Altered glycosylation of EVs in cancers: galectin-3-binding protein (LGALS3BP)

Extracellular vesicles (EVs) are membrane-bound structures secreted by various cell types, acting as carriers of complex cargos that facilitate intercellular communication. Their presence in biofluids highlights their potential for disease biomarker identification. Glycans, crucial components of EVs, undergo glycosylation, a key post-translational modification (PTM) involved in many biological processes. Aberrant glycosylation is linked to disease, particularly cancer.

This review examines alterations in EV glycosylation patterns in cancer and their biological implications. It synthesizes findings from cell studies and biofluid analyses (including blood and urine), emphasizing the potential of combined glycosylation profiles as circulating cancer detection. Key findings highlight the elevation of terminal sialic acid levels, dysregulation of N-glycan patterns, and the identification of galectin-3-binding protein (LGALS3BP) as a common pattern of altered glycosylated protein in cancer-derived EVs.

This review uniquely suggests a novel combination of the altered glycosylation pattern of cancer-derived EVs based on changes observed in current studies. By highlighting specific alterations that differentiate cancer-derived EVs from those of healthy origin, the analysis offers valuable insights into diagnostic and prognostic applications. These findings may facilitate the development of non-invasive biomarkers that enhance early cancer detection and monitoring.