PubMed:17172261 JSONTXT

{"project":"Glycosmos15-CL","denotations":[{"id":"T1","span":{"begin":194,"end":204},"obj":"Cell"},{"id":"T2","span":{"begin":213,"end":223},"obj":"Cell"},{"id":"T3","span":{"begin":271,"end":282},"obj":"Cell"},{"id":"T4","span":{"begin":613,"end":623},"obj":"Cell"},{"id":"T5","span":{"begin":1591,"end":1601},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000542"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000542"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000542"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000542"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000542"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

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{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":447,"end":469},"obj":"http://www.glycoepitope.jp/epitopes/EP0014"},{"id":"T2","span":{"begin":455,"end":469},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T3","span":{"begin":991,"end":1013},"obj":"http://www.glycoepitope.jp/epitopes/EP0014"},{"id":"T4","span":{"begin":999,"end":1013},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T5","span":{"begin":1336,"end":1351},"obj":"http://www.glycoepitope.jp/epitopes/EP0085"},{"id":"T6","span":{"begin":1449,"end":1463},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T7","span":{"begin":1523,"end":1537},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T8","span":{"begin":1662,"end":1684},"obj":"http://www.glycoepitope.jp/epitopes/EP0014"},{"id":"T9","span":{"begin":1670,"end":1684},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T10","span":{"begin":1686,"end":1709},"obj":"http://www.glycoepitope.jp/epitopes/EP0014"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":124,"end":134},"obj":"http://purl.obolibrary.org/obo/MAT_0000197"},{"id":"T2","span":{"begin":124,"end":134},"obj":"http://purl.obolibrary.org/obo/MAT_0000442"},{"id":"T3","span":{"begin":124,"end":129},"obj":"http://purl.obolibrary.org/obo/MAT_0000055"},{"id":"T4","span":{"begin":378,"end":389},"obj":"http://purl.obolibrary.org/obo/MAT_0000197"},{"id":"T5","span":{"begin":378,"end":389},"obj":"http://purl.obolibrary.org/obo/MAT_0000442"},{"id":"T6","span":{"begin":378,"end":383},"obj":"http://purl.obolibrary.org/obo/MAT_0000055"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

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{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":148,"end":156},"obj":"http://www.uniprot.org/uniprot/Q11130"},{"id":"T2","span":{"begin":568,"end":576},"obj":"http://www.uniprot.org/uniprot/Q11130"},{"id":"T3","span":{"begin":701,"end":709},"obj":"http://www.uniprot.org/uniprot/Q11130"},{"id":"T4","span":{"begin":768,"end":776},"obj":"http://www.uniprot.org/uniprot/Q11130"},{"id":"T5","span":{"begin":1783,"end":1791},"obj":"http://www.uniprot.org/uniprot/Q11130"},{"id":"T6","span":{"begin":544,"end":566},"obj":"http://www.uniprot.org/uniprot/Q11130"},{"id":"T7","span":{"begin":257,"end":267},"obj":"http://www.uniprot.org/uniprot/P14151"},{"id":"T8","span":{"begin":288,"end":298},"obj":"http://www.uniprot.org/uniprot/P14151"},{"id":"T9","span":{"begin":391,"end":401},"obj":"http://www.uniprot.org/uniprot/P14151"},{"id":"T10","span":{"begin":900,"end":910},"obj":"http://www.uniprot.org/uniprot/P14151"},{"id":"T11","span":{"begin":1975,"end":1985},"obj":"http://www.uniprot.org/uniprot/P14151"},{"id":"T12","span":{"begin":288,"end":306},"obj":"http://www.uniprot.org/uniprot/Q8NCG5"},{"id":"T13","span":{"begin":391,"end":409},"obj":"http://www.uniprot.org/uniprot/Q8NCG5"},{"id":"T14","span":{"begin":1975,"end":1992},"obj":"http://www.uniprot.org/uniprot/Q8NCG5"},{"id":"T15","span":{"begin":882,"end":890},"obj":"http://www.uniprot.org/uniprot/Q8IVK1"},{"id":"T16","span":{"begin":1734,"end":1742},"obj":"http://www.uniprot.org/uniprot/Q8IVK1"},{"id":"T17","span":{"begin":1808,"end":1816},"obj":"http://www.uniprot.org/uniprot/Q8IVK1"},{"id":"T18","span":{"begin":1118,"end":1139},"obj":"http://www.uniprot.org/uniprot/P34059"},{"id":"T19","span":{"begin":1370,"end":1374},"obj":"http://www.uniprot.org/uniprot/O43916"},{"id":"T20","span":{"begin":1415,"end":1419},"obj":"http://www.uniprot.org/uniprot/O43916"},{"id":"T21","span":{"begin":1549,"end":1553},"obj":"http://www.uniprot.org/uniprot/O43916"},{"id":"T22","span":{"begin":1774,"end":1778},"obj":"http://www.uniprot.org/uniprot/O43916"},{"id":"T23","span":{"begin":1880,"end":1884},"obj":"http://www.uniprot.org/uniprot/O43916"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":148,"end":156},"obj":"http://www.uniprot.org/uniprot/Q11131"},{"id":"T2","span":{"begin":568,"end":576},"obj":"http://www.uniprot.org/uniprot/Q11131"},{"id":"T3","span":{"begin":701