PubMed:19136585 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":134,"end":151},"obj":"https://glytoucan.org/Structures/Glycans/G20420WT"},{"id":"T2","span":{"begin":134,"end":151},"obj":"https://glytoucan.org/Structures/Glycans/G74621DY"},{"id":"T3","span":{"begin":134,"end":151},"obj":"https://glytoucan.org/Structures/Glycans/G84224TW"},{"id":"T4","span":{"begin":440,"end":447},"obj":"https://glytoucan.org/Structures/Glycans/G00047MO"},{"id":"T5","span":{"begin":452,"end":466},"obj":"https://glytoucan.org/Structures/Glycans/G00053MO"},{"id":"T6","span":{"begin":1787,"end":1804},"obj":"https://glytoucan.org/Structures/Glycans/G20420WT"},{"id":"T7","span":{"begin":1787,"end":1804},"obj":"https://glytoucan.org/Structures/Glycans/G74621DY"},{"id":"T8","span":{"begin":1787,"end":1804},"obj":"https://glytoucan.org/Structures/Glycans/G84224TW"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":134,"end":151},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":440,"end":447},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":452,"end":466},"obj":"Glycan_Motif"},{"id":"T8","span":{"begin":1787,"end":1804},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G84224TW"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G74621DY"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G20420WT"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G39023AU"},{"id":"A5","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00047MO"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81971FM"},{"id":"A7","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00053MO"},{"id":"A8","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G84224TW"},{"id":"A9","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G74621DY"},{"id":"A10","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G20420WT"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":134,"end":151},"obj":"https://glytoucan.org/Structures/Glycans/G20420WT"},{"id":"T2","span":{"begin":134,"end":151},"obj":"https://glytoucan.org/Structures/Glycans/G74621DY"},{"id":"T3","span":{"begin":134,"end":151},"obj":"https://glytoucan.org/Structures/Glycans/G84224TW"},{"id":"T4","span":{"begin":440,"end":447},"obj":"https://glytoucan.org/Structures/Glycans/G00047MO"},{"id":"T5","span":{"begin":452,"end":466},"obj":"https://glytoucan.org/Structures/Glycans/G00053MO"},{"id":"T6","span":{"begin":459,"end":466},"obj":"https://glytoucan.org/Structures/Glycans/G00047MO"},{"id":"T7","span":{"begin":1787,"end":1804},"obj":"https://glytoucan.org/Structures/Glycans/G20420WT"},{"id":"T8","span":{"begin":1787,"end":1804},"obj":"https://glytoucan.org/Structures/Glycans/G74621DY"},{"id":"T9","span":{"begin":1787,"end":1804},"obj":"https://glytoucan.org/Structures/Glycans/G84224TW"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":170,"end":177},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T2","span":{"begin":1203,"end":1210},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":199},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":200,"end":542},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":543,"end":796},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":797,"end":1029},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":1030,"end":1472},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1473,"end":1805},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1806,"end":2227},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":199},"obj":"Sentence"},{"id":"T2","span":{"begin":200,"end":542},"obj":"Sentence"},{"id":"T3","span":{"begin":543,"end":796},"obj":"Sentence"},{"id":"T4","span":{"begin":797,"end":1029},"obj":"Sentence"},{"id":"T5","span":{"begin":1030,"end":1472},"obj":"Sentence"},{"id":"T6","span":{"begin":1473,"end":1805},"obj":"Sentence"},{"id":"T7","span":{"begin":1806,"end":2227},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":199},"obj":"Sentence"},{"id":"T2","span":{"begin":200,"end":542},"obj":"Sentence"},{"id":"T3","span":{"begin":543,"end":796},"obj":"Sentence"},{"id":"T4","span":{"begin":797,"end":1029},"obj":"Sentence"},{"id":"T5","span":{"begin":1030,"end":1472},"obj":"Sentence"},{"id":"T6","span":{"begin":1473,"end":1805},"obj":"Sentence"},{"id":"T7","span":{"begin":1806,"end":2227},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":134,"end":151},"obj":"http://www.glycoepitope.jp/epitopes/EP0078"},{"id":"T2","span":{"begin":440,"end":447},"obj":"http://www.glycoepitope.jp/epitopes/EP0007"},{"id":"T3","span":{"begin":452,"end":466},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"T4","span":{"begin":1787,"end":1804},"obj":"http://