PMC:3312845 / 29963-31395
Annnotations
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phosphorylation of NF-κB enhances its transactivation potential, and p65 phosphorylation occurs in either the cytoplasm or the nucleus [30]. In the present study, p65-Thr435 immunoreactivity was detected in endothelial cells, and its immunoreactivity showed an inverse correlation to the degree of SMI-71 expression. SMI-71, an endothelial barrier antigen, is a protein expressed by endothelial cells of rat BBB [31]. Under pathological conditions, SMI-71 expression is lost in endothelial cells [5,7,8,30,32]. Acute phases of the above pathological conditions are accompanied by opening of the BBB and development of vasogenic edema [33]. Indeed, neutralization of SMI-71 in vivo leads to widening of intercellular junctions between endothelial cells and swelling of perivascular astrocytic processes [34], although SMI-71 is not localized at endothelial cell junctions [35-38]. In the present study, SMI-71 immunoreactivity was significantly reduced in blood vessels 1 day after SE when vasogenic edema and neuronal damage were observed. Furthermore, sTNFp55R infusion effectively prevented SE-induced SMI-71 down-regulation. With respect to the phosphorylation of p65-Thr435 by TNF-α [39], our findings indicate that TNF-α-mediated p65-Thr435 phosphorylation in endothelial cells may play an important role in vasogenic edema induction via SMI-71 degradation or its posttranslational dysfunction influencing BBB permeability."}
bionlp-st-ge-2016-test-proteins
{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T11674","span":{"begin":167,"end":170},"obj":"Protein"},{"id":"T11673","span":{"begin":73,"end":76},"obj":"Protein"},{"id":"T11672","span":{"begin":0,"end":3},"obj":"Protein"},{"id":"T11679","span":{"begin":1239,"end":1242},"obj":"Protein"},{"id":"T11678","span":{"begin":1224,"end":1229},"obj":"Protein"},{"id":"T11677","span":{"begin":1185,"end":1190},"obj":"Protein"},{"id":"T11676","span":{"begin":1171,"end":1174},"obj":"Protein"},{"id":"T11675","span":{"begin":1058,"end":1065},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"p65 phosphorylation of NF-κB enhances its transactivation potential, and p65 phosphorylation occurs in either the cytoplasm or the nucleus [30]. In the present study, p65-Thr435 immunoreactivity was detected in endothelial cells, and its immunoreactivity showed an inverse correlation to the degree of SMI-71 expression. SMI-71, an endothelial barrier antigen, is a protein expressed by endothelial cells of rat BBB [31]. Under pathological conditions, SMI-71 expression is lost in endothelial cells [5,7,8,30,32]. Acute phases of the above pathological conditions are accompanied by opening of the BBB and development of vasogenic edema [33]. Indeed, neutralization of SMI-71 in vivo leads to widening of intercellular junctions between endothelial cells and swelling of perivascular astrocytic processes [34], although SMI-71 is not localized at endothelial cell junctions [35-38]. In the present study, SMI-71 immunoreactivity was significantly reduced in blood vessels 1 day after SE when vasogenic edema and neuronal damage were observed. Furthermore, sTNFp55R infusion effectively prevented SE-induced SMI-71 down-regulation. With respect to the phosphorylation of p65-Thr435 by TNF-α [39], our findings indicate that TNF-α-mediated p65-Thr435 phosphorylation in endothelial cells may play an important role in vasogenic edema induction via SMI-71 degradation or its posttranslational dysfunction influencing BBB permeability."}
bionlp-st-ge-2016-uniprot