,"end":709},"obj":"http://www.uniprot.org/uniprot/Q11131"},{"id":"T4","span":{"begin":768,"end":776},"obj":"http://www.uniprot.org/uniprot/Q11131"},{"id":"T5","span":{"begin":1783,"end":1791},"obj":"http://www.uniprot.org/uniprot/Q11131"},{"id":"T6","span":{"begin":544,"end":566},"obj":"http://www.uniprot.org/uniprot/Q11131"},{"id":"T7","span":{"begin":257,"end":267},"obj":"http://www.uniprot.org/uniprot/P18337"},{"id":"T8","span":{"begin":288,"end":298},"obj":"http://www.uniprot.org/uniprot/P18337"},{"id":"T9","span":{"begin":391,"end":401},"obj":"http://www.uniprot.org/uniprot/P18337"},{"id":"T10","span":{"begin":900,"end":910},"obj":"http://www.uniprot.org/uniprot/P18337"},{"id":"T11","span":{"begin":1975,"end":1985},"obj":"http://www.uniprot.org/uniprot/P18337"},{"id":"T12","span":{"begin":882,"end":890},"obj":"http://www.uniprot.org/uniprot/Q02596"},{"id":"T13","span":{"begin":1734,"end":1742},"obj":"http://www.uniprot.org/uniprot/Q02596"},{"id":"T14","span":{"begin":1808,"end":1816},"obj":"http://www.uniprot.org/uniprot/Q02596"},{"id":"T15","span":{"begin":1370,"end":1374},"obj":"http://www.uniprot.org/uniprot/Q9EQC0"},{"id":"T16","span":{"begin":1415,"end":1419},"obj":"http://www.uniprot.org/uniprot/Q9EQC0"},{"id":"T17","span":{"begin":1549,"end":1553},"obj":"http://www.uniprot.org/uniprot/Q9EQC0"},{"id":"T18","span":{"begin":1774,"end":1778},"obj":"http://www.uniprot.org/uniprot/Q9EQC0"},{"id":"T19","span":{"begin":1880,"end":1884},"obj":"http://www.uniprot.org/uniprot/Q9EQC0"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":1160,"end":1174},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/4202"},{"id":"T2","span":{"begin":1495,"end":1500},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T3","span":{"begin":1574,"end":1579},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":1645,"end":1650},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T5","span":{"begin":1752,"end":1757},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":81,"end":89},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T2","span":{"begin":512,"end":520},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T3","span":{"begin":1121,"end":1129},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T4","span":{"begin":1278,"end":1286},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T5","span":{"begin":1344,"end":1351},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T6","span":{"begin":148,"end":152},"obj":"http://purl.obolibrary.org/obo/GO_0008424"},{"id":"T7","span":{"begin":568,"end":572},"obj":"http://purl.obolibrary.org/obo/GO_0008424"},{"id":"T8","span":{"begin":701,"end":705},"obj":"http://purl.obolibrary.org/obo/GO_0008424"},{"id":"T9","span":{"begin":768,"end":772},"obj":"http://purl.obolibrary.org/obo/GO_0008424"},{"id":"T10","span":{"begin":1783,"end":1787},"obj":"http://purl.obolibrary.org/obo/GO_0008424"},{"id":"T11","span":{"begin":1899,"end":1903},"obj":"http://purl.obolibrary.org/obo/GO_0008424"},{"id":"T12","span":{"begin":455,"end":461},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T13","span":{"begin":999,"end":1005},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T14","span":{"begin":1449,"end":1455},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T15","span":{"begin":1523,"end":1529},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T16","span":{"begin":1670,"end":1676},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T17","span":{"begin":483,"end":493},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T18","span":{"begin":495,"end":506},"obj":"http://purl.obolibrary.org/obo/GO_0036065"},{"id":"T19","span":{"begin":965,"end":976},"obj":"http://purl.obolibrary.org/obo/GO_0036065"},{"id":"T20","span":{"begin":2016,"end":2028},"obj":"http://purl.obolibrary.org/obo/GO_0036065"},{"id":"T21","span":{"begin":1336,"end":1368},"obj":"http://purl.obolibrary.org/obo/GO_0045130"},{"id":"T22","span":{"begin":1490,"end":1493},"obj":"http://purl.obolibrary.org/obo/GO_0043848"},{"id":"T23","span":{"begin":1641,"end":1644},"obj":"http://purl.obolibrary.org/obo/GO_0043848"},{"id":"T24","span":{"begin":1748,"end":1751},"obj":"http://purl.obolibrary.org/obo/GO_0043848"},{"id":"T25","span":{"begin":1944,"end":1976},"obj":"http://purl.obolibrary.org/obo/GO_1903196"},{"id":"T26","span":{"begin":1962,"end":1971},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":246,"end":253},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":246,"end":253},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T3","span":{"begin":246,"end":253},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T4","span":{"begin":246,"end":253},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T5","span":{"begin":259,"end":267},