PubMed:8872113 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":372,"end":382},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":456,"end":462},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":635,"end":645},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":694,"end":704},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":828,"end":839},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":1279,"end":1290},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G57321FI"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G57321FI"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":128},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":129,"end":330},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":331,"end":340},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":341,"end":660},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":661,"end":729},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":730,"end":856},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":857,"end":977},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":978,"end":1052},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1053,"end":1121},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1122,"end":1189},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1190,"end":1455},"obj":"Sentence"},{"id":"TextSentencer_T12","span":{"begin":1456,"end":1531},"obj":"Sentence"},{"id":"TextSentencer_T13","span":{"begin":1532,"end":1655},"obj":"Sentence"},{"id":"TextSentencer_T14","span":{"begin":1656,"end":1851},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":128},"obj":"Sentence"},{"id":"T2","span":{"begin":129,"end":330},"obj":"Sentence"},{"id":"T3","span":{"begin":331,"end":340},"obj":"Sentence"},{"id":"T4","span":{"begin":341,"end":660},"obj":"Sentence"},{"id":"T5","span":{"begin":661,"end":729},"obj":"Sentence"},{"id":"T6","span":{"begin":730,"end":856},"obj":"Sentence"},{"id":"T7","span":{"begin":857,"end":977},"obj":"Sentence"},{"id":"T8","span":{"begin":978,"end":1052},"obj":"Sentence"},{"id":"T9","span":{"begin":1053,"end":1121},"obj":"Sentence"},{"id":"T10","span":{"begin":1122,"end":1189},"obj":"Sentence"},{"id":"T11","span":{"begin":1190,"end":1455},"obj":"Sentence"},{"id":"T12","span":{"begin":1456,"end":1531},"obj":"Sentence"},{"id":"T13","span":{"begin":1532,"end":1655},"obj":"Sentence"},{"id":"T14","span":{"begin":1656,"end":1851},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":372,"end":382},"obj":"https://glytoucan.org/Structures/Glycans/G57321FI"},{"id":"T2","span":{"begin":456,"end":462},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T3","span":{"begin":635,"end":645},"obj":"https://glytoucan.org/Structures/Glycans/G57321FI"},{"id":"T4","span":{"begin":694,"end":704},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T5","span":{"begin":828,"end":839},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T6","span":{"begin":1279,"end":1290},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":372,"end":382},"obj":"http://www.glycoepitope.jp/epitopes/EP0021"},{"id":"T2","span":{"begin":635,"end":645},"obj":"http://www.glycoepitope.jp/epitopes/EP0021"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":150,"end":181},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0010381"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":372,"end":382},"obj":"Glycan"},{"id":"T2","span":{"begin":383,"end":389},"obj":"Glycan"},{"id":"T3","span":{"begin":456,"end":462},"obj":"Glycan"},{"id":"T4","span":{"begin":635,"end":645},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G57321FI"},{"id":"A5","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G57321FI"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A6","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A7","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G57321FI"},{"id":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G57321FI"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":372,"end":382},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":635,"end":645},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0021"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0021"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":150,"end":181},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