PubMed:12626414 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":502,"end":514},"obj":"https://glytoucan.org/Structures/Glycans/G80722US"},{"id":"T2","span":{"begin":1571,"end":1583},"obj":"https://glytoucan.org/Structures/Glycans/G80722US"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GlyCosmos600-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":502,"end":514},"obj":"https://glytoucan.org/Structures/Glycans/G80722US"},{"id":"T2","span":{"begin":1571,"end":1583},"obj":"https://glytoucan.org/Structures/Glycans/G80722US"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GlyCosmos600-CLO","denotations":[{"id":"T1","span":{"begin":368,"end":385},"obj":"http://purl.obolibrary.org/obo/CL_0000115"},{"id":"T2","span":{"begin":1286,"end":1290},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":1607,"end":1612},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":502,"end":514},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":1571,"end":1583},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G80722US"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G53231FE"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G80722US"},{"id":"A4","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G53231FE"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GlyCosmos600-GlycoGenes2","denotations":[{"id":"T1","span":{"begin":71,"end":82},"obj":"https://acgg.asia/db/ggdb/info/gg029"},{"id":"T2","span":{"begin":84,"end":95},"obj":"https://acgg.asia/db/ggdb/info/gg029"},{"id":"T3","span":{"begin":253,"end":264},"obj":"https://acgg.asia/db/ggdb/info/gg034"},{"id":"T4","span":{"begin":283,"end":296},"obj":"https://acgg.asia/db/ggdb/info/gg034"},{"id":"T5","span":{"begin":300,"end":304},"obj":"https://acgg.asia/db/ggdb/info/gg034"},{"id":"T6","span":{"begin":783,"end":794},"obj":"https://acgg.asia/db/ggdb/info/gg029"},{"id":"T7","span":{"begin":796,"end":807},"obj":"https://acgg.asia/db/ggdb/info/gg029"},{"id":"T8","span":{"begin":1055,"end":1066},"obj":"https://acgg.asia/db/ggdb/info/gg028"},{"id":"T9","span":{"begin":1068,"end":1079},"obj":"https://acgg.asia/db/ggdb/info/gg034"},{"id":"T10","span":{"begin":1337,"end":1348},"obj":"https://acgg.asia/db/ggdb/info/gg029"},{"id":"T11","span":{"begin":1441,"end":1452},"obj":"https://acgg.asia/db/ggdb/info/gg034"},{"id":"T12","span":{"begin":1454,"end":1465},"obj":"https://acgg.asia/db/ggdb/info/gg029"},{"id":"T13","span":{"begin":1647,"end":1658},"obj":"https://acgg.asia/db/ggdb/info/gg029"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":122},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":123,"end":238},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":239,"end":440},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":441,"end":691},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":692,"end":809},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":810,"end":1218},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1219,"end":1425},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1426,"end":1613},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1614,"end":1726},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":122},"obj":"Sentence"},{"id":"T2","span":{"begin":123,"end":238},"obj":"Sentence"},{"id":"T3","span":{"begin":239,"end":440},"obj":"Sentence"},{"id":"T4","span":{"begin":441,"end":691},"obj":"Sentence"},{"id":"T5","span":{"begin":692,"end":809},"obj":"Sentence"},{"id":"T6","span":{"begin":810,"end":1218},"obj":"Sentence"},{"id":"T7","span":{"begin":1219,"end":1425},"obj":"Sentence"},{"id":"T8","span":{"begin":1426,"end":1613},"obj":"Sentence"},{"id":"T9","span":{"begin":1614,"end":1726},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":502,"end":514},"obj":"https://glytoucan.org/Structures/Glycans/G80722US"},{"id":"T2","span":{"begin":1571,"end":1583},"obj":"https://glytoucan.org/Structures/Glycans/G80722US"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":396,"end":407},"obj":"http://purl.obolibrary.org/obo/MAT_0000197"},{"id":"T2","span":{"begin":396,"end":407},"obj":"http://purl.obolibrary.org/obo/MAT_0000442"},{"id":"T3","span":{"begin":396,"end":401},"obj":"http://purl.obolibrary.org/obo/MAT_0000055"},{"id":"T4","span":{"begin":679,"end":690},"obj":"http://purl.obolibrary.org/obo/MAT_0000197"},{"id":"T5","span":{"begin":679,"end":690},"obj":"http://purl.obolibrary.org/obo/MAT_0000442"},{"id":"T6","span":{"begin":679,"end":684},"obj":"http://purl.obolibrary.org/obo/MAT_0000055"},{"id":"T7","span":{"begin":1352,"end":1355},"obj":"http://purl.obolibrary.org/obo/MAT_0000043"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T18","span":{"begin":413,"end":432},"obj":"FMAID:62117"},{"id":"_T1","span":{"begin":41,"end":53},"obj":"FMAID:82737"},{"id":"_T2","span":{"begin":41,"end":53},"obj":"FMAID:197276"},{"id":"_T3","span":{"begin":368,"end":379},"obj":"FMAID:63916"},{"id":"_T4","span":{"begin":368,"end":379},"obj":"FMAID:162384"},{"id":"_T5","span":{"begin":368,"end":385},"obj":"FMAID:169653"},{"id":"_T6","span":{"begin":368,"end":385},"obj":"FMAID:66772"},{"id":"_T7","span":{"begin":368,"end":385},"obj":"FMAID:69075"},{"id":"_T8","span":{"begin":368,"end":385},"obj":"FMAID