PubMed:8182079 JSONTXT

{"project":"ggdb-test","denotations":[{"id":"T1","span":{"begin":106,"end":113},"obj":"https://acgg.asia/db/ggdb/info/gg003"},{"id":"T2","span":{"begin":106,"end":113},"obj":"https://acgg.asia/db/ggdb/info/gg004"},{"id":"T3","span":{"begin":106,"end":113},"obj":"https://acgg.asia/db/ggdb/info/gg005"},{"id":"T4","span":{"begin":106,"end":113},"obj":"https://acgg.asia/db/ggdb/info/gg006"},{"id":"T5","span":{"begin":106,"end":113},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T6","span":{"begin":106,"end":113},"obj":"https://acgg.asia/db/ggdb/info/gg008"},{"id":"T7","span":{"begin":166,"end":173},"obj":"https://acgg.asia/db/ggdb/info/gg003"},{"id":"T8","span":{"begin":166,"end":173},"obj":"https://acgg.asia/db/ggdb/info/gg004"},{"id":"T9","span":{"begin":166,"end":173},"obj":"https://acgg.asia/db/ggdb/info/gg005"},{"id":"T10","span":{"begin":166,"end":173},"obj":"https://acgg.asia/db/ggdb/info/gg006"},{"id":"T11","span":{"begin":166,"end":173},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T12","span":{"begin":166,"end":173},"obj":"https://acgg.asia/db/ggdb/info/gg008"},{"id":"T13","span":{"begin":522,"end":530},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T14","span":{"begin":722,"end":730},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T15","span":{"begin":1049,"end":1057},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T16","span":{"begin":1119,"end":1127},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T17","span":{"begin":1313,"end":1321},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T18","span":{"begin":1355,"end":1362},"obj":"https://acgg.asia/db/ggdb/info/gg004"},{"id":"T19","span":{"begin":1418,"end":1426},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T20","span":{"begin":1534,"end":1541},"obj":"https://acgg.asia/db/ggdb/info/gg004"},{"id":"T21","span":{"begin":1588,"end":1596},"obj":"https://acgg.asia/db/ggdb/info/gg007"}],"text":"Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes.\nThe sialyl Lewis x (NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)Glc-NAc) determinants serve as ligands in the selectin-mediated adhesion of leukocytes to activated endothelium or platelets. In our efforts to identify glycosyltransferases involved in the biosynthesis of those ligands, we achieved expression cloning of a novel human alpha 1,3-fucosyltransferase termed Fuc-TVII from a THP-1 cDNA library by enrichment of the Namalwa cells highly expressing that determinant with a fluorescence-activated cell sorter. Expression of the COOH-terminal catalytic domain of Fuc-TVII showed an alpha 1,3-fucosyltransferase activity for a type II oligosaccharide with a terminal alpha 2,3-linked sialic acid among various acceptors, consistent with that in vivo acceptor specificity. Alignment of the primary sequences of five alpha 1,3-fucosyltransferases and assignment of the chromosomal location of Fuc-TVII gene, together with that acceptor specificity, indicate that Fuc-TVII consists of a unique class of the alpha 1,3-fucosyltransferase family. Determination of the expression levels of these alpha 1,3-fucosyltransferases in various cells revealed that both Fuc-TVII and a myeloid fucosyltransferase Fuc-TIV were significantly expressed in myeloid lineage cells. Fuc-TVII-transfected Namalwa cells exhibited significant binding to E-selectin in contrast to little binding of the Fuc-TIV-transfected cells. These results suggest that Fuc-TVII may participate in the biosynthesis of the selectin ligands."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":99,"end":113},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":106,"end":113},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":159,"end":173},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":166,"end":173},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":842,"end":853},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00054MO"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G01187XC"},{"id":"A3","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00051MO"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00054MO"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G01187XC"},{"id":"A6","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00051MO"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"}],"text":"Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes.\nThe sialyl Lewis x (NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)Glc-NAc) determinants serve as ligands in the selectin-mediated adhesion of leukocytes to activated endothelium or platelets. In our efforts to identify glycosyltransferases involved in the biosynthesis of those ligands, we achieved expression cloning of a novel human alpha 1,3-fucosyltransferase termed Fuc-TVII from a THP-1 cDNA library by enrichment of the Namalwa cells highly expressing that determinant with a fluorescence-activated cell sorter. Expression of the COOH-terminal catalytic domain of Fuc-TVII showed an alpha 1,3-fucosyltransferase activity for a type II oligosaccharide with a terminal alpha 2,3-linked sialic acid among various acceptors, consistent with that in vivo acceptor specificity. Alignment of the primary sequences of five alpha 1,3-fucosyltransferases and assignment of the chromosomal location of Fuc-TVII gene, together with that acceptor specificity, indicate that Fuc-TVII consists of a unique class of the alpha 1,3-fucosyltransferase family. Determination of the expression levels of these alpha 1,3-fucosyltransferases in various cells revealed that both Fuc-TVII and a myeloid fucosyltransferase Fuc-TIV were significantly expressed in myeloid lineage cells. Fuc-TVII-transfected Namalwa cells exhibited significant binding to E-selectin in contrast to little binding of the Fuc-TIV-transfected cells. These results suggest that Fuc-TVII may participate in the biosynthesis of the selectin ligands."}

{"project":"GGDB-2020","denotations":[{"id":"T1","span":{"begin":106,"end":113},"obj":"https://acgg.asia/db/ggdb/info/gg004"},{"id":"T2","span":{"begin":106,"end":113},"obj":"https://acgg.asia/db/ggdb/info/gg005"},{"id":"T3","span":{"begin":106,"end":113},"obj":"https://acgg.asia/db/ggdb/info/gg006"},{"id":"T4","span":{"begin":106,"end":113},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T5","span":{"begin":106,"end":113},"obj":"https://acgg.asia/db/ggdb/info/gg008"},{"id":"T6","span":{"begin":106,"end":113},"obj":"https://acgg.asia/db/ggdb/info/gg003"},{"id":"T7","span":{"begin":166,"end":173},"obj":"https://acgg.asia/db/ggdb/info/gg004"},{"id":"T8","span":{"begin":166,"end":173},"obj":"https://acgg.asia/db/ggdb/info/gg005"},{"id":"T9","span":{"begin":166,"end":173},"obj":"https://acgg.asia/db/ggdb/info/gg006"},{"id":"T10","span":{"begin":166,"end":173},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T11","span":{"begin":166,"end":173},"obj":"https://acgg.asia/db/ggdb/info/gg008"},{"id":"T12","span":{"begin":166,"end":173},"obj":"https://acgg.asia/db/ggdb/info/gg003"},{"id":"T13","span":{"begin":522,"end":530},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T14","span":{"begin":722,"end":730},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T15","span":{"begin":1049,"end":1057},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T16","span":{"begin":1119,"end":1127},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T17","span":{"begin":1313,"end":1321},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T18","span":{"begin":1355,"end":1362},"obj":"https://acgg.asia/db/ggdb/info/gg004"},{"id":"T19","span":{"begin":1418,"end":1426},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"T20","span":{"begin":1534,"end":1541},"obj":"https://acgg.asia/db/ggdb/info/gg004"},{"id":"T21","span":{"begin":1588,"end":1596},"obj":"https://acgg.asia/db/ggdb/info/gg007"}],"text":"Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes.\nThe sialyl Lewis x (NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)Glc-NAc) determinants serve as ligands in the selectin-mediated adhesion of leukocytes to activated endothelium or platelets. In our efforts to identify glycosyltransferases involved in the biosynthesis of those ligands, we achieved expression cloning of a novel human alpha 1,3-fucosyltransferase termed Fuc-TVII from a THP-1 cDNA library by enrichment of the Namalwa cells highly expressing that determinant with a fluorescence-activated cell sorter. Expression of the COOH-terminal catalytic domain of Fuc-TVII showed an alpha 1,3-fucosyltransferase activity for a type II oligosaccharide with a terminal alpha 2,3-linked sialic acid among various acceptors, consistent with that in vivo acceptor specificity. Alignment of the primary sequences of five alpha 1,3-fucosyltransferases and assignment of the chromosomal location of Fuc-TVII gene, together with that acceptor specificity, indicate that Fuc-TVII consists of a unique class of the alpha 1,3-fucosyltransferase family. Determination of the expression levels of these alpha 1,3-fucosyltransferases in various cells revealed that both Fuc-TVII and a myeloid fucosyltransferase Fuc-TIV were significantly expressed in myeloid lineage cells. Fuc-TVII-transfected Namalwa cells exhibited significant binding to E-selectin in contrast to little binding of the Fuc-TIV-transfected cells. These results suggest that Fuc-TVII may participate in the biosynthesis of the selectin ligands."