0010381"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":30,"end":35},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":254,"end":261},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":857,"end":876},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":878,"end":881},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":884,"end":901},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":903,"end":906},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":909,"end":921},"obj":"OrganismTaxon"},{"id":"T8","span":{"begin":923,"end":926},"obj":"OrganismTaxon"},{"id":"T9","span":{"begin":929,"end":943},"obj":"OrganismTaxon"},{"id":"T10","span":{"begin":945,"end":948},"obj":"OrganismTaxon"},{"id":"T11","span":{"begin":954,"end":970},"obj":"OrganismTaxon"},{"id":"T12","span":{"begin":1004,"end":1007},"obj":"OrganismTaxon"},{"id":"T13","span":{"begin":1012,"end":1015},"obj":"OrganismTaxon"},{"id":"T14","span":{"begin":1058,"end":1061},"obj":"OrganismTaxon"},{"id":"T15","span":{"begin":1066,"end":1069},"obj":"OrganismTaxon"},{"id":"T16","span":{"begin":1133,"end":1136},"obj":"OrganismTaxon"},{"id":"T17","span":{"begin":1484,"end":1489},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"3567"},{"id":"A4","pred":"db_id","subj":"T4","obj":"3567"},{"id":"A5","pred":"db_id","subj":"T5","obj":"37501"},{"id":"A6","pred":"db_id","subj":"T6","obj":"37501"},{"id":"A7","pred":"db_id","subj":"T7","obj":"36461"},{"id":"A8","pred":"db_id","subj":"T8","obj":"36461"},{"id":"A9","pred":"db_id","subj":"T9","obj":"4202"},{"id":"A10","pred":"db_id","subj":"T10","obj":"4202"},{"id":"A11","pred":"db_id","subj":"T11","obj":"4565"},{"id":"A12","pred":"db_id","subj":"T12","obj":"37501"},{"id":"A13","pred":"db_id","subj":"T13","obj":"4202"},{"id":"A14","pred":"db_id","subj":"T14","obj":"36461"},{"id":"A15","pred":"db_id","subj":"T15","obj":"3567"},{"id":"A16","pred":"db_id","subj":"T16","obj":"3567"},{"id":"A17","pred":"db_id","subj":"T17","obj":"9606"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":36,"end":48},"obj":"Cell"},{"id":"T2","span":{"begin":38,"end":48},"obj":"Cell"},{"id":"T3","span":{"begin":205,"end":217},"obj":"Cell"},{"id":"T4","span":{"begin":207,"end":217},"obj":"Cell"},{"id":"T5","span":{"begin":345,"end":358},"obj":"Cell"},{"id":"T6","span":{"begin":668,"end":681},"obj":"Cell"},{"id":"T7","span":{"begin":1712,"end":1725},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000542"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000542"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A7","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000084"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":36,"end":48},"obj":"Body_part"},{"id":"T2","span":{"begin":205,"end":217},"obj":"Body_part"},{"id":"T3","span":{"begin":345,"end":358},"obj":"Body_part"},{"id":"T4","span":{"begin":668,"end":681},"obj":"Body_part"},{"id":"T5","span":{"begin":868,"end":876},"obj":"Body_part"},{"id":"T6","span":{"begin":1409,"end":1415},"obj":"Body_part"},{"id":"T7","span":{"begin":1712,"end":1725},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0001873"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000345"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL_0000084"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":128},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":129,"end":330},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":331,"end":340},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":341,"end":660},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":661,"end":729},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":730,"end":856},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":857,"end":977},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":978,"end":1052},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1053,"end":1121},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1122,"end":1189},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1190,"end":1455},"obj":"Sentence"},{"id":"TextSentencer_T12","span":{"begin":1456,"end":1531},"obj":"Sentence"},{"id":"TextSentencer_T13","span":{"begin":1532,"end":1655},"obj":"Sentence"},{"id":"TextSentencer_T14","span":{"begin":1656,"end":1851},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":128},"obj":"Sentence"},{"id":"T2","span":{"begin":129,"end":330},"obj":"Sentence"},{"id":"T3","span":{"begin":331,"end":340},"obj":"Sentence"},{"id":"T4","span":{"begin":341,"end":660},"obj":"Sentence"},{"id":"T5","span":{"begin":661,"end":729},"obj":"Sentence"},{"id":"T6","span":{"begin":730,"end":856},"obj":"Sentence"},{"id":"T7","span":{"begin":857,"end":977},"obj":"Sentence"},{"id":"T8","span":{"begin":978,"end":1052},"obj":"Sentence"},{"id":"T9","span":{"begin":1053,"end":1121},"obj":"Sentence"},{"id":"T10","span":{"begin":1122,"end":1189},"obj":"Sentence"},{"id":"T11","span":{"begin":1190,"end":1455},"obj":"Sentence"},{"id":"T12","span":{"begin":1456,"end":1531},"obj":"Sentence"},{"id":"T13","span":{"begin":1532,"end":1655},"obj":"Sentence"},{"id":"T14","span":{"begin":1656,"end":1851},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":128},"obj":"Sentence"},{"id":"T2","span":{"begin":129,"end":330},"obj":"Sentence"},{"id":"T3","span":{"begin":331,"end":340},"obj":"Sentence"},{"id":"T4","span":{"begin":341,"end":660},"obj":"Sentence"},{"id":"T5","span":{"begin":661,"end":729},"obj":"Sentence"},{"id":"T6","span":{"begin":730,"end":856},"obj":"Sentence"},{"id":"T7","span":{"begin":857,"end":977},"obj":"Sentence"},{"id":"T8","span":{"begin":978,"end":1052},"obj":"Sentence"},{"id":"T9","span":{"begin":1053,"end":1121},"obj":"Sentence"},{"id":"T10","span":{"begin":1122,"end":1189},"obj":"Sentence"},{"id":"T11","span":{"begin":1190,"end":1455},"obj":"Sentence"},{"id":"T12","span":{"begin":1456,"end":1531},"obj":"Sentence"},{"id":"T13","span":{"begin":1532,"end":1655},"obj":"Sentence"},{"id":"T14","span":{"begin":1656,"end":1851},"obj":"Sentence"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":372,"end":382},"obj":"Glycan"},{"id":"T2","span":{"begin":383,"end":389},"obj":"Glycan"},{"id":"T3","span":{"begin":456,"end":462},"obj":"Glycan"},{"id":"T4","span":{"begin":635,"end":645},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G57321FI"},{"id":"A5","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G57321FI"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A6","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A7","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G57321FI"},{"id":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G57321FI"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":372,"end":382},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":635,"end":645},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0021"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0021"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"GlyCosmos15-Lectin-Jamboree","denotations":[{"id":"T1","span":{"begin":878,"end":881},"obj":"Lectin"},{"id":"T2","span":{"begin":945,"end":948},"obj":"Lectin"},{"id":"T3","span":{"begin":972,"end":975},"obj":"Lectin"},{"id":"T4","span":{"begin":1012,"end":1015},"obj":"Lectin"},{"id":"T5","span":{"begin":1053,"end":1056},"obj":"Lectin"},{"id":"T6","span":{"begin":1066,"end":1069},"obj":"Lectin"},{"id":"T7","span":{"begin":1133,"end":1136},"obj":"Lectin"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"GL_004187"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"GL_003701"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"GL_003502"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"GL_003701"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"GL_003502"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"GL_004187"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"GL_004187"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":30,"end":35},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":254,"end":261},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":857,"end":876},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":878,"end":881},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":884,"end":901},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":903,"end":906},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":909,"end":921},"obj":"OrganismTaxon"},{"id":"T8","span":{"begin":923,"end":926},"obj":"OrganismTaxon"},{"id":"T9","span":{"begin":929,"end":943},"obj":"OrganismTaxon"},{"id":"T10","span":{"begin":945,"end":948},"obj":"OrganismTaxon"},{"id":"T11","span":{"begin":954,"end":970},"obj":"OrganismTaxon"},{"id":"T12","span":{"