Zhang NZ, Zhao LF, Zhang Q, Fang H, Song WL, Li WZ, Ge YS, Gao P. Core fucosylation and its roles in gastrointestinal glycoimmunology. World J Gastrointest Oncol 2023; 15(7): 1119-1134 [PMID: 37546555 DOI: 10.4251/wjgo.v15.i7.1119]
Corresponding Author of This Article
Peng Gao, MD, PhD, Director, Professor, Clinical Laboratory, The Second Hospital of Dalian Medical University, No. 467 Zhongshan Road, Shahekou District, Dalian 116023, Liaoning Province, China. gaop@dicp.ac.cn
Research Domain of This Article
Immunology
Article-Type of This Article
Review
Open-Access Policy of This Article
This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
Nian-Zhu Zhang, Li-Fen Zhao, Peng Gao, Clinical Laboratory, The Second Hospital of Dalian Medical University, Dalian 116023, Liaoning Province, China
Qian Zhang, Department of Cell Therapy, Shanghai Tianze Yuntai Biomedical Co., Ltd., Shanghai 200100, China
Hui Fang, Graduate School of Comprehensive Human Sciences, University of Tsukuba, Tsukuba 305-0005, Ibaraki, Japan
Wan-Li Song, Wen-Zhe Li, Guangdong Provincial Key Laboratory of Infectious Diseases and Molecular Immunopathology, Shantou University Medical College, Shantou 515041, Guangdong Province, China
Yu-Song Ge, Department of Neurology, The Second Hospital of Dalian Medical University, Dalian 116023, Liaoning Province, China
Author contributions: Zhang NZ and Zhao LF contributed equally to this work and wrote the manuscript; Gao P revised the review; Li WZ and Ge YS designed the structure of review; Zhang Q, Fang H, and Song WL prepared the figures and table; all authors have read and approve the final manuscript.
Supported bythe National Natural Science Foundation of China, No. 32171279; Natural Science Foundation of Liaoning Province, No. 2022-BS-254, and No. 2022-MS-317; and the Project of Dalian Medical Science Research, No. 2012026.
Conflict-of-interest statement: The authors declare no commercial or financial conflict of interest.
Open-Access: This article is an open-access article that was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution NonCommercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: https://creativecommons.org/Licenses/by-nc/4.0/
Corresponding author: Peng Gao, MD, PhD, Director, Professor, Clinical Laboratory, The Second Hospital of Dalian Medical University, No. 467 Zhongshan Road, Shahekou District, Dalian 116023, Liaoning Province, China. gaop@dicp.ac.cn
Received: January 18, 2023 Peer-review started: January 18, 2023 First decision: February 24, 2023 Revised: February 28, 2023 Accepted: May 8, 2023 Article in press: May 8, 2023 Published online: July 15, 2023 Processing time: 175 Days and 2.6 Hours
Abstract
Glycosylation is a common post-translational modification in eukaryotic cells. It is involved in the production of many biologically active glycoproteins and the regulation of protein structure and function. Core fucosylation plays a vital role in the immune response. Most immune system molecules are core fucosylated glycoproteins such as complements, cluster differentiation antigens, immunoglobulins, cytokines, major histocompatibility complex molecules, adhesion molecules, and immune molecule synthesis-related transcription factors. These core fucosylated glycoproteins play important roles in antigen recognition and clearance, cell adhesion, lymphocyte activation, apoptosis, signal transduction, and endocytosis. Core fucosylation is dominated by fucosyltransferase 8 (Fut8), which catalyzes the addition of α-1,6-fucose to the innermost GlcNAc residue of N-glycans. Fut8 is involved in humoral, cellular, and mucosal immunity. Tumor immunology is associated with aberrant core fucosylation. Here, we summarize the roles and potential modulatory mechanisms of Fut8 in various immune processes of the gastrointestinal system.
Core Tip: Core fucosylation is driven by fucosyltransferase 8 (Fut8), which catalyzes the addition of α-1,6-fucose to the innermost GlcNAc residue of N-glycans. Core fucosylation plays a vital role in immune responses. Most immune system molecules are core fucosylated glycoproteins that play important roles in antigen recognition and clearance, cell adhesion, lymphocyte activation, apoptosis, signal transduction, and endocytosis. Fut8 is involved in humoral immune responses, cellular immunity, mucosal immunity, and tumor immunology. Here, we summarize the roles and potential modulatory mechanisms of Fut8 in various immune responses of the gastrointestinal system.
