Abstract
Colorectal cancer (CRC) is one of the main causes of cancer death in the world. Post-translational modifications (PTMs) have been extensively studied in malignancies due to its relevance in tumor pathogenesis and therapy. This review is focused on the dysregulation of glycosyltransferase expression in CRC and its impact in cell function and in several biological pathways associated with CRC pathogenesis, prognosis and therapeutic approaches. Glycan structures act as interface molecules between cells and their environment and in several cases facilitate molecule function. CRC tissue shows alterations in glycan structures decorating molecules, such as annexin-1, mucins, heat shock protein 90 (Hsp90), β1 integrin, carcinoembryonic antigen (CEA), epidermal growth factor receptor (EGFR), insulin-like growth factor-binding protein 3 (IGFBP3), transforming growth factor beta (TGF-β) receptors, Fas (CD95), PD-L1, decorin, sorbin and SH3 domain-containing protein 1 (SORBS1), CD147 and glycosphingolipids. All of these are described as key molecules in oncogenesis and metastasis. Therefore, glycosylation in CRC can affect cell migration, cell–cell adhesion, actin polymerization, mitosis, cell membrane repair, apoptosis, cell differentiation, stemness regulation, intestinal mucosal barrier integrity, immune system regulation, T cell polarization and gut microbiota composition; all such functions are associated with the prognosis and evolution of the disease. According to these findings, multiple strategies have been evaluated to alter oligosaccharide processing and to modify glycoconjugate structures in order to control CRC progression and prevent metastasis. Additionally, immunotherapy approaches have contemplated the use of neo-antigens, generated by altered glycosylation, as targets for tumor-specific T cells or engineered CAR (Chimeric antigen receptors) T cells.
Highlights
Colorectal cancer (CRC) has been categorized worldwide as the third most common diagnosed cancer and the fourth most usual cause of cancer death [1]
Alterations of glycan biosynthesis associated with abnormal glycosylation patterns of several molecules have been related with oncogenesis, cell growth, apoptosis inhibition, increased motility, cell migration, cell adhesion, tumor cell invasiveness and metastasis
Alterations in glycosyltransferase levels and glycosylation patterns have been evidenced in inflammatory conditions, tumorigenesis and metastasis [5,6,7,8,65,66]
Summary
Colorectal cancer (CRC) has been categorized worldwide as the third most common diagnosed cancer and the fourth most usual cause of cancer death [1]. Differential glycoproteomics and glycolipid profiles have been identified and analyzed Molecules such as annexin A1, mucins, heat shock protein 90, β1 integrin, selectin ligands, carcinoembryonic antigen (CEA), epidermal growth factor receptor (EGFR), insulin-like growth factor-binding protein 3 (IGFBP3), transforming growth factor beta (TGF-β) receptors, Fas (CD95), PD-L1, sorbin and SH3 domain-containing protein 1 (SORBS1), decorin, CD147 and glycosphingolipids show variations in their glycosylation pattern in CRC tissues when they are compared with healthy tissues. These changes are associated with the prognosis and evolution of the disease and response to radiation or chemotherapy agents [10,19,20]. We intend to summarize the role of glycosyltransferases and glycosylation profile in CRC pathogenesis and discuss their therapeutic implications
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