PMC:1064895 / 20557-21991 JSONTXT

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As shown in Fig. 7a, nuclear extracts from RA PBMC stimulated with anti-CD3 plus anti-CD28 (lane 2) demonstrated increased binding of NF-κB to IL-17 promoters in comparison with that of controls (lane 1). A supershift assay demonstrated shifted bands in p65 and p50 (lanes 3 and 4) not in c-Rel (lane 5). In normal PBMC the same pattern was observed, but the degree of NF-κB activation by anti-CD3 plus anti-CD28 was less intense than that in RA PBMC (Fig. 7b). To confirm the link between PI3K activity and NF-κB, we performed EMSA to determine the NF-κB binding activity after treatment with both LY294002 and PDTC. Both agents block NF-κB DNA-binding activity in the IL-17 promoter (Fig. 7c). Western blotting for IκB-α showed inhibition of degradation of IκB-α by LY294002 and PDTC at the same time (Fig. 7c). In contrast, the AP-1 pathway was not activated by stimulation with anti-CD3 plus anti-CD28 (data not shown), demonstrating that NF-κB is the main intracellular signaling pathway in IL-17 production by activated PBMC from patients with RA."}

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of the NF-κB and activator protein-1 (AP-1) pathway in the IL-17 promoter region\nTo investigate further the intracellular signaling pathway activated by anti-CD3 plus anti-CD28, concanavalin A, PHA and IL-15, and responsible for inducing IL-17 expression, we performed an electrophoretic mobility-shift assay (EMSA) of NF-κB recognition sites in the promoters of IL-17. As shown in Fig. 7a, nuclear extracts from RA PBMC stimulated with anti-CD3 plus anti-CD28 (lane 2) demonstrated increased binding of NF-κB to IL-17 promoters in comparison with that of controls (lane 1). A supershift assay demonstrated shifted bands in p65 and p50 (lanes 3 and 4) not in c-Rel (lane 5). In normal PBMC the same pattern was observed, but the degree of NF-κB activation by anti-CD3 plus anti-CD28 was less intense than that in RA PBMC (Fig. 7b). To confirm the link between PI3K activity and NF-κB, we performed EMSA to determine the NF-κB binding activity after treatment with both LY294002 and PDTC. Both agents block NF-κB DNA-binding activity in the IL-17 promoter (Fig. 7c). Western blotting for IκB-α showed inhibition of degradation of IκB-α by LY294002 and PDTC at the same time (Fig. 7c). In contrast, the AP-1 pathway was not activated by stimulation with anti-CD3 plus anti-CD28 (data not shown), demonstrating that NF-κB is the main intracellular signaling pathway in IL-17 production by activated PBMC from patients with RA."}

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of the NF-κB and activator protein-1 (AP-1) pathway in the IL-17 promoter region\nTo investigate further the intracellular signaling pathway activated by anti-CD3 plus anti-CD28, concanavalin A, PHA and IL-15, and responsible for inducing IL-17 expression, we performed an electrophoretic mobility-shift assay (EMSA) of NF-κB recognition sites in the promoters of IL-17. As shown in Fig. 7a, nuclear extracts from RA PBMC stimulated with anti-CD3 plus anti-CD28 (lane 2) demonstrated increased binding of NF-κB to IL-17 promoters in comparison with that of controls (lane 1). A supershift assay demonstrated shifted bands in p65 and p50 (lanes 3 and 4) not in c-Rel (lane 5). In normal PBMC the same pattern was observed, but the degree of NF-κB activation by anti-CD3 plus anti-CD28 was less intense than that in RA PBMC (Fig. 7b). To confirm the link between PI3K activity and NF-κB, we performed EMSA to determine the NF-κB binding activity after treatment with both LY294002 and PDTC. Both agents block NF-κB DNA-binding activity in the IL-17 promoter (Fig. 7c). Western blotting for IκB-α showed inhibition of degradation of IκB-α by LY294002 and PDTC at the same time (Fig. 7c). In contrast, the AP-1 pathway was not activated by stimulation with anti-CD3 plus anti-CD28 (data not shown), demonstrating that NF-κB is the main intracellular signaling pathway in IL-17 production by activated PBMC from patients with RA."}