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T6","span":{"begin":290,"end":298},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T7","span":{"begin":393,"end":401},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T8","span":{"begin":902,"end":910},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T9","span":{"begin":1977,"end":1985},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T10","span":{"begin":299,"end":306},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T11","span":{"begin":402,"end":409},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12","span":{"begin":1986,"end":1992},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":1495,"end":1500},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":1574,"end":1579},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":1645,"end":1650},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":1752,"end":1757},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":1792,"end":1795},"obj":"http://purl.obolibrary.org/obo/GO_0005731"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":113,"end":134},"obj":"http://purl.obolibrary.org/obo/UBERON_0003968"},{"id":"T2","span":{"begin":124,"end":129},"obj":"http://purl.obolibrary.org/obo/UBERON_0002391"},{"id":"T3","span":{"begin":378,"end":383},"obj":"http://purl.obolibrary.org/obo/UBERON_0002391"},{"id":"T4","span":{"begin":124,"end":134},"obj":"http://purl.obolibrary.org/obo/UBERON_0000029"},{"id":"T5","span":{"begin":378,"end":389},"obj":"http://purl.obolibrary.org/obo/UBERON_0000029"},{"id":"T6","span":{"begin":335,"end":342},"obj":"http://purl.obolibrary.org/obo/UBERON_0001979"},{"id":"T7","span":{"begin":367,"end":389},"obj":"http://purl.obolibrary.org/obo/UBERON_0002509"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":124,"end":129},"obj":"http://purl.obolibrary.org/obo/MAT_0000055"},{"id":"T2","span":{"begin":124,"end":134},"obj":"http://purl.obolibrary.org/obo/MAT_0000442"},{"id":"T3","span":{"begin":124,"end":134},"obj":"http://purl.obolibrary.org/obo/MAT_0000197"},{"id":"T4","span":{"begin":378,"end":383},"obj":"http://purl.obolibrary.org/obo/MAT_0000055"},{"id":"T5","span":{"begin":378,"end":389},"obj":"http://purl.obolibrary.org/obo/MAT_0000442"},{"id":"T6","span":{"begin":378,"end":389},"obj":"http://purl.obolibrary.org/obo/MAT_0000197"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":455,"end":467},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T2","span":{"begin":999,"end":1011},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T3","span":{"begin":1449,"end":1461},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T4","span":{"begin":1523,"end":1535},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T5","span":{"begin":1670,"end":1682},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T6","span":{"begin":1695,"end":1707},"obj":"http://rdf.glycoinfo.org/glycan/G00053MO"},{"id":"T7","span":{"begin":455,"end":469},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T8","span":{"begin":999,"end":1013},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T9","span":{"begin":1449,"end":1463},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T10","span":{"begin":1523,"end":1537},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T11","span":{"begin":1670,"end":1684},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T12","span":{"begin":1695,"end":1709},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T13","span":{"begin":462,"end":467},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T14","span":{"begin":1006,"end":1011},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T15","span":{"begin":1456,"end":1461},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T16","span":{"begin":1530,"end":1535},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T17","span":{"begin":1677,"end":1682},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T18","span":{"begin":1702,"end":1707},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T19","span":{"begin":462,"end":469},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T20","span":{"begin":1006,"end":1013},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T21","span":{"begin":1456,"end":1463},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T22","span":{"begin":1530,"end":1537},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T23","span":{"begin":1677,"end":1684},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T24","span":{"begin":1702,"end":1709},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T25","span":{"begin":1336,"end":1351},"obj":"http://rdf.glycoinfo.org/glycan/G00020MO"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":257,"end":267},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T2","span":