PubMed:10561463 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":1159,"end":1166},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":1159,"end":1166},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":140},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":141,"end":272},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":273,"end":506},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":507,"end":694},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":695,"end":892},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":893,"end":1082},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1083,"end":1270},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1271,"end":1393},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":140},"obj":"Sentence"},{"id":"T2","span":{"begin":141,"end":272},"obj":"Sentence"},{"id":"T3","span":{"begin":273,"end":506},"obj":"Sentence"},{"id":"T4","span":{"begin":507,"end":694},"obj":"Sentence"},{"id":"T5","span":{"begin":695,"end":892},"obj":"Sentence"},{"id":"T6","span":{"begin":893,"end":1082},"obj":"Sentence"},{"id":"T7","span":{"begin":1083,"end":1270},"obj":"Sentence"},{"id":"T8","span":{"begin":1271,"end":1393},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":140},"obj":"Sentence"},{"id":"T2","span":{"begin":141,"end":272},"obj":"Sentence"},{"id":"T3","span":{"begin":273,"end":506},"obj":"Sentence"},{"id":"T4","span":{"begin":507,"end":694},"obj":"Sentence"},{"id":"T5","span":{"begin":695,"end":892},"obj":"Sentence"},{"id":"T6","span":{"begin":893,"end":1082},"obj":"Sentence"},{"id":"T7","span":{"begin":1083,"end":1270},"obj":"Sentence"},{"id":"T8","span":{"begin":1271,"end":1393},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1159,"end":1166},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":104,"end":132},"obj":"FMAID:82806"},{"id":"_T2","span":{"begin":104,"end":132},"obj":"FMAID:196801"},{"id":"_T3","span":{"begin":104,"end":132},"obj":"FMAID:199790"},{"id":"_T4","span":{"begin":104,"end":132},"obj":"FMAID:85436"},{"id":"_T5","span":{"begin":152,"end":164},"obj":"FMAID:200942"},{"id":"_T6","span":{"begin":152,"end":164},"obj":"FMAID:212684"},{"id":"_T7","span":{"begin":157,"end":164},"obj":"FMAID:146300"},{"id":"_T8","span":{"begin":157,"end":164},"obj":"FMAID:50594"},{"id":"_T9","span":{"begin":165,"end":177},"obj":"FMAID:167256"},{"id":"_T10","span":{"begin":165,"end":177},"obj":"FMAID:62925"},{"id":"_T11","span":{"begin":230,"end":258},"obj":"FMAID:196801"},{"id":"_T12","span":{"begin":230,"end":258},"obj":"FMAID:82806"},{"id":"_T13","span":{"begin":230,"end":258},"obj":"FMAID:199790"},{"id":"_T14","span":{"begin":230,"end":258},"obj":"FMAID:85436"},{"id":"_T15","span":{"begin":494,"end":499},"obj":"FMAID:7209"},{"id":"_T16","span":{"begin":494,"end":499},"obj":"FMAID:93687"},{"id":"_T17","span":{"begin":500,"end":505},"obj":"FMAID:68646"},{"id":"_T18","span":{"begin":500,"end":505},"obj":"FMAID:169002"},{"id":"_T19","span":{"begin":584,"end":596},"obj":"FMAID:82737"},{"id":"_T20","span":{"begin":584,"end":596},"obj":"FMAID:197276"},{"id":"_T21","span":{"begin":745,"end":751},"obj":"FMAID:196724"},{"id":"_T22","span":{"begin":999,"end":1011},"obj":"FMAID:200942"},{"id":"_T23","span":{"begin":999,"end":1011},"obj":"FMAID:212684"},{"id":"_T24","span":{"begin":1004,"end":1011},"obj":"FMAID:146300"},{"id":"_T25","span":{"begin":1004,"end":1011},"obj":"FMAID:50594"},{"id":"_T26","span":{"begin":1159,"end":1166},"obj":"FMAID:82801"},{"id":"_T27","span":{"begin":1159,"end":1166},"obj":"FMAID:196796"},{"id":"_T28","span":{"begin":1167,"end":1183},"obj":"FMAID:196731"},{"id":"_T29","span":{"begin":1167,"end":1183},"obj":"FMAID:82742"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":260,"end":263},"obj":"http://www.uniprot.org/uniprot/P06744"},{"id":"T2","span":{"begin":440,"end":443},"obj":"http://www.uniprot.org/uniprot/P06744"},{"id":"T3","span":{"begin":630,"end":633},"obj":"http://www.uniprot.org/uniprot/P06744"},{"id":"T4","span":{"begin":835,"end":838},"obj":"http://www.uniprot.org/uniprot/P06744"},{"id":"T5","span":{"begin":1041,"end":1044},"obj":"http://www.uniprot.org/uniprot/P06744"},{"id":"T6","span":{"begin":1087,"end":1090},"obj":"http://www.uniprot.org/uniprot/P06744"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":56,"end":61},"obj":"http://www.uniprot.org/uniprot/P01831"},{"id":"T2","span":{"begin":141,"end":146},"obj":"http://www.uniprot.org/uniprot/P01831"},{"id":"T3","span":{"begin":400,"end":405},"obj":"http://www.uniprot.org/uniprot/P01831"},{"id":"T4","span":{"begin":453,"end":458},"obj":"http://www.uniprot.org/uniprot/P01831"},{"id":"T5","span":{"begin":688,"end":693},"obj":"http://www.uniprot.org/uniprot/P01831"},{"id":"T6","span":{"begin":1054,"end":1059},"obj":"http://www.uniprot.org/uniprot/P01831"},{"id":"T7","span":{"begin":260,"end":263},"obj":"http://www.uniprot.org/uniprot/Q8C675"},{"id":"T8","span":{"begin":440,"end":443},"obj":"http://www.uniprot.org/uniprot/Q8C675"},{"id":"T9","span":{"begin":630,"end":633},"obj":"http://www.uniprot.org/uniprot/Q8C675"},{"id":"T10","span":{"begin":835,"end":838},"obj":"http://www.uniprot.org/uniprot/Q8C675"},{"id":"T11","span":{"begin":1041,"end":1044},"obj":"http://www.uniprot.org/uniprot/Q8C675"},{"id":"T12","span":{"begin":1087,"end":1090},"obj":"http://www.uniprot.org/uniprot/Q8C675"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":500,"end":505},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T2","span":{"begin":1280,"end":1290},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/127244"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":204,"end":217},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T2","span":{"begin":363,"end":376},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T3","span":{"begin":663,"end":675},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T4","span":{"begin":846,"end":852},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T5","span":{"begin":1324,"end":1330},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T6","span":{"begin":1218,"end":1228},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T7","span":{"begin":1238,"end":1249},"obj":"http://purl.obolibrary.org/obo/GO_0036065"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":133,"end":139},"obj":"http://purl.obolibrary.org/obo/GO_0043495"},{"id":"T2","span":{"begin":265,"end":271},"obj":"http://purl.obolibrary.org/obo/GO_0043495"},{"id":"T3","span":{"begin":291,"end":297},"obj":"http://purl.obolibrary.org/obo/GO_0043495"},{"id":"T4","span":{"begin":839,"end":845},"obj":"http://purl.obolibrary.org/obo/GO_0043495"},{"id":"T5","span":{"begin":1303,"end":1309},"obj":"http://purl.obolibrary.org/obo/GO_0043495"},{"id":"T6","span":{"begin":444,"end":452},"obj":"http://purl.obolibrary.org/obo/GO_0043495"},{"id":"T7","span":{"begin":634,"end":642},"obj":"http://purl.obolibrary.org/obo/GO_0043495"},{"id":"T8","span":{"begin":1045,"end":1053},"obj":"http://purl.obolibrary.org/obo/GO_0043495"},{"id":"T9","span":{"begin":1091,"end":1099},"obj":"http://purl.obolibrary.org/obo/GO_0043495"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":152,"end":156},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":500,"end":505},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":152,"end":164},"obj":"http://purl.obolibrary.org/obo/GO_0009986"},{"id":"T4","span":{"begin":999,"end":1011},"obj":"http://purl.obolibrary.org/obo/GO_0009986"},{"id":"T5","span":{"begin":1233,"end":1237},"obj":"http://purl.obolibrary.org/obo/GO_0019013"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":584,"end":596},"obj":"http://edamontology.org/topic_0152"},{"id":"T2","span":{"begin":826,"end":834},"obj":"http://edamontology.org/topic_0749"},{"id":"T3","span":{"begin":853,"end":861},"obj":"http://edamontology.org/topic_3168"},{"id":"T4","span":{"begin":853,"end":861},"obj":"http://edamontology.org/topic_0080"},{"id":"T5","span":{"begin":1331,"end":1339},"obj":"http://edamontology.org/topic_0080"},{"id":"T6","span":{"begin":1331,"end":1339},"obj":"http://edamontology.org/topic_3168"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":11,"end":21},"obj":"http://edamontology.org/operation_2409"},{"id":"T2","span":{"begin":11,"end":21},"obj":"http://edamontology.org/operation_0004"},{"id":"T3","span":{"begin":853,"end":861},"obj":"http://edamontology.org/operation_3218"},{"id":"T4","span":{"begin":853,"end":861},"obj":"http://edamontology.org/data_2044"},{"id":"T5","span":{"begin":1119,"end":1128},"obj":"http://edamontology.org/operation_2409"},{"id":"T6","span":{"begin":1119,"end":1128},"obj":"http://edamontology.org/operation_0004"},{"id":"T7","span":{"begin":1331,"end":1339},"obj":"http://edamontology.org/data_2044"},{"id":"T8","span":{"begin":1331,"end":1339},"obj":"http://edamontology.org/operation_3218"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":260,"end":271},"obj":"http://rdf.glycoinfo.org/glycan/G00045MO"},{"id":"T2","span":{"begin":440,"end":452},"obj":"http://rdf.glycoinfo.org/glycan/G00045MO"},{"id":"T3","span":{"begin":630,"end":642},"obj":"http://rdf.glycoinfo.org/glycan/G00045MO"},{"id":"T4","span":{"begin":1041,"end":1053},"obj":"http://rdf.glycoinfo.org/glycan/G00045MO"},{"id":"T5","span":{"begin":835,"end":845},"obj":"http://rdf.glycoinfo.org/glycan/G00045MO"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G41652MJ\""},{"id":"GlycanIUPAC_T2","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G20761YC\""},{"id":"GlycanIUPAC_T3","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G19807HM\""},{"id":"GlycanIUPAC_T4","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G20351TE\""},{"id":"GlycanIUPAC_T5","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G71957MR\""},{"id":"GlycanIUPAC_T6","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G59040AE\""},{"id":"GlycanIUPAC_T7","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G14987PW\""},{"id":"GlycanIUPAC_T8","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G95064PC\""},{"id":"GlycanIUPAC_T9","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G39143AQ\""},{"id":"GlycanIUPAC_T10","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G65149OO\""},{"id":"GlycanIUPAC_T11","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G02766SY\""},{"id":"GlycanIUPAC_T12","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G26019KJ\""},{"id":"GlycanIUPAC_T13","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G36429CZ\""},{"id":"GlycanIUPAC_T14","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G89633TP\""},{"id":"GlycanIUPAC_T15","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G28494FO\""},{"id":"GlycanIUPAC_T16","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G06219CP\""},{"id":"GlycanIUPAC_T17","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G44237SM\""},{"id":"GlycanIUPAC_T18","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G57948RL\""},{"id":"GlycanIUPAC_T19","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G64016DN\""},{"id":"GlycanIUPAC_T20","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G14536PC\""},{"id":"GlycanIUPAC_T21","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G14356FW\""},{"id":"GlycanIUPAC_T22","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G34565UO\""},{"id":"GlycanIUPAC_T23","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G67124MW\""},{"id":"GlycanIUPAC_T24","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G71457ZU\""},{"id":"GlycanIUPAC_T25","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G55228VZ\""},{"id":"GlycanIUPAC_T26","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G31034MJ\""},{"id":"GlycanIUPAC_T27","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G25776IP\""},{"id":"GlycanIUPAC_T28","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G64442BV\""},{"id":"GlycanIUPAC_T29","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G57018LE\""},{"id":"GlycanIUPAC_T30","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G61761GX\""},{"id":"GlycanIUPAC_T31","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G76318UX\""},{"id":"GlycanIUPAC_T32","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G61906ER\""},{"id":"GlycanIUPAC_T33","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G68723GR\""},{"id":"GlycanIUPAC_T34","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G19540LE\""},{"id":"GlycanIUPAC_T35","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G74944PO\""},{"id":"GlycanIUPAC_T36","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G89489ZJ\""},{"id":"GlycanIUPAC_T37","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G04434YU\""},{"id":"GlycanIUPAC_T38","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G21450PB\""},{"id":"GlycanIUPAC_T39","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G93629QY\""},{"id":"GlycanIUPAC_T40","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G02603TR\""},{"id":"GlycanIUPAC_T41","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G40280JP\""},{"id":"GlycanIUPAC_T42","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G95259IC\""},{"id":"GlycanIUPAC_T43","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G26900FE\""},{"id":"GlycanIUPAC_T44","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G21346KK\""},{"id":"GlycanIUPAC_T45","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G62509FF\""},{"id":"GlycanIUPAC_T46","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G83932AK\""},{"id":"GlycanIUPAC_T47","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G96978IB\""},{"id":"GlycanIUPAC_T48","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G34275DN\""},{"id":"GlycanIUPAC_T49","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G07071JF\""},{"id":"GlycanIUPAC_T50","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G80639QD\""},{"id":"GlycanIUPAC_T51","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G99460PJ\""},{"id":"GlycanIUPAC_T52","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G22024BZ\""},{"id":"GlycanIUPAC_T53","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G74097ZY\""},{"id":"GlycanIUPAC_T54","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G84439YP\""},{"id":"GlycanIUPAC_T55","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G52207WQ\""},{"id":"GlycanIUPAC_T56","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G90695MS\""},{"id":"GlycanIUPAC_T57","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G50398QX\""},{"id":"GlycanIUPAC_T58","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G12166ZT\""},{"id":"GlycanIUPAC_T59","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G48368BR\""},{"id":"GlycanIUPAC_T60","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G57407RW\""},{"id":"GlycanIUPAC_T61","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G00386TY\""},{"id":"GlycanIUPAC_T62","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G18723JK\""},{"id":"GlycanIUPAC_T63","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G93757OR\""},{"id":"GlycanIUPAC_T64","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G29006SI\""},{"id":"GlycanIUPAC_T65","