PubMed:17395692 JSONTXT

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and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

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{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":94},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":95,"end":365},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":366,"end":556},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":557,"end":1037},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":1038,"end":1132},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1133,"end":1432},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1433,"end":1612},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1613,"end":1877},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":94},"obj":"Sentence"},{"id":"T2","span":{"begin":95,"end":365},"obj":"Sentence"},{"id":"T3","span":{"begin":366,"end":556},"obj":"Sentence"},{"id":"T4","span":{"begin":557,"end":1037},"obj":"Sentence"},{"id":"T5","span":{"begin":1038,"end":1132},"obj":"Sentence"},{"id":"T6","span":{"begin":1133,"end":1432},"obj":"Sentence"},{"id":"T7","span":{"begin":1433,"end":1612},"obj":"Sentence"},{"id":"T8","span":{"begin":1613,"end":1877},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":94},"obj":"Sentence"},{"id":"T2","span":{"begin":95,"end":365},"obj":"Sentence"},{"id":"T3","span":{"begin":366,"end":556},"obj":"Sentence"},{"id":"T4","span":{"begin":557,"end":1037},"obj":"Sentence"},{"id":"T5","span":{"begin":1038,"end":1132},"obj":"Sentence"},{"id":"T6","span":{"begin":1133,"end":1432},"obj":"Sentence"},{"id":"T7","span":{"begin":1433,"end":1612},"obj":"Sentence"},{"id":"T8","span":{"begin":1613,"end":1877},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":43,"end":57},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T2","span":{"begin":50,"end":57},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"T3","span":{"begin":135,"end":149},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T4","span":{"begin":142,"end":149},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"T5","span":{"begin":151,"end":155},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T6","span":{"begin":520,"end":524},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T7","span":{"begin":670,"end":674},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T8","span":{"begin":756,"end":760},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T9","span":{"begin":926,"end":930},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T10","span":{"begin":984,"end":988},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T11","span":{"begin":1104,"end":1108},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T12","span":{"begin":1172,"end":1176},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T13","span":{"begin":1416,"end":1420},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T14","span":{"begin":1667,"end":1671},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T15","span":{"begin":1798,"end":1802},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":88,"end":93},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T2","span":{"begin":498,"end":503},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T3","span":{"begin":775,"end":780},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T4","span":{"begin":836,"end":841},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T5","span":{"begin":1641,"end":1646},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T6","span":{"begin":1856,"end":1861},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":498,"end":510},"obj":"HP_0003003"},{"id":"T2","span":{"begin":498,"end":510},"obj":"HP_0100273"},{"id":"T3","span":{"begin":504,"end":510},"obj":"HP_0002664"},{"id":"T4","span":{"begin":530,"end":536},"obj":"HP_0002664"},{"id":"T5","span":{"begin":775,"end":787},"obj":"HP_0003003"},{"id":"T6","span":{"begin":775,"end":787},"obj":"HP_0100273"},{"id":"T7","span":{"begin":781,"end":787},"obj":"HP_0002664"},{"id":"T8","span":{"begin":836,"end":848},"obj":"HP_0003003"},{"id":"T9","span":{"begin":836,"end":848},"obj":"HP_0100273"},{"id":"T10","span":{"begin":842,"end":848},"obj":"HP_0002664"},{"id":"T11","span":{"begin":1066,"end":1072},"obj":"HP_0002664"},{"id":"T12","span":{"begin":1641,"end":1653},"obj":"HP_0003003"},{"id":"T13","span":{"begin":1641,"end":1653},"obj":"HP_0100273"},{"id":"T14","span":{"begin":1647,"end":1653},"obj":"HP_0002664"},{"id":"T15","span":{"begin":1856,"end":1868},"obj":"HP_0003003"},{"id":"T16","span":{"begin":1856,"end":1868},"obj":"HP_0100273"},{"id":"T17","span":{"begin":1862,"end":1868},"obj":"HP_0002664"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":1262,"end":1264},"obj":"http://www.uniprot.org/uniprot/Q8SNA0"},{"id":"T2","span":{"begin":1564,"end":1572},"obj":"http://www.uniprot.org/uniprot/P21217"},{"id":"T3","span":{"begin":1577,"end":1585},"obj":"http://www.uniprot.org/uniprot/Q11130"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":1262,"end":1264},"obj":"http://www.uniprot.org/uniprot/P04441"},{"id":"T2","span":{"begin":1577,"end":1585},"obj":"http://www.uniprot.org/uniprot/Q11131"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":81,"end":87},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/6754"},{"id":"T2","span":{"begin":504,"end":510},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/6754"},{"id":"T3","span":{"begin":530,"end":536},