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Glycan-Motif

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":50,"end":69},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T2","span":{"begin":594,"end":613},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T3","span":{"begin":733,"end":752},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T4","span":{"begin":905,"end":924},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T5","span":{"begin":975,"end":994},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T6","span":{"begin":1109,"end":1128},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T7","span":{"begin":1182,"end":1201},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T8","span":{"begin":1444,"end":1463},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T9","span":{"begin":1680,"end":1699},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

GlyCosmos6-Glycan-Motif-Image

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":50,"end":69},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":594,"end":613},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":733,"end":752},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":905,"end":924},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":975,"end":994},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":1109,"end":1128},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":1182,"end":1201},"obj":"Glycan_Motif"},{"id":"T8","span":{"begin":1444,"end":1463},"obj":"Glycan_Motif"},{"id":"T9","span":{"begin":1680,"end":1699},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A8","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A9","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":138},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":139,"end":384},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":385,"end":679},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":680,"end":842},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":843,"end":1391},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1392,"end":1577},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1578,"end":1739},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":138},"obj":"Sentence"},{"id":"T2","span":{"begin":139,"end":384},"obj":"Sentence"},{"id":"T3","span":{"begin":385,"end":679},"obj":"Sentence"},{"id":"T4","span":{"begin":680,"end":842},"obj":"Sentence"},{"id":"T5","span":{"begin":843,"end":1391},"obj":"Sentence"},{"id":"T6","span":{"begin":1392,"end":1577},"obj":"Sentence"},{"id":"T7","span":{"begin":1578,"end":1739},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":138},"obj":"Sentence"},{"id":"T2","span":{"begin":139,"end":384},"obj":"Sentence"},{"id":"T3","span":{"begin":385,"end":679},"obj":"Sentence"},{"id":"T4","span":{"begin":680,"end":842},"obj":"Sentence"},{"id":"T5","span":{"begin":843,"end":1391},"obj":"Sentence"},{"id":"T6","span":{"begin":1392,"end":1577},"obj":"Sentence"},{"id":"T7","span":{"begin":1578,"end":1739},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":50,"end":69},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T2","span":{"begin":594,"end":613},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T3","span":{"begin":733,"end":752},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T4","span":{"begin":905,"end":924},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T5","span":{"begin":975,"end":994},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T6","span":{"begin":1109,"end":1128},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T7","span":{"begin":1182,"end":1201},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T8","span":{"begin":1444,"end":1463},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T9","span":{"begin":1680,"end":1699},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

