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Cell-surface adhesion molecules (CAMs) and their extracellular ligands are a broad class of proteins that facilitate physical interactions between cells and between cells and the extracellular matrix (ECM) [1]. These molecules, which include integrins, cadherins, selectins, and members of the immunoglobulin superfamily, are essential for maintaining tissue architecture and facilitating immune cell trafficking [2][3]. Beyond structural roles, they function as transmembrane receptors that transduce biochemical signals to regulate cell survival, proliferation, and differentiation [4]. In disease states, dysregulated adhesion facilitates the infiltration of inflammatory cells into tissues and the detachment and migration of tumor cells during metastasis [5]. Therapeutic interventions often utilize monoclonal antibodies or small molecules to block specific adhesion pathways, such as the α4β7 integrin in inflammatory bowel disease or αIIbβ3 in cardiovascular events [6]. While effective, these therapies carry risks such as progressive multifocal leukoencephalopathy (PML) or increased susceptibility to opportunistic infections due to the disruption of normal immune surveillance [7].
Competitive antagonism of adhesion receptors to prevent ligand binding, inhibition of leukocyte rolling and extravasation, and disruption of intracellular signaling pathways associated with cell migration.
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