{"begin":288,"end":298},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T3","span":{"begin":391,"end":401},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T4","span":{"begin":900,"end":910},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T5","span":{"begin":1975,"end":1985},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T6","span":{"begin":259,"end":267},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T7","span":{"begin":290,"end":298},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T8","span":{"begin":393,"end":401},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T9","span":{"begin":902,"end":910},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T10","span":{"begin":1977,"end":1985},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T11","span":{"begin":259,"end":267},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T12","span":{"begin":290,"end":298},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T13","span":{"begin":393,"end":401},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T14","span":{"begin":902,"end":910},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T15","span":{"begin":1977,"end":1985},"obj":"https://acgg.asia/db/lfdb/LfDB0043"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":462,"end":469},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":1006,"end":1013},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":1456,"end":1463},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T4","span":{"begin":1530,"end":1537},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T5","span":{"begin":1677,"end":1684},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T6","span":{"begin":1702,"end":1709},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T7","span":{"begin":455,"end":467},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T8","span":{"begin":999,"end":1011},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T9","span":{"begin":1449,"end":1461},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T10","span":{"begin":1523,"end":1535},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T11","span":{"begin":1670,"end":1682},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T12","span":{"begin":1695,"end":1707},"obj":"http://www.glycoepitope.jp/epitopes/EP0008"},{"id":"PD-GlycoEpitope-B_T13","span":{"begin":455,"end":469},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T14","span":{"begin":999,"end":1013},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T15","span":{"begin":1449,"end":1463},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T16","span":{"begin":1523,"end":1537},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T17","span":{"begin":1670,"end":1684},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T18","span":{"begin":1695,"end":1709},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"PD-GlycoEpitope-B_T19","span":{"begin":447,"end":469},"obj":"http://www.glycoepitope.jp/epitopes/EP0014"},{"id":"PD-GlycoEpitope-B_T20","span":{"begin":991,"end":1013},"obj":"http://www.glycoepitope.jp/epitopes/EP0014"},{"id":"PD-GlycoEpitope-B_T21","span":{"begin":1662,"end":1684},"obj":"http://www.glycoepitope.jp/epitopes/EP0014"},{"id":"PD-GlycoEpitope-B_T22","span":{"begin":1686,"end":1709},"obj":"http://www.glycoepitope.jp/epitopes/EP0014"},{"id":"PD-GlycoEpitope-B_T23","span":{"begin":1336,"end":1351},"obj":"http://www.glycoepitope.jp/epitopes/EP0085"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G93924TT\""},{"id":"GlycanIUPAC_T2","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G93924TT\""},{"id":"GlycanIUPAC_T3","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G25565DN\""},{"id":"GlycanIUPAC_T4","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G25565DN\""},{"id":"GlycanIUPAC_T5","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G97215EV\""},{"id":"GlycanIUPAC_T6","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G97215EV\""},{"id":"GlycanIUPAC_T7","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G79664KO\""},{"id":"GlycanIUPAC_T8","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G79664KO\""},{"id":"GlycanIUPAC_T9","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G24107FU\""},{"id":"GlycanIUPAC_T10","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G24107FU\""},{"id":"GlycanIUPAC_T11","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G09864UE\""},{"id":"GlycanIUPAC_T12","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G09864UE\""},{"id":"GlycanIUPAC_T13","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G28032MC\""},{"id":"GlycanIUPAC_T14","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G28032MC\""},{"id":"GlycanIUPAC_T15","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