GlycoBiology-FMA

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":547,"end":550},"obj":"http://www.uniprot.org/uniprot/P01138"},{"id":"T2","span":{"begin":826,"end":829},"obj":"http://www.uniprot.org/uniprot/P01138"},{"id":"T3","span":{"begin":1021,"end":1024},"obj":"http://www.uniprot.org/uniprot/P01138"},{"id":"T4","span":{"begin":1104,"end":1145},"obj":"http://www.uniprot.org/uniprot/O43505"},{"id":"T5","span":{"begin":1295,"end":1326},"obj":"http://www.uniprot.org/uniprot/Q06430"},{"id":"T6","span":{"begin":1295,"end":1326},"obj":"http://www.uniprot.org/uniprot/Q8N0V5"},{"id":"T7","span":{"begin":1295,"end":1326},"obj":"http://www.uniprot.org/uniprot/Q8NFS9"},{"id":"T8","span":{"begin":1341,"end":1347},"obj":"http://www.uniprot.org/uniprot/Q92988"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":1104,"end":1145},"obj":"http://www.uniprot.org/uniprot/Q8BWP8"},{"id":"T2","span":{"begin":1295,"end":1326},"obj":"http://www.uniprot.org/uniprot/P97402"},{"id":"T3","span":{"begin":1350,"end":1371},"obj":"http://www.uniprot.org/uniprot/P23336"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":100,"end":105},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T2","span":{"begin":351,"end":356},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T3","span":{"begin":370,"end":375},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":416,"end":421},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T5","span":{"begin":673,"end":678},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T6","span":{"begin":764,"end":769},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T7","span":{"begin":1004,"end":1009},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T8","span":{"begin":1041,"end":1046},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T9","span":{"begin":1210,"end":1215},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T10","span":{"begin":1341,"end":1345},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T11","span":{"begin":1341,"end":1345},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T12","span":{"begin":1482,"end":1487},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T13","span":{"begin":1539,"end":1544},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":217,"end":237},"obj":"http://purl.obolibrary.org/obo/GO_0030154"},{"id":"T2","span":{"begin":394,"end":403},"obj":"http://purl.obolibrary.org/obo/GO_0008152"},{"id":"T3","span":{"begin":532,"end":538},"obj":"http://purl.obolibrary.org/obo/GO_0040007"},{"id":"T4","span":{"begin":589,"end":623},"obj":"http://purl.obolibrary.org/obo/GO_0030311"},{"id":"T5","span":{"begin":900,"end":934},"obj":"http://purl.obolibrary.org/obo/GO_0030311"},{"id":"T6","span":{"begin":1439,"end":1473},"obj":"http://purl.obolibrary.org/obo/GO_0030311"},{"id":"T7","span":{"begin":614,"end":623},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T8","span":{"begin":925,"end":934},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T9","span":{"begin":1464,"end":1473},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T10","span":{"begin":1281,"end":1326},"obj":"http://purl.obolibrary.org/obo/GO_0047222"},{"id":"T11","span":{"begin":1281,"end":1326},"obj":"http://purl.obolibrary.org/obo/GO_0008454"},{"id":"T12","span":{"begin":1281,"end":1326},"obj":"http://purl.obolibrary.org/obo/GO_0008455"},{"id":"T13","span":{"begin":1281,"end":1328},"obj":"http://purl.obolibrary.org/obo/GO_0030144"},{"id":"T14","span":{"begin":1281,"end":1326},"obj":"http://purl.obolibrary.org/obo/GO_0047261"},{"id":"T15","span":{"begin":1281,"end":1326},"obj":"http://purl.obolibrary.org/obo/GO_0008917"},{"id":"T16","span":{"begin":1281,"end":1326},"obj":"http://purl.obolibrary.org/obo/GO_0017176"},{"id":"T17","span":{"begin":1281,"end":1326},"obj":"http://purl.obolibrary.org/obo/GO_0001888"},{"id":"T18","span":{"begin":1281,"end":1326},"obj":"http://purl.obolibrary.org/obo/GO_0003829"},{"id":"T19","span":{"begin":1281,"end":1326},"obj":"http://purl.obolibrary.org/obo/GO_0008109"},{"id":"T20","span":{"begin":1506,"end":1523},"obj":"http://purl.obolibrary.org/obo/GO_0031175"},{"id":"T21","span":{"begin":1506,"end":1523},"obj":"http://purl.obolibrary.org/obo/GO_0048812"},{"id":"T22","span":{"begin":1514,"end":1523},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":32,"end":36},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":100,"end":105},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":351,"end":356},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":370,"end":375},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":416,"end":421},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":673,"end":678},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T7","span":{"begin":764,"end":769},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T8","span":{"begin":1004,"end":1009},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T9","span":{"begin":1041,"end":1046},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T10","span":{"begin":1210,"end":1215},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T11","span":{"begin":1482,"end":1487},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T12","span":{"begin":1539,"end":1544},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T13","span":{"begin":32,"end":44},"obj":"http://purl.obolibrary.org/obo/GO_0009986"},{"id":"T14","span":{"begin":1506,"end":1513},"obj":"http://purl.obolibrary.org/obo/GO_0043005"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

UBERON-AE

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":211,"end":216},"obj":"http://purl.obolibrary.org/obo/UBERON_0001021"},{"id":"T2","span":{"begin":526,"end":531},"obj":"http://purl.obolibrary.org/obo/UBERON_0001021"},{"id":"T3","span":{"begin":1129,"end":1138},"obj":"http://purl.obolibrary.org/obo/UBERON_2000106"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

EDAM-topics

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":173,"end":185},"obj":"http://edamontology.org/topic_0152"},{"id":"T2","span":{"begin":280,"end":292},"obj":"http://edamontology.org/topic_0152"},{"id":"T3","span":{"begin":394,"end":403},"obj":"http://edamontology.org/topic_3407"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

