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Cell-surface glycoconjugates bearing terminal galactose are a diverse class of molecules, including glycoproteins and glycolipids, where galactose occupies the non-reducing end of the carbohydrate chain [Stockert, 1995]. These structures play critical roles in biological processes such as cell-cell recognition, adhesion, and the regulation of glycoprotein half-life in circulation. In the liver, terminal galactose residues are specifically recognized by the asialoglycoprotein receptor (ASGPR), which facilitates the internalization and degradation of desialylated proteins [Stockert, 1995]. This specific interaction is widely exploited in pharmacology for the targeted delivery of therapeutic agents, such as siRNA and chemotherapeutics, to hepatocytes [D'Souza & Devarajan, 2015]. Furthermore, alterations in terminal galactose expression, such as the exposure of the Thomsen-Friedenreich antigen, are frequently observed in various cancers, where they serve as markers for tumor progression or targets for lectin-based toxins [Pinho & Reis, 2015]. Understanding the distribution and density of these glycoconjugates is essential for developing high-affinity ligands and minimizing off-target effects in glycan-targeted therapies [Pinho & Reis, 2015].
Binding to terminal galactose residues to facilitate cellular uptake via receptor-mediated endocytosis or to induce direct cytotoxicity through ribosome-inactivating protein activity [Lord et al., 2003; D'Souza & Devarajan, 2015].
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