Adhesion and docking via integrins, ICAM-1, and MFG-E8 on dendritic cells and their exosomes

The adhesion and docking mechanism involving integrins, ICAM-1, and MFG-E8 on dendritic cells (DCs) and their exosomes (dexosomes) is a fundamental process for intercellular communication and immune regulation (Thery et al., 2002 [PMID: 12140582]). Dexosomes carry MHC-peptide complexes and adhesion molecules like ICAM-1 (CD54), which interact with integrins such as LFA-1 (CD11a/CD18) on the surface of DCs or T cells to facilitate antigen transfer and activation (Segura et al., 2005 [PMID: 15905584]). Additionally, Milk Fat Globule-EGF Factor 8 (MFG-E8), also known as lactadherin, acts as a molecular bridge by binding to phosphatidylserine on the exosome surface and to alpha-v beta-3 or alpha-v beta-5 integrins on the DC surface (Hanayama et al., 2002 [PMID: 11907578]). This multi-protein interaction ensures the efficient docking and internalization of exosomes, which is critical for the amplification of immune responses in cancer and infectious diseases. While the entire process is not a single therapeutic target, individual components like ICAM-1 and specific integrins are targeted by drugs such as Lifitegrast and Natalizumab to modulate inflammation and immune cell trafficking (Nolte-'t Hoen & Wauben, 2012 [PMID: 23071587]). Understanding this docking mechanism is vital for optimizing exosome-based drug delivery and immunotherapy.

Other names

Dendritic cell exosome dockingDexosome adhesion mechanismMFG-E8-mediated exosome uptakeExosome-DC interaction pathway

Inhibition of leukocyte adhesion and exosome-mediated antigen transfer by blocking integrin-ligand interactions