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The extracellular matrix (ECM) and cell-surface adhesion receptors constitute a complex network that provides structural support and biochemical signaling to cells. ECM proteins, such as collagen, laminin, and fibronectin, form the physical scaffold of tissues, while adhesion receptors like integrins, cadherins, and selectins mediate interactions between cells and their environment [1][2]. These interactions are critical for fundamental biological processes, including cell proliferation, migration, and survival [3]. Dysregulation of the ECM or its receptors is a hallmark of various pathologies, particularly cancer metastasis, where tumor cells exploit adhesion pathways to invade distant tissues, and fibrotic diseases characterized by excessive matrix deposition [4][5]. Therapeutically, this class is targeted by several monoclonal antibodies and small molecules, most notably those inhibiting integrins to treat cardiovascular events, autoimmune disorders, and inflammatory conditions [6]. However, targeting these ubiquitous proteins poses challenges, including potential systemic toxicity and the complexity of redundant signaling pathways [7]. This entry is flagged as incorrect because it represents a broad functional category of hundreds of distinct proteins rather than a single specific therapeutic target.
Drugs targeting this class typically act as competitive antagonists or monoclonal antibodies that bind to the extracellular domains of adhesion receptors (such as integrins), thereby preventing their interaction with ECM ligands or counter-receptors on other cells to inhibit signaling or physical attachment [5][6].
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