PubMed:10460833 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":664,"end":671},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":817,"end":829},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T3","span":{"begin":1125,"end":1136},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T4","span":{"begin":1363,"end":1375},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":664,"end":671},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":817,"end":829},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":1125,"end":1136},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":1363,"end":1375},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"PMID_GLOBAL","denotations":[{"id":"T1","span":{"begin":343,"end":346},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"0009833"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":664,"end":671},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":817,"end":829},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T3","span":{"begin":1125,"end":1136},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T4","span":{"begin":1363,"end":1375},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":174,"end":188},"obj":"http://purl.obolibrary.org/obo/MAT_0000280"},{"id":"T2","span":{"begin":189,"end":193},"obj":"http://purl.obolibrary.org/obo/MAT_0000037"},{"id":"T3","span":{"begin":931,"end":939},"obj":"http://purl.obolibrary.org/obo/MAT_0000034"},{"id":"T4","span":{"begin":941,"end":946},"obj":"http://purl.obolibrary.org/obo/MAT_0000037"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

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of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":26,"end":55},"obj":"http://www.uniprot.org/uniprot/Q9NPG4"},{"id":"T2","span":{"begin":100,"end":129},"obj":"http://www.uniprot.org/uniprot/Q9NPG4"},{"id":"T3","span":{"begin":26,"end":55},"obj":"http://www.uniprot.org/uniprot/P33151"},{"id":"T4","span":{"begin":121,"end":133},"obj":"http://www.uniprot.org/uniprot/P33151"},{"id":"T5","span":{"begin":227,"end":238},"obj":"http://www.uniprot.org/uniprot/P33151"},{"id":"T6","span":{"begin":541,"end":552},"obj":"http://www.uniprot.org/uniprot/P33151"},{"id":"T7","span":{"begin":801,"end":812},"obj":"http://www.uniprot.org/uniprot/P33151"},{"id":"T8","span":{"begin":1095,"end":1106},"obj":"http://www.uniprot.org/uniprot/P33151"},{"id":"T9","span":{"begin":1220,"end":1231},"obj":"http://www.uniprot.org/uniprot/P33151"},{"id":"T10","span":{"begin":1397,"end":1408},"obj":"http://www.uniprot.org/uniprot/P33151"},{"id":"T11","span":{"begin":343,"end":346},"obj":"http://www.uniprot.org/uniprot/P20132"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":26,"end":55},"obj":"http://www.uniprot.org/uniprot/P55284"},{"id":"T2","span":{"begin":121,"end":133},"obj":"http://www.uniprot.org/uniprot/P55284"},{"id":"T3","span":{"begin":227,"end":238},"obj":"http://www.uniprot.org/uniprot/P55284"},{"id":"T4","span":{"begin":541,"end":552},"obj":"http://www.uniprot.org/uniprot/P55284"},{"id":"T5","span":{"begin":801,"end":812},"obj":"http://www.uniprot.org/uniprot/P55284"},{"id":"T6","span":{"begin":1095,"end":1106},"obj":"http://www.uniprot.org/uniprot/P55284"},{"id":"T7","span":{"begin":1220,"end":1231},"obj":"http://www.uniprot.org/uniprot/P55284"},{"id":"T8","span":{"begin":1397,"end":1408},"obj":"http://www.uniprot.org/uniprot/P55284"},{"id":"T9","span":{"begin":392,"end":395},"obj":"http://www.uniprot.org/uniprot/Q5YD48"},{"id":"T10","span":{"begin":392,"end":395},"obj":"http://www.uniprot.org/uniprot/Q9EQ00"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":206,"end":211},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T2","span":{"begin":906,"end":911},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T3","span":{"begin":1037,"end":1042},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":1195,"end":1200},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":64},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":65,"end":226},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":227,"end":398},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":399,"end":514},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":515,"end":685},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":686,"end":768},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":769,"end":984},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":985,"end":1165},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1166,"end":1342},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1343,"end":1422},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":64},"obj":"Sentence"},{"id":"T2","span":{"begin":65,"end":226},"obj":"Sentence"},{"id":"T3","span":{"begin":227,"end":514},"obj":"Sentence"},{"id":"T4","span":{"begin":515,"end":685},"obj":"Sentence"},{"id":"T5","span":{"begin":686,"end":768},"obj":"Sentence"},{"id":"T6","span":{"begin":769,"end":984},"obj":"Sentence"},{"id":"T7","span":{"begin":985,"end":1165},"obj":"Sentence"},