Integrin beta-1 bearing alpha-2,3-sialylated glycans (ITGB1 (alpha-2,3-sialylated))

Integrin beta-1 bearing alpha-2,3-sialylated glycans is a specific post-translationally modified form of the ITGB1 receptor, characterized by the attachment of sialic acid residues via alpha-2,3 linkages to its N-glycan chains. This modification is primarily mediated by sialyltransferases such as ST3Gal-IV and ST3Gal-III, and it significantly alters the receptor's affinity for extracellular matrix ligands like collagen, fibronectin, and laminin. In many cancers, including gastric, colon, and melanoma, the hypersialylation of beta-1 integrins is a hallmark of the metastatic phenotype, as it promotes cell migration and invasion by activating the FAK/Src signaling pathway. Furthermore, this specific glycoform can modulate the cell's response to external stimuli, such as protecting tumor cells from Galectin-3-induced apoptosis. Therapeutic targeting of this molecule focuses on small-molecule sialyltransferase inhibitors or glycan-specific agents designed to disrupt these pro-malignant signaling axes while sparing the protein backbone's basal functions.

Other names

Sialylated integrin beta-1alpha-2,3-sialylated CD29ST3Gal-IV-modified beta-1 integrinalpha-2,3-sialylated ITGB1

Inhibition of sialyltransferase enzymes (e.g., ST3Gal-IV or ST3Gal-III) to prevent the addition of alpha-2,3-linked sialic acid to the integrin beta-1 subunit, thereby reducing integrin-mediated focal adhesion kinase (FAK) signaling and inhibiting tumor cell motility and invasion.