Glycosylated receptors and integrins on malignant cells

Glycosylated receptors and integrins on malignant cells represent a broad class of cell surface proteins, including growth factor receptors (such as EGFR and VEGFR) and adhesion molecules (integrins), that undergo significant structural changes through aberrant glycosylation during cancer progression. These post-translational modifications, characterized by increased N-glycan branching, hypersialylation, and the expression of truncated O-glycans, fundamentally alter the proteins' stability, ligand affinity, and spatial organization on the plasma membrane. In the tumor microenvironment, these glycosylated structures often interact with endogenous lectins like galectins to form a 'galectin lattice,' which prevents receptor endocytosis and sustains oncogenic signaling pathways related to survival and proliferation. Therapeutic strategies targeting this complex include the use of integrin inhibitors to block cell-matrix interactions and galectin antagonists to disrupt the lattice and restore normal receptor turnover. Consequently, these molecules are critical determinants of tumor growth, angiogenesis, and metastatic potential, serving as both therapeutic targets and diagnostic biomarkers.

Other names

Tumor-associated glycosylated receptorsGlycosylated cell surface proteinsAberrantly glycosylated integrinsCancer-associated glyco-receptors

Inhibition of ligand binding to integrins, disruption of galectin-glycan lattice formation, and inhibition of aberrant glycosylation enzymes.