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Updated: Jan 9, 2026

Glycan Node Analysis: A Bottom-up Approach to Glycomics
Published on: May 22, 2016
Decoding aberrant glycosylation in colorectal cancer: From Glycosyaltion characterization, expression regulation to
Zihan Li1, Xichen Dong1, Jian Liu1
1Medical Research Center, Beijing Chao-Yang Hospital, Capital Medical University, Beijing 100020, China.
Abstract:
Colorectal cancer (CRC) exhibits extensive alterations in glycosylation, characterized by remodeling of glycan chain structures, aberrant terminal modifications, and dysregulated glycosyltransferase activity. These alterations are intimately associated with malignant phenotypes, such as tumor invasion, migration and proliferation, and contribute to shaping an immunosuppressive tumor microenvironment (TME). In this review, we first delineate major glycosylation types implicated in CRC, including O-GalNAc glycosylation, O-GlcNAcylation, N-glycosylation, sialylation, glycosphingolipid, glycosaminoglycan, and other special antigens, and summarize the key enzymatic machinery governing their biosynthesis. We further explore how glycosylation reprogramming drives oncogenic signaling and cellular plasticity. Importantly, we highlight recent advances in CRC-specific glycosylation-based diagnostic, prognostic, and therapeutic strategies. By summarizing current mechanistic and translational insights, this review aims to establish a conceptual framework for elucidating CRC-specific glycosylation alterations and evaluating their clinical translational potential, with the goal of improving early diagnosis, prognostic assessment, and targeted therapeutic strategies.
Insights
Colorectal cancer (CRC) involves significant changes in glycosylation, impacting tumor growth and the tumor microenvironment (TME). Understanding these CRC glycosylation alterations is key for developing new diagnostic and therapeutic strategies.
Area of Science:
- Biochemistry
- Oncology
- Molecular Biology
Background:
- Colorectal cancer (CRC) displays widespread changes in glycosylation, affecting glycan structures, terminal modifications, and enzyme activity.
- These glycosylation alterations are linked to malignant behaviors like invasion, migration, proliferation, and the creation of an immunosuppressive tumor microenvironment (TME).
Purpose of the Study:
- To review major glycosylation types in CRC, including O-GalNAc glycosylation, O-GlcNAcylation, N-glycosylation, sialylation, glycosphingolipids, and glycosaminoglycans.
- To explore how glycosylation reprogramming influences oncogenic signaling and cellular plasticity in CRC.
- To highlight advancements in CRC-specific glycosylation-based diagnostics, prognostics, and therapeutics.
Main Methods:
- Literature review of glycosylation alterations in colorectal cancer.
- Summary of key enzymes involved in glycosylation biosynthesis.
- Analysis of the role of glycosylation in oncogenic signaling and TME modulation.
- Review of current diagnostic, prognostic, and therapeutic strategies targeting CRC glycosylation.
Main Results:
- Detailed delineation of various glycosylation types implicated in CRC.
- Explanation of the enzymatic machinery governing CRC glycosylation.
- Exploration of the link between glycosylation reprogramming, oncogenic signaling, and cellular plasticity.
- Identification of recent progress in CRC-specific glycosylation-based strategies.
Conclusions:
- Glycosylation alterations are central to CRC pathogenesis and TME.
- Understanding CRC glycosylation provides a framework for improved diagnostics and therapeutics.
- Targeting CRC-specific glycosylation holds promise for enhanced early diagnosis, prognostic assessment, and treatment strategies.
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