PubMed:10362842 JSONTXT

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Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":105,"end":110},"obj":"http://www.uniprot.org/uniprot/P61148"},{"id":"T2","span":{"begin":433,"end":438},"obj":"http://www.uniprot.org/uniprot/P61148"},{"id":"T3","span":{"begin":498,"end":503},"obj":"http://www.uniprot.org/uniprot/P61148"},{"id":"T4","span":{"begin":711,"end":716},"obj":"http://www.uniprot.org/uniprot/P61148"},{"id":"T5","span":{"begin":816,"end":821},"obj":"http://www.uniprot.org/uniprot/P61148"},{"id":"T6","span":{"begin":990,"end":995},"obj":"http://www.uniprot.org/uniprot/P61148"},{"id":"T7","span":{"begin":1265,"end":1270},"obj":"http://www.uniprot.org/uniprot/P61148"},{"id":"T8","span":{"begin":1420,"end":1425},"obj":"http://www.uniprot.org/uniprot/P61148"},{"id":"T9","span":{"begin":115,"end":120},"obj":"http://www.uniprot.org/uniprot/P15655"},{"id":"T10","span":{"begin":283,"end":288},"obj":"http://www.uniprot.org/uniprot/P15655"},{"id":"T11","span":{"begin":780,"end":785},"obj":"http://www.uniprot.org/uniprot/P15655"},{"id":"T12","span":{"begin":866,"end":871},"obj":"http://www.uniprot.org/uniprot/P15655"},{"id":"T13","span":{"begin":1140,"end":1145},"obj":"http://www.uniprot.org/uniprot/P15655"},{"id":"T14","span":{"begin":498,"end":511},"obj":"http://www.uniprot.org/uniprot/O70514"},{"id":"T15","span":{"begin":711,"end":724},"obj":"http://www.uniprot.org/uniprot/O70514"},{"id":"T16","span":{"begin":816,"end":829},"obj":"http://www.uniprot.org/uniprot/O70514"},{"id":"T17","span":{"begin":990,"end":1003},"obj":"http://www.uniprot.org/uniprot/O70514"},{"id":"T18","span":{"begin":1254,"end":1270},"obj":"http://www.uniprot.org/uniprot/O70514"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":219,"end":228},"obj":"http://purl.bioontology.org/ontology/STY/T192"},{"id":"T2","span":{"begin":957,"end":963},"obj":"http://purl.bioontology.org/ontology/STY/T096"},{"id":"T3","span":{"begin":1081,"end":1088},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/353209"},{"id":"T4","span":{"begin":1228,"end":1233},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":31,"end":37},"obj":"http://purl.obolibrary.org/obo/GO_0040007"},{"id":"T2","span":{"begin":90,"end":96},"obj":"http://purl.obolibrary.org/obo/GO_0040007"},{"id":"T3","span":{"begin":63,"end":70},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T4","span":{"begin":166,"end":173},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T5","span":{"begin":257,"end":264},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T6","span":{"begin":383,"end":390},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T7","span":{"begin":520,"end":527},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T8","span":{"begin":675,"end":682},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T9","span":{"begin":949,"end":956},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T10","span":{"begin":1012,"end":1019},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T11","span":{"begin":1063,"end":1070},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T12","span":{"begin":1183,"end":1190},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T13","span":{"begin":658,"end":666},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T14","span":{"begin":1193,"end":1202},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T15","span":{"begin":1307,"end":1316},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T16","span":{"begin":1077,"end":1080},"obj":"http://purl.obolibrary.org/obo/GO_0007568"},{"id":"T17","span":{"begin":1350,"end":1358},"obj":"http://purl.obolibrary.org/obo/GO_0007349"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"GO-MF","denotations":[{"id":"T33","span":{"begin":504,"end":511},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T34","span":{"begin":717,"end":724},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T35","span":{"begin":769,"end":776},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T36","span":{"begin":822,"end":829},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T37","span":{"begin":872,"end":879},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T38","span":{"begin":996,"end":1003},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T39","span":{"begin":1146,"end":1153},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T40","span":{"begin":1254,"end":1261},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T41","span":{"begin":47,"end":70},"obj":"http://purl.obolibrary.org/obo/GO_0008201"},{"id":"T42","span":{"begin":47,"end":70},"obj":"http://purl.obolibrary.org/obo/GO_1904399"},{"id":"T43","span":{"begin":504,"end":527},"obj":"http://purl.obolibrary.org/obo/GO_0008201"},{"id":"T44","span":{"begin":504,"end":527},"obj":"http://purl.obolibrary.org/obo/GO_1904399"},{"id":"T45","span":{