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Cancer cell surface antigens are a diverse group of molecules, including proteins, glycoproteins, and glycolipids, that are overexpressed or uniquely expressed on the plasma membrane of malignant cells (National Cancer Institute, 2023). These antigens serve as critical docking sites for therapeutic monoclonal antibodies (mAbs), which are engineered to recognize and bind them with high specificity (Nature Reviews Cancer, 2018). Upon binding, these antibodies can exert anti-tumor effects through several mechanisms: recruiting immune effector cells to induce antibody-dependent cellular cytotoxicity (ADCC), activating the complement system for complement-dependent cytotoxicity (CDC), or directly inhibiting oncogenic signaling pathways necessary for tumor growth and survival (PubMed, PMC6348551). Common examples of such targets include HER2 in breast cancer, CD20 in B-cell lymphomas, and EGFR in colorectal and head and neck cancers (Journal of Hematology & Oncology, 2021). While highly effective, the therapeutic utility of targeting these antigens is often limited by 'on-target, off-tumor' toxicities, where the antibody binds to healthy tissues expressing lower levels of the same antigen (Frontiers in Immunology, 2020). Modern advancements in this field include the development of antibody-drug conjugates (ADCs) and bispecific antibodies to enhance the potency and selectivity of targeting these surface markers (Nature Reviews Drug Discovery, 2022).
Therapeutic monoclonal antibodies target these antigens to induce cell death through antibody-dependent cellular cytotoxicity (ADCC), complement-dependent cytotoxicity (CDC), direct induction of apoptosis, or by blocking essential growth signaling pathways and ligand-receptor interactions (Nature Reviews Cancer, 2018; PubMed, PMC6348551).
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