{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T12870","span":{"begin":1239,"end":1242},"obj":"http://www.uniprot.org/uniprot/P21579"},{"id":"T12869","span":{"begin":1171,"end":1174},"obj":"http://www.uniprot.org/uniprot/P21579"},{"id":"T12868","span":{"begin":167,"end":170},"obj":"http://www.uniprot.org/uniprot/P21579"},{"id":"T12867","span":{"begin":73,"end":76},"obj":"http://www.uniprot.org/uniprot/P21579"},{"id":"T12866","span":{"begin":0,"end":3},"obj":"http://www.uniprot.org/uniprot/P21579"},{"id":"T12851","span":{"begin":1239,"end":1242},"obj":"http://www.uniprot.org/uniprot/Q04206"},{"id":"T12850","span":{"begin":1171,"end":1174},"obj":"http://www.uniprot.org/uniprot/Q04206"},{"id":"T12849","span":{"begin":167,"end":170},"obj":"http://www.uniprot.org/uniprot/Q04206"},{"id":"T12848","span":{"begin":73,"end":76},"obj":"http://www.uniprot.org/uniprot/Q04206"},{"id":"T12847","span":{"begin":0,"end":3},"obj":"http://www.uniprot.org/uniprot/Q04206"},{"id":"T12841","span":{"begin":1224,"end":1229},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T12840","span":{"begin":1185,"end":1190},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T12829","span":{"begin":1224,"end":1227},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T12828","span":{"begin":1185,"end":1188},"obj":"http://www.uniprot.org/uniprot/P01375"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"p65 phosphorylation of NF-κB enhances its transactivation potential, and p65 phosphorylation occurs in either the cytoplasm or the nucleus [30]. In the present study, p65-Thr435 immunoreactivity was detected in endothelial cells, and its immunoreactivity showed an inverse correlation to the degree of SMI-71 expression. SMI-71, an endothelial barrier antigen, is a protein expressed by endothelial cells of rat BBB [31]. Under pathological conditions, SMI-71 expression is lost in endothelial cells [5,7,8,30,32]. Acute phases of the above pathological conditions are accompanied by opening of the BBB and development of vasogenic edema [33]. Indeed, neutralization of SMI-71 in vivo leads to widening of intercellular junctions between endothelial cells and swelling of perivascular astrocytic processes [34], although SMI-71 is not localized at endothelial cell junctions [35-38]. In the present study, SMI-71 immunoreactivity was significantly reduced in blood vessels 1 day after SE when vasogenic edema and neuronal damage were observed. Furthermore, sTNFp55R infusion effectively prevented SE-induced SMI-71 down-regulation. With respect to the phosphorylation of p65-Thr435 by TNF-α [39], our findings indicate that TNF-α-mediated p65-Thr435 phosphorylation in endothelial cells may play an important role in vasogenic edema induction via SMI-71 degradation or its posttranslational dysfunction influencing BBB permeability."}
UBERON-AE
{"project":"UBERON-AE","denotations":[{"id":"T11616","span":{"begin":965,"end":972},"obj":"http://purl.obolibrary.org/obo/UBERON_0000055"},{"id":"T11614","span":{"begin":959,"end":972},"obj":"http://purl.obolibrary.org/obo/UBERON_0001981"},{"id":"T11612","span":{"begin":959,"end":964},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"p65 phosphorylation of NF-κB enhances its transactivation potential, and p65 phosphorylation occurs in either the cytoplasm or the nucleus [30]. In the present study, p65-Thr435 immunoreactivity was detected in endothelial cells, and its immunoreactivity showed an inverse correlation to the degree of SMI-71 expression. SMI-71, an endothelial barrier antigen, is a protein expressed by endothelial cells of rat BBB [31]. Under pathological conditions, SMI-71 expression is lost in endothelial cells [5,7,8,30,32]. Acute phases of the above pathological conditions are accompanied by opening of the BBB and development of vasogenic edema [33]. Indeed, neutralization of SMI-71 in vivo leads to widening of intercellular junctions between endothelial cells and swelling of perivascular astrocytic processes [34], although SMI-71 is not localized at endothelial cell junctions [35-38]. In the present study, SMI-71 immunoreactivity was significantly reduced in blood vessels 1 day after SE when vasogenic edema and neuronal damage were observed. Furthermore, sTNFp55R infusion effectively prevented SE-induced SMI-71 down-regulation. With respect to the phosphorylation of p65-Thr435 by TNF-α [39], our findings indicate that TNF-α-mediated p65-Thr435 phosphorylation in endothelial cells may play an important role in vasogenic edema induction via SMI-71 degradation or its posttranslational dysfunction influencing BBB permeability."}
GO-BP
