相关实验视频

Updated: Jan 13, 2026

Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography

Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography

Published on: January 18, 2020

免疫球蛋白GN-糖化预测缺血性中风的长期风险:一个嵌套的病例控制研究

Shuyu Sun^1,2, Jiheng Hao³, Chengxu Yu⁴

¹School of Public Health, Shandong First Medical University & Shandong Academy of Medical Sciences, Jinan, China.

Journal of translational medicine

|October 28, 2025

概括

免疫球蛋白G (IgG) 的化和银化降低与缺血性中风 (IS) 的发展有关. IgG N-glycan 档案可以作为预测长期IS风险的生物标志物.

科学领域:

生物化学生物化学
免疫学免疫学免疫学
神经学神经学

背景情况:

缺血性中风 (IS) 是全球成年人残疾和死亡的主要原因.
了解IS进展包括分析免疫球蛋白G (IgG) N-甘氨酸和炎症性细胞因子.
确定高IS风险个体的生物标志物对于早期干预至关重要.

研究的目的:

与IS进展相关的IgG N-甘氨酸指纹的特征.
为了识别与IS发展相关的循环炎性细胞因子.
选潜在的生物标志物来预测IS风险.

主要方法:

一项前性队列研究 (LCSRC) 追踪了1599名健康参与者,持续了9年.
血清IgG N-甘氨酸的概况使用水友相互作用染色学 (HILIC-UPLC) 来分析.
使用后勤回归来构建IS发生的预测模型.

主要成果:

在IS病例中,特定的IgG N-甘氨酸 (GP1-4,6-7,11,13,19,24) 升高,而其他病例 (GP5,8,14,18) 降低.
与对照组相比,IS患者的MMP-9,TNF-α和hs-CRP水平较高.
降低IgG的fucosylation,monogalactosylation和digalactosylation与降低IS风险显著相关;基于糖化基的模型实现了0.756.75的AUC.

结论:

降低IgG的fucosylation和galactosylation与IS的发展显著相关,可能是通过慢性炎症.
IgG N-糖基化指纹显示为预测长期IS风险的生物标志物具有前途.

关键词:

在N-glycosylation的过程中.生物标志物生物标志物免疫球蛋白G是一种免疫球蛋白.炎症炎症是一种炎症.缺血性中风是因为缺血性中风.嵌套病例控制研究研究.

更多相关视频

Profiling Anti-Neu5Gc IgG in Human Sera with a Sialoglycan Microarray Assay

Profiling Anti-Neu5Gc IgG in Human Sera with a Sialoglycan Microarray Assay

Published on: July 13, 2017

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

相关概念视频

Proteoglycans

Proteoglycans

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,...

Oligosaccharide Assembly

Oligosaccharide Assembly

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...

Transcytosis of IgG

Transcytosis of IgG

Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...