Integrins and extracellular matrix proteins (Integrins/ECM)

Integrins and extracellular matrix (ECM) proteins constitute a complex network of molecules essential for maintaining tissue architecture and mediating cellular communication [1]. Integrins are heterodimeric transmembrane receptors composed of alpha and beta subunits that facilitate cell-cell and cell-matrix adhesion, serving as a bridge for bidirectional signaling between the intracellular cytoskeleton and the extracellular environment [2]. ECM proteins, such as collagen, fibronectin, and laminin, provide the structural scaffold for tissues and act as ligands for integrin receptors to regulate processes like cell proliferation, migration, and survival [3]. Dysregulation of these interactions is a hallmark of various pathologies, including cancer metastasis, where integrin signaling promotes tumor cell invasion, and fibrotic diseases characterized by excessive ECM deposition [4]. Therapeutically, integrins are targeted by monoclonal antibodies and small molecules to treat conditions such as thrombosis, multiple sclerosis, and inflammatory bowel disease by inhibiting specific ligand-receptor interactions [5]. For instance, inhibitors of integrin alpha-IIb beta-3 are used as potent anti-platelet agents, while blockers of alpha-4 integrins manage chronic inflammation [5][6]. Despite their clinical utility, targeting these pathways presents challenges, including the risk of systemic side effects like bleeding or impaired immune surveillance [6]. The diversity of integrin-ECM pairings allows for highly specific biological responses, making them attractive yet complex targets for drug development [2][4].

Other names

Cell adhesion moleculesECM componentsMatrix proteinsAdhesion receptorsIntegrin receptors

Inhibition of ligand binding to heterodimeric integrin receptors to prevent cell-cell or cell-matrix adhesion and modulate downstream intracellular signaling pathways.