PubMed:22547138 JSON TXT

Annnotations TAB JSON ListView MergeView

GlyCosmos6-UBERON

{"project":"GlyCosmos6-UBERON","denotations":[{"id":"T1","span":{"begin":49,"end":53},"obj":"Body_part"},{"id":"T2","span":{"begin":379,"end":383},"obj":"Body_part"},{"id":"T3","span":{"begin":970,"end":975},"obj":"Body_part"},{"id":"T4","span":{"begin":1041,"end":1045},"obj":"Body_part"},{"id":"T5","span":{"begin":1348,"end":1353},"obj":"Body_part"},{"id":"T6","span":{"begin":1499,"end":1504},"obj":"Body_part"},{"id":"T7","span":{"begin":1713,"end":1717},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0035924"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL_0000000"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

Glycan-Motif

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":1348,"end":1361},"obj":"https://glytoucan.org/Structures/Glycans/G17108EX"},{"id":"T2","span":{"begin":1348,"end":1361},"obj":"https://glytoucan.org/Structures/Glycans/G58507AZ"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

GlyCosmos6-Glycan-Motif-Image

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":1348,"end":1361},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G58507AZ"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G17108EX"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1348,"end":1361},"obj":"https://glytoucan.org/Structures/Glycans/G17108EX"},{"id":"T2","span":{"begin":1348,"end":1361},"obj":"https://glytoucan.org/Structures/Glycans/G58507AZ"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":970,"end":975},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T2","span":{"begin":970,"end":975},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T3","span":{"begin":1348,"end":1353},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T4","span":{"begin":1348,"end":1353},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

GlyCosmos6-CLO

{"project":"GlyCosmos6-CLO","denotations":[{"id":"T1","span":{"begin":49,"end":53},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":377,"end":383},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T3","span":{"begin":379,"end":383},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":587,"end":591},"obj":"http://purl.obolibrary.org/obo/CLO_0008734"},{"id":"T5","span":{"begin":587,"end":591},"obj":"http://purl.obolibrary.org/obo/CLO_0051728"},{"id":"T6","span":{"begin":592,"end":597},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T7","span":{"begin":1041,"end":1045},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T8","span":{"begin":1713,"end":1717},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":60,"end":65},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":476,"end":481},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1836,"end":1841},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"NCBItxid:9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"NCBItxid:9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"NCBItxid:9606"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

