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The extracellular matrix (ECM) and cell-surface receptors constitute a dynamic structural and functional network essential for multicellular life. The ECM is composed of a diverse array of macromolecules, including fibrous proteins like collagens and elastins, and specialized glycoproteins such as fibronectin and laminin, which provide physical scaffolding and biochemical cues to cells [1, 3, 4]. Cell-surface receptors, most notably the integrin family, serve as the primary interface between the intracellular cytoskeleton and the extracellular environment, translating mechanical and chemical signals into cellular responses [2, 5]. Dysregulation of this system is a central feature in various pathologies; for instance, excessive ECM deposition leads to fibrosis, while its degradation and altered receptor signaling facilitate cancer cell invasion and metastasis [3, 4]. Therapeutically, this category is targeted by various agents, such as monoclonal antibodies that block integrin-mediated adhesion to treat inflammatory diseases or prevent thrombosis [5]. Because these components are ubiquitous and involved in fundamental processes like tissue repair, pharmacological intervention requires high specificity to avoid significant safety concerns such as impaired healing or immune suppression [4].
Inhibition of cell-matrix adhesion, blockade of ligand-receptor signaling, and modulation of extracellular matrix remodeling [3, 5].
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