:164926"},{"id":"_T9","span":{"begin":380,"end":385},"obj":"FMAID:68646"},{"id":"_T10","span":{"begin":380,"end":385},"obj":"FMAID:169002"},{"id":"_T11","span":{"begin":393,"end":407},"obj":"FMAID:171664"},{"id":"_T12","span":{"begin":396,"end":401},"obj":"FMAID:97585"},{"id":"_T13","span":{"begin":396,"end":401},"obj":"FMAID:217076"},{"id":"_T14","span":{"begin":396,"end":407},"obj":"FMAID:91368"},{"id":"_T15","span":{"begin":396,"end":407},"obj":"FMAID:5034"},{"id":"_T16","span":{"begin":413,"end":424},"obj":"FMAID:63916"},{"id":"_T17","span":{"begin":413,"end":424},"obj":"FMAID:162384"},{"id":"_T19","span":{"begin":413,"end":432},"obj":"FMAID:67762"},{"id":"_T20","span":{"begin":413,"end":432},"obj":"FMAID:166404"},{"id":"_T21","span":{"begin":413,"end":432},"obj":"FMAID:166393"},{"id":"_T22","span":{"begin":425,"end":432},"obj":"FMAID:167505"},{"id":"_T23","span":{"begin":425,"end":432},"obj":"FMAID:63130"},{"id":"_T24","span":{"begin":625,"end":635},"obj":"FMAID:167267"},{"id":"_T25","span":{"begin":625,"end":635},"obj":"FMAID:62931"},{"id":"_T26","span":{"begin":625,"end":635},"obj":"FMAID:167265"},{"id":"_T27","span":{"begin":625,"end":635},"obj":"FMAID:62933"},{"id":"_T28","span":{"begin":625,"end":635},"obj":"FMAID:62932"},{"id":"_T29","span":{"begin":625,"end":635},"obj":"FMAID:167268"},{"id":"_T30","span":{"begin":627,"end":635},"obj":"FMAID:165243"},{"id":"_T31","span":{"begin":627,"end":635},"obj":"FMAID:61795"},{"id":"_T32","span":{"begin":655,"end":668},"obj":"FMAID:263010"},{"id":"_T33","span":{"begin":655,"end":668},"obj":"FMAID:263009"},{"id":"_T34","span":{"begin":658,"end":668},"obj":"FMAID:167163"},{"id":"_T35","span":{"begin":658,"end":668},"obj":"FMAID:167176"},{"id":"_T36","span":{"begin":658,"end":668},"obj":"FMAID:62869"},{"id":"_T37","span":{"begin":658,"end":668},"obj":"FMAID:62870"},{"id":"_T38","span":{"begin":658,"end":668},"obj":"FMAID:167173"},{"id":"_T39","span":{"begin":658,"end":668},"obj":"FMAID:167174"},{"id":"_T40","span":{"begin":658,"end":668},"obj":"FMAID:62863"},{"id":"_T41","span":{"begin":658,"end":668},"obj":"FMAID:167171"},{"id":"_T42","span":{"begin":679,"end":684},"obj":"FMAID:217076"},{"id":"_T43","span":{"begin":679,"end":684},"obj":"FMAID:97585"},{"id":"_T44","span":{"begin":679,"end":690},"obj":"FMAID:5034"},{"id":"_T45","span":{"begin":679,"end":690},"obj":"FMAID:91368"},{"id":"_T46","span":{"begin":868,"end":880},"obj":"FMAID:167256"},{"id":"_T47","span":{"begin":868,"end":880},"obj":"FMAID:62925"},{"id":"_T48","span":{"begin":976,"end":982},"obj":"FMAID:196724"},{"id":"_T49","span":{"begin":1169,"end":1182},"obj":"FMAID:167256"},{"id":"_T50","span":{"begin":1169,"end":1182},"obj":"FMAID:62925"},{"id":"_T51","span":{"begin":1265,"end":1272},"obj":"FMAID:256050"},{"id":"_T52","span":{"begin":1352,"end":1355},"obj":"FMAID:45615"},{"id":"_T53","span":{"begin":1352,"end":1355},"obj":"FMAID:141929"},{"id":"_T54","span":{"begin":1352,"end":1374},"obj":"FMAID:167120"},{"id":"_T55","span":{"begin":1352,"end":1374},"obj":"FMAID:62820"},{"id":"_T56","span":{"begin":1367,"end":1374},"obj":"FMAID:256050"},{"id":"_T57","span":{"begin":1413,"end":1424},"obj":"FMAID:167173"},{"id":"_T58","span":{"begin":1413,"end":1424},"obj":"FMAID:167163"},{"id":"_T59","span":{"begin":1413,"end":1424},"obj":"FMAID:167176"},{"id":"_T60","span":{"begin":1413,"end":1424},"obj":"FMAID:167171"},{"id":"_T61","span":{"begin":1413,"end":1424},"obj":"FMAID:62870"},{"id":"_T62","span":{"begin":1413,"end":1424},"obj":"FMAID:62863"},{"id":"_T63","span":{"begin":1413,"end":1424},"obj":"FMAID:167174"},{"id":"_T64","span":{"begin":1413,"end":1424},"obj":"FMAID:62869"},{"id":"_T65","span":{"begin":1607,"end":1612},"obj":"FMAID:68646"},{"id":"_T66","span":{"begin":1607,"end":1612},"obj":"FMAID:169002"},{"id":"_T67","span":{"begin":1620,"end":1626},"obj":"FMAID:171168"},{"id":"_T68","span":{"begin":1620,"end":1626},"obj":"FMAID:30332"},{"id":"_T69","span":{"begin":1715,"end":1725},"obj":"FMAID:62932"},{"id":"_T70","span":{"begin":1715,"end":1725},"obj":"FMAID:167267"},{"id":"_T71","span":{"begin":1715,"end":1725},"obj":"FMAID:62933"},{"id":"_T72","span":{"begin":1715,"end":1725},"obj":"FMAID:62931"},{"id":"_T73","span":{"begin":1715,"end":1725},"obj":"FMAID:167265"},{"id":"_T74","span":{"begin":1715,"end":1725},"obj":"FMAID:167268"},{"id":"_T75","span":{"begin":1717,"end":1725},"obj":"FMAID:165243"},{"id":"_T76","span":{"begin":1717,"end":1725},"obj":"FMAID:61795"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":71,"end":82},"obj":"http://www.uniprot.org/uniprot/Q9GZS9"},{"id":"T2","span":{"begin":783,"end":794},"obj":"http://www.uniprot.org/uniprot/Q9GZS9"},{"id":"T3","span":{"begin":1337,"end":1348},"obj":"http://www.uniprot.org/uniprot/Q9GZS9"},{"id":"T4","span":{"begin":1454,"end":1465},"obj":"http://www.uniprot.org/uniprot/Q9GZS9"},{"id":"T5","span":{"begin":84,"end":95},"obj":"http://www.uniprot.org/uniprot/Q9GZS9"},{"id":"T6","span":{"begin":796,"end":807},"obj":"http://www.uniprot.org/uniprot/Q9GZS9"},{"id":"T7","span":{"begin":253,"end":264},"obj":"http://www.uniprot.org/uniprot/Q8NCG5"},{"id":"T8","span":{"begin":1068,"end":1079},"obj":"http://www.uniprot.org/uniprot