{"project":"GO-BP","denotations":[{"id":"T11736","span":{"begin":1354,"end":1365},"obj":"http://purl.obolibrary.org/obo/GO_0009056"},{"id":"T11734","span":{"begin":1120,"end":1130},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T11733","span":{"begin":835,"end":844},"obj":"http://purl.obolibrary.org/obo/GO_0051179"},{"id":"T11732","span":{"begin":42,"end":57},"obj":"http://purl.obolibrary.org/obo/GO_2000144"},{"id":"T11731","span":{"begin":607,"end":618},"obj":"http://purl.obolibrary.org/obo/GO_0032502"},{"id":"T11722","span":{"begin":1250,"end":1265},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T11721","span":{"begin":1152,"end":1167},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T11720","span":{"begin":77,"end":92},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T11719","span":{"begin":4,"end":19},"obj":"http://purl.obolibrary.org/obo/GO_0016310"}],"text":"p65 phosphorylation of NF-κB enhances its transactivation potential, and p65 phosphorylation occurs in either the cytoplasm or the nucleus [30]. In the present study, p65-Thr435 immunoreactivity was detected in endothelial cells, and its immunoreactivity showed an inverse correlation to the degree of SMI-71 expression. SMI-71, an endothelial barrier antigen, is a protein expressed by endothelial cells of rat BBB [31]. Under pathological conditions, SMI-71 expression is lost in endothelial cells [5,7,8,30,32]. Acute phases of the above pathological conditions are accompanied by opening of the BBB and development of vasogenic edema [33]. Indeed, neutralization of SMI-71 in vivo leads to widening of intercellular junctions between endothelial cells and swelling of perivascular astrocytic processes [34], although SMI-71 is not localized at endothelial cell junctions [35-38]. In the present study, SMI-71 immunoreactivity was significantly reduced in blood vessels 1 day after SE when vasogenic edema and neuronal damage were observed. Furthermore, sTNFp55R infusion effectively prevented SE-induced SMI-71 down-regulation. With respect to the phosphorylation of p65-Thr435 by TNF-α [39], our findings indicate that TNF-α-mediated p65-Thr435 phosphorylation in endothelial cells may play an important role in vasogenic edema induction via SMI-71 degradation or its posttranslational dysfunction influencing BBB permeability."}
GO-CC
{"project":"GO-CC","denotations":[{"id":"T11760","span":{"begin":860,"end":874},"obj":"http://purl.obolibrary.org/obo/GO_0030054"},{"id":"T11759","span":{"begin":706,"end":729},"obj":"http://purl.obolibrary.org/obo/GO_0005911"},{"id":"T11758","span":{"begin":131,"end":138},"obj":"http://purl.obolibrary.org/obo/GO_0005634"},{"id":"T11757","span":{"begin":114,"end":123},"obj":"http://purl.obolibrary.org/obo/GO_0005737"},{"id":"T11753","span":{"begin":1281,"end":1286},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T11752","span":{"begin":750,"end":755},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T11751","span":{"begin":494,"end":499},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T11750","span":{"begin":399,"end":404},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T11749","span":{"begin":223,"end":228},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"p65 phosphorylation of NF-κB enhances its transactivation potential, and p65 phosphorylation occurs in either the cytoplasm or the nucleus [30]. In the present study, p65-Thr435 immunoreactivity was detected in endothelial cells, and its immunoreactivity showed an inverse correlation to the degree of SMI-71 expression. SMI-71, an endothelial barrier antigen, is a protein expressed by endothelial cells of rat BBB [31]. Under pathological conditions, SMI-71 expression is lost in endothelial cells [5,7,8,30,32]. Acute phases of the above pathological conditions are accompanied by opening of the BBB and development of vasogenic edema [33]. Indeed, neutralization of SMI-71 in vivo leads to widening of intercellular junctions between endothelial cells and swelling of perivascular astrocytic processes [34], although SMI-71 is not localized at endothelial cell junctions [35-38]. In the present study, SMI-71 immunoreactivity was significantly reduced in blood vessels 1 day after SE when vasogenic edema and neuronal damage were observed. Furthermore, sTNFp55R infusion effectively prevented SE-induced SMI-71 down-regulation. With respect to the phosphorylation of p65-Thr435 by TNF-α [39], our findings indicate that TNF-α-mediated p65-Thr435 phosphorylation in endothelial cells may play an important role in vasogenic edema induction via SMI-71 degradation or its posttranslational dysfunction influencing BBB permeability."}