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":154},"obj":"Sentence"},{"id":"T2","span":{"begin":155,"end":342},"obj":"Sentence"},{"id":"T3","span":{"begin":343,"end":669},"obj":"Sentence"},{"id":"T4","span":{"begin":670,"end":929},"obj":"Sentence"},{"id":"T5","span":{"begin":930,"end":1198},"obj":"Sentence"},{"id":"T6","span":{"begin":1199,"end":1417},"obj":"Sentence"},{"id":"T7","span":{"begin":1418,"end":1560},"obj":"Sentence"},{"id":"T8","span":{"begin":1561,"end":1657},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":154},"obj":"Sentence"},{"id":"T2","span":{"begin":155,"end":342},"obj":"Sentence"},{"id":"T3","span":{"begin":343,"end":669},"obj":"Sentence"},{"id":"T4","span":{"begin":670,"end":929},"obj":"Sentence"},{"id":"T5","span":{"begin":930,"end":1198},"obj":"Sentence"},{"id":"T6","span":{"begin":1199,"end":1417},"obj":"Sentence"},{"id":"T7","span":{"begin":1418,"end":1560},"obj":"Sentence"},{"id":"T8","span":{"begin":1561,"end":1657},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes.\nThe sialyl Lewis x (NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)Glc-NAc) determinants serve as ligands in the selectin-mediated adhesion of leukocytes to activated endothelium or platelets. In our efforts to identify glycosyltransferases involved in the biosynthesis of those ligands, we achieved expression cloning of a novel human alpha 1,3-fucosyltransferase termed Fuc-TVII from a THP-1 cDNA library by enrichment of the Namalwa cells highly expressing that determinant with a fluorescence-activated cell sorter. Expression of the COOH-terminal catalytic domain of Fuc-TVII showed an alpha 1,3-fucosyltransferase activity for a type II oligosaccharide with a terminal alpha 2,3-linked sialic acid among various acceptors, consistent with that in vivo acceptor specificity. Alignment of the primary sequences of five alpha 1,3-fucosyltransferases and assignment of the chromosomal location of Fuc-TVII gene, together with that acceptor specificity, indicate that Fuc-TVII consists of a unique class of the alpha 1,3-fucosyltransferase family. Determination of the expression levels of these alpha 1,3-fucosyltransferases in various cells revealed that both Fuc-TVII and a myeloid fucosyltransferase Fuc-TIV were significantly expressed in myeloid lineage cells. Fuc-TVII-transfected Namalwa cells exhibited significant binding to E-selectin in contrast to little binding of the Fuc-TIV-transfected cells. These results suggest that Fuc-TVII may participate in the biosynthesis of the selectin ligands."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":99,"end":113},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T2","span":{"begin":106,"end":113},"obj":"https://glytoucan.org/Structures/Glycans/G00051MO"},{"id":"T3","span":{"begin":106,"end":113},"obj":"https://glytoucan.org/Structures/Glycans/G01187XC"},{"id":"T4","span":{"begin":159,"end":173},"obj":"https://glytoucan.org/Structures/Glycans/G00054MO"},{"id":"T5","span":{"begin":166,"end":173},"obj":"https://glytoucan.org/Structures/Glycans/G00051MO"},{"id":"T6","span":{"begin":166,"end":173},"obj":"https://glytoucan.org/Structures/Glycans/G01187XC"},{"id":"T7","span":{"begin":842,"end":853},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes.\nThe sialyl Lewis x (NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)Glc-NAc) determinants serve as ligands in the selectin-mediated adhesion of leukocytes to activated endothelium or platelets. In our efforts to identify glycosyltransferases involved in the biosynthesis of those ligands, we achieved expression cloning of a novel human alpha 1,3-fucosyltransferase termed Fuc-TVII from a THP-1 cDNA library by enrichment of the Namalwa cells highly expressing that determinant with a fluorescence-activated cell sorter. Expression of the COOH-terminal catalytic domain of Fuc-TVII showed an alpha 1,3-fucosyltransferase activity for a type II oligosaccharide with a terminal alpha 2,3-linked sialic acid among various acceptors, consistent with that in vivo acceptor specificity. Alignment of the primary sequences of five alpha 1,3-fucosyltransferases and assignment of the chromosomal location of Fuc-TVII gene, together with that acceptor specificity, indicate that Fuc-TVII consists of a unique class of the alpha 1,3-fucosyltransferase family. Determination of the expression levels of these alpha 1,3-fucosyltransferases in various cells revealed that both Fuc-TVII and a myeloid fucosyltransferase Fuc-TIV were significantly expressed in myeloid lineage cells. Fuc-TVII-transfected Namalwa cells exhibited significant binding to E-selectin in contrast to little binding of the Fuc-TIV-transfected cells. These results suggest that Fuc-TVII may participate in the biosynthesis of the selectin ligands."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":99,"end":113},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T2","span":{"begin":106,"end":113},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"T3","span":{"begin":159,"end":173},"obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"T4","span":{"begin":166,"end":173},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"}],"text":"Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes.\nThe sialyl Lewis x (NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)Glc-NAc) determinants serve as ligands in the selectin-mediated adhesion of leukocytes to activated endothelium or platelets. In our efforts to identify glycosyltransferases involved in the biosynthesis of those ligands, we achieved expression cloning of a novel human alpha 1,3-fucosyltransferase termed Fuc-TVII from a THP-1 cDNA library by enrichment of the Namalwa cells highly expressing that determinant with a fluorescence-activated cell sorter. Expression of the COOH-terminal catalytic domain of Fuc-TVII showed an alpha 1,3-fucosyltransferase activity for a type II oligosaccharide with a terminal alpha 2,3-linked sialic acid among various acceptors, consistent with that in vivo acceptor specificity. Alignment of the primary sequences of five alpha 1,3-fucosyltransferases and assignment of the chromosomal location of Fuc-TVII gene, together with that acceptor specificity, indicate that Fuc-TVII consists of a unique class of the alpha 1,3-fucosyltransferase family. Determination of the expression levels of these alpha 1,3-fucosyltransferases in various cells revealed that both Fuc-TVII and a myeloid fucosyltransferase Fuc-TIV were significantly expressed in myeloid lineage cells. Fuc-TVII-transfected Namalwa cells exhibited significant binding to E-selectin in contrast to little binding of the Fuc-TIV-transfected cells. These results suggest that Fuc-TVII may participate in the biosynthesis of the selectin ligands."}

{"project":"glycogenes","denotations":[{"id":"PD-GlycoGenes20190927-B_T1","span":{"begin":522,"end":530},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"PD-GlycoGenes20190927-B_T2","span":{"begin":722,"end":730},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"PD-GlycoGenes20190927-B_T3","span":{"begin":790,"end":792},"obj":"https://acgg.asia/db/ggdb/info/gg111"},{"id":"PD-GlycoGenes20190927-B_T4","span":{"begin":1049,"end":1057},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"PD-GlycoGenes20190927-B_T5","span":{"begin":1119,"end":1127},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"PD-GlycoGenes20190927-B_T6","span":{"begin":1313,"end":1321},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"PD-GlycoGenes20190927-B_T7","span":{"begin":1355,"end":1362},"obj":"https://acgg.asia/db/ggdb/info/gg004"},{"id":"PD-GlycoGenes20190927-B_T8","span":{"begin":1418,"end":1426},"obj":"https://acgg.asia/db/ggdb/info/gg007"},{"id":"PD-GlycoGenes20190927-B_T9","span":{"begin":1534,"end":1541},"obj":"https://acgg.asia/db/ggdb/info/gg004"},{"id":"PD-GlycoGenes20190927-B_T10","span":{"begin":1588,"end":1596},"obj":"https://acgg.asia/db/ggdb/info/gg007"}],"text":"Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes.\nThe sialyl Lewis x (NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)Glc-NAc) determinants serve as ligands in the selectin-mediated adhesion of leukocytes to activated endothelium or platelets. In our efforts to identify glycosyltransferases involved in the biosynthesis of those ligands, we achieved expression cloning of a novel human alpha 1,3-fucosyltransferase termed Fuc-TVII from a THP-1 cDNA library by enrichment of the Namalwa cells highly expressing that determinant with a fluorescence-activated cell sorter. Expression of the COOH-terminal catalytic domain of Fuc-TVII showed an alpha 1,3-fucosyltransferase activity for a type II oligosaccharide with a terminal alpha 2,3-linked sialic acid among various acceptors, consistent with that in vivo acceptor specificity. Alignment of the primary sequences of five alpha 1,3-fucosyltransferases and assignment of the chromosomal location of Fuc-TVII gene, together with that acceptor specificity, indicate that Fuc-TVII consists of a unique class of the alpha 1,3-fucosyltransferase family. Determination of the expression levels of these alpha 1,3-fucosyltransferases in various cells revealed that both Fuc-TVII and a myeloid fucosyltransferase Fuc-TIV were significantly expressed in myeloid lineage cells. Fuc-TVII-transfected Namalwa cells exhibited significant binding to E-selectin in contrast to little binding of the Fuc-TIV-transfected cells. These results suggest that Fuc-TVII may participate in the biosynthesis of the selectin ligands."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":106,"end":113},"obj":"Glycan"},{"id":"T2","span":{"begin":166,"end":173},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00051MO"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00051MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00051MO"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00051MO"}],"text":"Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes.\nThe sialyl Lewis x (NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)Glc-NAc) determinants serve as ligands in the selectin-mediated adhesion of leukocytes to activated endothelium or platelets. In our efforts to identify glycosyltransferases involved in the biosynthesis of those ligands, we achieved expression cloning of a novel human alpha 1,3-fucosyltransferase termed Fuc-TVII from a THP-1 cDNA library by enrichment of the Namalwa cells highly expressing that determinant with a fluorescence-activated cell sorter. Expression of the COOH-terminal catalytic domain of Fuc-TVII showed an alpha 1,3-fucosyltransferase activity for a type II oligosaccharide with a terminal alpha 2,3-linked sialic acid among various acceptors, consistent with that in vivo acceptor specificity. Alignment of the primary sequences of five alpha 1,3-fucosyltransferases and assignment of the chromosomal location of Fuc-TVII gene, together with that acceptor specificity, indicate that Fuc-TVII consists of a unique class of the alpha 1,3-fucosyltransferase family. Determination of the expression levels of these alpha 1,3-fucosyltransferases in various cells revealed that both Fuc-TVII and a myeloid fucosyltransferase Fuc-TIV were significantly expressed in myeloid lineage cells. Fuc-TVII-transfected Namalwa cells exhibited significant binding to E-selectin in contrast to little binding of the Fuc-TIV-transfected cells. These results suggest that Fuc-TVII may participate in the biosynthesis of the selectin ligands."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":480,"end":485},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes.\nThe sialyl Lewis x (NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)Glc-NAc) determinants serve as ligands in the selectin-mediated adhesion of leukocytes to activated endothelium or platelets. In our efforts to identify glycosyltransferases involved in the biosynthesis of those ligands, we achieved expression cloning of a novel human alpha 1,3-fucosyltransferase termed Fuc-TVII from a THP-1 cDNA library by enrichment of the Namalwa cells highly expressing that determinant with a fluorescence-activated cell sorter. Expression of the COOH-terminal catalytic domain of Fuc-TVII showed an alpha 1,3-fucosyltransferase activity for a type II oligosaccharide with a terminal alpha 2,3-linked sialic acid among various acceptors, consistent with that in vivo acceptor specificity. Alignment of the primary sequences of five alpha 1,3-fucosyltransferases and assignment of the chromosomal location of Fuc-TVII gene, together with that acceptor specificity, indicate that Fuc-TVII consists of a unique class of the alpha 1,3-fucosyltransferase family. Determination of the expression levels of these alpha 1,3-fucosyltransferases in various cells revealed that both Fuc-TVII and a myeloid fucosyltransferase Fuc-TIV were significantly expressed in myeloid lineage cells. Fuc-TVII-transfected Namalwa cells exhibited significant binding to E-selectin in contrast to little binding of the Fuc-TIV-transfected cells. These results suggest that Fuc-TVII may participate in the biosynthesis of the selectin ligands."}