/Q8NCG5"},{"id":"T9","span":{"begin":283,"end":296},"obj":"http://www.uniprot.org/uniprot/Q8NCG5"},{"id":"T10","span":{"begin":300,"end":304},"obj":"http://www.uniprot.org/uniprot/Q8NCG5"},{"id":"T11","span":{"begin":283,"end":286},"obj":"http://www.uniprot.org/uniprot/O14777"},{"id":"T12","span":{"begin":408,"end":432},"obj":"http://www.uniprot.org/uniprot/Q14515"},{"id":"T13","span":{"begin":625,"end":635},"obj":"http://www.uniprot.org/uniprot/P14151"},{"id":"T14","span":{"begin":1715,"end":1725},"obj":"http://www.uniprot.org/uniprot/P14151"},{"id":"T15","span":{"begin":1065,"end":1077},"obj":"http://www.uniprot.org/uniprot/Q9Y4C5"},{"id":"T16","span":{"begin":1078,"end":1090},"obj":"http://www.uniprot.org/uniprot/P05162"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":71,"end":82},"obj":"http://www.uniprot.org/uniprot/Q9QUP4"},{"id":"T2","span":{"begin":783,"end":794},"obj":"http://www.uniprot.org/uniprot/Q9QUP4"},{"id":"T3","span":{"begin":1337,"end":1348},"obj":"http://www.uniprot.org/uniprot/Q9QUP4"},{"id":"T4","span":{"begin":1454,"end":1465},"obj":"http://www.uniprot.org/uniprot/Q9QUP4"},{"id":"T5","span":{"begin":84,"end":95},"obj":"http://www.uniprot.org/uniprot/Q9QUP4"},{"id":"T6","span":{"begin":796,"end":807},"obj":"http://www.uniprot.org/uniprot/Q9QUP4"},{"id":"T7","span":{"begin":253,"end":264},"obj":"http://www.uniprot.org/uniprot/Q9R1I1"},{"id":"T8","span":{"begin":1068,"end":1079},"obj":"http://www.uniprot.org/uniprot/Q9R1I1"},{"id":"T9","span":{"begin":283,"end":296},"obj":"http://www.uniprot.org/uniprot/Q9R1I1"},{"id":"T10","span":{"begin":300,"end":304},"obj":"http://www.uniprot.org/uniprot/Q9R1I1"},{"id":"T11","span":{"begin":625,"end":635},"obj":"http://www.uniprot.org/uniprot/P18337"},{"id":"T12","span":{"begin":1715,"end":1725},"obj":"http://www.uniprot.org/uniprot/P18337"},{"id":"T13","span":{"begin":1065,"end":1077},"obj":"http://www.uniprot.org/uniprot/Q80WV3"},{"id":"T14","span":{"begin":1078,"end":1090},"obj":"http://www.uniprot.org/uniprot/Q9CQW5"},{"id":"T15","span":{"begin":1087,"end":1092},"obj":"http://www.uniprot.org/uniprot/O54891"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":0,"end":10},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/190658"},{"id":"T2","span":{"begin":0,"end":10},"obj":"http://purl.bioontology.org/ontology/STY/T052"},{"id":"T3","span":{"begin":380,"end":385},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":749,"end":756},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/353209"},{"id":"T5","span":{"begin":1265,"end":1272},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T6","span":{"begin":1367,"end":1374},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T7","span":{"begin":1607,"end":1612},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T8","span":{"begin":1627,"end":1635},"obj":"http://purl.bioontology.org/ontology/STY/T033"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":957,"end":966},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T2","span":{"begin":1466,"end":1477},"obj":"http://purl.obolibrary.org/obo/GO_0006351"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":627,"end":635},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T2","span":{"begin":1717,"end":1725},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T3","span":{"begin":1703,"end":1710},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":380,"end":385},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":1286,"end":1290},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":396,"end":401},"obj":"http://purl.obolibrary.org/obo/UBERON_0002391"},{"id":"T2","span":{"begin":679,"end":684},"obj":"http://purl.obolibrary.org/obo/UBERON_0002391"},{"id":"T3","span":{"begin":396,"end":407},"obj":"http://purl.obolibrary.org/obo/UBERON_0000029"},{"id":"T4","span":{"begin":679,"end":690},"obj":"http://purl.obolibrary.org/obo/UBERON_0000029"},{"id":"T5","span":{"begin":425,"end":432},"obj":"http://purl.obolibrary.org/obo/UBERON_0001979"},{"id":"T6","span":{"begin":1265,"end":1272},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"T7","span":{"begin":1367,"end":1374},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":41,"end":53},"obj":"http://edamontology.org/topic_0152"},{"id":"T2","span":{"begin":1219,"end":1222},"obj":"http://edamontology.org/topic_0195"},{"id":"T3","span":{"begin":1235,"end":1240},"obj":"http://edamontology.org/topic_3512"},{"id":"T4","span":{"begin":1466,"end":1477},"obj":"http://edamontology.org/topic_0203"},{"id":"T5","span":{"begin":1466,"end":1477},"obj":"http://edamontology.org/topic_3512"},{"id":"T6","span":{"begin":1466,"end":1477},"obj":"http://edamontology.org/topic_0110"},{"id":"T7","span":{"begin":1466,"end":1477},"obj":"http://edamontology.org/topic_3308"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":15,"end":33},"obj":"http://edamontology.org/data_0928"},{"id":"T2","span":{"begin":277,"end":282},"obj":"http://edamontology.org/data_2099"},{"id":"T3","span":{"begin":515,"end":524},"obj":"http://edamontology.org/data_0883"},{"id":"T4","span":{"begin":597,"end":608},"obj":"http://edamontology.org/operation_2423"},{"id":"T5","span":{"begin":647,"end":654},"obj":"http://edamontology.org/operation_2409"},{"id":"T6","span":{"begin":647,"end":654},"obj":"http://edamontology.org/operation_0004"},{"id":"T7","span":{"begin":895,"end":901},"obj":"http://edamontology.org/data_2048"},{"id":"T8","span":{"begin":1219,"end":1231},"obj":"http://edamontology.org/operation_0473"},{"id":"T9","span":{"begin":1223,"end":1231},"obj":"http://edamontology.org/operation_2945"},{"id":"T10","span":{"begin":1558,"end":1566},"obj":"http://edamontology.org/operation_3429"},{"id":"T11","span":{"begin":1678,"end":1688},"obj":"http://edamontology.org/operation_3429"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":157,"end":163},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":396,"end":401},"obj":"http://purl.obolibrary.org/obo/MAT_0000055"},{"id":"T2","span":{"begin":396,"end":407},"obj":"http://purl.obolibrary.org/obo/MAT_0000197"},{"id":"T3","span":{"begin":396,"end":407},"obj":"http://purl.obolibrary.org/obo/MAT_0000442"},{"id":"T4","span":{"begin":679,"end":684},"obj":"http://purl.obolibrary.org/obo/MAT_0000055"},{"id":"T5","span":{"begin":679,"end":690},"obj":"http://purl.obolibrary.org/obo/MAT_0000442"},{"id":"T6","span":{"begin":679,"end":690},"obj":"http://purl.obolibrary.org/obo/MAT_0000197"},{"id":"T7","span":{"begin":1352,"end":1355},"obj":"http://purl.obolibrary.org/obo/MAT_0000043"},{"id":"T8","span":{"begin":1620,"end":1626},"obj":"http://purl.obolibrary.org/obo/MAT_0000488"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

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rser_T243","obj":"EnjuParser_T242"},{"id":"EnjuParser_R250","pred":"arg1Of","subj":"EnjuParser_T243","obj":"EnjuParser_T244"},{"id":"EnjuParser_R251","pred":"arg2Of","subj":"EnjuParser_T246","obj":"EnjuParser_T244"},{"id":"EnjuParser_R252","pred":"arg2Of","subj":"EnjuParser_T246","obj":"EnjuParser_T245"},{"id":"EnjuParser_R253","pred":"arg1Of","subj":"EnjuParser_T249","obj":"EnjuParser_T247"},{"id":"EnjuParser_R254","pred":"arg1Of","subj":"EnjuParser_T249","obj":"EnjuParser_T248"},{"id":"EnjuParser_R255","pred":"arg1Of","subj":"EnjuParser_T249","obj":"EnjuParser_T250"},{"id":"EnjuParser_R256","pred":"arg2Of","subj":"EnjuParser_T255","obj":"EnjuParser_T250"},{"id":"EnjuParser_R257","pred":"arg1Of","subj":"EnjuParser_T255","obj":"EnjuParser_T251"},{"id":"EnjuParser_R258","pred":"arg1Of","subj":"EnjuParser_T252","obj":"EnjuParser_T253"},{"id":"EnjuParser_R259","pred":"arg2Of","subj":"EnjuParser_T255","obj":"EnjuParser_T253"},{"id":"EnjuParser_R260","pred":"arg1Of","subj":"EnjuParser_T255","obj":"EnjuParser_T254"},{"id":"EnjuParser_R261","pred":"arg2Of","subj":"EnjuParser_T252","obj":"EnjuParser_T255"},{"id":"EnjuParser_R262","pred":"arg1Of","subj":"EnjuParser_T255","obj":"EnjuParser_T256"},{"id":"EnjuParser_R263","pred":"arg2Of","subj":"EnjuParser_T257","obj":"EnjuParser_T256"},{"id":"EnjuParser_R264","pred":"arg2Of","subj":"EnjuParser_T259","obj":"EnjuParser_T257"},{"id":"EnjuParser_R265","pred":"arg1Of","subj":"EnjuParser_T259","obj":"EnjuParser_T258"},{"id":"EnjuParser_R266","pred":"arg1Of","subj":"EnjuParser_T259","obj":"EnjuParser_T260"},{"id":"EnjuParser_R267","pred":"arg2Of","subj":"EnjuParser_T261","obj":"EnjuParser_T260"}],"namespaces":[{"prefix":"_base","uri":"http://kmcs.nii.ac.jp/enju/"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GlyCosmos600-MAT","denotations":[{"id":"PD-MAT-B_T1","span":{"begin":1352,"end":1355},"obj":"http://purl.obolibrary.org/obo/MAT_0000043"},{"id":"PD-MAT-B_T2","span":{"begin":396,"end":401},"obj":"http://purl.obolibrary.org/obo/MAT_0000055"},{"id":"PD-MAT-B_T3","span":{"begin":679,"end":684},"obj":"http://purl.obolibrary.org/obo/MAT_0000055"},{"id":"PD-MAT-B_T4","span":{"begin":396,"end":407},"obj":"http://purl.obolibrary.org/obo/MAT_0000197"},{"id":"PD-MAT-B_T5","span":{"begin":679,"end":690},"obj":"http://purl.obolibrary.org/obo/MAT_0000197"},{"id":"PD-MAT-B_T6","span":{"begin":396,"end":407},"obj":"http://purl.obolibrary.org/obo/MAT_0000442"},{"id":"PD-MAT-B_T7","span":{"begin":679,"end":690},"obj":"http://purl.obolibrary.org/obo/MAT_0000442"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GlyCosmos600-GlycoProteins","denotations":[{"id":"PD-GlycoProteins-B_T1","span":{"begin":625,"end":635},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001898"},{"id":"PD-GlycoProteins-B_T2","span":{"begin":1715,"end":1725},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001898"},{"id":"PD-GlycoProteins-B_T3","span":{"begin":625,"end":635},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001899"},{"id":"PD-GlycoProteins-B_T4","span":{"begin":1715,"end":1725},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001899"},{"id":"PD-GlycoProteins-B_T5","span":{"begin":625,"end":635},"obj":"https://acgg.asia/db/gpdb/id/GPDB0003452"},{"id":"PD-GlycoProteins-B_T6","span":{"begin":1715,"end":1725},"obj":"https://acgg.asia/db/gpdb/id/GPDB0003452"},{"id":"PD-GlycoProteins-B_T7","span":{"begin":625,"end":635},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004144"},{"id":"PD-GlycoProteins-B_T8","span":{"begin":1715,"end":1725},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004144"},{"id":"PD-GlycoProteins-B_T9","span":{"begin":