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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
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CD45 and Basigin (CD147) Are Functional Ligands for Galectin-8 on Human Leukocytes
Jean-Philippe F Gourdine1,2, Porfirio Nava3, Alexander J Noll4
1Chemistry Department, Lewis & Clark College, Portland, OR 97219, USA.
Biomolecules
|September 27, 2025
Summary
Galectin-8 (Gal-8) binds to leukocyte glycoproteins CD45 and basigin, initiating a novel cell signaling pathway called preaparesis. This glycan recognition mechanism is crucial for understanding leukocyte interactions and immune responses.
Area of Science:
- Immunology
- Glycobiology
- Cell Signaling
Background:
- Leukocyte glycoprotein interactions via glycan recognition are poorly understood.
- Galectin-8 (Gal-8) induces phosphatidylserine exposure (preaparesis) on activated neutrophils.
- Receptors for Gal-8 on leukocytes remain unidentified.
Purpose of the Study:
- To identify glycoprotein ligands for Gal-8 on human leukocytes (HL-60 cells).
- To elucidate the role of identified ligands in Gal-8-mediated signaling.
Main Methods:
- Proteomics and affinity chromatography using full-length and domain-specific Gal-8.
- Analysis of HL-60 cells to identify Gal-8 glycoprotein receptors.
- Assays to assess the impact of CD45 phosphatase activity on Gal-8 signaling.
Main Results:
- CD45 (isoforms RA and RC) and basigin (CD147) were identified as major Gal-8 ligands.
- Gal-8 binding requires poly-N-acetyllactosamine modifications on CD45 and basigin.
- Inhibition of CD45 phosphatase activity attenuated Gal-8-induced preaparesis.
Conclusions:
- Galectin-8 uniquely recognizes CD45 and basigin on leukocytes.
- CD45 plays a role in Gal-8-induced preaparesis signaling.
- These findings advance understanding of glycan-mediated cell recognition and signaling in leukocytes.