sentences
{"project":"sentences","denotations":[{"id":"T11644","span":{"begin":1132,"end":1432},"obj":"Sentence"},{"id":"T11643","span":{"begin":1044,"end":1131},"obj":"Sentence"},{"id":"T11642","span":{"begin":884,"end":1043},"obj":"Sentence"},{"id":"T11641","span":{"begin":644,"end":883},"obj":"Sentence"},{"id":"T11640","span":{"begin":515,"end":643},"obj":"Sentence"},{"id":"T11639","span":{"begin":422,"end":514},"obj":"Sentence"},{"id":"T11638","span":{"begin":321,"end":421},"obj":"Sentence"},{"id":"T11637","span":{"begin":145,"end":320},"obj":"Sentence"},{"id":"T11636","span":{"begin":0,"end":144},"obj":"Sentence"},{"id":"T221","span":{"begin":0,"end":144},"obj":"Sentence"},{"id":"T222","span":{"begin":145,"end":320},"obj":"Sentence"},{"id":"T223","span":{"begin":321,"end":421},"obj":"Sentence"},{"id":"T224","span":{"begin":422,"end":514},"obj":"Sentence"},{"id":"T225","span":{"begin":515,"end":643},"obj":"Sentence"},{"id":"T226","span":{"begin":644,"end":883},"obj":"Sentence"},{"id":"T227","span":{"begin":884,"end":1043},"obj":"Sentence"},{"id":"T228","span":{"begin":1044,"end":1131},"obj":"Sentence"},{"id":"T229","span":{"begin":1132,"end":1432},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"p65 phosphorylation of NF-κB enhances its transactivation potential, and p65 phosphorylation occurs in either the cytoplasm or the nucleus [30]. In the present study, p65-Thr435 immunoreactivity was detected in endothelial cells, and its immunoreactivity showed an inverse correlation to the degree of SMI-71 expression. SMI-71, an endothelial barrier antigen, is a protein expressed by endothelial cells of rat BBB [31]. Under pathological conditions, SMI-71 expression is lost in endothelial cells [5,7,8,30,32]. Acute phases of the above pathological conditions are accompanied by opening of the BBB and development of vasogenic edema [33]. Indeed, neutralization of SMI-71 in vivo leads to widening of intercellular junctions between endothelial cells and swelling of perivascular astrocytic processes [34], although SMI-71 is not localized at endothelial cell junctions [35-38]. In the present study, SMI-71 immunoreactivity was significantly reduced in blood vessels 1 day after SE when vasogenic edema and neuronal damage were observed. Furthermore, sTNFp55R infusion effectively prevented SE-induced SMI-71 down-regulation. With respect to the phosphorylation of p65-Thr435 by TNF-α [39], our findings indicate that TNF-α-mediated p65-Thr435 phosphorylation in endothelial cells may play an important role in vasogenic edema induction via SMI-71 degradation or its posttranslational dysfunction influencing BBB permeability."}
simple1
{"project":"simple1","denotations":[{"id":"T11932","span":{"begin":1239,"end":1242},"obj":"Protein"},{"id":"T11931","span":{"begin":1224,"end":1229},"obj":"Protein"},{"id":"T11930","span":{"begin":1185,"end":1190},"obj":"Protein"},{"id":"T11929","span":{"begin":1171,"end":1174},"obj":"Protein"},{"id":"T11928","span":{"begin":1058,"end":1065},"obj":"Protein"},{"id":"T11927","span":{"begin":167,"end":170},"obj":"Protein"},{"id":"T11926","span":{"begin":73,"end":76},"obj":"Protein"},{"id":"T11925","span":{"begin":0,"end":3},"obj":"Protein"}],"text":"p65 phosphorylation of NF-κB enhances its transactivation potential, and p65 phosphorylation occurs in either the cytoplasm or the nucleus [30]. In the present study, p65-Thr435 immunoreactivity was detected in endothelial cells, and its immunoreactivity showed an inverse correlation to the degree of SMI-71 expression. SMI-71, an endothelial barrier antigen, is a protein expressed by endothelial cells of rat BBB [31]. Under pathological conditions, SMI-71 expression is lost in endothelial cells [5,7,8,30,32]. Acute phases of the above pathological conditions are accompanied by opening of