625,"end":635},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004189"},{"id":"PD-GlycoProteins-B_T10","span":{"begin":1715,"end":1725},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004189"},{"id":"PD-GlycoProteins-B_T11","span":{"begin":625,"end":635},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004364"},{"id":"PD-GlycoProteins-B_T12","span":{"begin":1715,"end":1725},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004364"},{"id":"PD-GlycoProteins-B_T13","span":{"begin":625,"end":635},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004956"},{"id":"PD-GlycoProteins-B_T14","span":{"begin":1715,"end":1725},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004956"},{"id":"PD-GlycoProteins-B_T15","span":{"begin":625,"end":635},"obj":"https://acgg.asia/db/gpdb/id/GPDB0008021"},{"id":"PD-GlycoProteins-B_T16","span":{"begin":1715,"end":1725},"obj":"https://acgg.asia/db/gpdb/id/GPDB0008021"},{"id":"PD-GlycoProteins-B_T17","span":{"begin":349,"end":353},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005542"},{"id":"PD-GlycoProteins-B_T18","span":{"begin":349,"end":353},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005543"},{"id":"PD-GlycoProteins-B_T19","span":{"begin":349,"end":353},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005544"},{"id":"PD-GlycoProteins-B_T20","span":{"begin":349,"end":353},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005545"},{"id":"PD-GlycoProteins-B_T21","span":{"begin":41,"end":70},"obj":"https://acgg.asia/db/gpdb/id/GPDB0003198"},{"id":"PD-GlycoProteins-B_T22","span":{"begin":41,"end":70},"obj":"https://acgg.asia/db/gpdb/id/GPDB0006077"},{"id":"PD-GlycoProteins-B_T23","span":{"begin":41,"end":70},"obj":"https://acgg.asia/db/gpdb/id/GPDB0007489"},{"id":"PD-GlycoProteins-B_T24","span":{"begin":41,"end":70},"obj":"https://acgg.asia/db/gpdb/id/GPDB0007505"},{"id":"PD-GlycoProteins-B_T25","span":{"begin":41,"end":70},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001556"},{"id":"PD-GlycoProteins-B_T26","span":{"begin":41,"end":70},"obj":"https://acgg.asia/db/gpdb/id/GPDB0007725"},{"id":"PD-GlycoProteins-B_T27","span":{"begin":54,"end":70},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001411"},{"id":"PD-GlycoProteins-B_T28","span":{"begin":168,"end":185},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001411"},{"id":"PD-GlycoProteins-B_T29","span":{"begin":757,"end":773},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001411"},{"id":"PD-GlycoProteins-B_T30","span":{"begin":912,"end":928},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001411"},{"id":"PD-GlycoProteins-B_T31","span":{"begin":1022,"end":1039},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001411"},{"id":"PD-GlycoProteins-B_T32","span":{"begin":1095,"end":1111},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001411"},{"id":"PD-GlycoProteins-B_T33","span":{"begin":54,"end":70},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002938"},{"id":"PD-GlycoProteins-B_T34","span":{"begin":168,"end":185},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002938"},{"id":"PD-GlycoProteins-B_T35","span":{"begin":757,"end":773},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002938"},{"id":"PD-GlycoProteins-B_T36","span":{"begin":912,"end":928},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002938"},{"id":"PD-GlycoProteins-B_T37","span":{"begin":1022,"end":1039},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002938"},{"id":"PD-GlycoProteins-B_T38","span":{"begin":1095,"end":1111},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002938"},{"id":"PD-GlycoProteins-B_T39","span":{"begin":54,"end":70},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004147"},{"id":"PD-GlycoProteins-B_T40","span":{"begin":168,"end":185},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004147"},{"id":"PD-GlycoProteins-B_T41","span":{"begin":757,"end":773},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004147"},{"id":"PD-GlycoProteins-B_T42","span":{"begin":912,"end":928},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004147"},{"id":"PD-GlycoProteins-B_T43","span":{"begin":1022,"end":1039},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004147"},{"id":"PD-GlycoProteins-B_T44","span":{"begin":1095,"end":1111},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004147"},{"id":"PD-GlycoProteins-B_T45","span":{"begin":54,"end":70},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004991"},{"id":"PD-GlycoProteins-B_T46","span":{"begin":168,"end":185},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004991"},{"id":"PD-GlycoProteins-B_T47","span":{"begin":757,"end":773},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004991"},{"id":"PD-GlycoProteins-B_T48","span":{"begin":912,"end":928},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004991"},{"id":"PD-GlycoProteins-B_T49","span":{"begin":1022,"end":1039},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004991"},{"id":"PD-GlycoProteins-B_T50","span":{"begin":1095,"end":1111},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004991"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":510,"end":514},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