TY - JOUR
T1 - Molecular cloning, expression, chromosomal assignment, and tissue-specific expression of a murine α-(1,3)-fucosyltransferase locus corresponding to the human ELAM-1 ligand fucosyl transferase
AU - Gersten, Kevin M.
AU - Natsuka, Shunji
AU - Trinchera, Marco
AU - Petryniak, Bronislawa
AU - Kelly, Robert J.
AU - Hiraiwa, Nozomu
AU - Jenkins, Nancy A.
AU - Gilbert, Debra J.
AU - Copeland, Neal G.
AU - Lowe, John B.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1995/10/20
Y1 - 1995/10/20
N2 - Terminal Fucα2-3GlcNAc moieties are displayed by mammalian cell surface glycoconjugates in a tissue-specific manner. These oligosaccharides participate in selectin-dependent leukocyte adhesion and have been implicated in adhesive events during murine embryogenesis. Other functions for these molecules remain to be defined, as do the tissue-specific expression patterns of the corresponding α-(1-3)-fucosyltransferase (α1-3FT) genes. This report characterizes a murine α1-3FT that shares 77% amino acid sequence identity with human ELAM ligand fucosyltransferase (ELFT, also termed Fuc-TIV). The corresponding gene maps to mouse chromosome 9 in a region of homology with the Fuc-TIV locus on human chromosome 11q. In vitro, the murine α1-3FT can efficiently fucosylate the trisaccharide Galα1-3Galβ1-4GlcNAc (apparent K(m) of 0.71 mM) to form an unusual tetrasaccharide (Galα1-3Ga1β1- 4[Fucα1-3]GlcNAc) described in periimplantation mouse tissues. The enzyme can also form the Lewis x determinant from Galβ1-4GlcNAc (K(m) = 2.05 mM), and the sialyl Lewis x determinant from NeuNAcα2-3Galβ1-4GlcNAc (K(m) = 1.78 mM). However, it does not yield sialyl Lewis x determinants when expressed in a mammalian cell line that maintains sialyl Lewis x precursors. Transcripts from this gene accumulate to low levels in hematopoietic organs, but are unexpectedly abundant in epithelia that line the stomach, small intestine, colon, and epididymus. Epithelial cell-specific expression of this gene suggests function(s) in addition to, and distinct from, its proposed role in selectin ligand synthesis.
AB - Terminal Fucα2-3GlcNAc moieties are displayed by mammalian cell surface glycoconjugates in a tissue-specific manner. These oligosaccharides participate in selectin-dependent leukocyte adhesion and have been implicated in adhesive events during murine embryogenesis. Other functions for these molecules remain to be defined, as do the tissue-specific expression patterns of the corresponding α-(1-3)-fucosyltransferase (α1-3FT) genes. This report characterizes a murine α1-3FT that shares 77% amino acid sequence identity with human ELAM ligand fucosyltransferase (ELFT, also termed Fuc-TIV). The corresponding gene maps to mouse chromosome 9 in a region of homology with the Fuc-TIV locus on human chromosome 11q. In vitro, the murine α1-3FT can efficiently fucosylate the trisaccharide Galα1-3Galβ1-4GlcNAc (apparent K(m) of 0.71 mM) to form an unusual tetrasaccharide (Galα1-3Ga1β1- 4[Fucα1-3]GlcNAc) described in periimplantation mouse tissues. The enzyme can also form the Lewis x determinant from Galβ1-4GlcNAc (K(m) = 2.05 mM), and the sialyl Lewis x determinant from NeuNAcα2-3Galβ1-4GlcNAc (K(m) = 1.78 mM). However, it does not yield sialyl Lewis x determinants when expressed in a mammalian cell line that maintains sialyl Lewis x precursors. Transcripts from this gene accumulate to low levels in hematopoietic organs, but are unexpectedly abundant in epithelia that line the stomach, small intestine, colon, and epididymus. Epithelial cell-specific expression of this gene suggests function(s) in addition to, and distinct from, its proposed role in selectin ligand synthesis.
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U2 - 10.1074/jbc.270.42.25047
DO - 10.1074/jbc.270.42.25047
M3 - Article
C2 - 7559635
AN - SCOPUS:0028823397
SN - 0021-9258
VL - 270
SP - 25047
EP - 25056
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 42
ER -