"begin":996,"end":1019},"obj":"http://purl.obolibrary.org/obo/GO_0008201"},{"id":"T46","span":{"begin":996,"end":1019},"obj":"http://purl.obolibrary.org/obo/GO_1904399"},{"id":"T47","span":{"begin":47,"end":70},"obj":"http://purl.obolibrary.org/obo/GO_0043395"},{"id":"T48","span":{"begin":504,"end":527},"obj":"http://purl.obolibrary.org/obo/GO_0043395"},{"id":"T49","span":{"begin":996,"end":1019},"obj":"http://purl.obolibrary.org/obo/GO_0043395"},{"id":"T50","span":{"begin":272,"end":286},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T51","span":{"begin":769,"end":783},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T52","span":{"begin":1254,"end":1268},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T53","span":{"begin":272,"end":288},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T54","span":{"begin":769,"end":785},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T55","span":{"begin":866,"end":879},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T56","span":{"begin":1140,"end":1153},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T57","span":{"begin":498,"end":511},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T58","span":{"begin":711,"end":724},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T59","span":{"begin":816,"end":829},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T60","span":{"begin":990,"end":1003},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T61","span":{"begin":1254,"end":1270},"obj":"http://purl.obolibrary.org/obo/GO_0017134"},{"id":"T62","span":{"begin":715,"end":732},"obj":"http://purl.obolibrary.org/obo/GO_0050683"},{"id":"T63","span":{"begin":820,"end":836},"obj":"http://purl.obolibrary.org/obo/GO_0050683"},{"id":"T64","span":{"begin":1144,"end":1160},"obj":"http://purl.obolibrary.org/obo/GO_0050682"},{"id":"T1","span":{"begin":47,"end":54},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":272,"end":279},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":504,"end":511},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T4","span":{"begin":717,"end":724},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T5","span":{"begin":769,"end":776},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T6","span":{"begin":822,"end":829},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T7","span":{"begin":872,"end":879},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T8","span":{"begin":996,"end":1003},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T9","span":{"begin":1146,"end":1153},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T10","span":{"begin":1254,"end":1261},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T11","span":{"begin":47,"end":54},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T12","span":{"begin":272,"end":279},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T13","span":{"begin":504,"end":511},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T14","span":{"begin":717,"end":724},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T15","span":{"begin":769,"end":776},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T16","span":{"begin":822,"end":829},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T17","span":{"begin":872,"end":879},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T18","span":{"begin":996,"end":1003},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T19","span":{"begin":1146,"end":1153},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T20","span":{"begin":1254,"end":1261},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T21","span":{"begin":47,"end":54},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T22","span":{"begin":272,"end":279},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T23","span":{"begin":504,"end":511},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T24","span":{"begin":717,"end":724},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T25","span":{"begin":769,"end":776},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T26","span":{"begin":822,"end":829},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T27","span":{"begin":872,"end":879},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T28","span":{"begin":996,"end":1003},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T29","span":{"begin":1146,"end":1153},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T30","span":{"begin":1254,"end":1261},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T31","span":{"begin":47,"end":54},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T32","span":{"begin":272,"end":279},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":202,"end":206},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":1228,"end":1233},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":202,"end":214},"obj":"http://purl.obolibrary.org/obo/GO_0009986"