"},{"id":"T2","span":{"begin":1579,"end":1583},"obj":"http://rdf.glycoinfo.org/glycan/G00054MO"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":627,"end":635},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T2","span":{"begin":1717,"end":1725},"obj":"https://acgg.asia/db/lfdb/LfDB0043"},{"id":"Lectin_T3","span":{"begin":627,"end":635},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T4","span":{"begin":1717,"end":1725},"obj":"https://acgg.asia/db/lfdb/LfDB0013"},{"id":"Lectin_T5","span":{"begin":625,"end":635},"obj":"https://acgg.asia/db/lfdb/LfDB0142"},{"id":"Lectin_T6","span":{"begin":1715,"end":1725},"obj":"https://acgg.asia/db/lfdb/LfDB0142"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G26693XF\""},{"id":"GlycanIUPAC_T2","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G01864SU\""},{"id":"GlycanIUPAC_T3","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G17605FD\""},{"id":"GlycanIUPAC_T4","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G41950LU\""},{"id":"GlycanIUPAC_T5","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G57195RJ\""},{"id":"GlycanIUPAC_T6","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G85391SA\""},{"id":"GlycanIUPAC_T7","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G89565QL\""},{"id":"GlycanIUPAC_T8","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G80869MR\""},{"id":"GlycanIUPAC_T9","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G55978NL\""},{"id":"GlycanIUPAC_T10","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G54644LT\""},{"id":"GlycanIUPAC_T11","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G25694UG\""},{"id":"GlycanIUPAC_T12","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G25126RB\""},{"id":"GlycanIUPAC_T13","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G51848AD\""},{"id":"GlycanIUPAC_T14","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G94667GM\""},{"id":"GlycanIUPAC_T15","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G30124BO\""},{"id":"GlycanIUPAC_T16","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G82777EZ\""},{"id":"GlycanIUPAC_T17","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G10151YZ\""},{"id":"GlycanIUPAC_T18","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G17585ZM\""},{"id":"GlycanIUPAC_T19","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G04411CJ\""},{"id":"GlycanIUPAC_T20","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G38254HJ\""},{"id":"GlycanIUPAC_T21","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G75188FS\""},{"id":"GlycanIUPAC_T22","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G70374VG\""},{"id":"GlycanIUPAC_T23","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G45176LJ\""},{"id":"GlycanIUPAC_T24","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G30874VW\""},{"id":"GlycanIUPAC_T25","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G69333MI\""},{"id":"GlycanIUPAC_T26","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G10676XO\""},{"id":"GlycanIUPAC_T27","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G14843DJ\""},{"id":"GlycanIUPAC_T28","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G47546FR\""},{"id":"GlycanIUPAC_T29","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G73695ZM\""},{"id":"GlycanIUPAC_T30","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G31923TJ\""},{"id":"GlycanIUPAC_T31","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G60519EP\""},{"id":"GlycanIUPAC_T32","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G07933IA\""},{"id":"GlycanIUPAC_T33","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G40745NH\""},{"id":"GlycanIUPAC_T34","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G54496YV\""},{"id":"GlycanIUPAC_T35","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T36","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T37","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T38","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T39","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T40","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T41","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T42","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T43","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T44","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T45","span":{"begin":157,"end":163},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""},{"id":"GlycanIUPAC_T46","span":{"begin":976,"end":982},"obj"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//rdf.glycoinfo.org/glycan/G12166ZT\""},{"id":"GlycanIUPAC_T226","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G48368BR\""},{"id":"GlycanIUPAC_T227","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G57407RW\""},{"id":"GlycanIUPAC_T228","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G00386TY\""},{"id":"GlycanIUPAC_T229","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G18723JK\""},{"id":"GlycanIUPAC_T230","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G93757OR\""},{"id":"GlycanIUPAC_T231","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G29006SI\""},{"id":"GlycanIUPAC_T232","