Literature DB >> 1702034

ELFT: a gene that directs the expression of an ELAM-1 ligand.

S E Goelz1, C Hession, D Goff, B Griffiths, R Tizard, B Newman, G Chi-Rosso, R Lobb.   

Abstract

The LECCAMs are a family of cell adhesion molecules implicated in certain inflammatory processes. ELAM-1, a LECCAM found on the surface of activated endothelial cells, can mediate adhesion of neutrophils, monocytes, and certain cell lines to endothelial cells in vitro. No ligand for any LECCAM has yet been fully characterized. Here we report the cloning of a cDNA, ELFT (ELAM-1 ligand fucosyltransferase), that can confer ELAM-1 binding activity when transfected into nonbinding cell lines. ELFT encodes a 46 kd protein that has alpha(1,3)fucosyltransferase activity, suggesting that a fucosylated carbohydrate structure is an essential component of the ELAM-1 ligand. Furthermore, ELFT is expressed specifically in cell types that bind to ELAM-1, suggesting that this enzyme is an important regulator of inflammatory events in vivo.

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Year:  1990        PMID: 1702034     DOI: 10.1016/0092-8674(90)90430-m

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  58 in total

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8.  Recombinant tumour necrosis factor-alpha and platelet-activating factor synergistically increase intercellular adhesion molecule-1 and E-selectin-dependent neutrophil adherence to endothelium in vitro.

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9.  Higher-affinity oligosaccharide ligands for E-selectin.

Authors:  R M Nelson; S Dolich; A Aruffo; O Cecconi; M P Bevilacqua
Journal:  J Clin Invest       Date:  1993-03       Impact factor: 14.808

10.  The ELAM ligand fucosyltransferase, ELFT, directs E-selectin binding to a secreted scaffold protein: a method to produce and purify large quantities of specific carbohydrate structures.

Authors:  W Meier; D R Leone; K Miatkowski; R Lobb; S E Goelz
Journal:  Biochem J       Date:  1993-08-15       Impact factor: 3.857

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