PubMed:10570220 JSON TXT

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GlyCosmos15-Species

{"project":"GlyCosmos15-Species","denotations":[{"id":"68","span":{"begin":1458,"end":1466},"obj":"Species"},{"id":"73","span":{"begin":1661,"end":1666},"obj":"Species"}],"attributes":[{"id":"A73","pred":"db_id","subj":"73","obj":"11676"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

Glycan-Motif

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":411,"end":418},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T2","span":{"begin":411,"end":418},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T3","span":{"begin":422,"end":433},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T4","span":{"begin":759,"end":766},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T5","span":{"begin":759,"end":766},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T6","span":{"begin":771,"end":782},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T7","span":{"begin":1035,"end":1042},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T8","span":{"begin":1035,"end":1042},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T9","span":{"begin":1046,"end":1057},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T10","span":{"begin":1103,"end":1110},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T11","span":{"begin":1236,"end":1243},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T12","span":{"begin":1236,"end":1243},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T13","span":{"begin":1256,"end":1263},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T14","span":{"begin":1367,"end":1374},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T15","span":{"begin":1367,"end":1374},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T16","span":{"begin":1376,"end":1387},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T17","span":{"begin":1588,"end":1595},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T18","span":{"begin":1588,"end":1595},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

GlyCosmos6-Glycan-Motif-Image

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":411,"end":418},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T2","span":{"begin":411,"end":418},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T3","span":{"begin":422,"end":433},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T4","span":{"begin":759,"end":766},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T5","span":{"begin":759,"end":766},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T6","span":{"begin":771,"end":782},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T7","span":{"begin":1035,"end":1042},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T8","span":{"begin":1035,"end":1042},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T9","span":{"begin":1046,"end":1057},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T10","span":{"begin":1103,"end":1110},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T11","span":{"begin":1236,"end":1243},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T12","span":{"begin":1236,"end":1243},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T13","span":{"begin":1256,"end":1263},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T14","span":{"begin":1367,"end":1374},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T15","span":{"begin":1367,"end":1374},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"},{"id":"T16","span":{"begin":1376,"end":1387},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T17","span":{"begin":1588,"end":1595},"obj":"https://glytoucan.org/Structures/Glycans/G00021MO"},{"id":"T18","span":{"begin":1588,"end":1595},"obj":"https://glytoucan.org/Structures/Glycans/G54161DR"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

Glycosmos6-GlycoEpitope

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":422,"end":433},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"T2","span":{"begin":771,"end":782},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"T3","span":{"begin":1046,"end":1057},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"T4","span":{"begin":1376,"end":1387},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

GlycoBiology-FMA

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":225,"end":228},"obj":"http://www.uniprot.org/uniprot/P01730"},{"id":"T2","span":{"begin":324,"end":338},"obj":"http://www.uniprot.org/uniprot/P34059"},{"id":"T3","span":{"begin":724,"end":738},"obj":"http://www.uniprot.org/uniprot/P34059"},{"id":"T4","span":{"begin":1439,"end":1444},"obj":"http://www.uniprot.org/uniprot/Q14624"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":225,"end":228},"obj":"http://www.uniprot.org/uniprot/P06332"},{"id":"T2","span":{"begin":324,"end":338},"obj":"http://www.uniprot.org/uniprot/Q571E4"},{"id":"T3","span":{"begin":724,"end":738},"obj":"http://www.uniprot.org/uniprot/Q571E4"},{"id":"T4","span":{"begin":1667,"end":1670},"obj":"http://www.uniprot.org/uniprot/P11370"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":262,"end":267},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T2","span":{"begin":297,"end":302},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T3","span":{"begin":505,"end":510},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":676,"end":681},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T5","span":{"begin":858,"end":863},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T6","span":{"begin":975,"end":980},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T7","span":{"begin":1183,"end":1188},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

sentences

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":324,"end":338},"obj":"http://purl.obolibrary.org/obo/GO_0043890"},{"id":"T2","span":{"begin":724,"end":738},"obj":"http://purl.obolibrary.org/obo/GO_0043890"},{"id":"T3","span":{"begin":434,"end":441},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T4","span":{"begin":783,"end":790},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T5","span":{"begin":1058,"end":1065},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T6","span":{"begin":1388,"end":1395},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T7","span":{"begin":1521,"end":1533},"obj":"http://purl.obolibrary.org/obo/GO_0097502"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

GO-MF

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":59,"end":63},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":111,"end":115},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":189,"end":193},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":262,"end":267},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":297,"end":302},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":505,"end":510},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T7","span":{"begin":676,"end":681},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T8","span":{"begin":858,"end":863},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T9","span":{"begin":975,"end":980},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T10","span":{"begin":1183,"end":1188},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T11","span":{"begin":111,"end":123},"obj":"http://purl.obolibrary.org/obo/GO_0009986"},{"id":"T12","span":{"begin":1725,"end":1737},"obj":"http://purl.obolibrary.org/obo/GO_0009986"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

