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CD52 cell surface glycoprotein (CD52), also known as CAMPATH-1 antigen, is a small, heavily glycosylated protein anchored to the cell membrane via a glycosylphosphatidylinositol (GPI) link [1, 3]. It is highly expressed on the surface of mature lymphocytes, monocytes, and dendritic cells, but is notably absent on hematopoietic stem cells [3, 10]. While its precise biological function remains partially elusive, it is involved in immune regulation, cell migration, and anti-adhesion, potentially through its interaction with the inhibitory receptor SIGLEC10 [3, 5, 12]. CD52 is a significant therapeutic target in oncology and immunology, particularly for the treatment of chronic lymphocytic leukemia (CLL) and relapsing-remitting multiple sclerosis (RRMS) [5, 10]. The monoclonal antibody alemtuzumab targets CD52 to induce rapid and profound depletion of circulating lymphocytes through mechanisms such as antibody-dependent cell-mediated cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC) [10, 14]. Despite its efficacy, targeting CD52 carries risks of severe infections and secondary autoimmune conditions due to the broad depletion of immune cells [9, 14]. Monitoring of lymphocyte counts and CD52 expression levels is often required to manage treatment efficacy and safety [8, 17].
Antibody-dependent cell-mediated cytotoxicity (ADCC), complement-dependent cytotoxicity (CDC), and induction of apoptosis leading to rapid and profound depletion of CD52-positive lymphocytes and monocytes.
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