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Cell adhesion molecules (CAMs) are a diverse group of cell-surface proteins that mediate the interaction between cells and the extracellular matrix or between adjacent cells. In the context of inflammation, these molecules—including selectins, integrins, and members of the immunoglobulin superfamily—are critical for the multi-step process of leukocyte recruitment from the blood into tissues. This process involves tethering, rolling, activation, firm adhesion, and transendothelial migration (diapedesis). Dysregulation of CAM expression or function is a hallmark of chronic inflammatory diseases, autoimmune disorders, and cancer metastasis. Consequently, CAMs are significant therapeutic targets; drugs like natalizumab and vedolizumab work by blocking specific integrins to prevent inflammatory cell infiltration into target organs like the brain or gut. Other agents, such as crizanlizumab, target selectins to manage conditions like sickle cell disease by preventing vaso-occlusive crises. Despite their therapeutic potential, targeting CAMs carries risks, such as impaired host defense and increased susceptibility to opportunistic infections.
Antagonism of cell-surface receptors to inhibit leukocyte-endothelial interactions, thereby blocking the multi-step adhesion cascade (tethering, rolling, firm adhesion) and preventing the extravasation of inflammatory cells into target tissues.
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