www.glycoepitope.jp/epitopes/EP0078"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":23,"end":53},"obj":"gene:10317"},{"id":"T1","span":{"begin":170,"end":187},"obj":"disease:C0699790"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":134,"end":151},"obj":"FMAID:82821"},{"id":"_T2","span":{"begin":134,"end":151},"obj":"FMAID:196817"},{"id":"_T3","span":{"begin":170,"end":177},"obj":"FMAID:104231"},{"id":"_T4","span":{"begin":170,"end":177},"obj":"FMAID:14543"},{"id":"_T5","span":{"begin":1081,"end":1088},"obj":"FMAID:90078"},{"id":"_T6","span":{"begin":1181,"end":1199},"obj":"FMAID:196810"},{"id":"_T7","span":{"begin":1181,"end":1199},"obj":"FMAID:82817"},{"id":"_T8","span":{"begin":1181,"end":1199},"obj":"FMAID:196812"},{"id":"_T9","span":{"begin":1181,"end":1199},"obj":"FMAID:196807"},{"id":"_T10","span":{"begin":1181,"end":1199},"obj":"FMAID:82813"},{"id":"_T11","span":{"begin":1181,"end":1199},"obj":"FMAID:82812"},{"id":"_T12","span":{"begin":1181,"end":1199},"obj":"FMAID:196814"},{"id":"_T13","span":{"begin":1181,"end":1199},"obj":"FMAID:196806"},{"id":"_T14","span":{"begin":1181,"end":1199},"obj":"FMAID:82811"},{"id":"_T15","span":{"begin":1181,"end":1199},"obj":"FMAID:82814"},{"id":"_T16","span":{"begin":1181,"end":1199},"obj":"FMAID:82818"},{"id":"_T17","span":{"begin":1181,"end":1199},"obj":"FMAID:196808"},{"id":"_T18","span":{"begin":1181,"end":1199},"obj":"FMAID:82815"},{"id":"_T19","span":{"begin":1181,"end":1199},"obj":"FMAID:196815"},{"id":"_T20","span":{"begin":1181,"end":1199},"obj":"FMAID:82819"},{"id":"_T21","span":{"begin":1181,"end":1199},"obj":"FMAID:196809"},{"id":"_T22","span":{"begin":1181,"end":1199},"obj":"FMAID:196813"},{"id":"_T23","span":{"begin":1203,"end":1210},"obj":"FMAID:104231"},{"id":"_T24","span":{"begin":1203,"end":1210},"obj":"FMAID:14543"},{"id":"_T25","span":{"begin":1221,"end":1226},"obj":"FMAID:68646"},{"id":"_T26","span":{"begin":1221,"end":1226},"obj":"FMAID:169002"},{"id":"_T27","span":{"begin":1466,"end":1471},"obj":"FMAID:169002"},{"id":"_T28","span":{"begin":1466,"end":1471},"obj":"FMAID:68646"},{"id":"_T29","span":{"begin":1531,"end":1549},"obj":"FMAID:82814"},{"id":"_T30","span":{"begin":1531,"end":1549},"obj":"FMAID:82817"},{"id":"_T31","span":{"begin":1531,"end":1549},"obj":"FMAID:82812"},{"id":"_T32","span":{"begin":1531,"end":1549},"obj":"FMAID:196807"},{"id":"_T33","span":{"begin":1531,"end":1549},"obj":"FMAID:196812"},{"id":"_T34","span":{"begin":1531,"end":1549},"obj":"FMAID:196809"},{"id":"_T35","span":{"begin":1531,"end":1549},"obj":"FMAID:196808"},{"id":"_T36","span":{"begin":1531,"end":1549},"obj":"FMAID:82819"},{"id":"_T37","span":{"begin":1531,"end":1549},"obj":"FMAID:196814"},{"id":"_T38","span":{"begin":1531,"end":1549},"obj":"FMAID:82813"},{"id":"_T39","span":{"begin":1531,"end":1549},"obj":"FMAID:82815"},{"id":"_T40","span":{"begin":1531,"end":1549},"obj":"FMAID:82811"},{"id":"_T41","span":{"begin":1531,"end":1549},"obj":"FMAID:196806"},{"id":"_T42","span":{"begin":1531,"end":1549},"obj":"FMAID:82818"},{"id":"_T43","span":{"begin":1531,"end":1549},"obj":"FMAID:196813"},{"id":"_T44","span":{"begin":1531,"end":1549},"obj":"FMAID:196810"},{"id":"_T45","span":{"begin":1531,"end":1549},"obj":"FMAID:196815"},{"id":"_T46","span":{"begin":1787,"end":1804},"obj":"FMAID:196817"},{"id":"_T47","span":{"begin":1787,"end":1804},"obj":"FMAID:82821"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":23,"end":51},"obj":"http://www.uniprot.org/uniprot/O75752"},{"id":"T2","span":{"begin":238,"end":266},"obj":"http://www.uniprot.org/uniprot/O75752"},{"id":"T3","span":{"begin":23,"end":51},"obj":"http://www.uniprot.org/uniprot/O60512"},{"id":"T4","span":{"begin":238,"end":266},"obj":"http://www.uniprot.org/uniprot/O60512"},{"id":"T5","span":{"begin":396,"end":402},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T6","span":{"begin":411,"end":417},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T7","span":{"begin":652,"end":658},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T8","span":{"begin":667,"end":673},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T9","span":{"begin":1361,"end":1367},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T10","span":{"begin":1373,"end":1379},"obj":"http://www.uniprot.org/uniprot/Q92988"},{"id":"T11","span":{"begin":561,"end":593},"obj":"http://www.uniprot.org/uniprot/Q06430"},{"id":"T12","span":{"begin":561,"end":593},"obj":"http://www.uniprot.org/uniprot/Q8N0V5"},{"id":"T13","span":{"begin":561,"end":593},"obj":"http://www.uniprot.org/uniprot/Q8NFS9"},{"id":"T14","span":{"begin":1460,"end":1463},"obj":"http://www.uniprot.org/uniprot/Q86WU2"},{"id":"T15","span":{"begin":1583,"end":1586},"obj":"http://www.uniprot.org/uniprot/Q86WU2"},{"id":"T16","span":{"begin":1718,"end":1721},"obj":"http://www.uniprot.org/uniprot/Q86WU2"},{"id":"T17","span":{"begin":1460,"end":1463},"obj":"http://www.uniprot.org/uniprot/P09622"},{"id":"T18","span":{"begin":1583,"end":1586},"obj":"http://www.uniprot.org/uniprot/P09622"},{"id":"T19","span":{"begin":1718,"end":1721},"obj":"http://www.uniprot.org/uniprot/P09622"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":30,"end":51},"obj":"http://www.uniprot.org/uniprot/P23336"},{"id":"T2","span":{"begin":245,"end":266},"obj":"http://www.uniprot.org/uniprot/P23336"},{"id":"T3","span":{"begin":561,"end":593},"obj":"http://www.uniprot.org/uniprot/P97402"},{"id":"T4","span":{"begin":1460,"end":1463},"obj":"http://www.uniprot.org/uniprot/Q7TNG8"},{"id":"T5","span":{"begin":1583,"end":1586},"obj":"http://www.uniprot.org/uniprot/Q7TNG8"},{"id":"T6","span":{"begin":1718,"end":1721},"obj":"http://www.uniprot.org/uniprot/Q7TNG8"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":23,"end":27},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T2","span":{"begin":23,"end":27},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T3","span":{"begin":178,"end":187},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/166034"},{"id":"T4","span":{"begin":238,"end":242},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T5","span":{"begin":238,"end":242},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T6","span":{"begin":268,"end":272},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T7","span":{"begin":268,"end":272},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T8","span":{"begin":304,"end":308},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T9","span":{"begin":304,"end":308},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T10","span":{"begin":396,"end":400},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T11","span":{"begin":396,"end":400},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T12","span":{"begin":411,"end":415},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T13","span":{"begin":411,"end":415},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T14","span":{"begin":554,"end":558},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T15","span":{"begin":554,"end":558},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T16","span":{"begin":652,"end":656},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T17","span":{"begin":652,"end":656},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T18","span":{"begin":667,"end":671},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T19","span":{"begin":667,"end":671},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T20","span":{"begin":703,"end":707},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T21","span":{"begin":703,"end":707},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T22","span":{"begin":1211,"end":1220},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/166034"},{"id":"T23","span":{"begin":1221,"end":1226},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T24","span":{"begin":1263,"end":1267},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T25","span":{"begin":1263,"end":1267},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T26","span":{"begin":1305,"end":1309},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T27","span":{"begin":1305,"end":1309},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T28","span":{"begin":1361,"end":1365},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T29","span":{"begin":1361,"end":1365},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T30","span":{"begin":1373,"end":1377},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T31","span":{"begin":1373,"end":1377},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T32","span":{"begin":1466,"end":1471},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T33","span":{"begin":1612,"end":1616},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T34","span":{"begin":1612,"end":1616},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T35","span":{"begin":1907,"end":1911},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/9973"},{"id":"T36","span":{"begin":2048,"end":2052},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T37","span":{"begin":2048,"end":2052},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":95,"end":104},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T2","span":{"begin":347,"end":359},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T3","span":{"begin":