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/6754"},{"id":"T4","span":{"begin":781,"end":787},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/6754"},{"id":"T5","span":{"begin":842,"end":848},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/6754"},{"id":"T6","span":{"begin":849,"end":854},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T7","span":{"begin":1066,"end":1072},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/6754"},{"id":"T8","span":{"begin":1123,"end":1131},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/353209"},{"id":"T9","span":{"begin":1321,"end":1330},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/871272"},{"id":"T10","span":{"begin":1407,"end":1415},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/871272"},{"id":"T11","span":{"begin":1647,"end":1653},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/6754"},{"id":"T12","span":{"begin":1654,"end":1661},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T13","span":{"begin":1862,"end":1868},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/6754"},{"id":"T14","span":{"begin":1869,"end":1876},"obj":"http://purl.bioontology.org/ontology/STY/T024"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":0,"end":12},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T2","span":{"begin":43,"end":49},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T3","span":{"begin":135,"end":141},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T4","span":{"begin":202,"end":212},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T5","span":{"begin":646,"end":651},"obj":"http://purl.obolibrary.org/obo/GO_0008424"},{"id":"T6","span":{"begin":1291,"end":1296},"obj":"http://purl.obolibrary.org/obo/GO_0008424"},{"id":"T7","span":{"begin":1391,"end":1395},"obj":"http://purl.obolibrary.org/obo/GO_0008424"},{"id":"T8","span":{"begin":1564,"end":1568},"obj":"http://purl.obolibrary.org/obo/GO_0008424"},{"id":"T9","span":{"begin":1577,"end":1581},"obj":"http://purl.obolibrary.org/obo/GO_0008424"},{"id":"T10","span":{"begin":1713,"end":1717},"obj":"http://purl.obolibrary.org/obo/GO_0008424"},{"id":"T11","span":{"begin":743,"end":752},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T12","span":{"begin":1683,"end":1692},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T13","span":{"begin":1384,"end":1406},"obj":"http://purl.obolibrary.org/obo/GO_0017060"},{"id":"T14","span":{"begin":1446,"end":1467},"obj":"http://purl.obolibrary.org/obo/GO_0001171"},{"id":"T15","span":{"begin":1454,"end":1467},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T16","span":{"begin":1520,"end":1531},"obj":"http://purl.obolibrary.org/obo/GO_0006351"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":849,"end":854},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":945,"end":949},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":945,"end":959},"obj":"http://purl.obolibrary.org/obo/GO_0005886"},{"id":"T4","span":{"begin":950,"end":959},"obj":"http://purl.obolibrary.org/obo/GO_0016020"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":88,"end":93},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"T2","span":{"begin":498,"end":503},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"T3","span":{"begin":775,"end":780},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"T4","span":{"begin":836,"end":841},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"T5","span":{"begin":1641,"end":1646},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"T6","span":{"begin":1856,"end":1861},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"T7","span":{"begin":1654,"end":1661},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"T8","span":{"begin":1869,"end":1876},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":88,"end":93},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T2","span":{"begin":498,"end":503},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T3","span":{"begin":775,"end":780},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T4","span":{"begin":836,"end":841},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T5","span":{"begin":1641,"end":1646},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T6","span":{"begin":1856,"end":1861},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":1654,"end":1661},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1869,"end":1876},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":88,"end":93},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":498,"end":503},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"PD-UBERON-AE-B_T5","span":{"begin":775,"end":780},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"PD-UBERON-AE-B_T6","span":{"begin":836,"end":841},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"PD-UBERON-AE-B_T7","span":{"begin":1641,"end":1646},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"PD-UBERON-AE-B_T8","span":{"begin":1856,"end":1861},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G23425WZ\""},{"id":"GlycanIUPAC_T2","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G02874VH\""},{"id":"GlycanIUPAC_T3","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G99699DW\""},{"id":"GlycanIUPAC_T4","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G22074RM\""},{"id":"GlycanIUPAC_T5","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G48535VZ\""},{"id":"GlycanIUPAC_T6","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G39738WL\""},{"id":"GlycanIUPAC_T7","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G42313WU\""},{"id":"GlycanIUPAC_T8","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G00393CK\""},{"id":"GlycanIUPAC_T9","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G42649EX\""},{"id":"GlycanIUPAC_T10","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G46880SB\""},{"id":"GlycanIUPAC_T11","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G75599IR\""},{"id":"GlycanIUPAC_T12","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G58985MU\""},{"id":"GlycanIUPAC_T13","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G92517PO\""},{"id":"GlycanIUPAC_T14","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G88512YL\""},{"id":"GlycanIUPAC_T15","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G41473NX\""},{"id":"GlycanIUPAC_T16","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G71089RB\""},{"id":"GlycanIUPAC_T17","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G73485GZ\""},{"id":"GlycanIUPAC_T18","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G61406KC\""},{"id":"GlycanIUPAC_T19","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G34412GZ\""},{"id":"GlycanIUPAC_T20","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G67209FP\""},{"id":"GlycanIUPAC_T21","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G61442IL\""},{"id":"GlycanIUPAC_T22","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G93729MV\""},{"id":"GlycanIUPAC_T23","span":{"begin":268,"end":274},"obj":"\"http://rdf.glycoinfo.org/glycan/G92144AE\""},{"id":"GlycanIUPAC_T24","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G93924TT\""},{"id":"GlycanIUPAC_T25","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G25565DN\""},{"id":"GlycanIUPAC_T26","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G97215EV\""},{"id":"GlycanIUPAC_T27","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G79664KO\""},{"id":"GlycanIUPAC_T28","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G24107FU\""},{"id":"GlycanIUPAC_T29","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G09864UE\""},{"id":"GlycanIUPAC_T30","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G28032MC\""},{"id":"GlycanIUPAC_T31","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G28005UP\""},{"id":"GlycanIUPAC_T32","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G92708AT\""},{"id":"GlycanIUPAC_T33","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G73757UC\""},{"id":"GlycanIUPAC_T34","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G51062DM\""},{"id":"GlycanIUPAC_T35","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G05866BJ\""},{"id":"GlycanIUPAC_T36","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G87394FZ\""},{"id":"GlycanIUPAC_T37","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G03871NF\""},{"id":"GlycanIUPAC_T38","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G29377VE\""},{"id":"GlycanIUPAC_T39","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G33457CX\""},{"id":"GlycanIUPAC_T40","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G97368GU\""},{"id":"GlycanIUPAC_T41","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G18512EL\""},{"id":"GlycanIUPAC_T42","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G41137VS\""},{"id":"GlycanIUPAC_T43","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G30521NA\""},{"id":"GlycanIUPAC_T44","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G19388CD\""},{"id":"GlycanIUPAC_T45","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G53151FU\""},{"id":"GlycanIUPAC_T46","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G27105XC\""},{"id":"GlycanIUPAC_T47","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G91210VM\""},{"id":"GlycanIUPAC_T48","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G40841DE\""},{"id":"GlycanIUPAC_T49","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G71241HP\""},{"id":"GlycanIUPAC_T50","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G84636BJ\""},{"id":"GlycanIUPAC_T51","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G47905LJ\""},{"id":"GlycanIUPAC_T52","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G39340DV\""},{"id":"GlycanIUPAC_T53","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G48801AQ\""},{"id":"GlycanIUPAC_T54","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G14573NX\""},{"id":"GlycanIUPAC_T55","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G56762TR\""},{"id":"GlycanIUPAC_T56","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G20013XO\""},{"id":"GlycanIUPAC_T57","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G39504DR\""},{"id":"GlycanIUPAC_T58","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G35218RQ\""},{"id":"GlycanIUPAC_T59","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G53048SH\""},{"id":"GlycanIUPAC_T60","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G78418IX\""},{"id":"GlycanIUPAC_T61","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G09780OD\""},{"id":"GlycanIUPAC_T62","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G56359GL\""},{"id":"GlycanIUPAC_T63","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G78941YC\""},{"id":"GlycanIUPAC_T64","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G26829FC\""},{"id":"GlycanIUPAC_T65","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G88538ZC\""},{"id":"GlycanIUPAC_T66","