Disease-associated glycans on cell surface proteins

Most of membrane molecules including cell surface receptors and secreted proteins including ligands are glycoproteins and glycolipids. Therefore, identifying the functional significance of glycans is crucial for developing an understanding of cell signaling and subsequent physiological and pathologital cellular events. In particular, the function of N-glycans associated with cell surface receptors has been extensively studied since they are directly involved in controlling cellular functions. In this review, we focus on the roles of glycosyltransferases that are involved in the modification of N-glycans and their target proteins such as epidermal growth factor receptor (EGFR), ErbB3, transforming growth factor beta (TGF-beta) receptor, T-cell receptors (TCR), beta-site APP cleaving enzyme (BACE1), glucose transporter 2 (GLUT2), E-cadherin, and alpha 5 beta 1 integrin in relation to diseases and epithelial mesenchymal transition (EMT) process. Above of those proteins are subjected to being modified by several glycosyltransferases such as N-acetylglucosaminyltransferase III (GnT-III), N-acetylglucosaminyltransferase IV (GnT-IV), N-acetylglucosaminyltransferase V (GnT-V), alpha 2,6 sialyltransferase 1 (ST6GAL1), and alpha 1,6 fucosyltransferase (Fut8), which are typical N-glycan branching enzymes and play pivotal roles in regulating the function of cell surface receptors in pathological cell signaling. (C) 2016 Elsevier Ltd. All rights reserved.