<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Li TA</submitter><funding>Flight Attendant Medical Research Institute</funding><funding>NIA NIH HHS</funding><funding>NIAID NIH HHS</funding><funding>National Disease Research Interchange</funding><funding>FDA HHS</funding><funding>NHLBI NIH HHS</funding><funding>National Institutes of Health</funding><funding>NIH HHS</funding><funding>Food and Drug Administration</funding><funding>NIGMS NIH HHS</funding><pagination>cwae065</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11364441</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>34(10)</volume><pubmed_abstract>Human sialic acid-binding immunoglobulin-like lectins (Siglecs) are expressed on subsets of immune cells. Siglec-8 is an immune inhibitory Siglec on eosinophils and mast cells, which are effectors in allergic disorders including eosinophilic esophagitis. Inhibition occurs when Siglec-8 is crosslinked by multivalent Siglec ligands in target tissues. Previously we discovered a high-affinity Siglec-8 sialoglycan ligand on human airways composed of terminally sialylated keratan sulfate chains carried on a single protein, DMBT1. Here we extend that approach to another allergic inflammatory target tissue, human esophagus. Lectin overlay histochemistry revealed that Siglec-8 ligands are expressed predominantly by esophageal submucosal glands, and are densely packed in submucosal ducts leading to </pubmed_abstract><journal>Glycobiology</journal><pubmed_title>Sialylated keratan sulfates on MUC5B are Siglec-8 ligands in the human esophagus.</pubmed_title><pmcid>PMC11364441</pmcid><funding_grant_id>R01 FD004086</funding_grant_id><funding_grant_id>R01 AG064908</funding_grant_id><funding_grant_id>T32 GM135083</funding_grant_id><funding_grant_id>HL141952</funding_grant_id><funding_grant_id>GM135083</funding_grant_id><funding_grant_id>K12 HL141952</funding_grant_id><funding_grant_id>FD004086</funding_grant_id><funding_grant_id>U19 AI136443</funding_grant_id><funding_grant_id>AG064908</funding_grant_id><funding_grant_id>U42 OD011158</funding_grant_id><funding_grant_id>AI136443</funding_grant_id><funding_grant_id>U42OD11158</funding_grant_id><pubmed_authors>Schnaar RL</pubmed_authors><pubmed_authors>Awol AK</pubmed_authors><pubmed_authors>Gonzalez-Gil A</pubmed_authors><pubmed_authors>Ackerman SJ</pubmed_authors><pubmed_authors>Li TA</pubmed_authors><pubmed_authors>Orsburn BC</pubmed_authors></additional><is_claimable>false</is_claimable><name>Sialylated keratan sulfates on MUC5B are Siglec-8 ligands in the human esophagus.</name><description>Human sialic acid-binding immunoglobulin-like lectins (Siglecs) are expressed on subsets of immune cells. Siglec-8 is an immune inhibitory Siglec on eosinophils and mast cells, which are effectors in allergic disorders including eosinophilic esophagitis. Inhibition occurs when Siglec-8 is crosslinked by multivalent Siglec ligands in target tissues. Previously we discovered a high-affinity Siglec-8 sialoglycan ligand on human airways composed of terminally sialylated keratan sulfate chains carried on a single protein, DMBT1. Here we extend that approach to another allergic inflammatory target tissue, human esophagus. Lectin overlay histochemistry revealed that Siglec-8 ligands are expressed predominantly by esophageal submucosal glands, and are densely packed in submucosal ducts leading to </description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Aug</publication><modification>2026-05-29T17:17:36.203Z</modification><creation>2026-04-08T05:26:10.631Z</creation></dates><accession>S-EPMC11364441</accession><cross_references><pubmed>39173029</pubmed><doi>10.1093/glycob/cwae065</doi></cross_references></HashMap>