A glycomic approach to the identification and characterization of glycoprotein function in cells transfected with glycosyltransferase genes

Citation
N. Taniguchi et al., A glycomic approach to the identification and characterization of glycoprotein function in cells transfected with glycosyltransferase genes, PROTEOMICS, 1(2), 2001, pp. 239-247
Citations number
67
Language
INGLESE
art.tipo
Review
Categorie Soggetti
Chemistry & Analysis
Journal title
PROTEOMICS
ISSN journal
1615-9853 → ACNP
Volume
1
Issue
2
Year of publication
2001
Pages
239 - 247
Database
ISI
SICI code
1615-9853(200102)1:2<239:AGATTI>2.0.ZU;2-T
Abstract
The transfection of glycoprotein glycosyltransferase genes into cells leads to modification of both the structure and function of the glycoproteins an d as a result, changes in glycome patterns. N-glycan branching enzymes hold some promise as a model system for the identification of glycome patterns. Both N-acetylglucosaminyltransferase III and alpha1-6 fucosyltransferase a re typical glycosyltransferases, which are involved in the branching of N-g lycans. The resulting enzymatic products, bisecting N-GlcNAc and alpha1-6 f ucose residues, are no longer modified by other glycosyltransferases and it is a relatively simple task to identify their modification by means of lec tins. In this review, the glycome patterns of glycosyltransferase gene tran sfectants and the non-transfectants were compared by two-dimensional gel el ectrophoresis and lectin staining, and the biological significance of the t wo genes are described. Analyses of glycome patterns by transfecting glycos yltransferase genes will lead to new fields of study in the area of postgen ome research.