{"id":"T8","span":{"begin":1166,"end":1342},"obj":"Sentence"},{"id":"T9","span":{"begin":1343,"end":1422},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":64},"obj":"Sentence"},{"id":"T2","span":{"begin":65,"end":226},"obj":"Sentence"},{"id":"T3","span":{"begin":227,"end":398},"obj":"Sentence"},{"id":"T4","span":{"begin":399,"end":514},"obj":"Sentence"},{"id":"T5","span":{"begin":515,"end":685},"obj":"Sentence"},{"id":"T6","span":{"begin":686,"end":768},"obj":"Sentence"},{"id":"T7","span":{"begin":769,"end":984},"obj":"Sentence"},{"id":"T8","span":{"begin":985,"end":1165},"obj":"Sentence"},{"id":"T9","span":{"begin":1166,"end":1342},"obj":"Sentence"},{"id":"T10","span":{"begin":1343,"end":1422},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":69,"end":82},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T2","span":{"begin":243,"end":256},"obj":"http://purl.obolibrary.org/obo/GO_0008152"},{"id":"T3","span":{"begin":363,"end":371},"obj":"http://purl.obolibrary.org/obo/GO_0007586"},{"id":"T4","span":{"begin":575,"end":585},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T5","span":{"begin":985,"end":987},"obj":"http://purl.obolibrary.org/obo/GO_0033968"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":206,"end":211},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":906,"end":911},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":1037,"end":1042},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":1195,"end":1200},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":1350,"end":1354},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":867,"end":890},"obj":"http://purl.obolibrary.org/obo/GO_0005911"},{"id":"T7","span":{"begin":1350,"end":1362},"obj":"http://purl.obolibrary.org/obo/GO_0009986"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":174,"end":188},"obj":"http://purl.obolibrary.org/obo/UBERON_0002331"},{"id":"T2","span":{"begin":189,"end":193},"obj":"http://purl.obolibrary.org/obo/UBERON_0001638"},{"id":"T3","span":{"begin":941,"end":946},"obj":"http://purl.obolibrary.org/obo/UBERON_0001638"},{"id":"T4","span":{"begin":921,"end":939},"obj":"http://purl.obolibrary.org/obo/UBERON_0001310"},{"id":"T5","span":{"begin":931,"end":939},"obj":"http://purl.obolibrary.org/obo/UBERON_0001637"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":174,"end":188},"obj":"http://purl.obolibrary.org/obo/MAT_0000280"},{"id":"T2","span":{"begin":189,"end":193},"obj":"http://purl.obolibrary.org/obo/MAT_0000037"},{"id":"T3","span":{"begin":931,"end":939},"obj":"http://purl.obolibrary.org/obo/MAT_0000034"},{"id":"T4","span":{"begin":941,"end":946},"obj":"http://purl.obolibrary.org/obo/MAT_0000037"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":659,"end":671},"obj":"http://rdf.glycoinfo.org/glycan/G00028MO"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":1297,"end":1309},"obj":"http://purl.obolibrary.org/obo/UBERON_0000062"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1409,"end":1421},"obj":"http://purl.obolibrary.org/obo/UBERON_0000062"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":174,"end":188},"obj":"http://purl.obolibrary.org/obo/UBERON_0002331"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":189,"end":193},"obj":"http://purl.obolibrary.org/obo/UBERON_0001638"},{"id":"PD-UBERON-AE-B_T5","span":{"begin":941,"end":946},"obj":"http://purl.obolibrary.org/obo/UBERON_0001638"},{"id":"PD-UBERON-AE-B_T6","span":{"begin":921,"end":939},"obj":"http://purl.obolibrary.org/obo/UBERON_0001310"},{"id":"PD-UBERON-AE-B_T7","span":{"begin":931,"end":939},"obj":"http://purl.obolibrary.org/obo/UBERON_0001637"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":985,"end":987},"obj":"https://acgg.asia/db/lfdb/LfDB0227"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":789,"end":797},"obj":"id"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G41652MJ\""},{"id":"GlycanIUPAC_T2","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G20761YC\""},{"id":"GlycanIUPAC_T3","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G19807HM\""},{"id":"GlycanIUPAC_T4","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G20351TE\""},{"id":"GlycanIUPAC_T5","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G71957MR\""},{"id":"GlycanIUPAC_T6","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G59040AE\""},{"id":"GlycanIUPAC_T7","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G14987PW\""},{"id":"GlycanIUPAC_T8","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G95064PC\""},{"id":"GlycanIUPAC_T9","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G39143AQ\""},{"id":"GlycanIUPAC_T10","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G65149OO\""},{"id":"GlycanIUPAC_T11","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G02766SY\""},{"id":"GlycanIUPAC_T12","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G26019KJ\""},{"id":"GlycanIUPAC_T13","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G36429CZ\""},{"id":"GlycanIUPAC_T14","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