GlycoBiology-FMA

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":247,"end":252},"obj":"FMAID:146304"},{"id":"_T2","span":{"begin":247,"end":252},"obj":"FMAID:50596"},{"id":"_T3","span":{"begin":414,"end":429},"obj":"FMAID:196776"},{"id":"_T4","span":{"begin":414,"end":429},"obj":"FMAID:82782"},{"id":"_T5","span":{"begin":459,"end":465},"obj":"FMAID:178661"},{"id":"_T6","span":{"begin":592,"end":597},"obj":"FMAID:169002"},{"id":"_T7","span":{"begin":592,"end":597},"obj":"FMAID:68646"},{"id":"_T8","span":{"begin":882,"end":895},"obj":"FMAID:82744"},{"id":"_T9","span":{"begin":882,"end":895},"obj":"FMAID:196733"},{"id":"_T10","span":{"begin":970,"end":975},"obj":"FMAID:256053"},{"id":"_T11","span":{"begin":1054,"end":1059},"obj":"FMAID:85813"},{"id":"_T12","span":{"begin":1170,"end":1182},"obj":"FMAID:82744"},{"id":"_T13","span":{"begin":1170,"end":1182},"obj":"FMAID:196733"},{"id":"_T14","span":{"begin":1348,"end":1353},"obj":"FMAID:256053"},{"id":"_T15","span":{"begin":1434,"end":1446},"obj":"FMAID:197276"},{"id":"_T16","span":{"begin":1434,"end":1446},"obj":"FMAID:82737"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":85,"end":95},"obj":"http://www.uniprot.org/uniprot/P56470"},{"id":"T2","span":{"begin":560,"end":565},"obj":"http://www.uniprot.org/uniprot/P56470"},{"id":"T3","span":{"begin":1154,"end":1159},"obj":"http://www.uniprot.org/uniprot/P56470"},{"id":"T4","span":{"begin":1293,"end":1298},"obj":"http://www.uniprot.org/uniprot/P56470"},{"id":"T5","span":{"begin":1309,"end":1314},"obj":"http://www.uniprot.org/uniprot/P56470"},{"id":"T6","span":{"begin":1477,"end":1482},"obj":"http://www.uniprot.org/uniprot/P56470"},{"id":"T7","span":{"begin":488,"end":493},"obj":"http://www.uniprot.org/uniprot/P09382"},{"id":"T8","span":{"begin":687,"end":689},"obj":"http://www.uniprot.org/uniprot/Q8SNA0"},{"id":"T9","span":{"begin":1199,"end":1201},"obj":"http://www.uniprot.org/uniprot/Q8SNA0"},{"id":"T10","span":{"begin":982,"end":985},"obj":"http://www.uniprot.org/uniprot/Q13686"},{"id":"T11","span":{"begin":1525,"end":1528},"obj":"http://www.uniprot.org/uniprot/Q13686"},{"id":"T12","span":{"begin":1132,"end":1137},"obj":"http://www.uniprot.org/uniprot/Q9H585"},{"id":"T13","span":{"begin":1143,"end":1157},"obj":"http://www.uniprot.org/uniprot/Q9NQ58"},{"id":"T14","span":{"begin":1379,"end":1384},"obj":"http://www.uniprot.org/uniprot/Q9NQ58"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":85,"end":95},"obj":"http://www.uniprot.org/uniprot/Q8K419"},{"id":"T2","span":{"begin":560,"end":565},"obj":"http://www.uniprot.org/uniprot/Q8K419"},{"id":"T3","span":{"begin":1154,"end":1159},"obj":"http://www.uniprot.org/uniprot/Q8K419"},{"id":"T4","span":{"begin":1293,"end":1298},"obj":"http://www.uniprot.org/uniprot/Q8K419"},{"id":"T5","span":{"begin":1309,"end":1314},"obj":"http://www.uniprot.org/uniprot/Q8K419"},{"id":"T6","span":{"begin":1477,"end":1482},"obj":"http://www.uniprot.org/uniprot/Q8K419"},{"id":"T7","span":{"begin":146,"end":150},"obj":"http://www.uniprot.org/uniprot/P47212"},{"id":"T8","span":{"begin":482,"end":486},"obj":"http://www.uniprot.org/uniprot/P47212"},{"id":"T9","span":{"begin":653,"end":657},"obj":"http://www.uniprot.org/uniprot/P47212"},{"id":"T10","span":{"begin":836,"end":840},"obj":"http://www.uniprot.org/uniprot/P47212"},{"id":"T11","span":{"begin":1724,"end":1728},"obj":"http://www.uniprot.org/uniprot/P47212"},{"id":"T12","span":{"begin":1842,"end":1846},"obj":"http://www.uniprot.org/uniprot/P47212"},{"id":"T13","span":{"begin":185,"end":188},"obj":"http://www.uniprot.org/uniprot/Q62225"},{"id":"T14","span":{"begin":488,"end":493},"obj":"http://www.uniprot.org/uniprot/P16045"},{"id":"T15","span":{"begin":687,"end":689},"obj":"http://www.uniprot.org/uniprot/P04441"},{"id":"T16","span":{"begin":1199,"end":1201},"obj":"http://www.uniprot.org/uniprot/P04441"},{"id":"T17","span":{"begin":1132,"end":1137},"obj":"http://www.uniprot.org/uniprot/Q9JL15"},{"id":"T18","span":{"begin":1143,"end":1157},"obj":"http://www.uniprot.org/uniprot/O08573"},{"id":"T19","span":{"begin":1379,"end":1384},"obj":"http://www.uniprot.org/uniprot/O08573"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":185,"end":188},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/245896"},{"id":"T2","span":{"begin":320,"end":326},"obj":"http://purl.bioontology.org/ontology/STY/T051"},{"id":"T3","span":{"begin":592,"end":597},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":976,"end":981},"obj":"http://purl.bioontology.org/ontology/STY/T096"},{"id":"T5","span":{"begin":1354,"end":1359},"obj":"http://purl.bioontology.org/ontology/STY/T096"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":117,"end":123},"obj":"http://purl.obolibrary.org/obo/GO_0040007"},{"id":"T2","span":{"begin":855,"end":863},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T3","span":{"begin":871,"end":881},"obj":"http://purl.obolibrary.org/obo/GO_0097503"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":253,"end":260},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":691,"end":698},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":1215,"end":1222},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T4","span":{"begin":253,"end":260},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T5","span":{"begin":691,"end":698},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T6","span":{"begin":1215,"end":1222},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T7","span":{"begin":253,"end":260},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T8","span":{"begin":691,"end":698},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T9","span":{"begin":1215,"end":1222},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T10","span":{"begin":253,"end":260},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T11","span":{"begin":691,"end":698},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12","span":{"begin":1215,"end":1222},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T13","span":{"begin":702,"end":709},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T14","span":{"begin":1021,"end":1028},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":49,"end":53},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":379,"end":383},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":1041,"end":1045},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":592,"end":597},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":49,"end":59},"obj":"http://purl.obolibrary.org/obo/GO_0009986"},{"id":"T6","span":{"begin":1713,"end":1723},"obj":"http://purl.obolibrary.org/obo/GO_0009986"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

