PubMed:10362840 JSON TXT

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CL-cell

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":231,"end":257},"obj":"Cell"},{"id":"T2","span":{"begin":1123,"end":1145},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0002139"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0002543"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

Glycan-Motif

GlyCosmos6-Glycan-Motif-Image

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":95},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":96,"end":258},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":259,"end":466},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":467,"end":610},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":611,"end":702},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":703,"end":795},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":796,"end":973},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":974,"end":1300},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1301,"end":1504},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":95},"obj":"Sentence"},{"id":"T2","span":{"begin":96,"end":258},"obj":"Sentence"},{"id":"T3","span":{"begin":259,"end":466},"obj":"Sentence"},{"id":"T4","span":{"begin":467,"end":610},"obj":"Sentence"},{"id":"T5","span":{"begin":611,"end":702},"obj":"Sentence"},{"id":"T6","span":{"begin":703,"end":795},"obj":"Sentence"},{"id":"T7","span":{"begin":796,"end":973},"obj":"Sentence"},{"id":"T8","span":{"begin":974,"end":1300},"obj":"Sentence"},{"id":"T9","span":{"begin":1301,"end":1504},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":95},"obj":"Sentence"},{"id":"T2","span":{"begin":96,"end":258},"obj":"Sentence"},{"id":"T3","span":{"begin":259,"end":466},"obj":"Sentence"},{"id":"T4","span":{"begin":467,"end":610},"obj":"Sentence"},{"id":"T5","span":{"begin":611,"end":702},"obj":"Sentence"},{"id":"T6","span":{"begin":703,"end":795},"obj":"Sentence"},{"id":"T7","span":{"begin":796,"end":973},"obj":"Sentence"},{"id":"T8","span":{"begin":974,"end":1300},"obj":"Sentence"},{"id":"T9","span":{"begin":1301,"end":1504},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

GlyCosmos6-Glycan-Motif-Structure

Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":1123,"end":1127},"obj":"http://purl.obolibrary.org/obo/MAT_0000037"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