G89633TP\""},{"id":"GlycanIUPAC_T15","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G28494FO\""},{"id":"GlycanIUPAC_T16","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G06219CP\""},{"id":"GlycanIUPAC_T17","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G44237SM\""},{"id":"GlycanIUPAC_T18","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G57948RL\""},{"id":"GlycanIUPAC_T19","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G64016DN\""},{"id":"GlycanIUPAC_T20","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G14536PC\""},{"id":"GlycanIUPAC_T21","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G14356FW\""},{"id":"GlycanIUPAC_T22","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G34565UO\""},{"id":"GlycanIUPAC_T23","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G67124MW\""},{"id":"GlycanIUPAC_T24","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G71457ZU\""},{"id":"GlycanIUPAC_T25","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G55228VZ\""},{"id":"GlycanIUPAC_T26","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G31034MJ\""},{"id":"GlycanIUPAC_T27","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G25776IP\""},{"id":"GlycanIUPAC_T28","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G64442BV\""},{"id":"GlycanIUPAC_T29","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G57018LE\""},{"id":"GlycanIUPAC_T30","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G61761GX\""},{"id":"GlycanIUPAC_T31","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G76318UX\""},{"id":"GlycanIUPAC_T32","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G61906ER\""},{"id":"GlycanIUPAC_T33","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G68723GR\""},{"id":"GlycanIUPAC_T34","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G19540LE\""},{"id":"GlycanIUPAC_T35","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G74944PO\""},{"id":"GlycanIUPAC_T36","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G89489ZJ\""},{"id":"GlycanIUPAC_T37","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G04434YU\""},{"id":"GlycanIUPAC_T38","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G21450PB\""},{"id":"GlycanIUPAC_T39","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G93629QY\""},{"id":"GlycanIUPAC_T40","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G02603TR\""},{"id":"GlycanIUPAC_T41","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G40280JP\""},{"id":"GlycanIUPAC_T42","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G95259IC\""},{"id":"GlycanIUPAC_T43","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G26900FE\""},{"id":"GlycanIUPAC_T44","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G21346KK\""},{"id":"GlycanIUPAC_T45","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G62509FF\""},{"id":"GlycanIUPAC_T46","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G83932AK\""},{"id":"GlycanIUPAC_T47","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G96978IB\""},{"id":"GlycanIUPAC_T48","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G34275DN\""},{"id":"GlycanIUPAC_T49","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G07071JF\""},{"id":"GlycanIUPAC_T50","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G80639QD\""},{"id":"GlycanIUPAC_T51","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G99460PJ\""},{"id":"GlycanIUPAC_T52","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G22024BZ\""},{"id":"GlycanIUPAC_T53","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G74097ZY\""},{"id":"GlycanIUPAC_T54","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G84439YP\""},{"id":"GlycanIUPAC_T55","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G52207WQ\""},{"id":"GlycanIUPAC_T56","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G90695MS\""},{"id":"GlycanIUPAC_T57","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G50398QX\""},{"id":"GlycanIUPAC_T58","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G12166ZT\""},{"id":"GlycanIUPAC_T59","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G48368BR\""},{"id":"GlycanIUPAC_T60","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G57407RW\""},{"id":"GlycanIUPAC_T61","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G00386TY\""},{"id":"GlycanIUPAC_T62","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G18723JK\""},{"id":"GlycanIUPAC_T63","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G93757OR\""},{"id":"GlycanIUPAC_T64","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G29006SI\""},{"id":"GlycanIUPAC_T65","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G03099OQ\""},{"id":"GlycanIUPAC_T66","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G53739OW\""},{"id":"GlycanIUPAC_T67","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G70440ZO\""},{"id":"GlycanIUPAC_T68","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G29951RR\""},{"id":"GlycanIUPAC_T69","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