begin":1004,"end":1007},"obj":"OrganismTaxon"},{"id":"T13","span":{"begin":1012,"end":1015},"obj":"OrganismTaxon"},{"id":"T14","span":{"begin":1058,"end":1061},"obj":"OrganismTaxon"},{"id":"T15","span":{"begin":1066,"end":1069},"obj":"OrganismTaxon"},{"id":"T16","span":{"begin":1133,"end":1136},"obj":"OrganismTaxon"},{"id":"T17","span":{"begin":1484,"end":1489},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"3567"},{"id":"A4","pred":"db_id","subj":"T4","obj":"3567"},{"id":"A5","pred":"db_id","subj":"T5","obj":"37501"},{"id":"A6","pred":"db_id","subj":"T6","obj":"37501"},{"id":"A7","pred":"db_id","subj":"T7","obj":"36461"},{"id":"A8","pred":"db_id","subj":"T8","obj":"36461"},{"id":"A9","pred":"db_id","subj":"T9","obj":"4202"},{"id":"A10","pred":"db_id","subj":"T10","obj":"4202"},{"id":"A11","pred":"db_id","subj":"T11","obj":"4565"},{"id":"A12","pred":"db_id","subj":"T12","obj":"37501"},{"id":"A13","pred":"db_id","subj":"T13","obj":"4202"},{"id":"A14","pred":"db_id","subj":"T14","obj":"36461"},{"id":"A15","pred":"db_id","subj":"T15","obj":"3567"},{"id":"A16","pred":"db_id","subj":"T16","obj":"3567"},{"id":"A17","pred":"db_id","subj":"T17","obj":"9606"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":36,"end":48},"obj":"Body_part"},{"id":"T2","span":{"begin":205,"end":217},"obj":"Body_part"},{"id":"T3","span":{"begin":345,"end":358},"obj":"Body_part"},{"id":"T4","span":{"begin":668,"end":681},"obj":"Body_part"},{"id":"T5","span":{"begin":868,"end":876},"obj":"Body_part"},{"id":"T6","span":{"begin":1409,"end":1415},"obj":"Body_part"},{"id":"T7","span":{"begin":1712,"end":1725},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0001873"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000345"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL_0000084"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":36,"end":48},"obj":"Cell"},{"id":"T2","span":{"begin":38,"end":48},"obj":"Cell"},{"id":"T3","span":{"begin":205,"end":217},"obj":"Cell"},{"id":"T4","span":{"begin":207,"end":217},"obj":"Cell"},{"id":"T5","span":{"begin":345,"end":358},"obj":"Cell"},{"id":"T6","span":{"begin":668,"end":681},"obj":"Cell"},{"id":"T7","span":{"begin":1712,"end":1725},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000542"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000542"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A7","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000084"}],"text":"Constitutively hyposialylated human T-lymphocyte clones in the Tn-syndrome: binding characteristics of plant and animal lectins.\nPreviously, beta 1,3-galactosyltransferase-deficient (Tn+) and normal (TF+) T-lymphocyte clones have been established from a patient suffering from Tn-syndrome [Thurnher et al. (1992) Eur J Immunol 22: 1835-42]. Tn+ T lymphocytes express only Tn antigen GalNAc alpha 1-O-R) while other O-glycan structures such as sialosyl-Tn (Neu5Ac alpha 2,6GalNAc alpha 1-O-R) or TF (Gal beta 1-3GalNAc alpha 1-O-R) antigens are absent from these cells as shown by flow cytometry using specific mABs for TF and sialosyl-Tn antigen, respectively. Normal T lymphocytes express the TF antigen and derivatives thereof. The surface glycans of Tn+ and TF+ cells were then analysed by flow cytometry using the following sialic acid-binding lectins: Amaranthus caudatus (ACA), Maackia amurensis (MAA), Limax flavus (LFA), Sambucus nigra (SNA) and Triticum vulgare (WGA). Equal and weak binding of MAA and SNA to both TF+ and Tn+ cells was found. WGA, LFA and ACA bound more strongly to TF+ cells than to Tn+ cells. Binding of ACA to TF+ cells was enhanced after sialidase treatment. To investigate the possible biological consequences of hyposialylation, binding of three sialic acid-dependent adhesion molecules to Tn+ and TF+ cells was estimated using radiolabelled Fc-chimeras of sialoadhesin (Sn), myelin-associated glycoprotein (MAG) and CD22. Equal and strong binding of human CD22 to both TF+ and Tn+ cells was found. Whereas binding of Sn and MAG to TF+ cells was strong (100%), binding to Tn+ cells amounted only to 33% (Sn) and 19% (MAG). These results indicate that the in vivo interactions of T lymphocytes in the Tn syndrome with CD22 are not likely to be affected, whereas adhesion mediated by Sn or MAG could be strongly reduced."}