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

The transfection of glycoprotein glycosyltransferase genes into cells leads to modification of both the structure and function of the glycoproteins and as a result, changes in glycome patterns. N‐glycan branching enzymes hold some promise as a model system for the identification of glycome patterns....

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Bibliographic Details
Published in:Proteomics (Weinheim) 2001-02, Vol.1 (2), p.239-247
Main Authors: Taniguchi, Naoyuki, Ekuni, Atsuko, Ko, Jeong Heon, Miyoshi, Eiji, Ikeda, Yoshitaka, Ihara, Yoshito, Nishikawa, Atsushi, Honke, Koichi, Takahashi, Motoko
Format: Article
Language:English
Subjects:
a-1,6-fucosyltransferase
Animals
Carbohydrate Sequence
Electrophoresis, Gel, Two-Dimensional
Fucosyltransferases - genetics
Fucosyltransferases - metabolism
Glycome
Glycoproteins - chemistry
Glycoproteins - genetics
Glycoproteins - physiology
glycosyltransferase
Glycosyltransferase genes
Glycosyltransferases - genetics
Glycosyltransferases - metabolism
Humans
Molecular Sequence Data
N-Acetylglucosaminyltransferases - genetics
N-Acetylglucosaminyltransferases - metabolism
Protein Processing, Post-Translational
Proteome
proteomics
Review
Substrate Specificity
Transfection
α1-6 fucosyltransferase
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Summary:The transfection of glycoprotein glycosyltransferase genes into cells leads to modification of both the structure and function of the glycoproteins and 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 α1–6 fucosyltransferase are typical glycosyltransferases, which are involved in the branching of N‐glycans. The resulting enzymatic products, bisecting N‐GlcNAc and α1–6 fucose residues, are no longer modified by other glycosyltransferases and it is a relatively simple task to identify their modification by means of lectins. In this review, the glycome patterns of glycosyltransferase gene transfectants and the nontransfectants were compared by two‐dimensional gel electrophoresis and lectin staining, and the biological significance of the two genes are described. Analyses of glycome patterns by transfecting glycosyltransferase genes will lead to new fields of study in the area of postgenome research.
ISSN:1615-9853
1615-9861
DOI:10.1002/1615-9861(200102)1:2<239::AID-PROT239>3.0.CO;2-K