Integrin (cellular receptor for extracellular matrix components) (Integrin (plural: Integrins))

Integrins are transmembrane receptors composed of α and β subunits, responsible for mediating cell adhesion to the extracellular matrix (ECM) by binding matrix proteins such as collagen, fibronectin, and laminin[1][2][3][5]. Integrin activation triggers both outside-in and inside-out signal transduction, regulating cell migration, proliferation, survival, and tissue morphology[1][2]. ECM components serve as structural scaffolds and signaling reservoirs, influencing cellular differentiation, growth, and tissue integrity[2][4][5]. Integrins and ECM interactions are essential for development, wound repair, immune responses, and are implicated in diseases such as cancer and fibrosis[2][5][3]. The therapeutic targeting of integrins focuses on blocking disease-relevant cell-matrix interactions and signaling pathways. "Cellular integrins / extracellular matrix components" is not a precise target name and would typically be split: "Integrin" is the pharmacologic target, while "extracellular matrix component" (e.g., collagen, fibronectin) is its ligand or structural context.

Other names

cell adhesion receptorscell surface integrinsmatrix receptors

Inhibition of integrin-mediated cell adhesion to ECM (anti-metastatic, anti-inflammatory) Blockade of integrin signaling cascades (anti-proliferative, pro-apoptotic) Prevention of extravasation in immune disorders (immune cell trafficking blockade)