Disease-associated glycans on cell surface proteins.

1. Mol Aspects Med. 2016 Oct;51:56-70. doi: 10.1016/j.mam.2016.04.008. Epub 2016 Apr 27. Disease-associated glycans on cell surface proteins. Takahashi M(1), Kizuka Y(2), Ohtsubo K(3), Gu J(4), Taniguchi N(5). Author information: (1)Department of Biochemistry, Sapporo Medical University School of Medicine, South-1 West-17, Chuo-ku, Sapporo 060-8556, Japan. (2)Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, Global Research Cluster, RIKEN, 2-1 Hirosawa, Wako 351-0198, Japan. (3)Department of Analytical Biochemistry, Faculty of Life Sciences, Kumamoto University, 4-24-1 Kuhonji, Chuo-ku, Kumamoto 862-0976, Japan. (4)Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Medical and Pharmaceutical University, 4-4-1 Komatsusima, Aobaku, Sendai, Miyagi 981-8558, Japan. (5)Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, Global Research Cluster, RIKEN, 2-1 Hirosawa, Wako 351-0198, Japan. Electronic address: dglycotani@riken.jp. 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 pathological 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 β (TGF-β) receptor, T-cell receptors (TCR), β-site APP cleaving enzyme (BACE1), glucose transporter 2 (GLUT2), E-cadherin, and α5β1 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), α2,6 sialyltransferase 1 (ST6GAL1), and α1,6 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. Copyright © 2016 Elsevier Ltd. All rights reserved. DOI: 10.1016/j.mam.2016.04.008 PMID: 27131428 [Indexed for MEDLINE]