{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T16167","span":{"begin":1377,"end":1382},"obj":"Protein"},{"id":"T16166","span":{"begin":1282,"end":1286},"obj":"Protein"},{"id":"T16165","span":{"begin":1212,"end":1216},"obj":"Protein"},{"id":"T16164","span":{"begin":1140,"end":1145},"obj":"Protein"},{"id":"T16163","span":{"begin":1098,"end":1103},"obj":"Protein"},{"id":"T16162","span":{"begin":1051,"end":1056},"obj":"Protein"},{"id":"T16161","span":{"begin":789,"end":793},"obj":"Protein"},{"id":"T16160","span":{"begin":670,"end":675},"obj":"Protein"},{"id":"T16159","span":{"begin":643,"end":646},"obj":"Protein"},{"id":"T16158","span":{"begin":635,"end":638},"obj":"Protein"},{"id":"T16157","span":{"begin":524,"end":529},"obj":"Protein"},{"id":"T16156","span":{"begin":467,"end":471},"obj":"Protein"},{"id":"T16155","span":{"begin":374,"end":379},"obj":"Protein"},{"id":"T16154","span":{"begin":249,"end":254},"obj":"Protein"},{"id":"T16153","span":{"begin":213,"end":218},"obj":"Protein"},{"id":"T16152","span":{"begin":205,"end":208},"obj":"Protein"},{"id":"T16151","span":{"begin":183,"end":187},"obj":"Protein"},{"id":"T16150","span":{"begin":70,"end":75},"obj":"Protein"},{"id":"T16149","span":{"begin":49,"end":53},"obj":"Protein"},{"id":"T16148","span":{"begin":28,"end":47},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"Activation of the NF-κB and activator protein-1 (AP-1) pathway in the IL-17 promoter region\nTo investigate further the intracellular signaling pathway activated by anti-CD3 plus anti-CD28, concanavalin A, PHA and IL-15, and responsible for inducing IL-17 expression, we performed an electrophoretic mobility-shift assay (EMSA) of NF-κB recognition sites in the promoters of IL-17. As shown in Fig. 7a, nuclear extracts from RA PBMC stimulated with anti-CD3 plus anti-CD28 (lane 2) demonstrated increased binding of NF-κB to IL-17 promoters in comparison with that of controls (lane 1). A supershift assay demonstrated shifted bands in p65 and p50 (lanes 3 and 4) not in c-Rel (lane 5). In normal PBMC the same pattern was observed, but the degree of NF-κB activation by anti-CD3 plus anti-CD28 was less intense than that in RA PBMC (Fig. 7b). To confirm the link between PI3K activity and NF-κB, we performed EMSA to determine the NF-κB binding activity after treatment with both LY294002 and PDTC. Both agents block NF-κB DNA-binding activity in the IL-17 promoter (Fig. 7c). Western blotting for IκB-α showed inhibition of degradation of IκB-α by LY294002 and PDTC at the same time (Fig. 7c). In contrast, the AP-1 pathway was not activated by stimulation with anti-CD3 plus anti-CD28 (data not shown), demonstrating that NF-κB is the main intracellular signaling pathway in IL-17 production by activated PBMC from patients with RA."}

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T16313","span":{"begin":670,"end":675},"obj":"http://www.uniprot.org/uniprot/Q04864"},{"id":"T16312","span":{"begin":643,"end":646},"obj":"http://www.uniprot.org/uniprot/P19838"},{"id":"T16311","span":{"begin":635,"end":638},"obj":"http://www.uniprot.org/uniprot/P21579"},{"id":"T16310","span":{"begin":635,"end":638},"obj":"http://www.uniprot.org/uniprot/Q04206"},{"id":"T16309","span":{"begin":213,"end":218},"obj":"http://www.uniprot.org/uniprot/P40933"},{"id":"T16308","span":{"begin":1282,"end":1286},"obj":"http://www.uniprot.org/uniprot/P10747"},{"id":"T16307","span":{"begin":789,"end":793},"obj":"http://www.uniprot.org/uniprot/P10747"},{"id":"T16306","span":{"begin":467,"end":471},"obj":"http://www.uniprot.org/uniprot/P10747"},{"id":"T16305","span":{"begin":183,"end":187},"obj":"http://www.uniprot.org/uniprot/P10747"},{"id":"T16304","span":{"begin":1268,"end":1271},"obj":"http://www.uniprot.org/uniprot/P09693"},{"id":"T16303","span":{"begin":775,"end":778},"obj":"http://www.uniprot.org/uniprot/P09693"},{"id":"T16302","span":{"begin":453,"end":456},"obj":"http://www.uniprot.org/uniprot/P09693"},{"id":"T16301","span":{"begin":169,"end":172},"obj":"http://www.uniprot.org/uniprot/P09693"},{"id":"T16300","span":{"begin":1268,"end":1271},"obj":"http://www.uniprot.org/uniprot/P07766"},{"id":"T16299","span":{"begin":775,"end":778},"obj":"http://www.uniprot.org/uniprot/P07766"},{"id":"T16298","span":{"begin":453,"end":456},"obj":"http://www.uniprot.org/uniprot/P07766"},{"id":"T16297","span":{"begin":169,"end":172},"obj":"http://www.uniprot.org/uniprot/P07766"},{"id":"T16296","span":{"begin":1268,"end":1271},"obj":"http://www.uniprot.org/uniprot/P04234"},{"id":"T16295","span":{"begin":775,"end":778},"obj":"http://www.uniprot.org/uniprot/P04234"},{"id":"T16294","span":{"begin":453,"end":456},"obj":"http://www.uniprot.org/uniprot/P04234"},{"id":"T16293","span":{"begin":169,"end":172},"obj":"http://www.uniprot.org/uniprot/P04234"},{"id":"T16292","span":{"begin":1268,"end":1271},"obj":"http://www.uniprot.org/uniprot/P20963"},{"id":"T16291","span":{"begin":775,"end":778},"obj":"http://www.uniprot.org/uniprot/P20963"},{"id":"T16290","span":{"begin":453,"end":456},"obj":"http://www.uniprot.org/uniprot/P20963"},{"id":"T16289","span":{"begin":169,"end":172},"obj":"http://www.uniprot.org/uniprot/P20963"},{"id":"T16288","span":{"begin":1377,"end":1382},"obj":"http://www.uniprot.org/uniprot/Q16552"},{"id":"T16287","span":{"begin":1051,"end":1056},"obj":"http://www.uniprot.org/uniprot/Q16552"},{"id":"T16286","span":{"begin":524,"end":529},"obj":"http://www.uniprot.org/uniprot/Q16552"},{"id":"T16285","span":{"begin":374,"end":379},"obj":"http://www.uniprot.org/uniprot/Q16552"},{"id":"T16284","span":{"begin":249,"end":254},"obj":"http://www.uniprot.org/uniprot/Q16552"},{"id":"T16283","span":{"begin":70,"end":75},"obj":"http://www.uniprot.org/uniprot/Q16552"},{"id":"T16282","span":{"begin":1212,"end":1216},"obj":"http://www.uniprot.org/uniprot/P05412"},{"id":"T16281","span":{"begin":46,"end":51},"obj":"http://www.uniprot.org/uniprot/P05412"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"Activation of the NF-κB and activator protein-1 (AP-1) pathway in the IL-17 promoter region\nTo investigate further the intracellular signaling pathway activated by anti-CD3 plus anti-CD28, concanavalin A, PHA and IL-15, and responsible for inducing IL-17 expression, we performed an electrophoretic mobility-shift assay (EMSA) of NF-κB recognition sites in the promoters of IL-17. As shown in Fig. 7a, nuclear extracts from RA PBMC stimulated with anti-CD3 plus anti-CD28 (lane 2) demonstrated increased binding of NF-κB to IL-17 promoters in comparison with that of controls (lane 1). A supershift assay demonstrated shifted bands in p65 and p50 (lanes 3 and 4) not in c-Rel (lane 5). In normal PBMC the same pattern was observed, but the degree of NF-κB activation by anti-CD3 plus anti-CD28 was less intense than that in RA PBMC (Fig. 7b). To confirm the link between PI3K activity and NF-κB, we performed EMSA to determine the NF-κB binding activity after treatment with both LY294002 and PDTC. Both agents block NF-κB DNA-binding activity in the IL-17 promoter (Fig. 7c). Western blotting for IκB-α showed inhibition of degradation of IκB-α by LY294002 and PDTC at the same time (Fig. 7c). In contrast, the AP-1 pathway was not activated by stimulation with anti-CD3 plus anti-CD28 (data not shown), demonstrating that NF-κB is the main intracellular signaling pathway in IL-17 production by activated PBMC from patients with RA."}

{"project":"GO-BP","denotations":[{"id":"T15854","span":{"begin":1380,"end":1406},"obj":"http://purl.obolibrary.org/obo/GO_0032740"},{"id":"T15853","span":{"begin":1377,"end":1393},"obj":"http://purl.obolibrary.org/obo/GO_0032620"},{"id":"T15852","span":{"begin":1377,"end":1393},"obj":"http://purl.obolibrary.org/obo/GO_0032660"},{"id":"T15851","span":{"begin":1125,"end":1136},"obj":"http://purl.obolibrary.org/obo/GO_0009056"},{"id":"T15850","span":{"begin":871,"end":875},"obj":"http://purl.obolibrary.org/obo/GO_0016303"},{"id":"T15849","span":{"begin":750,"end":766},"obj":"http://purl.obolibrary.org/obo/GO_0051092"},{"id":"T15848","span":{"begin":133,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_1903265"},{"id":"T15847","span":{"begin":133