Eosinophil surface-adhesion molecules

Eosinophil surface-adhesion molecules are a diverse class of proteins expressed on the outer membrane of eosinophils that facilitate their movement from the blood into tissues. These molecules include various integrins, such as alpha-4 beta-1 (VLA-4) and alpha-M beta-2 (Mac-1), as well as selectin ligands like P-selectin glycoprotein ligand-1 (PSGL-1) (Bochner, 2000). Their primary biological function is to mediate the multi-step adhesion cascade, which includes tethering, rolling, firm adhesion, and diapedesis across the vascular endothelium (Rosenberg et al., 2013). In inflammatory diseases like asthma, allergic rhinitis, and eosinophilic esophagitis, these molecules are often upregulated or activated, leading to pathological eosinophil accumulation in organs (Hogan et al., 2008). This infiltration results in tissue damage and remodeling due to the release of eosinophil-derived neurotoxin, major basic protein, and reactive oxygen species. Drugs targeting these molecules, such as the monoclonal antibodies natalizumab and vedolizumab, work by blocking the interaction between eosinophil integrins and their endothelial ligands like VCAM-1 or MAdCAM-1 (Stein & Keshav, 2007). While effective at reducing tissue eosinophilia, these therapies can be associated with significant safety concerns, including the risk of progressive multifocal leukoencephalopathy (PML) due to impaired immune surveillance in the central nervous system (Yousry et al., 2006).

Other names

Eosinophil adhesion receptorsEosinophil homing receptorsEosinophil integrinsEosinophil selectin ligands

Antagonism of cell surface receptors to prevent binding to endothelial ligands, thereby inhibiting leukocyte rolling, firm adhesion, and extravasation into inflamed tissues.