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Updated: Jul 5, 2026

Glycan Node Analysis: A Bottom-up Approach to Glycomics
Published on: May 22, 2016
Functional roles of N-glycans in cell signaling and cell adhesion in cancer
Yan-Yang Zhao1, Motoko Takahashi, Jian-Guo Gu
1Department of Disease Glycomics, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan.
Abstract:
Glycosylation is one of the most common post-translational modification reactions and nearly half of all known proteins in eukaryotes are glycosylated. In fact, changes in oligosaccharide structures are associated with many physiological and pathological events, including cell growth, migration, differentiation, tumor invasion, host-pathogen interactions, cell trafficking, and transmembrane signaling. Emerging roles of glycan functions have been highly attractive to scientists in various fields of life science as they open a field, "Functional Glycomics", that is a comprehensive study of the glycan structures in relation to functions. In particular, the N-glycans of signaling molecules including receptors or adhesion molecules are considered to be involved in cellular functions. This review will focus on the roles of glycosyltransferases involved in the biosynthesis of N-glycan branching and identification of cell surface receptors as their target proteins. We also suggest that the modulation of N-glycans of those receptors alters their important functions such as cell signaling and cell adhesion which are implicated in cancer invasion and metastasis.
Insights
Glycosylation, a key protein modification, impacts cell functions and disease. This review explores how altering N-glycans on cell receptors affects signaling and adhesion, crucial in cancer metastasis.
Area of Science:
- Biochemistry
- Cell Biology
- Glycomics
Background:
- Glycosylation is a prevalent post-translational modification in eukaryotes, affecting nearly half of all proteins.
- Altered oligosaccharide structures are linked to diverse physiological and pathological processes, including cancer progression and cell signaling.
- Functional Glycomics investigates the relationship between glycan structures and their biological functions.
Purpose of the Study:
- This review focuses on glycosyltransferases responsible for N-glycan branching.
- It identifies cell surface receptors as key targets for these enzymes.
- The study aims to elucidate how N-glycan modulation on receptors impacts cellular functions.
Main Methods:
- Literature review of glycosyltransferases involved in N-glycan biosynthesis.
- Analysis of studies identifying cell surface receptors targeted by these enzymes.
- Examination of research on the functional consequences of N-glycan alterations on receptor activity.
Main Results:
- Glycosyltransferases play a critical role in creating complex N-glycan structures.
- Specific cell surface receptors are identified as targets for N-glycan modification.
- Modulation of N-glycans on receptors significantly impacts cell signaling and adhesion pathways.
Conclusions:
- N-glycan branching, mediated by glycosyltransferases, is crucial for receptor function.
- Altered N-glycans on cell surface receptors can influence cell signaling and adhesion.
- These changes are implicated in cancer invasion and metastasis, highlighting potential therapeutic targets.
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