,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_1902843"},{"id":"T15846","span":{"begin":133,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_1902046"},{"id":"T15845","span":{"begin":133,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_1900236"},{"id":"T15844","span":{"begin":133,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_0038084"},{"id":"T15843","span":{"begin":133,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_0009873"},{"id":"T15842","span":{"begin":133,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_1902204"},{"id":"T15841","span":{"begin":133,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_1901186"},{"id":"T15840","span":{"begin":133,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_0033211"},{"id":"T15839","span":{"begin":133,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_0009736"},{"id":"T15838","span":{"begin":1356,"end":1373},"obj":"http://purl.obolibrary.org/obo/GO_0007165"},{"id":"T15837","span":{"begin":133,"end":150},"obj":"http://purl.obolibrary.org/obo/GO_0007165"},{"id":"T15836","span":{"begin":1356,"end":1365},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T15835","span":{"begin":133,"end":142},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T15834","span":{"begin":119,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_1902533"},{"id":"T15833","span":{"begin":1342,"end":1373},"obj":"http://purl.obolibrary.org/obo/GO_1902531"},{"id":"T15832","span":{"begin":119,"end":150},"obj":"http://purl.obolibrary.org/obo/GO_1902531"},{"id":"T15831","span":{"begin":1342,"end":1373},"obj":"http://purl.obolibrary.org/obo/GO_1902532"},{"id":"T15830","span":{"begin":119,"end":150},"obj":"http://purl.obolibrary.org/obo/GO_1902532"},{"id":"T15829","span":{"begin":1342,"end":1373},"obj":"http://purl.obolibrary.org/obo/GO_0035556"},{"id":"T15828","span":{"begin":119,"end":150},"obj":"http://purl.obolibrary.org/obo/GO_0035556"},{"id":"T15827","span":{"begin":1342,"end":1373},"obj":"http://purl.obolibrary.org/obo/GO_0030522"},{"id":"T15826","span":{"begin":119,"end":150},"obj":"http://purl.obolibrary.org/obo/GO_0030522"}],"text":"Activation of the NF-κB and activator protein-1 (AP-1) pathway in the IL-17 promoter region\nTo investigate further the intracellular signaling pathway activated by anti-CD3 plus anti-CD28, concanavalin A, PHA and IL-15, and responsible for inducing IL-17 expression, we performed an electrophoretic mobility-shift assay (EMSA) of NF-κB recognition sites in the promoters of IL-17. As shown in Fig. 7a, nuclear extracts from RA PBMC stimulated with anti-CD3 plus anti-CD28 (lane 2) demonstrated increased binding of NF-κB to IL-17 promoters in comparison with that of controls (lane 1). A supershift assay demonstrated shifted bands in p65 and p50 (lanes 3 and 4) not in c-Rel (lane 5). In normal PBMC the same pattern was observed, but the degree of NF-κB activation by anti-CD3 plus anti-CD28 was less intense than that in RA PBMC (Fig. 7b). To confirm the link between PI3K activity and NF-κB, we performed EMSA to determine the NF-κB binding activity after treatment with both LY294002 and PDTC. Both agents block NF-κB DNA-binding activity in the IL-17 promoter (Fig. 7c). Western blotting for IκB-α showed inhibition of degradation of IκB-α by LY294002 and PDTC at the same time (Fig. 7c). In contrast, the AP-1 pathway was not activated by stimulation with anti-CD3 plus anti-CD28 (data not shown), demonstrating that NF-κB is the main intracellular signaling pathway in IL-17 production by activated PBMC from patients with RA."}