452,"end":458},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T4","span":{"begin":734,"end":743},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T5","span":{"begin":1647,"end":1658},"obj":"http://purl.obolibrary.org/obo/GO_0036065"},{"id":"T6","span":{"begin":1744,"end":1755},"obj":"http://purl.obolibrary.org/obo/GO_0036065"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":188,"end":192},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":1221,"end":1226},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":1466,"end":1471},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":170,"end":177},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"T2","span":{"begin":1203,"end":1210},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"T3","span":{"begin":2093,"end":2102},"obj":"http://purl.obolibrary.org/obo/UBERON_2000106"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":1354,"end":1360},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"19136585-0#23#53#gene10317","span":{"begin":23,"end":53},"obj":"gene10317"},{"id":"19136585-0#170#187#diseaseC0699790","span":{"begin":170,"end":187},"obj":"diseaseC0699790"},{"id":"19136585-4#430#433#gene1738","span":{"begin":1460,"end":1463},"obj":"gene1738"},{"id":"19136585-4#173#190#diseaseC0699790","span":{"begin":1203,"end":1220},"obj":"diseaseC0699790"}],"relations":[{"id":"23#53#gene10317170#187#diseaseC0699790","pred":"associated_with","subj":"19136585-0#23#53#gene10317","obj":"19136585-0#170#187#diseaseC0699790"},{"id":"430#433#gene1738173#190#diseaseC0699790","pred":"associated_with","subj":"19136585-4#430#433#gene1738","obj":"19136585-4#173#190#diseaseC0699790"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":170,"end":177},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T2","span":{"begin":1203,"end":1210},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":440,"end":445},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T2","span":{"begin":459,"end":464},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T3","span":{"begin":452,"end":464},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":134,"end":151},"obj":"http://www.glycoepitope.jp/epitopes/EP0078"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":1787,"end":1804},"obj":"http://www.glycoepitope.jp/epitopes/EP0078"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":452,"end":466},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T4","span":{"begin":440,"end":447},"obj":"http://www.glycoepitope.jp/epitopes/EP0007"},{"id":"PD-GlycoEpitope-B_T5","span":{"begin":459,"end":466},"obj":"http://www.glycoepitope.jp/epitopes/EP0007"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

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UPAC_T137","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G67363FK\""},{"id":"GlycanIUPAC_T138","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G67363FK\""},{"id":"GlycanIUPAC_T139","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G17562KT\""},{"id":"GlycanIUPAC_T140","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G17562KT\""},{"id":"GlycanIUPAC_T141","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G17562KT\""},{"id":"GlycanIUPAC_T142","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G24774YJ\""},{"id":"GlycanIUPAC_T143","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G24774YJ\""},{"id":"GlycanIUPAC_T144","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G24774YJ\""},{"id":"GlycanIUPAC_T145","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G32162UO\""},{"id":"GlycanIUPAC_T146","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G32162UO\""},{"id":"GlycanIUPAC_T147","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G32162UO\""},{"id":"GlycanIUPAC_T148","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G89163RR\""},{"id":"GlycanIUPAC_T149","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G89163RR\""},{"id":"GlycanIUPAC_T150","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G89163RR\""},{"id":"GlycanIUPAC_T151","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G99522DY\""},{"id":"GlycanIUPAC_T152","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G99522DY\""},{"id":"GlycanIUPAC_T153","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G99522DY\""},{"id":"GlycanIUPAC_T154","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G59246IF\""},{"id":"GlycanIUPAC_T155","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G59246IF\""},{"id":"GlycanIUPAC_T156","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G59246IF\""},{"id":"GlycanIUPAC_T157","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