GlycoBiology-FMA

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":545,"end":547},"obj":"http://www.uniprot.org/uniprot/P49366"},{"id":"T2","span":{"begin":589,"end":591},"obj":"http://www.uniprot.org/uniprot/P49366"},{"id":"T3","span":{"begin":635,"end":637},"obj":"http://www.uniprot.org/uniprot/P49366"},{"id":"T4","span":{"begin":724,"end":726},"obj":"http://www.uniprot.org/uniprot/P49366"},{"id":"T5","span":{"begin":1028,"end":1030},"obj":"http://www.uniprot.org/uniprot/P49366"},{"id":"T6","span":{"begin":781,"end":786},"obj":"http://www.uniprot.org/uniprot/Q9UC54"},{"id":"T7","span":{"begin":908,"end":913},"obj":"http://www.uniprot.org/uniprot/Q9UC54"},{"id":"T8","span":{"begin":791,"end":794},"obj":"http://www.uniprot.org/uniprot/Q9BYM0"},{"id":"T9","span":{"begin":918,"end":921},"obj":"http://www.uniprot.org/uniprot/Q9BYM0"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":781,"end":786},"obj":"http://www.uniprot.org/uniprot/P15655"},{"id":"T2","span":{"begin":908,"end":913},"obj":"http://www.uniprot.org/uniprot/P15655"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":252,"end":257},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T2","span":{"begin":966,"end":972},"obj":"http://purl.bioontology.org/ontology/STY/T096"},{"id":"T3","span":{"begin":1140,"end":1145},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":1294,"end":1299},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T5","span":{"begin":1360,"end":1366},"obj":"http://purl.bioontology.org/ontology/STY/T096"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":144,"end":150},"obj":"http://purl.obolibrary.org/obo/GO_0040007"},{"id":"T2","span":{"begin":189,"end":195},"obj":"http://purl.obolibrary.org/obo/GO_0040007"},{"id":"T3","span":{"begin":1490,"end":1496},"obj":"http://purl.obolibrary.org/obo/GO_0040007"},{"id":"T4","span":{"begin":208,"end":226},"obj":"http://purl.obolibrary.org/obo/GO_0045840"},{"id":"T5","span":{"begin":1464,"end":1482},"obj":"http://purl.obolibrary.org/obo/GO_0045840"},{"id":"T6","span":{"begin":551,"end":553},"obj":"http://purl.obolibrary.org/obo/GO_0003987"},{"id":"T7","span":{"begin":551,"end":553},"obj":"http://purl.obolibrary.org/obo/GO_0043884"},{"id":"T8","span":{"begin":958,"end":965},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T9","span":{"begin":1352,"end":1359},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T10","span":{"begin":979,"end":997},"obj":"http://purl.obolibrary.org/obo/GO_0008283"},{"id":"T11","span":{"begin":1474,"end":1496},"obj":"http://purl.obolibrary.org/obo/GO_0045927"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":173,"end":188},"obj":"http://purl.obolibrary.org/obo/GO_0008201"},{"id":"T2","span":{"begin":181,"end":188},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":181,"end":188},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T4","span":{"begin":181,"end":188},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T5","span":{"begin":181,"end":188},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T6","span":{"begin":181,"end":202},"obj":"http://purl.obolibrary.org/obo/GO_0019838"},{"id":"T7","span":{"begin":181,"end":202},"obj":"http://purl.obolibrary.org/obo/GO_0048408"},{"id":"T8","span":{"begin":181,"end":202},"obj":"http://purl.obolibrary.org/obo/GO_0036458"},{"id":"T9","span":{"begin":181,"end":202},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T10","span":{"begin":181,"end":202},"obj":"http://purl.obolibrary.org/obo/GO_0048406"},{"id":"T11","span":{"begin":181,"end":202},"obj":"http://purl.obolibrary.org/obo/GO_0070851"},{"id":"T12","span":{"begin":1474,"end":1503},"obj":"http://purl.obolibrary.org/obo/GO_0008083"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":252,"end":257},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":1140,"end":1145},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":979,"end":983},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

UBERON-AE

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":1113,"end":1127},"obj":"http://purl.obolibrary.org/obo/UBERON_0002066"},{"id":"T2","span":{"begin":1113,"end":1139},"obj":"http://purl.obolibrary.org/obo/UBERON_0007777"},{"id":"T3","span":{"begin":1123,"end":1127},"obj":"http://purl.obolibrary.org/obo/UBERON_0001638"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

GlycoBiology-MAT

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":1123,"end":1127},"obj":"http://purl.obolibrary.org/obo/MAT_0000037"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

GlycoBiology-Motifs

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":23,"end":30},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T2","span":{"begin":173,"end":180},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T3","span":{"begin":293,"end":300},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T4","span":{"begin":437,"end":444},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T5","span":{"begin":474,"end":481},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T6","span":{"begin":556,"end":563},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T7","span":{"begin":594,"end":601},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T8","span":{"begin":640,"end":647},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T9","span":{"begin":727,"end":734},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T10","span":{"begin":829,"end":836},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T11","span":{"begin":1012,"end":1019},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T12","span":{"begin":1031,"end":1038},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T13","span":{"begin":1230,"end":1237},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

performance-test

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":1113,"end":1127},"obj":"http://purl.obolibrary.org/obo/UBERON_0002066"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1113,"end":1139},"obj":"http://purl.obolibrary.org/obo/UBERON_0007777"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":1123,"end":1127},"obj":"http://purl.obolibrary.org/obo/UBERON_0001638"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

Anatomy-MAT

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":1123,"end":1127},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000037"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

mondo_disease

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":545,"end":550},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0007790"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":1107,"end":1112},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":231,"end":257},"obj":"Body_part"},{"id":"T2","span":{"begin":1113,"end":1127},"obj":"Body_part"},{"id":"T3","span":{"begin":1128,"end":1145},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0002139"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002066"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL_0000115"}],"text":"Structural features in heparin that interact with VEGF165 and modulate its biological activity.\nThe 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor."}