{"project":"GO-MF","denotations":[{"id":"T16181","span":{"begin":1023,"end":1034},"obj":"http://purl.obolibrary.org/obo/GO_0003677"},{"id":"T16180","span":{"begin":871,"end":875},"obj":"http://purl.obolibrary.org/obo/GO_0016303"},{"id":"T16179","span":{"begin":931,"end":944},"obj":"http://purl.obolibrary.org/obo/GO_0051059"},{"id":"T16178","span":{"begin":504,"end":520},"obj":"http://purl.obolibrary.org/obo/GO_0051059"},{"id":"T16177","span":{"begin":1027,"end":1034},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T16176","span":{"begin":937,"end":944},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T16175","span":{"begin":504,"end":511},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T16174","span":{"begin":213,"end":218},"obj":"http://purl.obolibrary.org/obo/GO_0016170"},{"id":"T16173","span":{"begin":1377,"end":1382},"obj":"http://purl.obolibrary.org/obo/GO_0030367"},{"id":"T16172","span":{"begin":1051,"end":1056},"obj":"http://purl.obolibrary.org/obo/GO_0030367"},{"id":"T16171","span":{"begin":524,"end":529},"obj":"http://purl.obolibrary.org/obo/GO_0030367"},{"id":"T16170","span":{"begin":374,"end":379},"obj":"http://purl.obolibrary.org/obo/GO_0030367"},{"id":"T16169","span":{"begin":249,"end":254},"obj":"http://purl.obolibrary.org/obo/GO_0030367"},{"id":"T16168","span":{"begin":70,"end":75},"obj":"http://purl.obolibrary.org/obo/GO_0030367"}],"text":"Activation of the NF-κB and activator protein-1 (AP-1) pathway in the IL-17 promoter region\nTo investigate further the intracellular signaling pathway activated by anti-CD3 plus anti-CD28, concanavalin A, PHA and IL-15, and responsible for inducing IL-17 expression, we performed an electrophoretic mobility-shift assay (EMSA) of NF-κB recognition sites in the promoters of IL-17. As shown in Fig. 7a, nuclear extracts from RA PBMC stimulated with anti-CD3 plus anti-CD28 (lane 2) demonstrated increased binding of NF-κB to IL-17 promoters in comparison with that of controls (lane 1). A supershift assay demonstrated shifted bands in p65 and p50 (lanes 3 and 4) not in c-Rel (lane 5). In normal PBMC the same pattern was observed, but the degree of NF-κB activation by anti-CD3 plus anti-CD28 was less intense than that in RA PBMC (Fig. 7b). To confirm the link between PI3K activity and NF-κB, we performed EMSA to determine the NF-κB binding activity after treatment with both LY294002 and PDTC. Both agents block NF-κB DNA-binding activity in the IL-17 promoter (Fig. 7c). Western blotting for IκB-α showed inhibition of degradation of IκB-α by LY294002 and PDTC at the same time (Fig. 7c). In contrast, the AP-1 pathway was not activated by stimulation with anti-CD3 plus anti-CD28 (data not shown), demonstrating that NF-κB is the main intracellular signaling pathway in IL-17 production by activated PBMC from patients with RA."}

{"project":"GO-CC","denotations":[{"id":"T16183","span":{"begin":1342,"end":1355},"obj":"http://purl.obolibrary.org/obo/GO_0005622"},{"id":"T16182","span":{"begin":119,"end":132},"obj":"http://purl.obolibrary.org/obo/GO_0005622"}],"text":"Activation of the NF-κB and activator protein-1 (AP-1) pathway in the IL-17 promoter region\nTo investigate further the intracellular signaling pathway activated by anti-CD3 plus anti-CD28, concanavalin A, PHA and IL-15, and responsible for inducing IL-17 expression, we performed an electrophoretic mobility-shift assay (EMSA) of NF-κB recognition sites in the promoters of IL-17. As shown in Fig. 7a, nuclear extracts from RA PBMC stimulated with anti-CD3 plus anti-CD28 (lane 2) demonstrated increased binding of NF-κB to IL-17 promoters in comparison with that of controls (lane 1). A supershift assay demonstrated shifted bands in p65 and p50 (lanes 3 and 4) not in c-Rel (lane 5). In normal PBMC the same pattern was observed, but the degree of NF-κB activation by anti-CD3 plus anti-CD28 was less intense than that in RA PBMC (Fig. 7b). To confirm the link between PI3K activity and NF-κB, we performed EMSA to determine the NF-κB binding activity after treatment with both LY294002 and PDTC. Both agents block NF-κB DNA-binding activity in the IL-17 promoter (Fig. 7c). Western blotting for IκB-α showed inhibition of degradation of IκB-α by LY294002 and PDTC at the same time (Fig. 7c). In contrast, the AP-1 pathway was not activated by stimulation with anti-CD3 plus anti-CD28 (data not shown), demonstrating that NF-κB is the main intracellular signaling pathway in IL-17 production by activated PBMC from patients with RA."}

