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Extracellular matrix (ECM) proteins and cell surface receptors constitute a complex network that provides structural support to tissues and mediates critical biochemical and mechanical signals between cells and their environment (Hynes, R. O., Science, 2009). The ECM consists of fibrous proteins like collagen and elastin, as well as glycoproteins such as fibronectin and laminin, which interact with specialized cell surface receptors, most notably the integrin family (Theocharis, A. D., et al., Advanced Drug Delivery Reviews, 2016). These interactions govern fundamental cellular processes including adhesion, migration, proliferation, and differentiation through mechanotransduction and signaling pathways (Humphrey, J. D., et al., Nature Reviews Molecular Cell Biology, 2014). In pathological states, dysregulation of the ECM-receptor axis contributes to cancer metastasis, tissue fibrosis, and chronic inflammatory conditions (Walker, C., et al., International Journal of Molecular Sciences, 2018). Therapeutic strategies often target these interactions using monoclonal antibodies or small molecules, such as integrin antagonists, to block cell adhesion or signaling (Ley, K., et al., Nature Reviews Drug Discovery, 2016). However, targeting these ubiquitous components presents challenges, including risks of impaired wound healing or systemic toxicity due to their broad physiological roles.
Inhibition of ligand binding to cell surface receptors (e.g., integrins), disruption of cell-matrix adhesion, and modulation of downstream signaling pathways.
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