G95321NT\""},{"id":"GlycanIUPAC_T158","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G95321NT\""},{"id":"GlycanIUPAC_T159","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G95321NT\""},{"id":"GlycanIUPAC_T160","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G17531ZI\""},{"id":"GlycanIUPAC_T161","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G17531ZI\""},{"id":"GlycanIUPAC_T162","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G17531ZI\""},{"id":"GlycanIUPAC_T163","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G54322SU\""},{"id":"GlycanIUPAC_T164","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G54322SU\""},{"id":"GlycanIUPAC_T165","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G54322SU\""},{"id":"GlycanIUPAC_T166","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G72010DO\""},{"id":"GlycanIUPAC_T167","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G72010DO\""},{"id":"GlycanIUPAC_T168","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G72010DO\""},{"id":"GlycanIUPAC_T169","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G44269EP\""},{"id":"GlycanIUPAC_T170","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G44269EP\""},{"id":"GlycanIUPAC_T171","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G44269EP\""},{"id":"GlycanIUPAC_T172","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G57335AD\""},{"id":"GlycanIUPAC_T173","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G57335AD\""},{"id":"GlycanIUPAC_T174","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G57335AD\""},{"id":"GlycanIUPAC_T175","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G60837LL\""},{"id":"GlycanIUPAC_T176","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G60837LL\""},{"id":"GlycanIUPAC_T177","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G60837LL\""},{"id":"GlycanIUPAC_T178","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G61929XX\""},{"id":"GlycanIUPAC_T179","span":{"begin":648,"end":651},"obj":"\"http://rdf.glycoinfo.org/glycan/G61929XX\""},{"id":"GlycanIUPAC_T180","span":{"begin":2010,"end":2013},"obj":"\"http://rdf.glycoinfo.org/glycan/G61929XX\""},{"id":"GlycanIUPAC_T181","span":{"begin":392,"end":395},"obj":"\"http://rdf.glycoinfo.org/glycan/G88747RA\""},{"id":"GlycanIUPAC_T182","span":{"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""},{"id":"GlycanIUPAC_T363","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G85391SA\""},{"id":"GlycanIUPAC_T364","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G89565QL\""},{"id":"GlycanIUPAC_T365","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G80869MR\""},{"id":"GlycanIUPAC_T366","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G55978NL\""},{"id":"GlycanIUPAC_T367","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G54644LT\""},{"id":"GlycanIUPAC_T368","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G25694UG\""},{"id":"GlycanIUPAC_T369","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G25126RB\""},{"id":"GlycanIUPAC_T370","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G51848AD\""},{"id":"GlycanIUPAC_T371","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G94667GM\""},{"id":"GlycanIUPAC_T372","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G30124BO\""},{"id":"GlycanIUPAC_T373","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G82777EZ\""},{"id":"GlycanIUPAC_T374","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G10151YZ\""},{"id":"GlycanIUPAC_T375","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G17585ZM\""},{"id":"GlycanIUPAC_T376","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G04411CJ\""},{"id":"GlycanIUPAC_T377","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G38254HJ\""},{"id":"GlycanIUPAC_T378","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G75188FS\""},{"id":"GlycanIUPAC_T379","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G70374VG\""},{"id":"GlycanIUPAC_T380","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G45176LJ\""},{"id":"GlycanIUPAC_T381","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G30874VW\""},{"id":"GlycanIUPAC_T382","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G69333MI\""},{"id":"GlycanIUPAC_T383","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G10676XO\""},{"id":"GlycanIUPAC_T384","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G14843DJ\""},{"id":"GlycanIUPAC_T385","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G47546FR\""},{"id":"GlycanIUPAC_T386","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G73695ZM\""},{"id":"GlycanIUPAC_T387