activity was significantly increased in Cebpb+/+ MEFs and abrogated in Cebpb−/− MEFs (Fig. 8A), indicating that endogenous C/EBP-β is required for LPS-induced SerpinB2 proximal promoter activity.\n10.1371/journal.pone.0057855.g008 Figure 8 C/EBP-β is necessary for SerpinB2 proximal promoter activity.\n(A) The SerpinB2 proximal promoter is significantly activated in LPS-stimulated Cebpb+/+ MEFs and not in Cebpb−/− MEFs. Murine SerpinB2 gene promoter activity measured in Cebpb+/+ and Cebpb−/− MEFs expressing the pGLmP-539 SerpinB2 promoter-luciferase reporter in the presence or absence of LPS (100 ng/mL). Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. The results represent the mean and SEM of at least three independent experiments performed in triplicate. (*, p\u003c0.05, one-way ANOVA)."}

    BioNLP16_Messiy

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Promotes LPS-inducible Murine SerpinB2 Proximal Promoter Activity\nSince C/EBP-β binds to the SerpinB2 proximal promoter in an LPS-inducible manner both in vitro and in vivo, we wanted to address the question of whether C/EBP-β was an essential factor for driving transcription from the SerpinB2 promoter in cells in response to LPS. The ability of endogenous C/EBP-β to direct transcription from the SerpinB2 proximal promoter was examined by transfection of the pGLmP-539 murine SerpinB2 luciferase reporter construct into Cebpb+/+ and Cebpb−/− MEFs. We found that LPS-stimulated SerpinB2 promoter activity was significantly increased in Cebpb+/+ MEFs and abrogated in Cebpb−/− MEFs (Fig. 8A), indicating that endogenous C/EBP-β is required for LPS-induced SerpinB2 proximal promoter activity.\n10.1371/journal.pone.0057855.g008 Figure 8 C/EBP-β is necessary for SerpinB2 proximal promoter activity.\n(A) The SerpinB2 proximal promoter is significantly activated in LPS-stimulated Cebpb+/+ MEFs and not in Cebpb−/− MEFs. Murine SerpinB2 gene promoter activity measured in Cebpb+/+ and Cebpb−/− MEFs expressing the pGLmP-539 SerpinB2 promoter-luciferase reporter in the presence or absence of LPS (100 ng/mL). Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. The results represent the mean and SEM of at least three independent experiments performed in triplicate. (*, p\u003c0.05, one-way ANOVA)."}

    DLUT931

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Promotes LPS-inducible Murine SerpinB2 Proximal Promoter Activity\nSince C/EBP-β binds to the SerpinB2 proximal promoter in an LPS-inducible manner both in vitro and in vivo, we wanted to address the question of whether C/EBP-β was an essential factor for driving transcription from the SerpinB2 promoter in cells in response to LPS. The ability of endogenous C/EBP-β to direct transcription from the SerpinB2 proximal promoter was examined by transfection of the pGLmP-539 murine SerpinB2 luciferase reporter construct into Cebpb+/+ and Cebpb−/− MEFs. We found that LPS-stimulated SerpinB2 promoter activity was significantly increased in Cebpb+/+ MEFs and abrogated in Cebpb−/− MEFs (Fig. 8A), indicating that endogenous C/EBP-β is required for LPS-induced SerpinB2 proximal promoter activity.\n10.1371/journal.pone.0057855.g008 Figure 8 C/EBP-β is necessary for SerpinB2 proximal promoter activity.\n(A) The SerpinB2 proximal promoter is significantly activated in LPS-stimulated Cebpb+/+ MEFs and not in Cebpb−/− MEFs. Murine SerpinB2 gene promoter activity measured in Cebpb+/+ and Cebpb−/− MEFs expressing the pGLmP-539 SerpinB2 promoter-luciferase reporter in the presence or absence of LPS (100 ng/mL). Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. The results represent the mean and SEM of at least three independent experiments performed in triplicate. (*, p\u003c0.05, one-way ANOVA)."}

