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Updated: Aug 22, 2026

Glycan Node Analysis: A Bottom-up Approach to Glycomics
Published on: May 22, 2016
Harnessing changes in cellular glycosylation in new cancer treatment strategies
1Department of Molecular and Applied Biosciences, School of Biosciences, University of Westminster, 115 New Cavendish St., London, W1W 6UW, UK. m.v.dwek@westminster.ac.uk
Abstract:
The majority of proteins are modified in post-translational events and one of the most common of these is glycosylation. Many reports describe alterations to the normal cellular glycosylation in cancer but detailed knowledge of the underlying structures and mechanisms that result in the altered glycosylation of cancer glycoproteins have been hindered by the inherent complexity of glycans themselves. Improved analytical tools for the study of glycosylation and application of molecular techniques for the characterisation of the genes encoding glycosyltransferases have, however, enabled the structural identification of some of the cancer-associated changes in glycosylation. The observed alterations in protein glycosylation in cancer have led to clinical trials in which glycans on cancer cell-surface proteins are targeted. These new approaches to cancer treatment include immunotherapy and carbohydrate-processing inhibitor-based strategies. Compounds that mimic glycans involved in the metastatic dissemination of cancer are also actively sought. The results that have been obtained and the long-term potential of these new approaches are discussed in this review article.
Insights
Cancer cells exhibit altered protein glycosylation, a common post-translational modification. Researchers are developing new analytical tools and therapies targeting these cancer-specific glycan structures for improved treatments.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Post-translational modification of proteins, particularly glycosylation, is crucial for cellular function.
- Aberrant glycosylation patterns are frequently observed in cancer cells, impacting disease progression.
- The complexity of glycans has historically limited the detailed understanding of cancer-associated glycosylation changes.
Purpose of the Study:
- To review the current understanding of altered protein glycosylation in cancer.
- To highlight advancements in analytical and molecular techniques for studying cancer glycosylation.
- To discuss emerging therapeutic strategies targeting cancer-specific glycans.
Main Methods:
- Utilizing advanced analytical tools for glycan structure identification.
- Applying molecular techniques to characterize genes encoding glycosyltransferases.
- Reviewing clinical trial data and preclinical research on glycan-targeted cancer therapies.
Main Results:
- Structural identification of several cancer-associated glycosylation changes is now possible.
- Targeting cancer cell-surface glycans shows promise in clinical trials.
- Development of immunotherapies and inhibitor-based strategies are advancing cancer treatment.
Conclusions:
- Advances in technology have improved the study of complex cancer glycosylation.
- Targeting aberrant glycosylation represents a promising frontier in cancer therapy.
- Further research into glycan mimics could aid in preventing cancer metastasis.
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