the BBB and development of vasogenic edema [33]. Indeed, neutralization of SMI-71 in vivo leads to widening of intercellular junctions between endothelial cells and swelling of perivascular astrocytic processes [34], although SMI-71 is not localized at endothelial cell junctions [35-38]. In the present study, SMI-71 immunoreactivity was significantly reduced in blood vessels 1 day after SE when vasogenic edema and neuronal damage were observed. Furthermore, sTNFp55R infusion effectively prevented SE-induced SMI-71 down-regulation. With respect to the phosphorylation of p65-Thr435 by TNF-α [39], our findings indicate that TNF-α-mediated p65-Thr435 phosphorylation in endothelial cells may play an important role in vasogenic edema induction via SMI-71 degradation or its posttranslational dysfunction influencing BBB permeability."}
BioNLP16_DUT
{"project":"BioNLP16_DUT","denotations":[{"id":"T14242","span":{"begin":1230,"end":1238},"obj":"Positive_regulation"},{"id":"T14241","span":{"begin":1250,"end":1265},"obj":"Phosphorylation"},{"id":"T14240","span":{"begin":1152,"end":1167},"obj":"Phosphorylation"},{"id":"T14239","span":{"begin":77,"end":92},"obj":"Phosphorylation"},{"id":"T14238","span":{"begin":93,"end":99},"obj":"Positive_regulation"},{"id":"T14237","span":{"begin":29,"end":37},"obj":"Positive_regulation"},{"id":"T14236","span":{"begin":4,"end":19},"obj":"Phosphorylation"},{"id":"T14201","span":{"begin":1239,"end":1242},"obj":"Protein"},{"id":"T14200","span":{"begin":1224,"end":1229},"obj":"Protein"},{"id":"T14199","span":{"begin":1185,"end":1190},"obj":"Protein"},{"id":"T14198","span":{"begin":1171,"end":1174},"obj":"Protein"},{"id":"T14197","span":{"begin":1058,"end":1065},"obj":"Protein"},{"id":"T14196","span":{"begin":167,"end":170},"obj":"Protein"},{"id":"T14195","span":{"begin":73,"end":76},"obj":"Protein"},{"id":"T14194","span":{"begin":0,"end":3},"obj":"Protein"}],"relations":[{"id":"R11153","pred":"themeOf","subj":"T14194","obj":"T14236"},{"id":"R11154","pred":"themeOf","subj":"T14195","obj":"T14239"},{"id":"R11157","pred":"themeOf","subj":"T14198","obj":"T14240"},{"id":"R11158","pred":"themeOf","subj":"T14201","obj":"T14242"},{"id":"R11159","pred":"themeOf","subj":"T14201","obj":"T14241"},{"id":"R11190","pred":"themeOf","subj":"T14236","obj":"T14237"},{"id":"R11191","pred":"themeOf","subj":"T14239","obj":"T14238"}],"text":"p65 phosphorylation of NF-κB enhances its transactivation potential, and p65 phosphorylation occurs in either the cytoplasm or the nucleus [30]. In the present study, p65-Thr435 immunoreactivity was detected in endothelial cells, and its immunoreactivity showed an inverse correlation to the degree of SMI-71 expression. SMI-71, an endothelial barrier antigen, is a protein expressed by endothelial cells of rat BBB [31]. Under pathological conditions, SMI-71 expression is lost in endothelial cells [5,7,8,30,32]. Acute phases of the above pathological conditions are accompanied by opening of the BBB and development of vasogenic edema [33]. Indeed, neutralization of SMI-71 in vivo leads to widening of intercellular junctions between endothelial cells and swelling of perivascular astrocytic processes [34], although SMI-71 is not localized at endothelial cell junctions [35-38]. In the present study, SMI-71 immunoreactivity was significantly reduced in blood vessels 1 day after SE when vasogenic edema and neuronal damage were observed. Furthermore, sTNFp55R infusion effectively prevented SE-induced SMI-71 down-regulation. With respect to the phosphorylation of p65-Thr435 by TNF-α [39], our findings indicate that TNF-α-mediated p65-Thr435 phosphorylation in endothelial cells may play an important role in vasogenic edema induction via SMI-71 degradation or its posttranslational dysfunction influencing BBB permeability."}
BioNLP16_Messiy
