CD146 interacts with galectin-3 to mediate endothelial cell migration.
Here, we investigated the role of the cell membrane protein CD146 in galectin-3-mediated endothelial cell migration at the molecular level. Our results show that knocking down CD146 significantly attenuates galectin-3-mediated cell migration. Pull-down assays, gel filtration, and biolayer interferometry further demonstrate that galectin-3 binds to the CD146 ectodomain (eFL) with ... a KD of ~1.1 ?m. To identify the galectin-3-binding site, we used mass spectrometry to show that CD146 eFL has four N-glycosites, with PNGase F treatment indicating that N-glycans define the binding epitope. Galectin-3 likely interacts with Domain 5 on CD146 eFL, because it contains poly-N-acetyllactosamine sites, and deletion of this domain significantly reduces binding. Overall, our findings provide a better understanding of how galectin-3 interacts with cell membrane receptors to mediate endothelial cell migration.
Mesh Terms:
Blood Proteins, CD146 Antigen, Cell Line, Cell Movement, Endothelial Cells, Galectin 3, Galectins, Humans, Protein Domains
Blood Proteins, CD146 Antigen, Cell Line, Cell Movement, Endothelial Cells, Galectin 3, Galectins, Humans, Protein Domains
FEBS Lett
Date: Jun. 01, 2018
PubMed ID: 29741757
View in: Pubmed Google Scholar
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