PO-248 Novel insights on the role of glycosylation in cancer: molecular functions and clinical applications

Introduction Glycosylation alterations are frequently found in cancer and specific aberrant glycan structures are associated with tumour development and progression.1 The characterisation of glycosylation modifications occurring in cancer is of high interest and represents a source of putative new biomarkers for cancer detection, therapeutic intervention and patient stratification. Material and methods Glycomics, glycoproteomics, glycoprofiling, and in situ Proximity Ligation Assays of glycoengineered cancer cell models and tissue samples from gastrointestinal cancer patients were performed. Results and discussions This presentation reports the recent discoveries applying several novel approaches for: (A) the characterisation of glycosylation changes in the cancer cells; (B) the identification of the aberrant expression of specific glycan structures in cancer, like terminal sialylated glycans, which lead to the activation of tyrosine kinase receptors, such as HER2, MET, and RON;2,3,4,5 (C) the identification of altered glycosylated proteins, carrying simple mucin-type carbohydrate structures, in engineered cancer cell models and in sera of cancer patients.5,6 Conclusion These results demonstrate aberrant glycan structures as key functional players in tumour biology and highlight their potential as novel biomarkers and as therapeutic targets in the clinical management of cancer patients.1,5,6