Extracellular matrix-receptor interaction signaling pathway (ECM-receptor interaction)

The extracellular matrix (ECM)-receptor interaction signaling pathway (KEGG: hsa04512) is a fundamental biological network that mediates communication between the extracellular environment and the intracellular space [2]. It consists of a diverse set of ECM components, including collagens, laminins, and fibronectins, which interact with specific cell surface receptors such as integrins, CD44, and syndecans to mediate cell-matrix adhesion and signal transduction [2, 8]. These interactions are essential for maintaining tissue structure and regulating critical cellular processes like adhesion, migration, differentiation, and survival [2, 6]. In pathological contexts, abnormal ECM-receptor signaling is a major contributor to cancer progression, facilitating epithelial-mesenchymal transition (EMT) and metastasis, as well as driving the development of organ fibrosis [4, 5, 6]. Pharmacological targeting of this pathway primarily involves the use of monoclonal antibodies or small molecules that block specific integrin receptors to treat cardiovascular, inflammatory, and oncological diseases [7, 10]. Additionally, downstream effectors like focal adhesion kinase (FAK) are being explored as therapeutic targets to disrupt the signaling consequences of these interactions [6, 10].

Other names

ECM-receptor interactionCell-extracellular matrix interactionKEGG pathway hsa04512

Drugs targeting this pathway typically function by blocking the binding of extracellular matrix ligands (such as fibronectin, collagen, or VCAM-1) to their respective transmembrane receptors (primarily integrins), thereby inhibiting downstream signaling cascades like FAK/Src and preventing cellular processes such as platelet aggregation, leukocyte extravasation, or tumor cell migration [1, 7, 10].