","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G31923TJ\""},{"id":"GlycanIUPAC_T388","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G60519EP\""},{"id":"GlycanIUPAC_T389","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G07933IA\""},{"id":"GlycanIUPAC_T390","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G40745NH\""},{"id":"GlycanIUPAC_T391","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G54496YV\""},{"id":"GlycanIUPAC_T392","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T393","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T394","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T395","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T396","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T397","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T398","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T399","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T400","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T401","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T402","span":{"begin":1354,"end":1360},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":170,"end":177},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1203,"end":1210},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":2093,"end":2102},"obj":"http://purl.obolibrary.org/obo/UBERON_2000106"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":170,"end":187},"obj":"Disease"},{"id":"T2","span":{"begin":1203,"end":1220},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0002032"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0002032"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":440,"end":447},"obj":"Glycan"},{"id":"T2","span":{"begin":452,"end":466},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39023AU"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39023AU"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00053MO"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00053MO"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":178,"end":187},"obj":"Phenotype"},{"id":"T2","span":{"begin":1211,"end":1220},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0030731"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0030731"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":170,"end":187},"obj":"Disease"},{"id":"T2","span":{"begin":1203,"end":1220},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0002032"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0002032"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":164,"end":169},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":764,"end":768},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A2","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000775"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":2093,"end":2102},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_2000106"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":170,"end":177},"obj":"Body_part"},{"id":"T2","span":{"begin":1203,"end":1210},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000526"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":199},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":200,"end":542},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":543,"end":796},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":797,"end":1029},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":1030,"end":1472},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1473,"end":1805},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1806,"end":2227},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":199},"obj":"Sentence"},{"id":"T2","span":{"begin":200,"end":542},"obj":"Sentence"},{"id":"T3","span":{"begin":543,"end":796},"obj":"Sentence"},{"id":"T4","span":{"begin":797,"end":1029},"obj":"Sentence"},{"id":"T5","span":{"begin":1030,"end":1472},"obj":"Sentence"},{"id":"T6","span":{"begin":1473,"end":1805},"obj":"Sentence"},{"id":"T7","span":{"begin":1806,"end":2227},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":199},"obj":"Sentence"},{"id":"T2","span":{"begin":200,"end":542},"obj":"Sentence"},{"id":"T3","span":{"begin":543,"end":796},"obj":"Sentence"},{"id":"T4","span":{"begin":797,"end":1029},"obj":"Sentence"},{"id":"T5","span":{"begin":1030,"end":1472},"obj":"Sentence"},{"id":"T6","span":{"begin":1473,"end":1805},"obj":"Sentence"},{"id":"T7","span":{"begin":1806,"end":2227},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":199},"obj":"Sentence"},{"id":"T2","span":{"begin":200,"end":542},"obj":"Sentence"},{"id":"T3","span":{"begin":543,"end":796},"obj":"Sentence"},{"id":