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Introduction <p>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.</p> Areas covered <p>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 <i>N</i>-glycan patterns, and the identification of galectin-3-binding protein (LGALS3BP) as a common pattern of altered glycosylated protein in cancer-derived EVs.</p> Expert opinion/commentary <p>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.</p> Graphical abstract <p>Overview of glycosylation in normal cells and cancer cells. In this review, we proposed dysregulated glycosylation patterns, particularly involving galectin-3 binding proteins (LGALS3BP), sialic acid, and N-glycans, which are commonly observed in cancer cells, leading to the release of cancer-derived extracellular vesicles (EVs). Integration of these elements into biomarker panels holds promise for early cancer detection. Figure adapted and compiled from “Glycans 1” by BioRender.com (2021). Retrieved from <a href="https://app.biorender.com/">https://app.biorender.com/</a> biorender-templates. Figure created in BioRender.</p> <p></p>

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

  • 期刊论文

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  • 发表日期：

    2025年7月15日

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  • Jie-Yi Koh Kok,
  • Bey-Hing Goh,
  • Wai-Leng Lee

摘要

Introduction

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.

Areas covered

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.

Expert opinion/commentary

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.

Graphical abstract

Overview of glycosylation in normal cells and cancer cells. In this review, we proposed dysregulated glycosylation patterns, particularly involving galectin-3 binding proteins (LGALS3BP), sialic acid, and N-glycans, which are commonly observed in cancer cells, leading to the release of cancer-derived extracellular vesicles (EVs). Integration of these elements into biomarker panels holds promise for early cancer detection. Figure adapted and compiled from “Glycans 1” by BioRender.com (2021). Retrieved from https://app.biorender.com/ biorender-templates. Figure created in BioRender.