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G46593ZR\""},{"id":"GlycanIUPAC_T67","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G43523TH\""},{"id":"GlycanIUPAC_T68","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G36445ON\""},{"id":"GlycanIUPAC_T69","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G67363FK\""},{"id":"GlycanIUPAC_T70","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G17562KT\""},{"id":"GlycanIUPAC_T71","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G24774YJ\""},{"id":"GlycanIUPAC_T72","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G32162UO\""},{"id":"GlycanIUPAC_T73","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G89163RR\""},{"id":"GlycanIUPAC_T74","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G99522DY\""},{"id":"GlycanIUPAC_T75","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G59246IF\""},{"id":"GlycanIUPAC_T76","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G95321NT\""},{"id":"GlycanIUPAC_T77","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G17531ZI\""},{"id":"GlycanIUPAC_T78","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G54322SU\""},{"id":"GlycanIUPAC_T79","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G72010DO\""},{"id":"GlycanIUPAC_T80","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G44269EP\""},{"id":"GlycanIUPAC_T81","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G57335AD\""},{"id":"GlycanIUPAC_T82","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G60837LL\""},{"id":"GlycanIUPAC_T83","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G61929XX\""},{"id":"GlycanIUPAC_T84","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G88747RA\""},{"id":"GlycanIUPAC_T85","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G47955HA\""},{"id":"GlycanIUPAC_T86","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G60982WS\""},{"id":"GlycanIUPAC_T87","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G37035KG\""},{"id":"GlycanIUPAC_T88","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G46297FI\""},{"id":"GlycanIUPAC_T89","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G35475KI\""},{"id":"GlycanIUPAC_T90","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G29771JN\""},{"id":"GlycanIUPAC_T91","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G61285YR\""},{"id":"GlycanIUPAC_T92","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G54785MW\""},{"id":"GlycanIUPAC_T93","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G53039GT\""},{"id":"GlycanIUPAC_T94","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G00601HK\""},{"id":"GlycanIUPAC_T95","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G10485IJ\""},{"id":"GlycanIUPAC_T96","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G16393IB\""},{"id":"GlycanIUPAC_T97","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G98436FZ\""},{"id":"GlycanIUPAC_T98","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G18825IA\""},{"id":"GlycanIUPAC_T99","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G61281HQ\""},{"id":"GlycanIUPAC_T100","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G07798TI\""},{"id":"GlycanIUPAC_T101","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G55921QA\""},{"id":"GlycanIUPAC_T102","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G99066DL\""},{"id":"GlycanIUPAC_T103","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G33451PQ\""},{"id":"GlycanIUPAC_T104","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G02111XU\""},{"id":"GlycanIUPAC_T105","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G85193OM\""},{"id":"GlycanIUPAC_T106","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G89174YQ\""},{"id":"GlycanIUPAC_T107","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G28802LE\""},{"id":"GlycanIUPAC_T108","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G56061JK\""},{"id":"GlycanIUPAC_T109","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G68941BC\""},{"id":"GlycanIUPAC_T110","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G55436FC\""},{"id":"GlycanIUPAC_T111","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G24002PU\""},{"id":"GlycanIUPAC_T112","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G61387SV\""},{"id":"GlycanIUPAC_T113","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G31834HW\""},{"id":"GlycanIUPAC_T114","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G35324RT\""},{"id":"GlycanIUPAC_T115","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G34803QO\""},{"id":"GlycanIUPAC_T116","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G92898FF\""},{"id":"GlycanIUPAC_T117","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G01318VX\""},{"id":"GlycanIUPAC_T118","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G83200MX\""},{"id":"GlycanIUPAC_T119","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G56286UC\""},{"id":"GlycanIUPAC_T120","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G07304QA\""},{"id":"GlycanIUPAC_T121","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G06868OU\""},{"id":"GlycanIUPAC_T122","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G12647BS\""},{"id":"GlycanIUPAC_T123","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G51841DF\""},{"id":"GlycanIUPAC_T124","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G32122AJ\""},{"id":"GlycanIUPAC_T125","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G41125MN\""},{"id":"