糖基化
糖尿病
化学
计算生物学
生物化学
生物
内分泌学
作者
Yihan Chen,Suyue Lu,Shuo Shan,Weihao Wu,Xinxin He,Mohamed A. Farag,Weichao Chen,Chao Zhao
出处
期刊:Phytomedicine
[Elsevier BV]
日期:2025-03-23
卷期号:141: 156673-156673
被引量:6
标识
DOI:10.1016/j.phymed.2025.156673
摘要
BACKGROUND: Protein glycosylation as a common post-translational modification that has significant impacts on protein folding, enzymatic activity, and interfering with receptor functioning. In recent years, with the rapid development of glycopeptide enrichment and analysis technology and the deepening of glycosylation research, glycosylation has gradually become a sign of disease occurrence and development. Multiple investigations suggest that protein glycosylation affect the advances of diabetes and aging. PURPOSE AND METHODS: This review was focused on the action mechanisms of glycosylated proteins production, permanent abnormalities in extracellular matrix component function, inflammatory and reactive oxygen species production, as well as the glycosylated characterizations of diabetes and aging. Further, advances in glycosylation analysis and detection methods are presented for the first time, highlighting for needed future developments. All literatures were gathered from PubMed and Google Scholar. RESULTS: Herein, we review how protein glycosylation impacts the progression of diabetes and aging. Specifically, we focus on various types of glycosylation, including N-linked glycosylation, O-linked glycosylation, C-glycosylation, S-glycosylation, and glycophosphatidylinositol (GPI) anchors. N-linked glycosylation and O-linked glycosylation are commonly observed glycosylation forms, wherein O-GlcNAcylation plays a significant role in diabetes, while N-glycan could serve as biomarkers for identifying inflammation and aging. CONCLUSIONS: Protein glycosylation produces a vastly larger number of core glycan structures through utilizing at least 173 glycosyltransferases and repeated common scaffolds. Single protein may contain multiple glycosylation sites, and the structure and occupancy of glycan at each site may be different, resulting in the macro heterogeneity of protein glycosylation. This review will contribute to how protein glycosylation impacts the life progress of cells and its association with diseases.
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