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":1049,"end":1054},"obj":"http://purl.obolibrary.org/obo/UBERON_0000947"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":1049,"end":1054},"obj":"http://purl.obolibrary.org/obo/MAT_0000035"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":55,"end":70},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":158,"end":173},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":249,"end":264},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"PD-GlycoEpitope-B_T4","span":{"begin":375,"end":390},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"PD-GlycoEpitope-B_T5","span":{"begin":512,"end":527},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"PD-GlycoEpitope-B_T6","span":{"begin":667,"end":682},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"PD-GlycoEpitope-B_T7","span":{"begin":1004,"end":1019},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"PD-GlycoEpitope-B_T8","span":{"begin":1055,"end":1070},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"PD-GlycoEpitope-B_T9","span":{"begin":1175,"end":1190},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"PD-GlycoEpitope-B_T10","span":{"begin":1359,"end":1374},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":608,"end":612},"obj":"\"http://rdf.glycoinfo.org/glycan/G93013RN\""},{"id":"GlycanIUPAC_T2","span":{"begin":917,"end":921},"obj":"\"http://rdf.glycoinfo.org/glycan/G93013RN\""},{"id":"GlycanIUPAC_T3","span":{"begin":1320,"end":1324},"obj":"\"http://rdf.glycoinfo.org/glycan/G93013RN\""},{"id":"GlycanIUPAC_T4","span":{"begin":608,"end":612},"obj":"\"http://rdf.glycoinfo.org/glycan/G40820ST\""},{"id":"GlycanIUPAC_T5","span":{"begin":917,"end":921},"obj":"\"http://rdf.glycoinfo.org/glycan/G40820ST\""},{"id":"GlycanIUPAC_T6","span":{"begin":1320,"end":1324},"obj":"\"http://rdf.glycoinfo.org/glycan/G40820ST\""},{"id":"GlycanIUPAC_T7","span":{"begin":608,"end":612},"obj":"\"http://rdf.glycoinfo.org/glycan/G55034GQ\""},{"id":"GlycanIUPAC_T8","span":{"begin":917,"end":921},"obj":"\"http://rdf.glycoinfo.org/glycan/G55034GQ\""},{"id":"GlycanIUPAC_T9","span":{"begin":1320,"end":1324},"obj":"\"http://rdf.glycoinfo.org/glycan/G55034GQ\""}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":1049,"end":1054},"obj":"http://purl.obolibrary.org/obo/UBERON_0000947"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":1049,"end":1054},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000035"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":78},"obj":"Sentence"},{"id":"T2","span":{"begin":79,"end":229},"obj":"Sentence"},{"id":"T3","span":{"begin":230,"end":439},"obj":"Sentence"},{"id":"T4","span":{"begin":440,"end":655},"obj":"Sentence"},{"id":"T5","span":{"begin":656,"end":786},"obj":"Sentence"},{"id":"T6","span":{"begin":787,"end":964},"obj":"Sentence"},{"id":"T7","span":{"begin":965,"end":1161},"obj":"Sentence"},{"id":"T8","span":{"begin":1162,"end":1271},"obj":"Sentence"},{"id":"T9","span":{"begin":1272,"end":1426},"obj":"Sentence"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":55,"end":70},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":158,"end":173},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":249,"end":264},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":375,"end":390},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":512,"end":527},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":667,"end":682},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":1004,"end":1019},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":1055,"end":1070},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T9","span":{"begin":1175,"end":1190},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T10","span":{"begin":1359,"end":1374},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A9","pred":"glycoepitope_id","subj":"T9","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A10","pred":"glycoepitope_id","subj":"T10","obj":"http://www.glycoepitope.jp/epitopes/EP0086"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":1043,"end":1048},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":20,"end":30},"obj":"Body_part"},{"id":"T2","span":{"begin":79,"end":89},"obj":"Body_part"},{"id":"T3","span":{"begin":1049,"end":1054},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000057"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000057"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000947"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":20,"end":30},"obj":"Cell"},{"id":"T2","span":{"begin":79,"end":89},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000057"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000057"}],"text":"Characterization of fibroblast growth factor 1 binding heparan sulfate domain.\nFibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1."}