Glycans play a crucial role in cancer development and progression. Altered glycosylation patterns are a hallmark of malignant transformation, affecting cell signaling, immune evasion, metastasis, and tumor microenvironment interactions.
Cancer cells often express abnormal glycans, such as increased sialylation, fucosylation, or truncated O-glycans, which can serve as biomarkers for diagnosis and prognosis.
Moreover, tumor-associated glycans (TACAs) are being explored as targets for novel immunotherapies and glycan-based vaccines, making glycomics a valuable tool in oncology research and clinical applications. The following table summarizes some key glycan signatures observed across distinct cancer types:
| Cancer type | Altered Glycan Structures |
|---|---|
| Pancreatic cancer | Increase of core fucosylation and LeX in tri-antenary glycan |
| Prostate cancer | Increased levels of core fucosylated agalatosylated biantennary glycans containing sialyl Lewis X. Increased levels of tri- and tetra-antennary N-glycans Increased levels of sialylated glycans and a small group of truncated glycans. Decreased level of glycans containing bisecting GlcNAc. Decreased levels of high-mannose-type glycans. |
| Gastric cancer | Increased levels of triantennary glycan carrying 2,6-linked sialic acid and trisialylated triantennary glycans carrying sialyl Lewis X. Decreasing levels of fucosylated non- and monosialylated glycans. Decreased levels of biantennary asialo monogalactosylated glycan. |
| Breast cancer | Agalctosyl biantennary glycans G0F and glycans containing sLex epitope A3F1G1 and A2F1G1. Highly sialylated antenna fucosylated glycans. High-mannose type structures. |
| Follicular lymphoma | IgG and IgM variable regions present an increased level of glycans containing one or more oligomannose sugars. Significant increase in potential glycosylation sites in the variable region. Increase of agaltosyl biantennary G0F and glycans containing sLeX epitope A3F1G1 and A2FG1 |
| Ovarian cancer | Increased levels of coree fucosylated agalactosyl biantennary glycans and glycans containing sialyl Lewis X. Increased levels of tri- and tetra-antennary N-glycans. Increased levels of sialylated glycans and a small group of truncated glycans. Decreased levels of glycans containing a bisecting GlcNAc. Drecreased levels of several neutral glycans, including high-mannose-type glycans. |
| Hepatocelullar carcinoma | Increased levels of fucosylated triantennary glycans. Highly increased fucosylation. Increased sialylation and high mannose structures. Increased fucosylation and sialylation of haptoglobin. |
| Colon cancer | Levels of FUT3-7 anf FUT-8, responsible for alpha 1,3-4 fucosylation at haptoglobin Asn21. |
Cancer & Custom Glycan Synthesis Service
We have a broad experience working on oncology-related projects. Here we present just 3 examples of potential synthetic projects, but Asparia’s experience supports the development of a wide diversity of Custom Synthesis Services:
TACAs’ synthesis for vaccine development
Synthetic tumor-associated carbohydrate antigens (TACAs), such as the sialyl LewisX, Lewis A, and GloboH antigen, are chemically synthesized and conjugated to carrier proteins or T-helper epitopes to boost immunogenicity.
Glycan Analytical standards for new biomarker identification and cancer diagnostics
Custom synthetic glycans—often stable isotope‑labeled (e.g., labelled with 13C or non-labelled standards)—are generated to serve as quantitative reference standards in LC‑MS workflows, enabling exact mass, retention-time, and abundance matching for candidate glycan biomarker identification and cancer diagnostics. N and O-glycosylation patterns exhibit even higher precision as they are specific for a particular glycoform of an overexpressed glycoprotein marker.
Our key study detailed the development of patented CarboQuant ^13C‑labeled glycan standards for absolute quantification of N‑glycans in serum proteins via MS. These synthetic standards allowed the construction of calibration curves and reproducible quantitation in clinical samples.
Conjugate design for developing therapeutic antibodies
TACAs can be prepared by chemoenzymatic synthesis with linkers for conjugation to carriers. When conjugated to carriers, such as PEG – PEGylated – these glycans can be used as antigens to develop therapeutic antibodies. Their hydrophilicity and PEG spacers enhance solubility and prevent aggregation, while stable linkages and PEGylation increase circulation half-life and systemic stability. TACAS conjugated to carrier proteins are used as antigens to develop therapeutic antibodies or ADC (antibody-drug-conjugates).
Let us know about your synthetic project, and we will present the best approach
Cancer & Glycan Analysis Service
Working on different oncology-related projects for 8 years has allowed us to gain experience with various types of analytical samples. Discover how our Glycoanalytical Services support your oncology R&D pipelines:
Glycan profiling
Asparia offers a comprehensive glycan profiling service portfolio to identify differences in glycosylation patterns of cancer cells and proteins. Some of these changes include increased sialylation, fucosylation, or branching:
- Increased core fucosylation and branching in alpha-fetoprotein (AFP) improve specificity in hepatocellular carcinoma diagnosis
- Identifying sialyl-Tn antigens can serve as a biomarker in breast and colon cancers.
- Tn antigen (GalNAcα1-O-Ser/Thr) and sialyl-Tn (sTn) antigen (Neu5Acα2-6GalNAcα1-O-Ser/Thr) are truncated O-glycans that are commonly overexpressed in cancer cells due to altered glycosylation pathways.
General Structural Analysis
Thanks to a General Structural Assignment Analysis, precise identification of tumor-associated glycans can be determined and used as diagnostic or prognostic biomarkers and even therapeutic targets. For instance, characterizing aberrant glycosylation on PSA might improve specificity in prostate cancer screening.
Glycoproteomics
- mAbs’ efficacy and stability depend heavily on their precise molecular structure, and the Intact Mass Service helps to confirm the complete molecular weight, detect PTMs, and identify protein variants or degradation products.
- N-glycosylation Site Occupation Analysis & Glycosylation Site-specific Glycan Profile can identify partially glycosylated or abnormally glycosylated sites, uncovering changes in tumor-associated proteins.
Microarray Technology
- Lectin Arrays are widely used in cancer research to identify aberrant glycosylation patterns, helping in biomarker discovery, patient stratification, and monitoring treatment responses.
- Glycan arrays are used to analyze the binding specificities of glycan-binding proteins like lectins or carbohydrate-binding antibodies. They can be used to analyze the specificity of an immune response towards vaccination with TACAs.
Related publications and resources
A selection of our most relevant scientific publications and resources that form about Oncology & Glycans
Aizpurua-Olaizola O, Sastre Toraño J, Falcon-Perez JM, Williams C, Reichardt N, Boons G-J. Mass spectrometry for glycan biomarker discovery. Trends Analyt Chem. 2018;100:7–14.
Echeverria B, Etxebarria J, Ruiz N, Hernandez Á, Calvo J, Haberger M, et al. Chemo-enzymatic synthesis of (13)C labeled complex N-glycans as internal standards for the absolute glycan quantification by mass spectrometry. Anal Chem. 2015;87(22):11460–7.
Asparia Glycomics. Glycan Signatures in Cancer – Identifying aberrant glycosylation patterns via arrays as biomarkers for cancer. 2025