GlycoBiology-Motifs

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":411,"end":418},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T2","span":{"begin":759,"end":766},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T3","span":{"begin":1035,"end":1042},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T4","span":{"begin":1236,"end":1243},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T5","span":{"begin":1367,"end":1374},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T6","span":{"begin":1588,"end":1595},"obj":"http://rdf.glycoinfo.org/glycan/G54161DR"},{"id":"T7","span":{"begin":422,"end":433},"obj":"http://rdf.glycoinfo.org/glycan/G00018MO"},{"id":"T8","span":{"begin":771,"end":782},"obj":"http://rdf.glycoinfo.org/glycan/G00018MO"},{"id":"T9","span":{"begin":1046,"end":1057},"obj":"http://rdf.glycoinfo.org/glycan/G00018MO"},{"id":"T10","span":{"begin":1376,"end":1387},"obj":"http://rdf.glycoinfo.org/glycan/G00018MO"},{"id":"T11","span":{"begin":422,"end":441},"obj":"http://rdf.glycoinfo.org/glycan/G00018MO"},{"id":"T12","span":{"begin":771,"end":790},"obj":"http://rdf.glycoinfo.org/glycan/G00018MO"},{"id":"T13","span":{"begin":1046,"end":1065},"obj":"http://rdf.glycoinfo.org/glycan/G00018MO"},{"id":"T14","span":{"begin":1376,"end":1395},"obj":"http://rdf.glycoinfo.org/glycan/G00018MO"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

GlycoBiology-Epitope

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":422,"end":433},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":771,"end":782},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":1046,"end":1057},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"PD-GlycoEpitope-B_T4","span":{"begin":1376,"end":1387},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"PD-GlycoEpitope-B_T5","span":{"begin":517,"end":519},"obj":"http://www.glycoepitope.jp/epitopes/AN0785"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

GlyCosmos15-Glycan

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":422,"end":433},"obj":"Glycan"},{"id":"T2","span":{"begin":771,"end":782},"obj":"Glycan"},{"id":"T3","span":{"begin":1046,"end":1057},"obj":"Glycan"},{"id":"T4","span":{"begin":1376,"end":1387},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A5","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A6","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A7","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

Glycan-GlyCosmos

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":422,"end":433},"obj":"Glycan"},{"id":"T2","span":{"begin":771,"end":782},"obj":"Glycan"},{"id":"T3","span":{"begin":1046,"end":1057},"obj":"Glycan"},{"id":"T4","span":{"begin":1376,"end":1387},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A5","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A6","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A7","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

GlyCosmos-GlycoEpitope

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":422,"end":433},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":771,"end":782},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":1046,"end":1057},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":1376,"end":1387},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0081"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

GlyCosmos15-CL

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":51,"end":63},"obj":"Cell"},{"id":"T2","span":{"begin":181,"end":193},"obj":"Cell"},{"id":"T3","span":{"begin":247,"end":256},"obj":"Cell"},{"id":"T5","span":{"begin":658,"end":681},"obj":"Cell"},{"id":"T6","span":{"begin":1165,"end":1188},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000499"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000499"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000576"},{"id":"A4","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0001054"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000386"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0000386"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

GlyCosmos15-UBERON

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":51,"end":63},"obj":"Body_part"},{"id":"T2","span":{"begin":181,"end":193},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000499"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000499"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

GlyCosmos15-GlycoEpitope

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":422,"end":433},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":771,"end":782},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":1046,"end":1057},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":1376,"end":1387},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0081"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

GlyCosmos15-Sentences

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":92},"obj":"Sentence"},{"id":"T2","span":{"begin":93,"end":402},"obj":"Sentence"},{"id":"T3","span":{"begin":403,"end":587},"obj":"Sentence"},{"id":"T4","span":{"begin":588,"end":682},"obj":"Sentence"},{"id":"T5","span":{"begin":683,"end":919},"obj":"Sentence"},{"id":"T6","span":{"begin":920,"end":991},"obj":"Sentence"},{"id":"T7","span":{"begin":992,"end":1078},"obj":"Sentence"},{"id":"T8","span":{"begin":1079,"end":1189},"obj":"Sentence"},{"id":"T9","span":{"begin":1190,"end":1408},"obj":"Sentence"},{"id":"T10","span":{"begin":1409,"end":1596},"obj":"Sentence"},{"id":"T11","span":{"begin":1597,"end":1738},"obj":"Sentence"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

GlyCosmos15-FMA

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":111,"end":123},"obj":"Body_part"},{"id":"T2","span":{"begin":247,"end":256},"obj":"Body_part"},{"id":"T3","span":{"begin":1458,"end":1461},"obj":"Body_part"},{"id":"T4","span":{"begin":1661,"end":1664},"obj":"Body_part"},{"id":"T5","span":{"begin":1725,"end":1737},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:67653"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:62864"},{"id":"A3","pred":"db_id","subj":"T3","obj":"FMA:278683"},{"id":"A4","pred":"db_id","subj":"T4","obj":"FMA:278683"},{"id":"A5","pred":"db_id","subj":"T5","obj":"FMA:67653"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":51,"end":63},"obj":"Body_part"},{"id":"T2","span":{"begin":181,"end":193},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000499"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000499"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}

CL-cell

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":51,"end":63},"obj":"Cell"},{"id":"T2","span":{"begin":181,"end":193},"obj":"Cell"},{"id":"T3","span":{"begin":247,"end":256},"obj":"Cell"},{"id":"T5","span":{"begin":658,"end":681},"obj":"Cell"},{"id":"T6","span":{"begin":1165,"end":1188},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000499"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000499"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000576"},{"id":"A4","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0001054"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000386"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0000386"}],"text":"Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha.\nWe show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha binding to the cells by 45-52% and 42-56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1alpha attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha binding to the cells by 30-33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1alpha attachment to the cells. Accordingly, SDF-1alpha specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1alpha can interact with GAGs and glycans at the cell surface."}