"T4","span":{"begin":797,"end":1029},"obj":"Sentence"},{"id":"T5","span":{"begin":1030,"end":1472},"obj":"Sentence"},{"id":"T6","span":{"begin":1473,"end":1805},"obj":"Sentence"},{"id":"T7","span":{"begin":1806,"end":2227},"obj":"Sentence"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":440,"end":447},"obj":"Glycan"},{"id":"T2","span":{"begin":452,"end":466},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39023AU"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39023AU"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00053MO"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00053MO"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":134,"end":151},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":440,"end":447},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":452,"end":466},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":1787,"end":1804},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0078"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0007"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0078"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":164,"end":169},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":134,"end":151},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":440,"end":447},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":452,"end":466},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":1787,"end":1804},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0078"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0007"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0078"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":2093,"end":2102},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_2000106"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":170,"end":177},"obj":"Body_part"},{"id":"T2","span":{"begin":1203,"end":1210},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000526"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":178,"end":187},"obj":"Phenotype"},{"id":"T2","span":{"begin":1211,"end":1220},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0030731"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0030731"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":764,"end":768},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000096"},{"id":"A2","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000775"}],"text":"Enhanced expression of beta 3-galactosyltransferase 5 activity is sufficient to induce in vivo synthesis of extended type 1 chains on lactosylceramides of selected human colonic carcinoma cell lines.\nIn general, an elevated expression of beta 3-galactosyltransferase (beta 3GalT) activity contributed by beta 3GalT5 correlates well with increased biosynthesis and expression of type 1 chain (Gal beta 1-3GlcNAc beta 1-) derivatives such as Lewis A and sialyl Lewis A, which are mostly recognized as terminal epitopes and not further extended. Most known beta 3-N-acetylglucosaminyltransferases show a higher activity toward extending type 2 chain (Gal beta 1-4GlcNAc beta 1-), and an over-expression of beta 3GalT5 could suppress the formation of the type 2 chain poly-N-acetyllactosaminoglycans. The potential of extending instead the predominant type 1 chain termini synthesized under such circumstances was, however, not investigated, partly due to technical difficulty in unambiguous identification of extended type 1 chains. Using an advanced mass spectrometry-based glycomic mapping and glycan sequencing approach, we show here that type 1 chains carried on the lacto-series glycosphingolipids of colonic carcinoma cells can be extended when the endogenous beta 3GalT activity relative to competing beta 4GalT activity, as defined against a common GlcNAc beta 1-3Gal beta 1-4Glc acceptor, is sufficiently high, as found in Colo205 and SW1116, but not in DLD-1 cells. In support of this positive correlation, the lacto-series glycosphingolipids isolated from stably transfected DLD-1 clones over-expressing beta 3GalT5 were shown to comprise fucosylated dimeric type 1 chains, whereas a mock transfectant and the DLD-1 parent carried only fucosylated dimeric type 2 chains on their lactosylceramides. It suggests that while the natural expression of extended type 1 chain is likely to be determined by many contributing factors including the relative amounts of competing glycosyltransferases and the UDP-Gal level, the enhanced expression of beta 3GalT5 is sufficient to promote in vivo extension of type 1 chains by furnishing a significantly higher amount of type 1 chain precursors relative to competing type 2 chains."}