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G03099OQ\""},{"id":"GlycanIUPAC_T233","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G53739OW\""},{"id":"GlycanIUPAC_T234","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G70440ZO\""},{"id":"GlycanIUPAC_T235","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G29951RR\""},{"id":"GlycanIUPAC_T236","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G58402TI\""},{"id":"GlycanIUPAC_T237","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G39875TP\""},{"id":"GlycanIUPAC_T238","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G83439QV\""},{"id":"GlycanIUPAC_T239","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G41762RC\""},{"id":"GlycanIUPAC_T240","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G91604UI\""},{"id":"GlycanIUPAC_T241","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G88447WE\""},{"id":"GlycanIUPAC_T242","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G93634BS\""},{"id":"GlycanIUPAC_T243","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G02587BH\""},{"id":"GlycanIUPAC_T244","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G43511MX\""},{"id":"GlycanIUPAC_T245","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G64958DH\""},{"id":"GlycanIUPAC_T246","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G30384TR\""},{"id":"GlycanIUPAC_T247","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G15624EX\""},{"id":"GlycanIUPAC_T248","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G22706ST\""},{"id":"GlycanIUPAC_T249","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G57408PI\""},{"id":"GlycanIUPAC_T250","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G86403XX\""},{"id":"GlycanIUPAC_T251","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G78043YB\""},{"id":"GlycanIUPAC_T252","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G18952JK\""},{"id":"GlycanIUPAC_T253","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G49020ND\""},{"id":"GlycanIUPAC_T254","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G63590YW\""},{"id":"GlycanIUPAC_T255","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G22793KS\""},{"id":"GlycanIUPAC_T256","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G64134SS\""},{"id":"GlycanIUPAC_T257","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G17338HY\""},{"id":"GlycanIUPAC_T258","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G99745XF\""},{"id":"GlycanIUPAC_T259","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G27782HN\""},{"id":"GlycanIUPAC_T260","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G57496DC\""},{"id":"GlycanIUPAC_T261","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G93169WB\""},{"id":"GlycanIUPAC_T262","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G05518TD\""},{"id":"GlycanIUPAC_T263","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G62603DN\""},{"id":"GlycanIUPAC_T264","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G59574FS\""},{"id":"GlycanIUPAC_T265","span":{"begin":1507,"end":1510},"obj":"\"http://rdf.glycoinfo.org/glycan/G47567WC\""}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":1265,"end":1272},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1367,"end":1374},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":396,"end":401},"obj":"http://purl.obolibrary.org/obo/UBERON_0002391"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":679,"end":684},"obj":"http://purl.obolibrary.org/obo/UBERON_0002391"},{"id":"PD-UBERON-AE-B_T5","span":{"begin":396,"end":407},"obj":"http://purl.obolibrary.org/obo/UBERON_0000029"},{"id":"PD-UBERON-AE-B_T6","span":{"begin":679,"end":690},"obj":"http://purl.obolibrary.org/obo/UBERON_0000029"},{"id":"PD-UBERON-AE-B_T7","span":{"begin":425,"end":432},"obj":"http://purl.obolibrary.org/obo/UBERON_0001979"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":396,"end":407},"obj":"Body_part"},{"id":"T3","span":{"begin":679,"end":690},"obj":"Body_part"},{"id":"T5","span":{"begin":1352,"end":1355},"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"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000043"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"GlyCosmos600-FMA","denotations":[{"id":"T1","span":{"begin":41,"end":53},"obj":"Body_part"},{"id":"T2","span":{"begin":349,"end":353},"obj":"Body_part"},{"id":"T3","span":{"begin":368,"end":385},"obj":"Body_part"},{"id":"T4","span":{"begin":380,"end":385},"obj":"Body_part"},{"id":"T5","span":{"begin":396,"end":407},"obj":"Body_part"},{"id":"T6","span":{"begin":396,"end":401},"obj":"Body_part"},{"id":"T7","span":{"begin":425,"end":432},"obj":"Body_part"},{"id":"T8","span":{"begin":625,"end":635},"obj":"Body_part"},{"id":"T9","span":{"begin":658,"end":668},"obj":"Body_part"},{"id":"T10","span":{"begin":679,"end":690},"obj":"Body_part"},{"id":"T11","span":{"begin":679,"end":684},"obj":"Body_part"},{"id":"T12","span":{"begin":868,"end":880},"obj":"Body_part"},{"id":"T13","span":{"begin":976,"end":982},"obj":"Body_part"},{"id":"T14","span":{"begin":1169,"end":1182},"obj":"Body_part"},{"id":"T15","span":{"begin":1265,"end":1272},"obj":"Body_part"},{"id":"T16","span":{"begin