    bionlp-st-ge-2016-test-ihmc

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Promotes LPS-inducible Murine SerpinB2 Proximal Promoter Activity\nSince C/EBP-β binds to the SerpinB2 proximal promoter in an LPS-inducible manner both in vitro and in vivo, we wanted to address the question of whether C/EBP-β was an essential factor for driving transcription from the SerpinB2 promoter in cells in response to LPS. The ability of endogenous C/EBP-β to direct transcription from the SerpinB2 proximal promoter was examined by transfection of the pGLmP-539 murine SerpinB2 luciferase reporter construct into Cebpb+/+ and Cebpb−/− MEFs. We found that LPS-stimulated SerpinB2 promoter activity was significantly increased in Cebpb+/+ MEFs and abrogated in Cebpb−/− MEFs (Fig. 8A), indicating that endogenous C/EBP-β is required for LPS-induced SerpinB2 proximal promoter activity.\n10.1371/journal.pone.0057855.g008 Figure 8 C/EBP-β is necessary for SerpinB2 proximal promoter activity.\n(A) The SerpinB2 proximal promoter is significantly activated in LPS-stimulated Cebpb+/+ MEFs and not in Cebpb−/− MEFs. Murine SerpinB2 gene promoter activity measured in Cebpb+/+ and Cebpb−/− MEFs expressing the pGLmP-539 SerpinB2 promoter-luciferase reporter in the presence or absence of LPS (100 ng/mL). Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. The results represent the mean and SEM of at least three independent experiments performed in triplicate. (*, p\u003c0.05, one-way ANOVA)."}

    bionlp-st-ge-2016-test-tees

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Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. 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    testone

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Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. The results represent the mean and SEM of at least three independent experiments performed in triplicate. (*, p\u003c0.05, one-way ANOVA)."}

    test3

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Promotes LPS-inducible Murine SerpinB2 Proximal Promoter Activity\nSince C/EBP-β binds to the SerpinB2 proximal promoter in an LPS-inducible manner both in vitro and in vivo, we wanted to address the question of whether C/EBP-β was an essential factor for driving transcription from the SerpinB2 promoter in cells in response to LPS. The ability of endogenous C/EBP-β to direct transcription from the SerpinB2 proximal promoter was examined by transfection of the pGLmP-539 murine SerpinB2 luciferase reporter construct into Cebpb+/+ and Cebpb−/− MEFs. We found that LPS-stimulated SerpinB2 promoter activity was significantly increased in Cebpb+/+ MEFs and abrogated in Cebpb−/− MEFs (Fig. 8A), indicating that endogenous C/EBP-β is required for LPS-induced SerpinB2 proximal promoter activity.\n10.1371/journal.pone.0057855.g008 Figure 8 C/EBP-β is necessary for SerpinB2 proximal promoter activity.\n(A) The SerpinB2 proximal promoter is significantly activated in LPS-stimulated Cebpb+/+ MEFs and not in Cebpb−/− MEFs. Murine SerpinB2 gene promoter activity measured in Cebpb+/+ and Cebpb−/− MEFs expressing the pGLmP-539 SerpinB2 promoter-luciferase reporter in the presence or absence of LPS (100 ng/mL). Cells were co-transfected with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and luciferase units normalized to β-galactosidase activity. (B) C/EBP-β gene schematic depicting gene structure and phospho-acceptor sites. (C) Phosphorylation of C/EBP-β at Serine 64 negatively regulates LPS-stimulated SerpinB2 promoter activity. Cebpb−/− MEFs were co-transfected with expression plasmids encoding wild-type C/EBP-β or the indicated C/EBP-β phospho-acceptor mutants, along with the pGLmP-539 SerpinB2 promoter-luciferase reporter and β-galactosidase reporter plasmids, and stimulated with LPS for 4 hrs. Luciferase activity was quantified and normalized to β-galactosidase activity. The western blot (below the graphs) confirms the expression of the respective C/EBP-β phospho-acceptor mutants. The C/EBP-βT217A -transfected MEFs express both the 38 kDa and 35 kDa isoforms of C/EBP-β. The results represent the mean and SEM of at least three independent experiments performed in triplicate. (*, p\u003c0.05, one-way ANOVA)."}