Linked Life Data

7901202

Source:http://linkedlifedata.com/resource/pubmed/id/7901202

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1993-12-1
pubmed:databankReference
pubmed:abstractText
This report describes the isolation of a cDNA encoding a novel human Gal beta (1-3/1-4)GlcNac alpha 2,3-sialyl-transferase involved in the biosynthesis of the sialyl Lewis x determinant (NeuAc alpha 2-3 Gal beta 1-4(Fuc alpha 1-3)GlcNAc). A cDNA library of the human melanoma cell line WM266-4 was constructed in an Epstein-Barr virus-based cloning vector. Selection of the B-cell line Namalwa expressing transfected cDNAs in the presence of the cytotoxic lectin Ricinus communis agglutinin 120 gave a cDNA encoding a protein with type II transmembrane topology, as found for mammalian glycosyltransferases. The use of this lectin, which is specific to galactose residues (especially the Gal beta 1-4GlcNAc structure), originates from our prediction that the modification of the Gal beta 1-4GlcNAc structure (a backbone of the sialyl Lewis x structure) by glycosyltransferases may increase the levels of resistance to this lectin. Comparison of this cDNA sequence with those of three other cloned sialyltransferases revealed two conserved regions shared by all four enzymes. Expression of the COOH-terminal catalytic domain of this protein showed alpha 2,3-sialyltransferase activity with substrate specificity different from that of CMP-N-acetylneuraminate:N-acetyllactosaminide alpha-2,3-sialyltransferase (Gal-beta 1-3(4)GlcNAc alpha 2,3-sialyltransferase, EC 2.4.99.6). Furthermore, expression of this cDNA in Namalwa cells increased the level of sialyl Lewis x antigens. The cloning approach based on lectin resistance may be useful for the isolation of cDNAs encoding other mammalian glycosyltransferases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
22782-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7901202-Amino Acid Sequence, pubmed-meshheading:7901202-Animals, pubmed-meshheading:7901202-Antigens, CD15, pubmed-meshheading:7901202-Base Sequence, pubmed-meshheading:7901202-Blotting, Northern, pubmed-meshheading:7901202-Carbohydrate Sequence, pubmed-meshheading:7901202-Cloning, Molecular, pubmed-meshheading:7901202-Conserved Sequence, pubmed-meshheading:7901202-DNA, Complementary, pubmed-meshheading:7901202-DNA Primers, pubmed-meshheading:7901202-Drug Resistance, pubmed-meshheading:7901202-Gene Expression, pubmed-meshheading:7901202-Gene Library, pubmed-meshheading:7901202-Genetic Vectors, pubmed-meshheading:7901202-Humans, pubmed-meshheading:7901202-Melanoma, pubmed-meshheading:7901202-Molecular Sequence Data, pubmed-meshheading:7901202-Polymerase Chain Reaction, pubmed-meshheading:7901202-Rats, pubmed-meshheading:7901202-Restriction Mapping, pubmed-meshheading:7901202-Ricin, pubmed-meshheading:7901202-Sequence Homology, Amino Acid, pubmed-meshheading:7901202-Sialyltransferases, pubmed-meshheading:7901202-Transcription, Genetic, pubmed-meshheading:7901202-Transfection, pubmed-meshheading:7901202-Tumor Cells, Cultured
pubmed:year
1993
pubmed:articleTitle
Expression cloning of a novel Gal beta (1-3/1-4) GlcNAc alpha 2,3-sialyltransferase using lectin resistance selection.
pubmed:affiliation
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Japan.
pubmed:publicationType
Journal Article, Comparative Study