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Cancer cell membrane glycoproteins are a heterogeneous group of proteins localized to the plasma membrane of cancer cells, characterized by the covalent attachment of carbohydrate (glycan) chains. These glycoproteins play crucial roles in cancer biology, including cell signaling, adhesion, immune evasion, and metastasis. Their glycan structures are frequently altered in cancer, contributing to disease progression and serving as diagnostic and prognostic biomarkers. Notable examples include the epidermal growth factor receptor (EGFR), human epidermal growth factor receptor 2 (HER2), and mucins such as MUC1, all of which are validated therapeutic targets in various cancers. Aberrant glycosylation (e.g., increased sialylation, fucosylation, branching) on these molecules is associated with poor prognosis, drug resistance, and metastatic potential. Cancer cell membrane glycoproteins are collectively considered therapeutic targets, primarily through the development of monoclonal antibodies, small-molecule inhibitors, and glycan-targeting agents, though no single agent targets this entire class. The diversity and plasticity of glycosylation patterns present significant challenges for drug development, including tumor heterogeneity and the emergence of resistance.
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