":1286,"end":1290},"obj":"Body_part"},{"id":"T17","span":{"begin":1352,"end":1355},"obj":"Body_part"},{"id":"T18","span":{"begin":1367,"end":1374},"obj":"Body_part"},{"id":"T19","span":{"begin":1413,"end":1424},"obj":"Body_part"},{"id":"T20","span":{"begin":1607,"end":1612},"obj":"Body_part"},{"id":"T21","span":{"begin":1715,"end":1725},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"fma_id","subj":"T1","obj":"http://purl.org/sig/ont/fma/fma82737"},{"id":"A2","pred":"fma_id","subj":"T2","obj":"http://purl.org/sig/ont/fma/fma67122"},{"id":"A3","pred":"fma_id","subj":"T3","obj":"http://purl.org/sig/ont/fma/fma66772"},{"id":"A4","pred":"fma_id","subj":"T4","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A5","pred":"fma_id","subj":"T5","obj":"http://purl.org/sig/ont/fma/fma5034"},{"id":"A6","pred":"fma_id","subj":"T6","obj":"http://purl.org/sig/ont/fma/fma9671"},{"id":"A7","pred":"fma_id","subj":"T7","obj":"http://purl.org/sig/ont/fma/fma63130"},{"id":"A8","pred":"fma_id","subj":"T8","obj":"http://purl.org/sig/ont/fma/fma62931"},{"id":"A9","pred":"fma_id","subj":"T9","obj":"http://purl.org/sig/ont/fma/fma62863"},{"id":"A10","pred":"fma_id","subj":"T10","obj":"http://purl.org/sig/ont/fma/fma5034"},{"id":"A11","pred":"fma_id","subj":"T11","obj":"http://purl.org/sig/ont/fma/fma9671"},{"id":"A12","pred":"fma_id","subj":"T12","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A13","pred":"fma_id","subj":"T13","obj":"http://purl.org/sig/ont/fma/fma82737"},{"id":"A14","pred":"fma_id","subj":"T14","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A15","pred":"fma_id","subj":"T15","obj":"http://purl.org/sig/ont/fma/fma9637"},{"id":"A16","pred":"fma_id","subj":"T16","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A17","pred":"fma_id","subj":"T17","obj":"http://purl.org/sig/ont/fma/fma7199"},{"id":"A18","pred":"fma_id","subj":"T18","obj":"http://purl.org/sig/ont/fma/fma9637"},{"id":"A19","pred":"fma_id","subj":"T19","obj":"http://purl.org/sig/ont/fma/fma62863"},{"id":"A20","pred":"fma_id","subj":"T20","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A21","pred":"fma_id","subj":"T21","obj":"http://purl.org/sig/ont/fma/fma62931"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":368,"end":385},"obj":"Body_part"},{"id":"T2","span":{"begin":396,"end":432},"obj":"Body_part"},{"id":"T3","span":{"begin":434,"end":438},"obj":"Body_part"},{"id":"T4","span":{"begin":658,"end":668},"obj":"Body_part"},{"id":"T5","span":{"begin":679,"end":690},"obj":"Body_part"},{"id":"T6","span":{"begin":1352,"end":1355},"obj":"Body_part"},{"id":"T9","span":{"begin":1413,"end":1424},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000115"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_8410038"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_8410037"},{"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_0000029"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0001007"},{"id":"A7","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0001555"},{"id":"A8","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0004907"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL_0000542"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":368,"end":385},"obj":"Cell"},{"id":"T2","span":{"begin":658,"end":668},"obj":"Cell"},{"id":"T3","span":{"begin":1413,"end":1424},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000115"},{"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"}],"text":"Activities and expression pattern of the carbohydrate sulfotransferase GlcNAc6ST-3 (I-GlcNAc6ST): functional implications.\nIn recent years, a family of five GlcNAc-6-O-sulfotransferases, called the GlcNAc6STs, has been molecularly cloned. One of these, GlcNAc6ST-2 (originally named HEC-GlcNAc6ST or LSST), shows a very restricted expression at the mRNA level in high endothelial cells (HECs) of lymph nodes high endothelial venules (HEVs). This enzyme has been shown to be involved in elaborating the 6-sulfo sLex structure on a set of mucin-like acceptors within HECs, thus providing a critical recognition determinant for L-selectin during the process of lymphocyte homing to lymph nodes. Limited information has been available about the closely related sulfotransferase known as GlcNAc6ST-3 (I-GlcNAc6ST). Here, employing transfection experiments with a series of glycoprotein acceptors, we report that this sulfotransferase has a marked preference for sulfating O-linked sugars of mucin-type acceptors, whereas other sulfotransferases in the family (GlcNAc6ST-1, GlcNAc6ST-2) and a Gal-6-O-sulfotransferase exhibit strong activity on both mucin-type acceptors and glycoproteins with predominantly N-linked chains. PCR analysis of cDNAs derived from a panel of tissues and purified cell populations confirms the strong expression of GlcNAc6ST-3 in gut-associated tissues and extends the expression to include lymphocytes. In contrast to GlcNAc6ST-2, GlcNAc6ST-3 transcripts are present minimally, if at all, in HECs; moreover, this enzyme is not able to generate the 6-sulfo sLex epitope in transfected cells. These latter findings argue that GlcNAc6ST-3 is not involved in generating HEV-expressed ligands for L-selectin."}