Integrins and extracellular matrix components (Integrins/ECM)

Integrins are a large family of heterodimeric transmembrane receptors, consisting of alpha and beta subunits, that facilitate cell-cell and cell-extracellular matrix (ECM) adhesion (Hynes, 2002, Cell). The ECM components, such as collagen, fibronectin, and laminin, serve as ligands that trigger outside-in signaling pathways regulating cell survival, proliferation, and migration (Humphries et al., 2006, Journal of Cell Science). Conversely, inside-out signaling regulates the affinity of integrins for their ligands, which is crucial for processes like platelet aggregation and leukocyte extravasation (Ley et al., 2016, Nature Reviews Immunology). In disease states, dysregulation of the integrin-ECM axis contributes to tumor metastasis, pathological angiogenesis, chronic inflammation, and fibrotic tissue buildup (Desgrosellier & Cheresh, 2010, Nature Reviews Cancer). Therapeutic strategies often involve monoclonal antibodies or small molecules designed to block specific integrin-ligand interactions, such as those targeting alpha-IIb-beta-3 for anti-thrombotic effects or alpha-4-beta-7 for inflammatory bowel disease (Coller, 2001, JCI).

Other names

Cell adhesion moleculesECM-receptor interactionIntegrin-ligand complexAdhesion receptors

Inhibition of integrin-mediated cell adhesion and signaling by blocking the interaction between integrin receptors and their extracellular matrix ligands (e.g., fibrinogen, fibronectin, or VCAM-1) (Ley et al., 2016, Nature Reviews Immunology).