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pubmed-article:8752218pubmed:abstractTextalpha(1,3)Fucosylated oligosaccharides represent components of leukocyte counterreceptors for E- and P-selectins and of L-selectin ligands expressed by lymph node high endothelial venules (HEV). The identity of the alpha(1,3)fucosyltransferase(s) required for their expression has been uncertain, as has a requirement for alpha(1,3)fucosylation in HEV L-selectin ligand activity. We demonstrate here that mice deficient in alpha(1,3) fucosyltransferase Fuc-TVII exhibit a leukocyte adhesion deficiency characterized by absent leukocyte E- and P-selectin ligand activity and deficient HEV L-selectin ligand activity. Selectin ligand deficiency is distinguished by blood leukocytosis, impaired leukocyte extravasation in inflammation, and faulty lymphocyte homing. These observations demonstrate an essential role for Fuc-TVII in E-, P-, and L-selectin ligand biosynthesis and imply that this locus can control leukocyte trafficking in health and disease.lld:pubmed
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pubmed-article:8752218pubmed:articleTitleThe alpha(1,3)fucosyltransferase Fuc-TVII controls leukocyte trafficking through an essential role in L-, E-, and P-selectin ligand biosynthesis.lld:pubmed
pubmed-article:8752218pubmed:affiliationHoward Hughes Medical Institute, University of Michigan Medical School, Ann Arbor 48109-0650, USA.lld:pubmed
pubmed-article:8752218pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8752218pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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