GlycanIUPAC_T126","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G16093XS\""},{"id":"GlycanIUPAC_T127","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G62425IX\""},{"id":"GlycanIUPAC_T128","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G15673TO\""},{"id":"GlycanIUPAC_T129","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G32857IK\""},{"id":"GlycanIUPAC_T130","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G60047CJ\""},{"id":"GlycanIUPAC_T131","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G55718ZB\""},{"id":"GlycanIUPAC_T132","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G88355ZE\""},{"id":"GlycanIUPAC_T133","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G11283PA\""},{"id":"GlycanIUPAC_T134","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G71737IZ\""},{"id":"GlycanIUPAC_T135","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G60912WZ\""},{"id":"GlycanIUPAC_T136","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G99655SO\""},{"id":"GlycanIUPAC_T137","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G10300TW\""},{"id":"GlycanIUPAC_T138","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G89509FL\""},{"id":"GlycanIUPAC_T139","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G31465TH\""},{"id":"GlycanIUPAC_T140","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G94101LU\""},{"id":"GlycanIUPAC_T141","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G38610BB\""},{"id":"GlycanIUPAC_T142","span":{"begin":294,"end":297},"obj":"\"http://rdf.glycoinfo.org/glycan/G85893UF\""}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":43,"end":55},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T2","span":{"begin":135,"end":147},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T3","span":{"begin":43,"end":57},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T4","span":{"begin":135,"end":149},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T5","span":{"begin":50,"end":55},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T6","span":{"begin":142,"end":147},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T7","span":{"begin":50,"end":57},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T8","span":{"begin":142,"end":149},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T9","span":{"begin":151,"end":155},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T10","span":{"begin":520,"end":524},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T11","span":{"begin":670,"end":674},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T12","span":{"begin":756,"end":760},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T13","span":{"begin":926,"end":930},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T14","span":{"begin":984,"end":988},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T15","span":{"begin":1104,"end":1108},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T16","span":{"begin":1172,"end":1176},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T17","span":{"begin":1416,"end":1420},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T18","span":{"begin":1667,"end":1671},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T19","span":{"begin":1798,"end":1802},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":50,"end":57},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":142,"end":149},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":43,"end":55},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T4","span":{"begin":135,"end":147},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T5","span":{"begin":43,"end":57},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T6","span":{"begin":135,"end":149},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":81,"end":93},"obj":"Disease"},{"id":"T2","span":{"begin":498,"end":510},"obj":"Disease"},{"id":"T3","span":{"begin":530,"end":536},"obj":"Disease"},{"id":"T4","span":{"begin":775,"end":787},"obj":"Disease"},{"id":"T5","span":{"begin":836,"end":848},"obj":"Disease"},{"id":"T6","span":{"begin":1055,"end":1072},"obj":"Disease"},{"id":"T7","span":{"begin":1641,"end":1653},"obj":"Disease"},{"id":"T8","span":{"begin":1856,"end":1868},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0021063"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0021063"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0004992"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MONDO_0021063"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0021063"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0005575"},{"id":"A7","pred":"mondo_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MONDO_0021063"},{"id":"A8","pred":"mondo_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/MONDO_0021063"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":43,"end":57},"obj":"Glycan"},{"id":"T2","span":{"begin":135,"end":149},"obj":"Glycan"},{"id":"T3","span":{"begin":151,"end":155},"obj":"Glycan"},{"id":"T4","span":{"begin":268,"end":274},"obj":"Glycan"},{"id":"T5","span":{"begin":520,"end":524},"obj":"Glycan"},{"id":"T6","span":{"begin":670,"end":674},"obj":"Glycan"},{"id":"T7","span":{"begin":756,"end":760},"obj":"Glycan"},{"id":"T8","span":{"begin":926,"end":930},"obj":"Glycan"},{"id":"T9","span":{"begin":984,"end":988},"obj":"Glycan"},{"id":"T10","span":{"begin":1104,"end":1108},"obj":"Glycan"},{"id":"T11","span":{"begin":1172,"end":1176},"obj":"Glycan"},{"id":"T12","span