EDAM-DFO

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":0,"end":10},"obj":"http://edamontology.org/operation_2424"},{"id":"T2","span":{"begin":200,"end":207},"obj":"http://edamontology.org/operation_2409"},{"id":"T3","span":{"begin":200,"end":207},"obj":"http://edamontology.org/operation_0004"},{"id":"T4","span":{"begin":280,"end":302},"obj":"http://edamontology.org/data_1462"},{"id":"T5","span":{"begin":293,"end":302},"obj":"http://edamontology.org/data_0883"},{"id":"T6","span":{"begin":362,"end":375},"obj":"http://edamontology.org/operation_3227"},{"id":"T7","span":{"begin":394,"end":412},"obj":"http://edamontology.org/operation_3715"},{"id":"T8","span":{"begin":627,"end":648},"obj":"http://edamontology.org/data_1519"},{"id":"T9","span":{"begin":683,"end":693},"obj":"http://edamontology.org/operation_2424"},{"id":"T10","span":{"begin":1226,"end":1236},"obj":"http://edamontology.org/operation_3465"},{"id":"T11","span":{"begin":1406,"end":1417},"obj":"http://edamontology.org/operation_2246"},{"id":"T12","span":{"begin":1514,"end":1523},"obj":"http://edamontology.org/format_1915"},{"id":"T13","span":{"begin":1514,"end":1523},"obj":"http://edamontology.org/operation_0335"},{"id":"T14","span":{"begin":1645,"end":1656},"obj":"http://edamontology.org/data_2108"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

GlycoBiology-Epitope

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":404,"end":412},"obj":"id"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

performance-test

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":211,"end":216},"obj":"http://purl.obolibrary.org/obo/UBERON_0001021"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":526,"end":531},"obj":"http://purl.obolibrary.org/obo/UBERON_0001021"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":1129,"end":1138},"obj":"http://purl.obolibrary.org/obo/UBERON_2000106"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

mondo_disease

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":1722,"end":1738},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0004974"},{"id":"A2","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0008233"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

HP-phenotype

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":1722,"end":1738},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002666"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

Lectin-Jamboree

{"project":"Lectin-Jamboree","denotations":[{"id":"T1","span":{"begin":495,"end":501},"obj":"lectin"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

Lectin-Jamboree-Sentence

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":138},"obj":"Sentence"},{"id":"T2","span":{"begin":139,"end":384},"obj":"Sentence"},{"id":"T3","span":{"begin":385,"end":679},"obj":"Sentence"},{"id":"T4","span":{"begin":680,"end":842},"obj":"Sentence"},{"id":"T5","span":{"begin":843,"end":1391},"obj":"Sentence"},{"id":"T6","span":{"begin":1392,"end":1577},"obj":"Sentence"},{"id":"T7","span":{"begin":1578,"end":1739},"obj":"Sentence"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":211,"end":221},"obj":"Body_part"},{"id":"T2","span":{"begin":526,"end":531},"obj":"Body_part"},{"id":"T3","span":{"begin":1129,"end":1138},"obj":"Body_part"},{"id":"T4","span":{"begin":1506,"end":1513},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000540"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0001021"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_2000106"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0043005"}],"text":"Comparison of the expression of cell surface poly-N-acetyllactosamine-type oligosaccharides in PC12 cells with those in its variant PC12D.\nTo explore the biological role of carbohydrate chains in the process of nerve cell differentiation, we carried out a characterization of the carbohydrate structure of glycoproteins by comparing conventional PC12 cells with variant cells (PC12D). In vitro metabolic labeling of cells with either [(3)H] glucosamine or [(3)H] threonine, together with tomato lectin staining, revealed that nerve growth factor (NGF) stimulation caused a decrease in the poly-N-acetyllactosamine synthesis of high-molecular-weight glycopeptides from PC12 cells. By comparison, the amount of glycopeptides with poly-N-acetyllactosamine from PC12D cells was already significantly low and it was not changed by NGF stimulation. By assaying the glycosyltransferases that participate in poly-N-acetyllactosamine synthesis, the decrease in the amount of the poly-N-acetyllactosamine in PC12D cells as well as NGF-stimulated PC12 cells could be accounted for by a reduction in the activity of poly-N-acetyllactosamine extension enzyme (GnT-i), because the amount of poly-N-acetyllactosamine in both cells precisely correlated with changes in GnT-i activity, whereas the activities of N-acetylglucosaminyltransferase V (GnT-V) and beta 1-4 galactosyltransferase remained unchanged. These results demonstrate that the decrease in poly-N-acetyllactosamine synthesis in PC12 cells occurred prior to neurite formation, whereas PC12D cells were insensitive to this effect. Next, we showed that GnT-i but not GnT-V catalyzed a rate-limiting reaction in the expression of poly-N-acetyllactosamine chains, especially in pheochromocytoma."}