G28005UP\""},{"id":"GlycanIUPAC_T16","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G28005UP\""},{"id":"GlycanIUPAC_T17","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G92708AT\""},{"id":"GlycanIUPAC_T18","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G92708AT\""},{"id":"GlycanIUPAC_T19","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G73757UC\""},{"id":"GlycanIUPAC_T20","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G73757UC\""},{"id":"GlycanIUPAC_T21","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G51062DM\""},{"id":"GlycanIUPAC_T22","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G51062DM\""},{"id":"GlycanIUPAC_T23","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G05866BJ\""},{"id":"GlycanIUPAC_T24","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G05866BJ\""},{"id":"GlycanIUPAC_T25","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G87394FZ\""},{"id":"GlycanIUPAC_T26","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G87394FZ\""},{"id":"GlycanIUPAC_T27","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G03871NF\""},{"id":"GlycanIUPAC_T28","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G03871NF\""},{"id":"GlycanIUPAC_T29","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G29377VE\""},{"id":"GlycanIUPAC_T30","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G29377VE\""},{"id":"GlycanIUPAC_T31","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G33457CX\""},{"id":"GlycanIUPAC_T32","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G33457CX\""},{"id":"GlycanIUPAC_T33","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G97368GU\""},{"id":"GlycanIUPAC_T34","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G97368GU\""},{"id":"GlycanIUPAC_T35","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G18512EL\""},{"id":"GlycanIUPAC_T36","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G18512EL\""},{"id":"GlycanIUPAC_T37","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G41137VS\""},{"id":"GlycanIUPAC_T38","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G41137VS\""},{"id":"GlycanIUPAC_T39","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G30521NA\""},{"id":"GlycanIUPAC_T40","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G30521NA\""},{"id":"GlycanIUPAC_T41","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G19388CD\""},{"id":"GlycanIUPAC_T42","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G19388CD\""},{"id":"GlycanIUPAC_T43","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G53151FU\""},{"id":"GlycanIUPAC_T44","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G53151FU\""},{"id":"GlycanIUPAC_T45","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glyc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AC_T180","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G31834HW\""},{"id":"GlycanIUPAC_T181","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G35324RT\""},{"id":"GlycanIUPAC_T182","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G35324RT\""},{"id":"GlycanIUPAC_T183","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G34803QO\""},{"id":"GlycanIUPAC_T184","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G34803QO\""},{"id":"GlycanIUPAC_T185","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G92898FF\""},{"id":"GlycanIUPAC_T186","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G92898FF\""},{"id":"GlycanIUPAC_T187","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G01318VX\""},{"id":"GlycanIUPAC_T188","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G01318VX\""},{"id":"GlycanIUPAC_T189","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G83200MX\""},{"id":"GlycanIUPAC_T190","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G83200MX\""},{"id":"GlycanIUPAC_T191","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G56286UC\""},{"id":"GlycanIUPAC_T192","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G56286UC\""},{"id":"GlycanIUPAC_T193","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G07304QA\""},{"id":"GlycanIUPAC_T194","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G07304QA\""},{"id":"GlycanIUPAC_T195","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G06868OU\""},{"id":"GlycanIUPAC_T196","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G06868OU\""},{"id":"GlycanIUPAC_T197","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G12647BS\""},{"id":"GlycanIUPAC_T198","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G12647BS\""},{"id":"GlycanIUPAC_T199","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G51841DF\""},{"id":"GlycanIUPAC_T200","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G51841DF\""},{"id":"GlycanIUPAC_T201","