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G03099OQ\""},{"id":"GlycanIUPAC_T66","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G53739OW\""},{"id":"GlycanIUPAC_T67","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G70440ZO\""},{"id":"GlycanIUPAC_T68","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G29951RR\""},{"id":"GlycanIUPAC_T69","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G58402TI\""},{"id":"GlycanIUPAC_T70","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G39875TP\""},{"id":"GlycanIUPAC_T71","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G83439QV\""},{"id":"GlycanIUPAC_T72","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G41762RC\""},{"id":"GlycanIUPAC_T73","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G91604UI\""},{"id":"GlycanIUPAC_T74","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G88447WE\""},{"id":"GlycanIUPAC_T75","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G93634BS\""},{"id":"GlycanIUPAC_T76","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G02587BH\""},{"id":"GlycanIUPAC_T77","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G43511MX\""},{"id":"GlycanIUPAC_T78","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G64958DH\""},{"id":"GlycanIUPAC_T79","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G30384TR\""},{"id":"GlycanIUPAC_T80","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G15624EX\""},{"id":"GlycanIUPAC_T81","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G22706ST\""},{"id":"GlycanIUPAC_T82","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G57408PI\""},{"id":"GlycanIUPAC_T83","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G86403XX\""},{"id":"GlycanIUPAC_T84","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G78043YB\""},{"id":"GlycanIUPAC_T85","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G18952JK\""},{"id":"GlycanIUPAC_T86","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G49020ND\""},{"id":"GlycanIUPAC_T87","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G63590YW\""},{"id":"GlycanIUPAC_T88","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G22793KS\""},{"id":"GlycanIUPAC_T89","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G64134SS\""},{"id":"GlycanIUPAC_T90","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G17338HY\""},{"id":"GlycanIUPAC_T91","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G99745XF\""},{"id":"GlycanIUPAC_T92","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G27782HN\""},{"id":"GlycanIUPAC_T93","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G57496DC\""},{"id":"GlycanIUPAC_T94","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G93169WB\""},{"id":"GlycanIUPAC_T95","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G05518TD\""},{"id":"GlycanIUPAC_T96","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G62603DN\""},{"id":"GlycanIUPAC_T97","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G59574FS\""},{"id":"GlycanIUPAC_T98","span":{"begin":600,"end":603},"obj":"\"http://rdf.glycoinfo.org/glycan/G47567WC\""},{"id":"GlycanIUPAC_T99","span":{"begin":745,"end":751},"obj":"\"http://rdf.glycoinfo.org/glycan/G59665TO\""},{"id":"GlycanIUPAC_T100","span":{"begin":745,"end":751},"obj":"\"http://rdf.glycoinfo.org/glycan/G32915EI\""},{"id":"GlycanIUPAC_T101","span":{"begin":745,"end":751},"obj":"\"http://rdf.glycoinfo.org/glycan/G60625TS\""}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":478,"end":493},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10029"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":494,"end":499},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000992"}],"text":"The glycan processing and site occupancy of recombinant Thy-1 is markedly affected by the presence of a glycosylphosphatidylinositol anchor.\nThy-1 is a cell surface glycoprotein containing three N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The effect of the anchor on its N-linked glyco-sylation was investigated by comparing the glycosylation of soluble recombinant Thy-1 (sThy-1) with that of recombinant GPI anchored Thy-1, both expressed in Chinese hamster ovary cells. The sThy-1 was produced in a variety of isoforms including some which lacked carbohydrate on all three sequons whereas the GPI anchored form appeared fully glycosylated like native Thy-1. This was surprising as the attachment of N-linked sugars occurs cotranslationally and it was not expected that the presence of a C-terminal GPI anchor signal sequence would affect sequon occupancy. Furthermore sThy-1 lacking glycosylation could be produced with the inhibitor tunicamycin but in contrast cell surface expression of unglycosylated GPI anchored Thy-1 could not be obtained. The GPI anchored form appeared less processed with almost 4-fold more oligo-mannose oligosaccharides than in sThy-1 and also with less sialylated and core fucosylated biantennary glycans. Possible mechanisms whereby the anchor or the anchor signal sequence, control site occupancy and maturation are discussed."}