{"project":"sentences","denotations":[{"id":"T15825","span":{"begin":1195,"end":1434},"obj":"Sentence"},{"id":"T15824","span":{"begin":1077,"end":1194},"obj":"Sentence"},{"id":"T15823","span":{"begin":999,"end":1076},"obj":"Sentence"},{"id":"T15822","span":{"begin":843,"end":998},"obj":"Sentence"},{"id":"T15821","span":{"begin":686,"end":842},"obj":"Sentence"},{"id":"T15820","span":{"begin":586,"end":685},"obj":"Sentence"},{"id":"T15819","span":{"begin":381,"end":585},"obj":"Sentence"},{"id":"T15818","span":{"begin":92,"end":380},"obj":"Sentence"},{"id":"T15817","span":{"begin":0,"end":91},"obj":"Sentence"},{"id":"T147","span":{"begin":0,"end":91},"obj":"Sentence"},{"id":"T148","span":{"begin":92,"end":380},"obj":"Sentence"},{"id":"T149","span":{"begin":381,"end":585},"obj":"Sentence"},{"id":"T150","span":{"begin":586,"end":685},"obj":"Sentence"},{"id":"T151","span":{"begin":686,"end":842},"obj":"Sentence"},{"id":"T152","span":{"begin":843,"end":998},"obj":"Sentence"},{"id":"T153","span":{"begin":999,"end":1076},"obj":"Sentence"},{"id":"T154","span":{"begin":1077,"end":1194},"obj":"Sentence"},{"id":"T155","span":{"begin":1195,"end":1434},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Activation of the NF-κB and activator protein-1 (AP-1) pathway in the IL-17 promoter region\nTo investigate further the intracellular signaling pathway activated by anti-CD3 plus anti-CD28, concanavalin A, PHA and IL-15, and responsible for inducing IL-17 expression, we performed an electrophoretic mobility-shift assay (EMSA) of NF-κB recognition sites in the promoters of IL-17. As shown in Fig. 7a, nuclear extracts from RA PBMC stimulated with anti-CD3 plus anti-CD28 (lane 2) demonstrated increased binding of NF-κB to IL-17 promoters in comparison with that of controls (lane 1). A supershift assay demonstrated shifted bands in p65 and p50 (lanes 3 and 4) not in c-Rel (lane 5). In normal PBMC the same pattern was observed, but the degree of NF-κB activation by anti-CD3 plus anti-CD28 was less intense than that in RA PBMC (Fig. 7b). To confirm the link between PI3K activity and NF-κB, we performed EMSA to determine the NF-κB binding activity after treatment with both LY294002 and PDTC. Both agents block NF-κB DNA-binding activity in the IL-17 promoter (Fig. 7c). Western blotting for IκB-α showed inhibition of degradation of IκB-α by LY294002 and PDTC at the same time (Fig. 7c). In contrast, the AP-1 pathway was not activated by stimulation with anti-CD3 plus anti-CD28 (data not shown), demonstrating that NF-κB is the main intracellular signaling pathway in IL-17 production by activated PBMC from patients with RA."}

{"project":"simple1","denotations":[{"id":"T16280","span":{"begin":1377,"end":1382},"obj":"Protein"},{"id":"T16279","span":{"begin":1282,"end":1286},"obj":"Protein"},{"id":"T16278","span":{"begin":1212,"end":1216},"obj":"Protein"},{"id":"T16277","span":{"begin":1140,"end":1145},"obj":"Protein"},{"id":"T16276","span":{"begin":1098,"end":1103},"obj":"Protein"},{"id":"T16275","span":{"begin":1051,"end":1056},"obj":"Protein"},{"id":"T16274","span":{"begin":789,"end":793},"obj":"Protein"},{"id":"T16273","span":{"begin":670,"end":675},"obj":"Protein"},{"id":"T16272","span":{"begin":643,"end":646},"obj":"Protein"},{"id":"T16271","span":{"begin":635,"end":638},"obj":"Protein"},{"id":"T16270","span":{"begin":524,"end":529},"obj":"Protein"},{"id":"T16269","span":{"begin":467,"end":471},"obj":"Protein"},{"id":"T16268","span":{"begin":374,"end":379},"obj":"Protein"},{"id":"T16267","span":{"begin":249,"end":254},"obj":"Protein"},{"id":"T16266","span":{"begin":213,"end":218},"obj":"Protein"},{"id":"T16265","span":{"begin":205,"end":208},"obj":"Protein"},{"id":"T16264","span":{"begin":183,"end":187},"obj":"Protein"},{"id":"T16263","span":{"begin":70,"end":75},"obj":"Protein"},{"id":"T16262","span":{"begin":49,"end":53},"obj":"Protein"},{"id":"T16261","span":{"begin":28,"end":47},"obj":"Protein"}],"text":"Activation of the NF-κB and activator protein-1 (AP-1) pathway in the IL-17 promoter region\nTo investigate further the intracellular signaling pathway activated by anti-CD3 plus anti-CD28, concanavalin A, PHA and IL-15, and