ArticleCellular oncology (Dordrecht, Netherlands)2021
Terminal α2,6-sialylation of epidermal growth factor receptor modulates antibody therapy response of colorectal cancer cells.
Article in Cellular oncology (Dordrecht, Netherlands), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 45 citations in OpenAlex.
- GOLPH3-mediated sialylation of CXCR4 drives malignant progression and M2 macrophage polarization in colorectal cancer.Apoptosis : an international journal on programmed cell death · 2026Article
- Sulfonylurea Bioisosteres of Sulfonic Acid in JFD 00458-Based ST6GAL1 Inhibitors Enhance Membrane Permeability.ChemMedChem · 2026Article
- Effects of N361 Glycosylation on Epidermal Growth Factor Receptor Biological Function.Cancers · 2026Article
- Surface plasmon resonance microscopy reveals N-glycosylation driven modulation of affinity and avidity of ErbB receptors in whole single pancreatic cancer cells.Glycobiology · 2025Article
- ST6GAL1-Mediated Sialylation Stabilizes PD-L1 and Drives Immunosuppressive Tumor Microenvironment in Colorectal Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- An engineered PD1-Fc fusion produced in N. benthamiana plants efficiently blocks PD1/PDL1 interaction.Plant cell reports · 2025Article
- Glycosylation in Cancer.Handbook of experimental pharmacology · 2025Review
- Aberrations in the glycosylation of receptor tyrosine kinases: A focus on lung adenocarcinoma.CytoJournal · 2025Review
- The role of glycan-lectin interactions in the tumor microenvironment: immunosuppression regulators of colorectal cancer.American journal of cancer research · 2025Review
- An overview of mechanisms, biomarkers, and treatment strategies for acquired anti-EGFR resistance in RAS wild-type colorectal cancer.Frontiers in pharmacology · 2025Review
- Plant-derived Durvalumab variants show efficient PD-1/PD-L1 blockade and therapeutically favourable FcR binding.Plant biotechnology journal · 2024Article
- High-Throughput Mass Spectrometry Analysis ofJournal of proteome research · 2024Article
- Article
- Structural dynamics of the active HER4 and HER2/HER4 complexes is finely tuned by different growth factors and glycosylation.bioRxiv : the preprint server for biology · 2024Article
- ST6GAL1 sialyltransferase promotes acinar to ductal metaplasia and pancreatic cancer progression.JCI insight · 2023Article
- Role of the ST6GAL1 sialyltransferase in regulating ovarian cancer cell metabolism.Glycobiology · 2023Article
- Sialylation of EGFR by ST6GAL1 induces receptor activation and modulates trafficking dynamics.bioRxiv : the preprint server for biology · 2023Article
- Role of tumor cell sialylation in pancreatic cancer progression.Advances in cancer research · 2023Review
- High sensitivity glycomics in biomedicine.Mass spectrometry reviews · 2022Review
- Glycans as Targets for Drug Delivery in Cancer.Cancers · 2022Review
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 4 countries.
Funding
Abstract
backgroundThe epidermal growth factor receptor (EGFR) is a key protein involved in cancer development. Monoclonal antibodies targeting EGFR are approved for the treatment of metastatic colorectal cancer (CRC). Despite the beneficial clinical effects observed in subgroups of patients, the acquisition of resistance to treatment remains a major concern. Protein N-glycosylation of cellular receptors is known to regulate physiological processes leading to activation of downstream signaling pathways. In the present study, the role of EGFR-specific terminal ⍺2,6-sialylation was analyzed in modulation of the malignant phenotype of CRC cells and their resistance to monoclonal antibody Cetuximab-based therapy.
methodsGlycoengineered CRC cell models with specific sialyltransferase ST6GAL1 expression levels were applied to evaluate EGFR activation, cell surface glycosylation and therapeutic response to Cetuximab.
resultsGlycoproteomic analysis revealed EGFR as a major target of ST6Gal1-mediated ⍺2,6-sialylation in a glycosite-specific manner. Mechanistically, CRC cells with increased ST6Gal1 expression and displaying terminal ⍺2,6-sialylation showed a marked resistance to Cetuximab-induced cytotoxicity. Moreover, we found that this resistance was accompanied by downregulation of EGFR expression and its activation.
conclusionsOur data indicate that EGFR ⍺2,6-sialylation is a key factor in modulating the susceptibility of CRC cells to antibody targeted therapy, thereby disclosing a potential novel biomarker and providing key molecular information for tailor made anti-cancer strategies.
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