":{"begin":1416,"end":1420},"obj":"Glycan"},{"id":"T13","span":{"begin":1667,"end":1671},"obj":"Glycan"},{"id":"T14","span":{"begin":1798,"end":1802},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A15","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A16","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A17","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A18","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A19","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A20","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A21","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A22","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A23","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A24","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A11","pred":"glycosmos_id","subj":"T11","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A25","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A12","pred":"glycosmos_id","subj":"T12","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A26","pred":"image","subj":"T12","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A13","pred":"glycosmos_id","subj":"T13","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A27","pred":"image","subj":"T13","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A14","pred":"glycosmos_id","subj":"T14","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A28","pred":"image","subj":"T14","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":81,"end":87},"obj":"Phenotype"},{"id":"T2","span":{"begin":498,"end":510},"obj":"Phenotype"},{"id":"T3","span":{"begin":530,"end":536},"obj":"Phenotype"},{"id":"T4","span":{"begin":775,"end":787},"obj":"Phenotype"},{"id":"T5","span":{"begin":836,"end":848},"obj":"Phenotype"},{"id":"T6","span":{"begin":1055,"end":1072},"obj":"Phenotype"},{"id":"T7","span":{"begin":1641,"end":1653},"obj":"Phenotype"},{"id":"T8","span":{"begin":1856,"end":1868},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002664"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0003003"},{"id":"A3","pred":"hp_id","subj":"T3","obj":"HP:0002664"},{"id":"A4","pred":"hp_id","subj":"T4","obj":"HP:0003003"},{"id":"A5","pred":"hp_id","subj":"T5","obj":"HP:0003003"},{"id":"A6","pred":"hp_id","subj":"T6","obj":"HP:0003003"},{"id":"A7","pred":"hp_id","subj":"T7","obj":"HP:0003003"},{"id":"A8","pred":"hp_id","subj":"T8","obj":"HP:0003003"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":43,"end":57},"obj":"Glycan"},{"id":"T2","span":{"begin":135,"end":149},"obj":"Glycan"},{"id":"T3","span":{"begin":151,"end":155},"obj":"Glycan"},{"id":"T4","span":{"begin":268,"end":274},"obj":"Glycan"},{"id":"T5","span":{"begin":520,"end":524},"obj":"Glycan"},{"id":"T6","span":{"begin":670,"end":674},"obj":"Glycan"},{"id":"T7","span":{"begin":756,"end":760},"obj":"Glycan"},{"id":"T8","span":{"begin":926,"end":930},"obj":"Glycan"},{"id":"T9","span":{"begin":984,"end":988},"obj":"Glycan"},{"id":"T10","span":{"begin":1104,"end":1108},"obj":"Glycan"},{"id":"T11","span":{"begin":1172,"end":1176},"obj":"Glycan"},{"id":"T12","span":{"begin":1416,"end":1420},"obj":"Glycan"},{"id":"T13","span":{"begin":1667,"end":1671},"obj":"Glycan"},{"id":"T14","span":{"begin":1798,"end":1802},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A15","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A16","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A17","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A18","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A19","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A20","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A21","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A22","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A23","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A24","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A11","pred":"glycosmos_id","subj":"T11","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A25","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A12","pred":"glycosmos_id","subj":"T12","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A26","pred":"image","subj":"T12","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A13","pred":"glycosmos_id","subj":"T13","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A27","pred":"image","subj":"T13","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"},{"id":"A14","pred":"glycosmos_id","subj":"T14","obj":"https://glycosmos.org/glycans/show/G00054MO"},{"id":"A28","pred":"image","subj":"T14","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00054MO"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":43,"end":57},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":135,"end":149},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":151,"end":155},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":520,"end":524},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":670,"end":674},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":756,"end":760},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":926,"end":930},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":984,"end":988},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T9","span":{"begin":1104,"end":1108},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T10","span":{"begin":1172,"end":1176},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T11","span":{"begin":1416,"end":1420},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T12","span":{"begin":1667,"end":1671},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T13","span":{"begin":1798,"end":1802},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A9","pred":"glycoepitope_id","subj":"T9","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A10","pred":"glycoepitope_id","subj":"T10","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A11","pred":"glycoepitope_id","subj":"T11","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A12","pred":"glycoepitope_id","subj":"T12","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A13","pred":"glycoepitope_id","subj":"T13","obj":"http://www.glycoepitope.jp/epitopes/EP0012"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":81,"end":87},"obj":"Phenotype"},{"id":"T2","span":{"begin":498,"end":510},"obj":"Phenotype"},{"id":"T3","span":{"begin":530,"end":536},"obj":"Phenotype"},{"id":"T4","span":{"begin":775,"end":787},"obj":"Phenotype"},{"id":"T5","span":{"begin":836,"end":848},"obj":"Phenotype"},{"id":"T6","span":{"begin":1055,"end":1072},"obj":"Phenotype"},{"id":"T7","span":{"begin":1641,"end":1653},"obj":"Phenotype"},{"id":"T8","span":{"begin":1856,"end":1868},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002664"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0003003"},{"id":"A3","pred":"hp_id","subj":"T3","obj":"HP:0002664"},{"id":"A4","pred":"hp_id","subj":"T4","obj":"HP:0003003"},{"id":"A5","pred":"hp_id","subj":"T5","obj":"HP:0003003"},{"id":"A6","pred":"hp_id","subj":"T6","obj":"HP:0003003"},{"id":"A7","pred":"hp_id","subj":"T7","obj":"HP:0003003"},{"id":"A8","pred":"hp_id","subj":"T8","obj":"HP:0003003"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":842,"end":854},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0001064"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":81,"end":93},"obj":"Disease"},{"id":"T2","span":{"begin":498,"end":510},"obj":"Disease"},{"id":"T5","span":{"begin":530,"end":536},"obj":"Disease"},{"id":"T6","span":{"begin":775,"end":787},"obj":"Disease"},{"id":"T9","span":{"begin":836,"end":848},"obj":"Disease"},{"id":"T12","span":{"begin":1055,"end":1072},"obj":"Disease"},{"id":"T14","span":{"begin":1641,"end":1653},"obj":"Disease"},{"id":"T17","span":{"begin":1856,"end":1868},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"MONDO:0021063"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"MONDO:0002032"},{"id":"A3","pred":"mondo_id","subj":"T2","obj":"MONDO:0005575"},{"id":"A4","pred":"mondo_id","subj":"T2","obj":"MONDO:0021063"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"MONDO:0004992"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"MONDO:0002032"},{"id":"A7","pred":"mondo_id","subj":"T6","obj":"MONDO:0005575"},{"id":"A8","pred":"mondo_id","subj":"T6","obj":"MONDO:0021063"},{"id":"A9","pred":"mondo_id","subj":"T9","obj":"MONDO:0002032"},{"id":"A10","pred":"mondo_id","subj":"T9","obj":"MONDO:0005575"},{"id":"A11","pred":"mondo_id","subj":"T9","obj":"MONDO:0021063"},{"id":"A12","pred":"mondo_id","subj":"T12","obj":"MONDO:0005575"},{"id":"A13","pred":"mondo_id","subj":"T12","obj":"MONDO:0024331"},{"id":"A14","pred":"mondo_id","subj":"T14","obj":"MONDO:0002032"},{"id":"A15","pred":"mondo_id","subj":"T14","obj":"MONDO:0005575"},{"id":"A16","pred":"mondo_id","subj":"T14","obj":"MONDO:0021063"},{"id":"A17","pred":"mondo_id","subj":"T17","obj":"MONDO:0002032"},{"id":"A18","pred":"mondo_id","subj":"T17","obj":"MONDO:0005575"},{"id":"A19","pred":"mondo_id","subj":"T17","obj":"MONDO:0021063"}],"namespaces":[{"prefix":"MONDO","uri":"http://purl.obolibrary.org/obo/MONDO_"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":43,"end":57},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":135,"end":149},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":151,"end":155},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":520,"end":524},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":670,"end":674},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":756,"end":760},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":926,"end":930},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":984,"end":988},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T9","span":{"begin":1104,"end":1108},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T10","span":{"begin":1172,"end":1176},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T11","span":{"begin":1416,"end":1420},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T12","span":{"begin":1667,"end":1671},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T13","span":{"begin":1798,"end":1802},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A9","pred":"glycoepitope_id","subj":"T9","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A10","pred":"glycoepitope_id","subj":"T10","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A11","pred":"glycoepitope_id","subj":"T11","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A12","pred":"glycoepitope_id","subj":"T12","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A13","pred":"glycoepitope_id","subj":"T13","obj":"http://www.glycoepitope.jp/epitopes/EP0012"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":94},"obj":"Sentence"},{"id":"T2","span":{"begin":95,"end":365},"obj":"Sentence"},{"id":"T3","span":{"begin":366,"end":556},"obj":"Sentence"},{"id":"T4","span":{"begin":557,"end":1037},"obj":"Sentence"},{"id":"T5