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The integrin family and other extracellular matrix (ECM)-binding cell surface receptors are a diverse group of transmembrane proteins that mediate cell-to-cell and cell-to-matrix adhesion (UniProt, 2023). Integrins, the most prominent members, are heterodimeric receptors consisting of alpha and beta subunits that facilitate bidirectional signaling, linking the extracellular environment to the intracellular cytoskeleton (NCBI Bookshelf, 2002). Other receptors in this category include CD44, syndecans, and discoidin domain receptors, which also interact with ECM components like collagen, fibronectin, and laminin (PubMed, PMID: 22595016). These receptors are vital for biological processes such as cell migration, proliferation, and survival, but their dysregulation is a hallmark of cancer metastasis, fibrosis, and inflammatory diseases (Nature Reviews Molecular Cell Biology, 2014). Therapeutic targeting of these receptors, particularly integrins, has led to the development of several approved drugs, including monoclonal antibodies and small molecules that block ligand binding to prevent thrombosis or treat autoimmune conditions (StatPearls, 2023).
Antagonism of the extracellular binding domain to prevent interaction with extracellular matrix (ECM) ligands (such as fibronectin, laminin, or collagen) or counter-receptors on other cells, thereby inhibiting adhesion-dependent signaling and cellular recruitment (PubMed, PMID: 28839150).
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