{"project":"Glycosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":99,"end":113},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":159,"end":173},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0012"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0012"}],"text":"Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes.\nThe sialyl Lewis x (NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)Glc-NAc) determinants serve as ligands in the selectin-mediated adhesion of leukocytes to activated endothelium or platelets. In our efforts to identify glycosyltransferases involved in the biosynthesis of those ligands, we achieved expression cloning of a novel human alpha 1,3-fucosyltransferase termed Fuc-TVII from a THP-1 cDNA library by enrichment of the Namalwa cells highly expressing that determinant with a fluorescence-activated cell sorter. Expression of the COOH-terminal catalytic domain of Fuc-TVII showed an alpha 1,3-fucosyltransferase activity for a type II oligosaccharide with a terminal alpha 2,3-linked sialic acid among various acceptors, consistent with that in vivo acceptor specificity. Alignment of the primary sequences of five alpha 1,3-fucosyltransferases and assignment of the chromosomal location of Fuc-TVII gene, together with that acceptor specificity, indicate that Fuc-TVII consists of a unique class of the alpha 1,3-fucosyltransferase family. Determination of the expression levels of these alpha 1,3-fucosyltransferases in various cells revealed that both Fuc-TVII and a myeloid fucosyltransferase Fuc-TIV were significantly expressed in myeloid lineage cells. Fuc-TVII-transfected Namalwa cells exhibited significant binding to E-selectin in contrast to little binding of the Fuc-TIV-transfected cells. These results suggest that Fuc-TVII may participate in the biosynthesis of the selectin ligands."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":143,"end":153},"obj":"Body_part"},{"id":"T2","span":{"begin":293,"end":303},"obj":"Body_part"},{"id":"T3","span":{"begin":317,"end":328},"obj":"Body_part"},{"id":"T4","span":{"begin":332,"end":341},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000738"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000738"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001986"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000233"}],"text":"Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes.\nThe sialyl Lewis x (NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)Glc-NAc) determinants serve as ligands in the selectin-mediated adhesion of leukocytes to activated endothelium or platelets. In our efforts to identify glycosyltransferases involved in the biosynthesis of those ligands, we achieved expression cloning of a novel human alpha 1,3-fucosyltransferase termed Fuc-TVII from a THP-1 cDNA library by enrichment of the Namalwa cells highly expressing that determinant with a fluorescence-activated cell sorter. Expression of the COOH-terminal catalytic domain of Fuc-TVII showed an alpha 1,3-fucosyltransferase activity for a type II oligosaccharide with a terminal alpha 2,3-linked sialic acid among various acceptors, consistent with that in vivo acceptor specificity. Alignment of the primary sequences of five alpha 1,3-fucosyltransferases and assignment of the chromosomal location of Fuc-TVII gene, together with that acceptor specificity, indicate that Fuc-TVII consists of a unique class of the alpha 1,3-fucosyltransferase family. Determination of the expression levels of these alpha 1,3-fucosyltransferases in various cells revealed that both Fuc-TVII and a myeloid fucosyltransferase Fuc-TIV were significantly expressed in myeloid lineage cells. Fuc-TVII-transfected Namalwa cells exhibited significant binding to E-selectin in contrast to little binding of the Fuc-TIV-transfected cells. These results suggest that Fuc-TVII may participate in the biosynthesis of the selectin ligands."}