Epithelial cell adhesion molecule (Ep-CAM) is a transmembrane glycoprotein predominantly expressed on the surface of various epithelial cells. It plays a critical role in cell-cell adhesion, ensuring that cells within epithelial tissues are bound together. Structurally, Ep-CAM comprises a large extracellular domain responsible for mediating cell-cell interactions, a single transmembrane domain, and a short cytoplasmic tail. Beyond its adhesive functions, Ep-CAM is also involved in cell signaling, proliferation, migration, and differentiation. Due to its widespread expression across numerous epithelial tissues, it serves as a pivotal player in maintaining tissue architecture and function.
Ep-CAM inhibitors encompass a range of molecules designed to modulate the activity of the Ep-CAM protein. These inhibitors aim to interfere with the normal functioning of Ep-CAM, which can be achieved through various mechanisms. Some inhibitors block the extracellular domain of Ep-CAM, preventing its interaction with adjacent cells and thus disrupting cell-cell adhesion. Others might inhibit the intracellular signaling pathways associated with Ep-CAM, thereby altering its downstream effects on cellular processes. Still, others could prevent the proper localization or expression of Ep-CAM on the cell surface.
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