多个免疫细胞中的蛋白O-GlcNAcylation及其治疗潜力
Huanhuan Cai1,2, Wei Xiong1,2, Haoyan Zhu1,2
1Department of Cardiology, Zhongnan Hospital of Wuhan University, Wuhan, China.
Frontiers in immunology
|September 7, 2023
概括
一种蛋白质修饰的O-GlcNAcylation对于免疫细胞功能至关重要. 本综述详细介绍了O-GlcNAc转移酶 (OGT) 和O-GlcNAcase (OGA) 如何通过六胺生物合成途径 (HBP) 调节免疫反应.
科学领域:
- 生物化学 生物化学
- 免疫学 免疫学 免疫学
- 分子生物学分子生物学
背景情况:
- O-GlcNAcylation是一种动态的翻译后修饰,涉及O-GlcNAc被O-GlcNAc转移酶 (OGT) 添加到蛋白质中,并被O-GlcNAcase (OGA) 删除.
- 这种修饰在免疫系统中普遍存在,并与各种生理和病理过程有关.
- 六胺生物合成途径 (HBP) 与O-GlcNAcylation和免疫细胞调节有关.
研究的目的:
- 提供关于免疫系统中蛋白质O-GlcNAcylation的当前研究的全面概述.
- 阐明O-GlcNAcylation影响免疫细胞生长,成熟和功能的分子机制.
- 突出O-GlcNAcylation在免疫细胞调节中的关键作用.
主要方法:
- 对O-GlcNAcylation和免疫学现有研究的文献综述.
- 对免疫细胞中O-GlcNAcylation的分子机制的分析.
- 对胺生物合成途径 (HBP) 的发现及其与O-GlcNAcylation的联系的综合.
主要成果:
- O-GlcNAcylation通过复杂的分子通路显著影响免疫细胞功能.
- OGT和OGA之间的动态相互作用决定了O-GlcNAcylation的程度,从而调节了免疫反应.
- 证据表明,HBP,O-GlcNAcylation和免疫细胞增殖和活动的调节之间存在强烈的相关性.
结论:
- 蛋白质O-GlcNAcylation是免疫细胞平衡和功能的关键调节者.
- 需要进一步的研究才能充分了解O-GlcNAcylation在免疫中的确切作用和治疗潜力.
- 准O-GlcNAcylation通路可能为调节疾病中的免疫反应提供新的策略.
相关概念视频
Proteoglycans
3.9K
Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
3.9K
Protein Glycosylation
7.0K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Glycosylation occurs in...
7.0K
Oligosaccharide Assembly
2.9K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
2.9K


