http://purl.uniprot.org/citations/15563466 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15563466 | http://www.w3.org/2000/01/rdf-schema#comment | "Sialic acid-binding immunoglobulin-like lectin 8 (Siglec-8) is selectively expressed on human eosinophils, basophils, and mast cells, where it regulates their function and survival. Previous studies demonstrated sialic acid-dependent binding of Siglec-8 but failed to reveal significant substructure specificity or high affinity of that binding. To test a broader range of potential ligands, a Siglec-8-Ig chimeric protein was tested for binding to 172 different glycan structures immobilized as biotinylated glycosides on a 384-well streptavidin-coated plate. Of these, approximately 40 structures were sialylated. Among these, avid binding was detected to a single defined glycan, NeuAcalpha2-3(6-O-sulfo)Galbeta1-4[Fucalpha1-3]GlcNAc, also referred to in the literature as 6'-sulfo-sLex. Notably, neither unsulfated sLex (NeuAcalpha2-3Galbeta1-4[Fucalpha1-3]GlcNAc) nor an isomer with the sulfate on the 6-position of the GlcNAc residue (6-sulfo-sLex, NeuAcalpha2-3Galbeta1-4[Fucalpha1-3](6-O-sulfo)GlcNAc) supported detectable binding. Subsequent secondary screening was performed using surface plasmon resonance. Biotin glycosides immobilized on streptavidin biosensor chips were exposed to Siglec-8-Ig in solution. Whereas surfaces derivatized with sLex and 6-sulfo-sLex failed to support detectable Siglec-8 binding, 6'-sulfo-sLex supported significant binding with a Kd of 2.3 microm. In a separate test of binding specificity, aminopropyl glycosides were covalently immobilized at different concentrations on activated (N-hydroxysuccinimidyl) glass surfaces (Schott-Nexterion Slide H). Subsequent exposure to Siglec-8-Ig precomplexed with fluorescein isothiocyanate anti-human Fc resulted in fluorescent signals at immobilized concentrations of 6'-sulfo-sLex of <5 pmol/spot. In contrast, sLex and 6-sulfo-sLex did not support any Siglec-8 binding at the highest concentration tested (300 pmol/spot). We conclude that Siglec-8 binds preferentially to the sLex structure bearing an additional sulfate ester on the galactose 6-hydroxyl."xsd:string |
http://purl.uniprot.org/citations/15563466 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m412378200"xsd:string |
http://purl.uniprot.org/citations/15563466 | http://purl.uniprot.org/core/author | "Mehta P."xsd:string |
http://purl.uniprot.org/citations/15563466 | http://purl.uniprot.org/core/author | "Blixt O."xsd:string |
http://purl.uniprot.org/citations/15563466 | http://purl.uniprot.org/core/author | "White J.R."xsd:string |
http://purl.uniprot.org/citations/15563466 | http://purl.uniprot.org/core/author | "Schnaar R.L."xsd:string |
http://purl.uniprot.org/citations/15563466 | http://purl.uniprot.org/core/author | "Bochner B.S."xsd:string |
http://purl.uniprot.org/citations/15563466 | http://purl.uniprot.org/core/author | "Alvarez R.A."xsd:string |
http://purl.uniprot.org/citations/15563466 | http://purl.uniprot.org/core/author | "Bovin N.V."xsd:string |
http://purl.uniprot.org/citations/15563466 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15563466 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/15563466 | http://purl.uniprot.org/core/pages | "4307-4312"xsd:string |
http://purl.uniprot.org/citations/15563466 | http://purl.uniprot.org/core/title | "Glycan array screening reveals a candidate ligand for Siglec-8."xsd:string |
http://purl.uniprot.org/citations/15563466 | http://purl.uniprot.org/core/volume | "280"xsd:string |
http://purl.uniprot.org/citations/15563466 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15563466 |
http://purl.uniprot.org/citations/15563466 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15563466 |
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http://purl.uniprot.org/uniprot/Q9NYZ4 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15563466 |
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