","span":{"begin":1038,"end":1132},"obj":"Sentence"},{"id":"T6","span":{"begin":1133,"end":1432},"obj":"Sentence"},{"id":"T7","span":{"begin":1433,"end":1612},"obj":"Sentence"},{"id":"T8","span":{"begin":1613,"end":1877},"obj":"Sentence"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":88,"end":93},"obj":"Body_part"},{"id":"T2","span":{"begin":498,"end":503},"obj":"Body_part"},{"id":"T3","span":{"begin":775,"end":780},"obj":"Body_part"},{"id":"T4","span":{"begin":836,"end":841},"obj":"Body_part"},{"id":"T5","span":{"begin":945,"end":959},"obj":"Body_part"},{"id":"T6","span":{"begin":1641,"end":1646},"obj":"Body_part"},{"id":"T7","span":{"begin":1856,"end":1861},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/GO_0005886"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":88,"end":93},"obj":"Body_part"},{"id":"T2","span":{"begin":498,"end":503},"obj":"Body_part"},{"id":"T3","span":{"begin":775,"end":780},"obj":"Body_part"},{"id":"T4","span":{"begin":836,"end":841},"obj":"Body_part"},{"id":"T5","span":{"begin":945,"end":959},"obj":"Body_part"},{"id":"T6","span":{"begin":1641,"end":1646},"obj":"Body_part"},{"id":"T7","span":{"begin":1654,"end":1661},"obj":"Body_part"},{"id":"T8","span":{"begin":1856,"end":1861},"obj":"Body_part"},{"id":"T9","span":{"begin":1869,"end":1876},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:14543"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:14543"},{"id":"A3","pred":"db_id","subj":"T3","obj":"FMA:14543"},{"id":"A4","pred":"db_id","subj":"T4","obj":"FMA:14543"},{"id":"A5","pred":"db_id","subj":"T5","obj":"FMA:63841"},{"id":"A6","pred":"db_id","subj":"T6","obj":"FMA:14543"},{"id":"A7","pred":"db_id","subj":"T7","obj":"FMA:9637"},{"id":"A8","pred":"db_id","subj":"T8","obj":"FMA:14543"},{"id":"A9","pred":"db_id","subj":"T9","obj":"FMA:9637"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":88,"end":93},"obj":"Body_part"},{"id":"T2","span":{"begin":498,"end":503},"obj":"Body_part"},{"id":"T3","span":{"begin":775,"end":780},"obj":"Body_part"},{"id":"T4","span":{"begin":836,"end":841},"obj":"Body_part"},{"id":"T5","span":{"begin":1641,"end":1646},"obj":"Body_part"},{"id":"T6","span":{"begin":1856,"end":1861},"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"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"A6","pred":"mat_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MAT_0000526"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":88,"end":93},"obj":"Body_part"},{"id":"T2","span":{"begin":498,"end":503},"obj":"Body_part"},{"id":"T3","span":{"begin":775,"end":780},"obj":"Body_part"},{"id":"T4","span":{"begin":836,"end":841},"obj":"Body_part"},{"id":"T5","span":{"begin":945,"end":959},"obj":"Body_part"},{"id":"T6","span":{"begin":1641,"end":1646},"obj":"Body_part"},{"id":"T7","span":{"begin":1856,"end":1861},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/GO_0005886"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":88,"end":93},"obj":"Body_part"},{"id":"T2","span":{"begin":498,"end":503},"obj":"Body_part"},{"id":"T3","span":{"begin":775,"end":780},"obj":"Body_part"},{"id":"T4","span":{"begin":836,"end":841},"obj":"Body_part"},{"id":"T5","span":{"begin":1641,"end":1646},"obj":"Body_part"},{"id":"T6","span":{"begin":1856,"end":1861},"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"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"A6","pred":"mat_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MAT_0000526"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":842,"end":854},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0001064"}],"text":"Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon.\nThe carbohydrate determinants Sd(a) and sialyl Lewis x (sLex) both result from substitution of an alpha2,3-sialylated type 2 chain: the first with an N-acetylgalactosamine (GalNAc) beta1,4-linked to Gal and the second by an alpha1,3-linked fucose on N-acetylglucosamine. The Sd(a) antigen is synthesized by Sd(a) beta1,4-N-acetylgalactosaminyltransferase II (beta4GalNAcT-II), which is downregulated in colon cancer, whereas sLex is a cancer-associated antigen. In view of the possible competition between beta4GalNAcT-II and the fucosyltransferases (FucTs) synthesizing the sLex antigen, we investigated whether beta4GalNAcT-II acts as a negative regulator of sLex expression in colon cancer. beta4GalNAcT-II cDNA, when expressed in LS174T colon cancer cells, induces the expression of the Sd(a) antigen, a dramatic inhibition of sLex expression on cell membranes, and the replacement of sLex with the Sd(a) antigen on 290 kDa glycoproteins. Unexpectedly, in colorectal cancer specimens, beta4GalNAcT-II and sLex show a direct relation. The reasons appear to be (i) Sd(a) and sLex antigens are expressed by different glycoproteins of 340 and 290 kDa, respectively; (ii) the activity of alpha1,3-FucTs on 3'-sialyllactosamine parallels that of beta4GalNAcT-II; and (iii) both beta4GalNAcT-II and FucT activities parallel sLex expression. Quantitative reverse transcription-polymerase chain reaction analysis reveals that the transcripts of beta4GalNAcT-II and those of FucT-III and FucT-VII are positively correlated. These data indicate that in colon cancer tissues, the sLex antigen is regulated mainly by the total FucT activity on 3'-sialyllactosamine acceptors and that beta4GalNAcT-II can inhibit sLex expression in an experimental model, although not in colon cancer tissues."}