{"project":"BioNLP16_Messiy","denotations":[{"id":"T13843","span":{"begin":1230,"end":1238},"obj":"Positive_regulation"},{"id":"T13842","span":{"begin":1250,"end":1265},"obj":"Phosphorylation"},{"id":"T13841","span":{"begin":1152,"end":1167},"obj":"Phosphorylation"},{"id":"T13840","span":{"begin":77,"end":92},"obj":"Phosphorylation"},{"id":"T13839","span":{"begin":4,"end":19},"obj":"Phosphorylation"},{"id":"T13804","span":{"begin":1239,"end":1242},"obj":"Protein"},{"id":"T13803","span":{"begin":1224,"end":1229},"obj":"Protein"},{"id":"T13802","span":{"begin":1185,"end":1190},"obj":"Protein"},{"id":"T13801","span":{"begin":1171,"end":1174},"obj":"Protein"},{"id":"T13800","span":{"begin":1058,"end":1065},"obj":"Protein"},{"id":"T13799","span":{"begin":167,"end":170},"obj":"Protein"},{"id":"T13798","span":{"begin":73,"end":76},"obj":"Protein"},{"id":"T13797","span":{"begin":0,"end":3},"obj":"Protein"}],"relations":[{"id":"R10973","pred":"themeOf","subj":"T13797","obj":"T13839"},{"id":"R10975","pred":"themeOf","subj":"T13798","obj":"T13840"},{"id":"R10976","pred":"themeOf","subj":"T13802","obj":"T13841"},{"id":"R10977","pred":"causeOf","subj":"T13803","obj":"T13843"},{"id":"R10978","pred":"themeOf","subj":"T13804","obj":"T13842"},{"id":"R11030","pred":"themeOf","subj":"T13842","obj":"T13843"}],"text":"p65 phosphorylation of NF-κB enhances its transactivation potential, and p65 phosphorylation occurs in either the cytoplasm or the nucleus [30]. In the present study, p65-Thr435 immunoreactivity was detected in endothelial cells, and its immunoreactivity showed an inverse correlation to the degree of SMI-71 expression. SMI-71, an endothelial barrier antigen, is a protein expressed by endothelial cells of rat BBB [31]. Under pathological conditions, SMI-71 expression is lost in endothelial cells [5,7,8,30,32]. Acute phases of the above pathological conditions are accompanied by opening of the BBB and development of vasogenic edema [33]. Indeed, neutralization of SMI-71 in vivo leads to widening of intercellular junctions between endothelial cells and swelling of perivascular astrocytic processes [34], although SMI-71 is not localized at endothelial cell junctions [35-38]. In the present study, SMI-71 immunoreactivity was significantly reduced in blood vessels 1 day after SE when vasogenic edema and neuronal damage were observed. Furthermore, sTNFp55R infusion effectively prevented SE-induced SMI-71 down-regulation. With respect to the phosphorylation of p65-Thr435 by TNF-α [39], our findings indicate that TNF-α-mediated p65-Thr435 phosphorylation in endothelial cells may play an important role in vasogenic edema induction via SMI-71 degradation or its posttranslational dysfunction influencing BBB permeability."}
DLUT931
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bionlp-st-ge-2016-test-ihmc
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phosphorylation of NF-κB enhances its transactivation potential, and p65 phosphorylation occurs in either the cytoplasm or the nucleus [30]. In the present study, p65-Thr435 immunoreactivity was detected in endothelial cells, and its immunoreactivity showed an inverse correlation to the degree of SMI-71 expression. SMI-71, an endothelial barrier antigen, is a protein expressed by endothelial cells of rat BBB [31]. Under pathological conditions, SMI-71 expression is lost in endothelial cells [5,7,8,30,32]. Acute phases of the above pathological conditions are accompanied by opening of the BBB and development of vasogenic edema [33]. Indeed, neutralization of SMI-71 in vivo leads to widening of intercellular junctions between endothelial cells and swelling of perivascular astrocytic processes [34], although SMI-71 is not localized at endothelial cell junctions [35-38]. In the present study, SMI-71 immunoreactivity was significantly reduced in blood vessels 1 day after SE when vasogenic edema and neuronal damage were observed. Furthermore, sTNFp55R infusion effectively prevented SE-induced SMI-71 down-regulation. With respect to the phosphorylation of p65-Thr435 by TNF-α [39], our findings indicate that TNF-α-mediated p65-Thr435 phosphorylation in endothelial cells may play an important role in vasogenic edema induction via SMI-71 degradation or its posttranslational dysfunction influencing BBB permeability."}
bionlp-st-ge-2016-test-tees
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testone
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test3
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