Scholarlink

<p>Galectin-3 (Gal-3) is a carbohydrate-binding protein which plays crucial roles in inflammation, immune response, and cell signaling. At the ocular surface, Gal-3 is also known to crosslink transmembrane mucins to support barrier function. However, the biological role of Gal-3 in circulating tear fluid remains largely unexplored. Similarly, whether Gal-3 engages extracellular glycoprotein ligands in tears to affect biological processes is unknown. Herein, we combine lectin ELISA, affinity enrichment, mass spectrometry (MS)-based glycoproteomics, and lectin blotting to uncover Gal-3 interactors and their associated glycoepitopes. Overall, we report nearly 100 proteins enriched from tear fluid across 3 different patients, identifying proteins involved in immune response, inflammation, and antimicrobial activity. Most notably, we report lacritin as a ligand for Gal-3 and demonstrate that their binding is spliceoform-specific and dependent on lacritin multimerization. Taken together, this study elucidates new ligands for Gal-3 in tear film&#xa0;and investigates new biochemical mechanisms that fine-tune Gal-3 binding events.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Mapping galectin-3 ligands in human tear fluid establishes spliceoform-dependent lacritin binding

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年5月26日

查看全文
  • Vincent Chang,
  • Isaac Lian,
  • Keira E. Mahoney,
  • Jeffrey Romano,
  • Ali Reza Afshari,
  • Ryan J. Chen,
  • Xiangjun Chen,
  • Fredrik Fineide,
  • Ayyad Zartasht Khan,
  • Tor Paaske Utheim,
  • Niclas G. Karlsson,
  • Gordon W. Laurie,
  • Stacy A. Malaker

摘要

Galectin-3 (Gal-3) is a carbohydrate-binding protein which plays crucial roles in inflammation, immune response, and cell signaling. At the ocular surface, Gal-3 is also known to crosslink transmembrane mucins to support barrier function. However, the biological role of Gal-3 in circulating tear fluid remains largely unexplored. Similarly, whether Gal-3 engages extracellular glycoprotein ligands in tears to affect biological processes is unknown. Herein, we combine lectin ELISA, affinity enrichment, mass spectrometry (MS)-based glycoproteomics, and lectin blotting to uncover Gal-3 interactors and their associated glycoepitopes. Overall, we report nearly 100 proteins enriched from tear fluid across 3 different patients, identifying proteins involved in immune response, inflammation, and antimicrobial activity. Most notably, we report lacritin as a ligand for Gal-3 and demonstrate that their binding is spliceoform-specific and dependent on lacritin multimerization. Taken together, this study elucidates new ligands for Gal-3 in tear film and investigates new biochemical mechanisms that fine-tune Gal-3 binding events.