Yihan Chen , Suyue Lu , Shuo Shan , Weihao Wu , Xinxin He , Mohamed A. Farag , Weichao Chen , Chao Zhao
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引用次数: 0
Abstract
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.
背景蛋白质糖基化作为一种常见的翻译后修饰,对蛋白质的折叠、酶活性以及受体功能的干扰都有重要影响。近年来,随着糖肽富集和分析技术的快速发展以及糖基化研究的不断深入,糖基化逐渐成为疾病发生和发展的标志。多项研究表明,蛋白质糖基化会影响糖尿病和衰老的进程。目的和方法本综述主要关注糖基化蛋白质产生的作用机制、细胞外基质成分功能的永久性异常、炎症和活性氧的产生,以及糖尿病和衰老的糖基化特征。此外,报告还首次介绍了糖基化分析和检测方法的进展,强调了未来发展的需要。所有文献均来自 PubMed 和 Google Scholar。具体来说,我们关注各种类型的糖基化,包括N-连接糖基化、O-连接糖基化、C-糖基化、S-糖基化和糖磷脂酰肌醇(GPI)锚。N-连接糖基化和O-连接糖基化是常见的糖基化形式,其中O-GlcNAcylation在糖尿病中起着重要作用,而N-糖基化可作为识别炎症和衰老的生物标记物。单个蛋白质可能含有多个糖基化位点,而每个位点的糖基化结构和占有率可能不同,这就造成了蛋白质糖基化的宏观异质性。本综述将有助于了解蛋白质糖基化如何影响细胞的生命进程及其与疾病的关联。
期刊介绍:
Phytomedicine is a therapy-oriented journal that publishes innovative studies on the efficacy, safety, quality, and mechanisms of action of specified plant extracts, phytopharmaceuticals, and their isolated constituents. This includes clinical, pharmacological, pharmacokinetic, and toxicological studies of herbal medicinal products, preparations, and purified compounds with defined and consistent quality, ensuring reproducible pharmacological activity. Founded in 1994, Phytomedicine aims to focus and stimulate research in this field and establish internationally accepted scientific standards for pharmacological studies, proof of clinical efficacy, and safety of phytomedicines.