PubMed:7538131 JSONTXT

{"project":"ngly1-sample4","denotations":[{"id":"T1","span":{"begin":1153,"end":1159},"obj":"chem:24139"},{"id":"T2","span":{"begin":1086,"end":1092},"obj":"chem:24139"}],"text":"Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin.\nL-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1--\u003e3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1--\u003e3[GlcNAc beta 1--\u003e6]GalNAc or larger core structures with additional GlcNAc residues. The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are discussed."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":604,"end":618},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":611,"end":618},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":979,"end":988},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":1048,"end":1054},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":1212,"end":1218},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00054MO"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G01187XC"},{"id":"A3","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00051MO"},{"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/G00033MO"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00033MO"}],"text":"Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin.\nL-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1--\u003e3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1--\u003e3[GlcNAc beta 1--\u003e6]GalNAc or larger core structures with additional GlcNAc residues. The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are discussed."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":85},"obj":"Sentence"},{"id":"T2","span":{"begin":86,"end":245},"obj":"Sentence"},{"id":"T3","span":{"begin":246,"end":337},"obj":"Sentence"},{"id":"T4","span":{"begin":338,"end":526},"obj":"Sentence"},{"id":"T5","span":{"begin":527,"end":692},"obj":"Sentence"},{"id":"T6","span":{"begin":693,"end":924},"obj":"Sentence"},{"id":"T7","span":{"begin":925,"end":1169},"obj":"Sentence"},{"id":"T8","span":{"begin":1170,"end":1368},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":85},"obj":"Sentence"},{"id":"T2","span":{"begin":86,"end":245},"obj":"Sentence"},{"id":"T3","span":{"begin":246,"end":337},"obj":"Sentence"},{"id":"T4","span":{"begin":338,"end":526},"obj":"Sentence"},{"id":"T5","span":{"begin":527,"end":692},"obj":"Sentence"},{"id":"T6","span":{"begin":693,"end":924},"obj":"Sentence"},{"id":"T7","span":{"begin":925,"end":1169},"obj":"Sentence"},{"id":"T8","span":{"begin":1170,"end":1368},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin.\nL-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1--\u003e3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1--\u003e3[GlcNAc beta 1--\u003e6]GalNAc or larger core structures with additional GlcNAc residues. The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are discussed."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":325,"end":336},"obj":"http://purl.obolibrary.org/obo/MAT_0000197"},{"id":"T2","span":{"begin":325,"end":336},"obj":"http://purl.obolibrary.org/obo/MAT_0000442"},{"id":"T3","span":{"begin":325,"end":330},"obj":"http://purl.obolibrary.org/obo/MAT_0000055"}],"text":"Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin.\nL-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1--\u003e3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1--\u003e3[GlcNAc beta 1--\u003e6]GalNAc or larger core structures with additional GlcNAc residues. The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are discussed."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":604,"end":618},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T2","span":{"begin":611,"end":618},"obj":"https://glytoucan.org/Structures/Glycans/G00051MO"},{"id":"T3","span":{"begin":611,"end":618},"obj":"https://glytoucan.org/Structures/Glycans/G01187XC"},{"id":"T4","span":{"begin":979,"end":988},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"}],"text":"Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin.\nL-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1--\u003e3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1--\u003e3[GlcNAc beta 1--\u003e6]GalNAc or larger core structures with additional GlcNAc residues. The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are discussed."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":604,"end":618},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T2","span":{"begin":611,"end":618},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"T3","span":{"begin":979,"end":988},"obj":"http://www.glycoepitope.jp/epitopes/EP0020"}],"text":"Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin.\nL-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1--\u003e3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1--\u003e3[GlcNAc beta 1--\u003e6]GalNAc or larger core structures with additional GlcNAc residues. The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are discussed."}

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":1086,"end":1092},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":1153,"end":1159},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin.\nL-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1--\u003e3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1--\u003e3[GlcNAc beta 1--\u003e6]GalNAc or larger core structures with additional GlcNAc residues. The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are discussed."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":325,"end":336},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000197"},{"id":"A2","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000442"}],"text":"Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin.\nL-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1--\u003e3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1--\u003e3[GlcNAc beta 1--\u003e6]GalNAc or larger core structures with additional GlcNAc residues. The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are discussed."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":611,"end":618},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00051MO"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00051MO"}],"text":"Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin.\nL-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1--\u003e3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1--\u003e3[GlcNAc beta 1--\u003e6]GalNAc or larger core structures with additional GlcNAc residues. The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are discussed."}

{"project":"Glycosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":604,"end":618},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":979,"end":988},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0020"}],"text":"Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin.\nL-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1--\u003e3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1--\u003e3[GlcNAc beta 1--\u003e6]GalNAc or larger core structures with additional GlcNAc residues. The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are discussed."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":102,"end":111},"obj":"Body_part"},{"id":"T2","span":{"begin":184,"end":194},"obj":"Body_part"},{"id":"T3","span":{"begin":198,"end":209},"obj":"Body_part"},{"id":"T4","span":{"begin":275,"end":284},"obj":"Body_part"},{"id":"T5","span":{"begin":304,"end":314},"obj":"Body_part"},{"id":"T6","span":{"begin":325,"end":336},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000738"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000738"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001986"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000738"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0000542"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000029"}],"text":"Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin.\nL-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1--\u003e3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1--\u003e3[GlcNAc beta 1--\u003e6]GalNAc or larger core structures with additional GlcNAc residues. The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are discussed."}

{"project":"Glycosmos15-CL","denotations":[{"id":"T1","span":{"begin":102,"end":111},"obj":"Cell"},{"id":"T2","span":{"begin":184,"end":194},"obj":"Cell"},{"id":"T3","span":{"begin":275,"end":284},"obj":"Cell"},{"id":"T4","span":{"begin":304,"end":314},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000738"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000738"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000738"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000542"}],"text":"Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin.\nL-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1--\u003e3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1--\u003e3[GlcNAc beta 1--\u003e6]GalNAc or larger core structures with additional GlcNAc residues. The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are discussed."}