ArticleGlycobiology2018
Sialylated keratan sulfate proteoglycans are Siglec-8 ligands in human airways.
Article in Glycobiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 64 citations in OpenAlex.
- A glycosaminoglycan microarray identifies galectin-4 binding to sulfated glycosaminoglycans.Biochemistry and biophysics reports · 2026Article
- B3GNT7 regulates mucin glycosylation and protects against colitis and infection.bioRxiv : the preprint server for biology · 2026Article
- An ultrasensitive and modular platform to detect Siglec ligands and control immune cell function.Science advances · 2025Article
- Eosinophils in inflammatory bowel disease pathogenesis: an ROS-centric view.Frontiers in allergy · 2025Article
- Chemoenzymatic Synthesis of SulfatedJACS Au · 2024Article
- Sialic acid in the regulation of blood cell production, differentiation and turnover.Immunology · 2024Review
- GlcNAc6ST2/CHST4 Is Essential for the Synthesis of R-10G-Reactive Keratan Sulfate/SulfatedMolecules (Basel, Switzerland) · 2024Article
- Siglec 15 as a biomarker or a druggable molecule for non-small cell lung cancer.Journal of cancer research and clinical oncology · 2023Review
- Exploiting Substrate Specificities of 6-JACS Au · 2023Article
- Siglecs as potential targets of therapy in human mast cell- and/or eosinophil-associated diseases.Seminars in immunology · 2023Review
- The vertebrate sialylation machinery: structure-function and molecular evolution of GT-29 sialyltransferases.Glycoconjugate journal · 2023Review
- Siglecs in allergy and asthma.Molecular aspects of medicine · 2023Review
- Human sialoglycan ligands for immune inhibitory Siglecs.Molecular aspects of medicine · 2023Review
- (Glycan Binding) Activity-Based Protein Profiling in Cells Enabled by Mass Spectrometry-Based Proteomics.Israel journal of chemistry · 2023Article
- Article
- Flow Cytometry-Based Detection of Siglec Ligands.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Computationally guided conversion of the specificity of E-selectin to mimic that of Siglec-8.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Reading the glyco-code: New approaches to studying protein-carbohydrate interactions.Current opinion in structural biology · 2022Review
- Complementary Role of GlcNAc6ST2 and GlcNAc6ST3 in Synthesis of CL40-Reactive Sialylated and Sulfated Glycans in the Mouse Pleural Mesothelium.Molecules (Basel, Switzerland) · 2022Article
- Human brain sialoglycan ligand for CD33, a microglial inhibitory Siglec implicated in Alzheimer's disease.The Journal of biological chemistry · 2022Article
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Authors and funding
12 authors at 5 institutions in 1 country.
Funding
Abstract
Human siglecs are a family of 14 sialic acid-binding proteins, most of which are expressed on subsets of immune cells where they regulate immune responses. Siglec-8 is expressed selectively on human allergic inflammatory cells-primarily eosinophils and mast cells-where engagement causes eosinophil apoptosis and inhibits mast cell mediator release. Evidence supports a model in which human eosinophils and mast cells bind to Siglec-8 sialoglycan ligands on inflammatory target tissues to resolve allergic inflammation and limit tissue damage. To identify Siglec-8-binding sialoglycans from human airways, proteins extracted from postmortem human trachea were resolved by size-exclusion chromatography and composite agarose-acrylamide gel electrophoresis, blotted and probed by Siglec-8-Fc blot overlay. Three size classes of Siglec-8 ligands were identified: 250 kDa, 600 kDa and 1 MDa, each of which was purified by affinity chromatography using a recombinant pentameric form of Siglec-8. Proteomic mass spectrometry identified all size classes as the proteoglycan aggrecan, a finding validated by immunoblotting. Glycan array studies demonstrated Siglec-8 binding to synthetic glycans with a terminal Neu5Acα2-3(6-sulfo)-Gal determinant, a quantitatively minor terminus on keratan sulfate (KS) chains of aggrecan. Treating human tracheal extracts with sialidase or keratanase eliminated Siglec-8 binding, indicating sialylated KS chains as Siglec-8-binding determinants. Treating human tracheal histological sections with keratanase also completely eliminated the binding of Siglec-8-Fc. Finally, Siglec-8 ligand purified from human trachea extracts induced increased apoptosis of freshly isolated human eosinophils in vitro. We conclude that sialylated KS proteoglycans are endogenous human airway ligands that bind Siglec-8 and may regulate allergic inflammation.
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