Schematic view of putative mechanisms responsible for galectin-3 enhancement of LPS-induced neutrophil activation.

<p>Monomeric Galectin-3 interacts with LPS glycans from LPS aggregates via its C-terminal domain. LPS/Gal 3 interactions induce Gal 3 oligomerization, which promotes the dissolution of LPS aggregates, stabilizes LPS monomers and enhances the LPS interaction with surface receptors, leading to increased neutrophil activation. CD14 only is shown as the initial LPS ligand on neutrophils, because it is highly glycosylated and could, potentially, interact directly with Gal 3. Moreover, being GPI-anchored, CD14 would be most easily clustered on the cell surface. However, this implies a secondary clustering of TLR/MD2, which would transmit or modulate signals into the cell.