Decoding sugar functions by identifying target glycoproteins
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Updated: Jul 20, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
Published on: December 26, 2011
Naoyuki Taniguchi1, Eiji Miyoshi, Jianguo Gu
1Department of Disease Glycomics, Institute for Microbial Diseases, Osaka University, 2-1 Suita, Osaka 565-0871, Japan. tani52@wd5.so-net.ne.jp <tani52@wd5.so-net.ne.jp>
Abstract:
Identification of the glycosyltransferase genes that are involved in the biosynthesis of glycoconjugates has opened up new avenues in glycobiology, the decoding of the function of sugar chains. Specific biosynthesis of branched N-glycan structures by glycosyltransferases functionally modifies target glycoproteins, as observed in the recognition of cancer cells. A mouse model with a specific defect in alpha1-6 fucosylation showed emphysema-like changes of the lung and severe degradation of lung alveoli that derived from the dysregulation of signaling through the transforming growth factor-beta receptor. Functional glycomics and the identification of target proteins will provide a new way to elucidate the nature of disease in the post-genomic era.
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