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
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.