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Tumor-associated glycans are abnormal carbohydrate structures found on glycoproteins or glycolipids at the surface of cancer cells, most notably in epithelial-derived tumors (carcinomas)[5][1][3]. These aberrant glycans arise from altered glycosyltransferase expression in cancer and are typically represented by incomplete or truncated O-glycans (like Tn, sialyl-Tn, and TF antigens), or by increased fucosylation and sialylation (such as sialyl-Lewis antigens)[5][1]. Unlike their fully processed counterparts in healthy tissues, these tumor-associated glycans exhibit increased immunogenicity and play key roles in cancer progression by altering cell–cell and cell–matrix interactions, promoting cell motility and metastasis, and modulating the anti-tumor immune response, frequently contributing to immune evasion[1][4][5]. Tumor-associated glycans serve as clinically relevant biomarkers for diagnosis, prognosis, and monitoring, and represent promising but challenging targets for immunotherapy and vaccine development in oncology[3][5][8][6].
Antibody-mediated targeting and immune activation (antibodies bind tumor glycans to induce tumor cell death or alter immune response)[5]. Blocking glycan–lectin interactions to inhibit metastasis or immune evasion[1][5].
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