2024
DOI: 10.1038/s41467-024-46557-5
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Thermophoretic glycan profiling of extracellular vesicles for triple-negative breast cancer management

Yike Li,
Shaohua Zhang,
Chao Liu
et al.

Abstract: Triple-negative breast cancer (TNBC) is a highly metastatic and heterogeneous type of breast cancer with poor outcomes. Precise, non-invasive methods for diagnosis, monitoring and prognosis of TNBC are particularly challenging due to a paucity of TNBC biomarkers. Glycans on extracellular vesicles (EVs) hold the promise as valuable biomarkers, but conventional methods for glycan analysis are not feasible in clinical practice. Here, we report that a lectin-based thermophoretic assay (EVLET) streamlines vibrating… Show more

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Cited by 3 publications
(1 citation statement)
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“…Lectins, known as carbohydrate-binding proteins, have been extensively utilized to elucidate the global glycome of sEV preparations. Mass spectrometry represents another versatile platform for profiling complex glycan structures and even identifying glycosylation sites of proteins within sEV isolates. , Recently, novel approaches have emerged, including DNA assemblies combined with lectin recognition, metabolic glycan labeling, and chemoenzymatic-based strategy, for exploring protein-specific glycosylation on sEVs. Nonetheless, the glycan analysis strategies mentioned above primarily conduct ensemble-averaged analysis of sEV glycans. It is worth noting that sEVs exhibit high heterogeneity in both protein and nucleic acid compositions, as evidenced by single-sEV technologies such as fluorescence-based microscopy imaging, droplet digital PCR (ddPCR), and nano-flow cytometry (nFCM). Whether sEVs are uniformly glycosylated or display heterogeneous glycosignatures remains to be investigated …”
Section: Introductionmentioning
confidence: 99%
“…Lectins, known as carbohydrate-binding proteins, have been extensively utilized to elucidate the global glycome of sEV preparations. Mass spectrometry represents another versatile platform for profiling complex glycan structures and even identifying glycosylation sites of proteins within sEV isolates. , Recently, novel approaches have emerged, including DNA assemblies combined with lectin recognition, metabolic glycan labeling, and chemoenzymatic-based strategy, for exploring protein-specific glycosylation on sEVs. Nonetheless, the glycan analysis strategies mentioned above primarily conduct ensemble-averaged analysis of sEV glycans. It is worth noting that sEVs exhibit high heterogeneity in both protein and nucleic acid compositions, as evidenced by single-sEV technologies such as fluorescence-based microscopy imaging, droplet digital PCR (ddPCR), and nano-flow cytometry (nFCM). Whether sEVs are uniformly glycosylated or display heterogeneous glycosignatures remains to be investigated …”
Section: Introductionmentioning
confidence: 99%