UBERON-AE

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":970,"end":975},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"T2","span":{"begin":1348,"end":1353},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

Allie

{"project":"Allie","denotations":[{"id":"SS1_22547138_1_0","span":{"begin":135,"end":144},"obj":"expanded"},{"id":"SS2_22547138_1_0","span":{"begin":146,"end":150},"obj":"abbr"},{"id":"SS1_22547138_5_0","span":{"begin":1434,"end":1466},"obj":"expanded"},{"id":"SS2_22547138_5_0","span":{"begin":1468,"end":1472},"obj":"abbr"}],"relations":[{"id":"AE1_22547138_1_0","pred":"abbreviatedTo","subj":"SS1_22547138_1_0","obj":"SS2_22547138_1_0"},{"id":"AE1_22547138_5_0","pred":"abbreviatedTo","subj":"SS1_22547138_5_0","obj":"SS2_22547138_5_0"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

GlycoBiology-MAT

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":970,"end":975},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T2","span":{"begin":970,"end":975},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T3","span":{"begin":1348,"end":1353},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T4","span":{"begin":1348,"end":1353},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":107},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":108,"end":261},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":262,"end":502},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":503,"end":1072},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":1073,"end":1409},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1410,"end":1590},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1591,"end":1729},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1730,"end":1847},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":107},"obj":"Sentence"},{"id":"T2","span":{"begin":108,"end":261},"obj":"Sentence"},{"id":"T3","span":{"begin":262,"end":502},"obj":"Sentence"},{"id":"T4","span":{"begin":503,"end":1072},"obj":"Sentence"},{"id":"T5","span":{"begin":1073,"end":1409},"obj":"Sentence"},{"id":"T6","span":{"begin":1410,"end":1590},"obj":"Sentence"},{"id":"T7","span":{"begin":1591,"end":1729},"obj":"Sentence"},{"id":"T8","span":{"begin":1730,"end":1847},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":107},"obj":"Sentence"},{"id":"T2","span":{"begin":108,"end":261},"obj":"Sentence"},{"id":"T3","span":{"begin":262,"end":502},"obj":"Sentence"},{"id":"T4","span":{"begin":503,"end":1072},"obj":"Sentence"},{"id":"T5","span":{"begin":1073,"end":1409},"obj":"Sentence"},{"id":"T6","span":{"begin":1410,"end":1590},"obj":"Sentence"},{"id":"T7","span":{"begin":1591,"end":1729},"obj":"Sentence"},{"id":"T8","span":{"begin":1730,"end":1847},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

GlyTouCan-IUPAC

GlycoBiology-Motifs

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":970,"end":981},"obj":"http://rdf.glycoinfo.org/glycan/G00066MO"},{"id":"T2","span":{"begin":1348,"end":1359},"obj":"http://rdf.glycoinfo.org/glycan/G00066MO"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

Lectin

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":85,"end":95},"obj":"https://acgg.asia/db/lfdb/LfDB0272"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}

performance-test

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":970,"end":975},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1348,"end":1353},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"Comparative study of the glycan specificities of cell-bound human tandem-repeat-type galectin-4, -8 and -9.\nAdhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galβ1-3GlcNAc or Galβ1-3GalNAc as basic motifs was commonly better than that to canonical Galβ1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galβ1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals."}