responsible for inducing IL-17 expression, we performed an electrophoretic mobility-shift assay (EMSA) of NF-κB recognition sites in the promoters of IL-17. As shown in Fig. 7a, nuclear extracts from RA PBMC stimulated with anti-CD3 plus anti-CD28 (lane 2) demonstrated increased binding of NF-κB to IL-17 promoters in comparison with that of controls (lane 1). A supershift assay demonstrated shifted bands in p65 and p50 (lanes 3 and 4) not in c-Rel (lane 5). In normal PBMC the same pattern was observed, but the degree of NF-κB activation by anti-CD3 plus anti-CD28 was less intense than that in RA PBMC (Fig. 7b). To confirm the link between PI3K activity and NF-κB, we performed EMSA to determine the NF-κB binding activity after treatment with both LY294002 and PDTC. Both agents block NF-κB DNA-binding activity in the IL-17 promoter (Fig. 7c). Western blotting for IκB-α showed inhibition of degradation of IκB-α by LY294002 and PDTC at the same time (Fig. 7c). In contrast, the AP-1 pathway was not activated by stimulation with anti-CD3 plus anti-CD28 (data not shown), demonstrating that NF-κB is the main intracellular signaling pathway in IL-17 production by activated PBMC from patients with RA."}

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of the NF-κB and activator protein-1 (AP-1) pathway in the IL-17 promoter region\nTo investigate further the intracellular signaling pathway activated by anti-CD3 plus anti-CD28, concanavalin A, PHA and IL-15, and responsible for inducing IL-17 expression, we performed an electrophoretic mobility-shift assay (EMSA) of NF-κB recognition sites in the promoters of IL-17. As shown in Fig. 7a, nuclear extracts from RA PBMC stimulated with anti-CD3 plus anti-CD28 (lane 2) demonstrated increased binding of NF-κB to IL-17 promoters in comparison with that of controls (lane 1). A supershift assay demonstrated shifted bands in p65 and p50 (lanes 3 and 4) not in c-Rel (lane 5). In normal PBMC the same pattern was observed, but the degree of NF-κB activation by anti-CD3 plus anti-CD28 was less intense than that in RA PBMC (Fig. 7b). To confirm the link between PI3K activity and NF-κB, we performed EMSA to determine the NF-κB binding activity after treatment with both LY294002 and PDTC. Both agents block NF-κB DNA-binding activity in the IL-17 promoter (Fig. 7c). Western blotting for IκB-α showed inhibition of degradation of IκB-α by LY294002 and PDTC at the same time (Fig. 7c). In contrast, the AP-1 pathway was not activated by stimulation with anti-CD3 plus anti-CD28 (data not shown), demonstrating that NF-κB is the main intracellular signaling pathway in IL-17 production by activated PBMC from patients with RA."}

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As shown in Fig. 7a, nuclear extracts from RA PBMC stimulated with anti-CD3 plus anti-CD28 (lane 2) demonstrated increased binding of NF-κB to IL-17 promoters in comparison with that of controls (lane 1). A supershift assay demonstrated shifted bands in p65 and p50 (lanes 3 and 4) not in c-Rel (lane 5). In normal PBMC the same pattern was observed, but the degree of NF-κB activation by anti-CD3 plus anti-CD28 was less intense than that in RA PBMC (Fig. 7b). To confirm the link between PI3K activity and NF-κB, we performed EMSA to determine the NF-κB binding activity after treatment with both LY294002 and PDTC. Both agents block NF-κB DNA-binding activity in the IL-17 promoter (Fig. 7c). Western blotting for IκB-α showed inhibition of degradation of IκB-α by LY294002 and PDTC at the same time (Fig. 7c). In contrast, the AP-1 pathway was not activated by stimulation with anti-CD3 plus anti-CD28 (data not shown), demonstrating that NF-κB is the main intracellular signaling pathway in IL-17 production by activated PBMC from patients with RA."}