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G32122AJ\""},{"id":"GlycanIUPAC_T202","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G32122AJ\""},{"id":"GlycanIUPAC_T203","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G41125MN\""},{"id":"GlycanIUPAC_T204","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G41125MN\""},{"id":"GlycanIUPAC_T205","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G16093XS\""},{"id":"GlycanIUPAC_T206","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G16093XS\""},{"id":"GlycanIUPAC_T207","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G62425IX\""},{"id":"GlycanIUPAC_T208","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G62425IX\""},{"id":"GlycanIUPAC_T209","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G15673TO\""},{"id":"GlycanIUPAC_T210","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G15673TO\""},{"id":"GlycanIUPAC_T211","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G32857IK\""},{"id":"GlycanIUPAC_T212","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G32857IK\""},{"id":"GlycanIUPAC_T213","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G60047CJ\""},{"id":"GlycanIUPAC_T214","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G60047CJ\""},{"id":"GlycanIUPAC_T215","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G55718ZB\""},{"id":"GlycanIUPAC_T216","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G55718ZB\""},{"id":"GlycanIUPAC_T217","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G88355ZE\""},{"id":"GlycanIUPAC_T218","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G88355ZE\""},{"id":"GlycanIUPAC_T219","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G11283PA\""},{"id":"GlycanIUPAC_T220","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G11283PA\""},{"id":"GlycanIUPAC_T221","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G71737IZ\""},{"id":"GlycanIUPAC_T222","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G71737IZ\""},{"id":"GlycanIUPAC_T223","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G60912WZ\""},{"id":"GlycanIUPAC_T224","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G60912WZ\""},{"id":"GlycanIUPAC_T225","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G99655SO\""},{"id":"GlycanIUPAC_T226","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G99655SO\""},{"id":"GlycanIUPAC_T227","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G10300TW\""},{"id":"GlycanIUPAC_T228","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G10300TW\""},{"id":"GlycanIUPAC_T229","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G89509FL\""},{"id":"GlycanIUPAC_T230","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G89509FL\""},{"id":"GlycanIUPAC_T231","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G31465TH\""},{"id":"GlycanIUPAC_T232","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G31465TH\""},{"id":"GlycanIUPAC_T233","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G94101LU\""},{"id":"GlycanIUPAC_T234","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G94101LU\""},{"id":"GlycanIUPAC_T235","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G38610BB\""},{"id":"GlycanIUPAC_T236","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G38610BB\""},{"id":"GlycanIUPAC_T237","span":{"begin":1141,"end":1144},"obj":"\"http://rdf.glycoinfo.org/glycan/G85893UF\""},{"id":"GlycanIUPAC_T238","span":{"begin":1287,"end":1290},"obj":"\"http://rdf.glycoinfo.org/glycan/G85893UF\""}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":124,"end":129},"obj":"http://purl.obolibrary.org/obo/UBERON_0002391"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":378,"end":383},"obj":"http://purl.obolibrary.org/obo/UBERON_0002391"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":124,"end":134},"obj":"http://purl.obolibrary.org/obo/UBERON_0000029"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":378,"end":389},"obj":"http://purl.obolibrary.org/obo/UBERON_0000029"},{"id":"PD-UBERON-AE-B_T5","span":{"begin":113,"end":134},"obj":"http://purl.obolibrary.org/obo/UBERON_0003968"},{"id":"PD-UBERON-AE-B_T6","span":{"begin":335,"end":342},"obj":"http://purl.obolibrary.org/obo/UBERON_0001979"},{"id":"PD-UBERON-AE-B_T7","span":{"begin":367,"end":389},"obj":"http://purl.obolibrary.org/obo/UBERON_0002509"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":124,"end":134},"obj":"Body_part"},{"id":"T3","span":{"begin":378,"end":389},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000197"},{"id":"A2","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000442"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000197"},{"id":"A4","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000442"