Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1994-7-14
pubmed:databankReference
pubmed:abstractText
The sialyl Lewis x determinant (NeuAc alpha 2,3Gal beta 1, 4[Fuc alpha 1,3]GlcNAc) is an essential component of leukocyte counterreceptors for E-selectin and P-selectin. The final step in sialyl Lewis x synthesis is catalyzed by alpha-1,3-fucosyltransferases acting on sialylated glycoconjugate precursors. Cultured human leukocytic cell lines express an alpha-1,3-fucosyltransferase gene termed Fuc-TIV or ELFT but do not express the other three cloned human alpha-1,3-fucosyltransferase genes to any significant degree. The physiological role of Fuc-TIV/ELFT in sialyl Lewis x biosynthesis is uncertain, however, since it can catalyze the synthesis of this determinant in some, but not all, transfected cell lines in a manner that is dependent upon the glycosylation phenotype of the host cell. We report here the molecular cloning of a cDNA encoding a new human leukocyte alpha-1,3-fucosyltransferase, termed Fuc-TVII, capable of synthesizing the sialyl Lewis x moiety. The cDNA sequence predicts a 341-amino acid-long type II transmembrane protein typical of mammalian glycosyltransferases. When expressed in mammalian cells, the Fuc-TVII cDNA directs the synthesis of cell surface sialyl Lewis x moieties but not the Lewis x, Lewis a, sialyl Lewis a, or VIM-2 determinants. Fuc-TVII can efficiently utilize alpha-2,3-sialyllactosamine in vitro to form the sialyl Lewis x tetrasaccharide but does not utilize lactosamine to form the Lewis x moiety. Northern blot analyses show that the Fuc-TVII gene is transcribed in HL-60 cells, a human promyelocytic cell line, and in YT cells, a natural killer-like cell line. Fuc-TVII represents a leukocytic alpha-1,3-fucosyltransferase that can participate in selectin ligand synthesis via its ability to catalyze the synthesis of sialyl Lewis x determinants.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16789-94
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8207002-Amino Acid Sequence, pubmed-meshheading:8207002-Animals, pubmed-meshheading:8207002-Base Sequence, pubmed-meshheading:8207002-CHO Cells, pubmed-meshheading:8207002-Carbohydrate Sequence, pubmed-meshheading:8207002-Cell Line, pubmed-meshheading:8207002-Cercopithecus aethiops, pubmed-meshheading:8207002-Chromosome Mapping, pubmed-meshheading:8207002-Chromosomes, Human, Pair 11, pubmed-meshheading:8207002-Cloning, Molecular, pubmed-meshheading:8207002-Cricetinae, pubmed-meshheading:8207002-DNA, pubmed-meshheading:8207002-DNA, Complementary, pubmed-meshheading:8207002-DNA Primers, pubmed-meshheading:8207002-Fucosyltransferases, pubmed-meshheading:8207002-Humans, pubmed-meshheading:8207002-Killer Cells, Natural, pubmed-meshheading:8207002-Leukemia, Promyelocytic, Acute, pubmed-meshheading:8207002-Leukocytes, pubmed-meshheading:8207002-Mice, pubmed-meshheading:8207002-Molecular Sequence Data, pubmed-meshheading:8207002-Oligosaccharides, pubmed-meshheading:8207002-Polymerase Chain Reaction, pubmed-meshheading:8207002-Protein Structure, Secondary, pubmed-meshheading:8207002-Recombinant Proteins, pubmed-meshheading:8207002-Sequence Homology, Amino Acid, pubmed-meshheading:8207002-Substrate Specificity, pubmed-meshheading:8207002-Transfection, pubmed-meshheading:8207002-Tumor Cells, Cultured
pubmed:year
1994
pubmed:articleTitle
Molecular cloning of a cDNA encoding a novel human leukocyte alpha-1,3-fucosyltransferase capable of synthesizing the sialyl Lewis x determinant.
pubmed:affiliation
Howard Hughes Medical Institute, University of Michigan Medical School, Ann Arbor 48109.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't