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The fucosylated core 1 O-glycan epitope on CD49c (Integrin alpha-3) is a tumor-associated post-translational modification found predominantly on gastrointestinal cancer cells (Arlen et al., 2010, PMID: 20505107). While the protein backbone, CD49c, is widely expressed and functions as a receptor for laminin in cell-matrix adhesion (UniProt P26006), this specific glycosylation pattern is highly restricted to malignant tissues, particularly in colorectal and pancreatic adenocarcinomas (Lupu et al., 2016). This epitope is the primary target of the monoclonal antibody enserectimab, also known as NPC-1C or NEO-102, which was developed to treat refractory gastrointestinal cancers (ClinicalTrials.gov NCT01930929). The presence of this glycan is believed to result from the dysregulation of glycosyltransferases during oncogenesis, making it a specific marker for tumor cells. Therapeutic targeting of this epitope leverages immune-mediated mechanisms such as antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC) to selectively eliminate cancer cells (Patel et al., 2013). Clinical studies have explored its utility as both a therapeutic target and a diagnostic biomarker for patient stratification in gastrointestinal malignancies.
Enserectimab (NPC-1C) binds to the fucosylated core 1 O-glycan on CD49c, triggering antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC) against tumor cells (Arlen et al., 2010).
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