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":167,"end":171},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":715,"end":719},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":782,"end":786},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":1084,"end":1088},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1467,"end":1482},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":1829,"end":1833},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10088"},{"id":"A2","pred":"db_id","subj":"T2","obj":"10088"},{"id":"A3","pred":"db_id","subj":"T3","obj":"10088"},{"id":"A4","pred":"db_id","subj":"T4","obj":"10088"},{"id":"A5","pred":"db_id","subj":"T5","obj":"10029"},{"id":"A6","pred":"db_id","subj":"T6","obj":"10088"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"Glycosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":447,"end":469},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":991,"end":1013},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":1336,"end":1351},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":1449,"end":1463},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":1523,"end":1537},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":1662,"end":1684},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":1686,"end":1709},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0014"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0014"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0085"},{"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/EP0014"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0014"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":113,"end":134},"obj":"Body_part"},{"id":"T2","span":{"begin":194,"end":204},"obj":"Body_part"},{"id":"T3","span":{"begin":213,"end":223},"obj":"Body_part"},{"id":"T4","span":{"begin":271,"end":282},"obj":"Body_part"},{"id":"T5","span":{"begin":318,"end":342},"obj":"Body_part"},{"id":"T6","span":{"begin":344,"end":347},"obj":"Body_part"},{"id":"T7","span":{"begin":367,"end":389},"obj":"Body_part"},{"id":"T8","span":{"begin":613,"end":623},"obj":"Body_part"},{"id":"T9","span":{"begin":1483,"end":1488},"obj":"Body_part"},{"id":"T10","span":{"begin":1591,"end":1601},"obj":"Body_part"},{"id":"T11","span":{"begin":1822,"end":1825},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0003968"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000542"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL_0000542"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000542"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_8410037"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_8410037"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0002509"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/CL_0000542"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0000992"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/CL_0000542"},{"id":"A11","pred":"uberon_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/UBERON_8410037"}],"text":"Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.\nLymphocyte homing is mediated by binding of L-selectin on lymphocytes with L-selectin ligands present on high-endothelial venules (HEV) of peripheral and mesenteric lymph nodes. L-selectin ligands are specific O-linked carbohydrates, 6-sulfo sialyl Lewis X, composed of sialylated, fucosylated, and sulfated glycans. Abrogation of fucosyltransferase-VII (FucT-VII) results in almost complete loss of lymphocyte homing, but structural analysis of carbohydrates has not been carried out on FucT-VII null mice. To determine whether functional losses seen in FucT-VII null mice are caused by structural changes in carbohydrates, we elucidated the carbohydrate structure of GlyCAM-1, a major L-selectin counter-receptor. Our results show that most alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X are absent and 6-sulfo N-acetyllactosamine is increased in the mutant mice. Surprisingly, the amount of 6'-sulfated galactose (Gal) that bound to Sumbucus nigra agglutinin column was also increased. We found that structures of those oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase (KSST). We then showed that overexpression of KSST suppresses the expression of sialyl Lewis X on Chinese hamster ovary (CHO) cells engineered to express sialyl Lewis X. Moreover, KSST expression in those cells suppressed lymphocyte rolling compared with mock-transfected CHO cells expressing 6-sulfo sialyl Lewis X. 6'-Sulfo sialyl Lewis X can neither be found in GlyCAM-1 from CHO cells expressing both KSST and FucT-VII nor be found in GlyCAM-1 from HEV of mice. These results combined together suggest that KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation."}