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Fc-BCAM is a recombinant fusion protein consisting of the extracellular domain of the Basal Cell Adhesion Molecule (BCAM) fused to the Fc region of an immunoglobulin (typically IgG1). BCAM, also known as the Lutheran blood group glycoprotein (Lu), is a cell surface receptor that specifically binds to the laminin alpha-5 (LAMA5) chain, a key component of the extracellular matrix in basement membranes. In various malignancies, particularly ovarian cancer, the interaction between membrane-bound BCAM and LAMA5 facilitates tumor cell adhesion, migration, and the formation of spheroids, which are critical for peritoneal metastatic spread. Fc-BCAM acts as a decoy receptor or 'trap' by competitively binding to LAMA5, thereby preventing the interaction between endogenous BCAM on cancer cells and the basement membrane. This inhibition disrupts the mechanical and signaling pathways required for metastasis and tumor progression.
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