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| pubmed-article:8182079 | lifeskim:mentions | umls-concept:C0599958 | lld:lifeskim |
| pubmed-article:8182079 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:8182079 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:8182079 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:8182079 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:8182079 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:8182079 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:8182079 | lifeskim:mentions | umls-concept:C0253307 | lld:lifeskim |
| pubmed-article:8182079 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:8182079 | pubmed:dateCreated | 1994-6-16 | lld:pubmed |
| pubmed-article:8182079 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8182079 | pubmed:abstractText | The 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. | lld:pubmed |
| pubmed-article:8182079 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8182079 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8182079 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8182079 | pubmed:month | May | lld:pubmed |
| pubmed-article:8182079 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8182079 | pubmed:author | pubmed-author:SasakiKK | lld:pubmed |
| pubmed-article:8182079 | pubmed:author | pubmed-author:HanaiNN | lld:pubmed |
| pubmed-article:8182079 | pubmed:author | pubmed-author:OhtaSS | lld:pubmed |
| pubmed-article:8182079 | pubmed:author | pubmed-author:NishiTT | lld:pubmed |
| pubmed-article:8182079 | pubmed:author | pubmed-author:WatanabeEE | lld:pubmed |
| pubmed-article:8182079 | pubmed:author | pubmed-author:KurataKK | lld:pubmed |
| pubmed-article:8182079 | pubmed:author | pubmed-author:NagataMM | lld:pubmed |
| pubmed-article:8182079 | pubmed:author | pubmed-author:FunayamaKK | lld:pubmed |
| pubmed-article:8182079 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8182079 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:8182079 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:8182079 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8182079 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8182079 | pubmed:pagination | 14730-7 | lld:pubmed |
| pubmed-article:8182079 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
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| pubmed-article:8182079 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8182079 | pubmed:articleTitle | Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes. | lld:pubmed |
| pubmed-article:8182079 | pubmed:affiliation | Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Japan. | lld:pubmed |
| pubmed-article:8182079 | pubmed:publicationType | Journal Article | lld:pubmed |
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