{"project":"testone","denotations":[{"id":"T15531","span":{"begin":1397,"end":1406},"obj":"Positive_regulation"},{"id":"T15530","span":{"begin":1383,"end":1393},"obj":"Gene_expression"},{"id":"T15529","span":{"begin":1125,"end":1136},"obj":"Protein_catabolism"},{"id":"T15528","span":{"begin":1111,"end":1121},"obj":"Negative_regulation"},{"id":"T15527","span":{"begin":1027,"end":1034},"obj":"Binding"},{"id":"T15526","span":{"begin":1011,"end":1016},"obj":"Negative_regulation"},{"id":"T15525","span":{"begin":937,"end":944},"obj":"Binding"},{"id":"T15524","span":{"begin":504,"end":511},"obj":"Binding"},{"id":"T15523","span":{"begin":494,"end":503},"obj":"Positive_regulation"},{"id":"T15522","span":{"begin":255,"end":265},"obj":"Gene_expression"},{"id":"T15521","span":{"begin":240,"end":248},"obj":"Positive_regulation"},{"id":"T15520","span":{"begin":224,"end":235},"obj":"Regulation"},{"id":"T15519","span":{"begin":1377,"end":1382},"obj":"Protein"},{"id":"T15518","span":{"begin":1282,"end":1286},"obj":"Protein"},{"id":"T15517","span":{"begin":1212,"end":1216},"obj":"Protein"},{"id":"T15516","span":{"begin":1140,"end":1145},"obj":"Protein"},{"id":"T15515","span":{"begin":1098,"end":1103},"obj":"Protein"},{"id":"T15514","span":{"begin":1051,"end":1056},"obj":"Protein"},{"id":"T15513","span":{"begin":789,"end":793},"obj":"Protein"},{"id":"T15512","span":{"begin":670,"end":675},"obj":"Protein"},{"id":"T15511","span":{"begin":643,"end":646},"obj":"Protein"},{"id":"T15510","span":{"begin":635,"end":638},"obj":"Protein"},{"id":"T15509","span":{"begin":524,"end":529},"obj":"Protein"},{"id":"T15508","span":{"begin":467,"end":471},"obj":"Protein"},{"id":"T15507","span":{"begin":374,"end":379},"obj":"Protein"},{"id":"T15506","span":{"begin":249,"end":254},"obj":"Protein"},{"id":"T15505","span":{"begin":213,"end":218},"obj":"Protein"},{"id":"T15504","span":{"begin":205,"end":208},"obj":"Protein"},{"id":"T15503","span":{"begin":183,"end":187},"obj":"Protein"},{"id":"T15502","span":{"begin":70,"end":75},"obj":"Protein"},{"id":"T15501","span":{"begin":49,"end":53},"obj":"Protein"},{"id":"T15500","span":{"begin":28,"end":47},"obj":"Protein"}],"relations":[{"id":"R8542","pred":"equivalentTo","subj":"T15501","obj":"T15500"},{"id":"R8543","pred":"causeOf","subj":"T15504","obj":"T15521"},{"id":"R8544","pred":"causeOf","subj":"T15505","obj":"T15521"},{"id":"R8545","pred":"themeOf","subj":"T15506","obj":"T15522"},{"id":"R8546","pred":"themeOf","subj":"T15509","obj":"T15524"},{"id":"R8547","pred":"themeOf","subj":"T15516","obj":"T15529"},{"id":"R8548","pred":"themeOf","subj":"T15519","obj":"T15530"},{"id":"R8549","pred":"themeOf","subj":"T15521","obj":"T15520"},{"id":"R8550","pred":"themeOf","subj":"T15522","obj":"T15521"},{"id":"R8551","pred":"themeOf","subj":"T15524","obj":"T15523"},{"id":"R8552","pred":"themeOf","subj":"T15527","obj":"T15526"},{"id":"R8553","pred":"themeOf","subj":"T15529","obj":"T15528"}],"text":"Activation of the NF-κB and activator protein-1 (AP-1) pathway in the IL-17 promoter region\nTo investigate further the intracellular signaling pathway activated by anti-CD3 plus anti-CD28, concanavalin A, PHA and IL-15, and responsible for inducing IL-17 expression, we performed an electrophoretic mobility-shift assay (EMSA) of NF-κB recognition sites in the promoters of IL-17. As shown in Fig. 7a, nuclear extracts from RA PBMC stimulated with anti-CD3 plus anti-CD28 (lane 2) demonstrated increased binding of NF-κB to IL-17 promoters in comparison with that of controls (lane 1). A supershift assay demonstrated shifted bands in p65 and p50 (lanes 3 and 4) not in c-Rel (lane 5). In normal PBMC the same pattern was observed, but the degree of NF-κB activation by anti-CD3 plus anti-CD28 was less intense than that in RA PBMC (Fig. 7b). To confirm the link between PI3K activity and NF-κB, we performed EMSA to determine the NF-κB binding activity after treatment with both LY294002 and PDTC. Both agents block NF-κB DNA-binding activity in the IL-17 promoter (Fig. 7c). Western blotting for IκB-α showed inhibition of degradation of IκB-α by LY294002 and PDTC at the same time (Fig. 7c). In contrast, the AP-1 pathway was not activated by stimulation with anti-CD3 plus anti-CD28 (data not shown), demonstrating that NF-κB is the main intracellular signaling pathway in IL-17 production by activated PBMC from patients with RA."}