G58402TI\""},{"id":"GlycanIUPAC_T70","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G39875TP\""},{"id":"GlycanIUPAC_T71","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G83439QV\""},{"id":"GlycanIUPAC_T72","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G41762RC\""},{"id":"GlycanIUPAC_T73","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G91604UI\""},{"id":"GlycanIUPAC_T74","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G88447WE\""},{"id":"GlycanIUPAC_T75","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G93634BS\""},{"id":"GlycanIUPAC_T76","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G02587BH\""},{"id":"GlycanIUPAC_T77","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G43511MX\""},{"id":"GlycanIUPAC_T78","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G64958DH\""},{"id":"GlycanIUPAC_T79","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G30384TR\""},{"id":"GlycanIUPAC_T80","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G15624EX\""},{"id":"GlycanIUPAC_T81","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G22706ST\""},{"id":"GlycanIUPAC_T82","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G57408PI\""},{"id":"GlycanIUPAC_T83","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G86403XX\""},{"id":"GlycanIUPAC_T84","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G78043YB\""},{"id":"GlycanIUPAC_T85","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G18952JK\""},{"id":"GlycanIUPAC_T86","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G49020ND\""},{"id":"GlycanIUPAC_T87","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G63590YW\""},{"id":"GlycanIUPAC_T88","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G22793KS\""},{"id":"GlycanIUPAC_T89","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G64134SS\""},{"id":"GlycanIUPAC_T90","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G17338HY\""},{"id":"GlycanIUPAC_T91","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G99745XF\""},{"id":"GlycanIUPAC_T92","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G27782HN\""},{"id":"GlycanIUPAC_T93","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G57496DC\""},{"id":"GlycanIUPAC_T94","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G93169WB\""},{"id":"GlycanIUPAC_T95","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G05518TD\""},{"id":"GlycanIUPAC_T96","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G62603DN\""},{"id":"GlycanIUPAC_T97","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G59574FS\""},{"id":"GlycanIUPAC_T98","span":{"begin":1121,"end":1124},"obj":"\"http://rdf.glycoinfo.org/glycan/G47567WC\""}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":20,"end":25},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":94,"end":99},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":168,"end":173},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":915,"end":920},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":174,"end":188},"obj":"Body_part"},{"id":"T2","span":{"begin":189,"end":211},"obj":"Body_part"},{"id":"T3","span":{"begin":867,"end":890},"obj":"Body_part"},{"id":"T4","span":{"begin":894,"end":911},"obj":"Body_part"},{"id":"T5","span":{"begin":921,"end":939},"obj":"Body_part"},{"id":"T6","span":{"begin":1025,"end":1042},"obj":"Body_part"},{"id":"T7","span":{"begin":1155,"end":1164},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002331"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0002543"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/GO_0005911"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000115"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0001310"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000115"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0007651"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":174,"end":188},"obj":"Body_part"},{"id":"T2","span":{"begin":189,"end":193},"obj":"Body_part"},{"id":"T3","span":{"begin":931,"end":939},"obj":"Body_part"},{"id":"T4","span":{"begin":941,"end":946},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000280"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000037"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000034"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000037"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":189,"end":211},"obj":"Cell"},{"id":"T2","span":{"begin":894,"end":911},"obj":"Cell"},{"id":"T3","span":{"begin":1025,"end":1042},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0002543"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000115"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000115"}],"text":"Characterization of human vascular endothelial cadherin glycans.\nThe glycosylation pattern of human vascular endothelial cadherin (VE-cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d-[6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS-PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization."}