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Cadherin-1, widely known as E-cadherin, is a 120 kDa transmembrane glycoprotein that serves as a master regulator of calcium-dependent cell-cell adhesion in epithelial tissues. The 'O-mannosylated 70 kDa E-cadherin' refers to a specific pathological fragment or state of the protein associated with its post-translational modification by the POMT1/POMT2 enzyme complex. O-mannosylation is essential for the stability and functional localization of E-cadherin at the cell membrane; in the absence of this modification, the protein becomes unstable and is proteolytically cleaved into a characteristic 70 kDa fragment. This fragment and the overall loss of E-cadherin O-mannosylation are key biomarkers for gastric cancer progression and the epithelial-mesenchymal transition (EMT). While E-cadherin is primarily a tumor suppressor, its specific glycoforms and degradation products are targets for experimental monoclonal antibodies and diagnostic assays aimed at monitoring tumor invasiveness and restoring adhesive function.
Restoration of cell-cell adhesion, inhibition of epithelial-mesenchymal transition (EMT), stabilization of the mature 120 kDa protein, and neutralization of pro-oncogenic soluble fragments.
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