ArticleGlycobiology2020
Detecting substrate glycans of fucosyltransferases with fluorophore-conjugated fucose and methods for glycan electrophoresis.
Article in Glycobiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Defined Glycan Ligands for Detecting Rare l-Sugar-Binding Proteins.Journal of the American Chemical Society · 2025Article
- Novel blood-based FUT7 DNA methylation is associated with lung cancer: especially for lung squamous cell carcinoma.Clinical epigenetics · 2022Article
- Endoglycosidase assay using enzymatically synthesized fluorophore-labeled glycans as substrates to uncover enzyme substrate specificities.Communications biology · 2022Article
- Fluorescent glycan fingerprinting of SARS2 spike proteins.Scientific reports · 2021Article
- Development of Lectin Modified Fluorescent Magnetic Particles for Highly Sensitive Detection of Glycoconjugates.Sensors (Basel, Switzerland) · 2021Article
- Chemical reporters to study mammalian O-glycosylation.Biochemical Society transactions · 2021Review
- FUT7 Promotes the Epithelial-Mesenchymal Transition and Immune Infiltration in Bladder Urothelial Carcinoma.Journal of inflammation research · 2021Article
- Fluorescent Detection ofBioconjugate chemistry · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Like sialylation, fucose usually locates at the nonreducing ends of various glycans on glycoproteins and constitutes important glycan epitopes. Detecting the substrate glycans of fucosyltransferases is important for understanding how these glycan epitopes are regulated in response to different growth conditions and external stimuli. Here we report the detection of these glycans on glycoproteins as well as in their free forms via enzymatic incorporation of fluorophore-conjugated fucose using FUT2, FUT6, FUT7, FUT8 and FUT9. Specifically, we describe the detection of the substrate glycans of these enzymes on fetal bovine fetuin, recombinant H1N1 viral neuraminidase and therapeutic antibodies. The detected glycans include complex and high-mannose N-glycans. By establishing a series of precursors for the synthesis of Lewis X and sialyl Lewis X structures, we not only provide convenient electrophoresis methods for studying glycosylation but also demonstrate the substrate specificities and some kinetic features of these enzymes. Our results support the notion that fucosyltransferases are key targets for regulating the synthesis of Lewis X and sialyl Lewis X structures.
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