风湿性关节炎的综合糖化签名
Oleg A Mayboroda1, Guinevere S M Lageveen-Kammeijer1,2, Manfred Wuhrer1
1Center for Proteomics and Metabolomics, Leiden University Medical Center, 2333 ZA Leiden, The Netherlands.
Biomolecules
|July 29, 2023
概括
这项研究揭示了一种常见的类风湿性关节炎 (RA) 糖化特征,跨越免疫球蛋白G (IgG),免疫球蛋白A (IgA) 和全血清N-葡萄糖 (TSNG). 这种签名独立于自身抗体状态,可以帮助诊断和监测RA.
科学领域:
- 免疫学 免疫学 免疫学
- 葡萄糖生物学 葡萄糖生物学
- 类风湿病学 类风湿病学
背景情况:
- 风湿性关节炎 (RA) 是一种普遍存在的自身免疫性疾病,影响关节和其他器官.
- 改变的抗体糖化是RA的已知特征,之前的研究主要集中在免疫球蛋白G (IgG) 上.
- 最近的发现表明,免疫球蛋白A (IgA) 和全血清N-葡萄糖 (TSNG) 糖化变化在RA中也很重要.
研究的目的:
- 在类风湿性关节炎 (RA) 中整合和比较IgG,IgA和TSNG的糖化特征.
- 评估这些糖化模式与RA的关联,自身抗体阳性和疾病活性.
- 为了确定RA的常见的糖化签名.
主要方法:
- 在妊娠引起的类风湿性关节炎改善 (PARA) 队列中分析IgG,IgA和TSNG糖化模式.
- 在RA患者和对照人群之间对糖基化特征的比较.
- 评估糖化模式与疾病特征之间的相关性.
主要成果:
- 在RA患者中确定了IgG,IgA和TSNG的独特的糖化特征.
- 证明这些糖化变化与RA疾病活性有关.
- 揭示了一种常见的,复合的RA糖化签名,独立于自身抗体状态.
结论:
- IgG,IgA和TSNG的糖化模式共同形成了类风湿性关节炎 (RA) 的显著特征.
- 这种复合的RA糖化签名是疾病存在和活性的潜在生物标志物.
- 识别的签名与自身抗体状态的独立性提供了一种新的诊断和监测方法.
相关概念视频
Genome-wide Association Studies-GWAS
13.6K
Genome-wide association studies or GWAS are used to identify whether common SNPs are associated with certain diseases. Suppose specific SNPs are more frequently observed in individuals with a particular disease than those without the disease. In that case, those SNPs are said to be associated with the disease. Chi-square analysis is performed to check the probability of the allele likely to be associated with the disease.
GWAS does not require the identification of the target gene involved in...
GWAS does not require the identification of the target gene involved in...
13.6K
Glycosaminoglycans
4.9K
Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
4.9K
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
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
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
The JAK-STAT Signaling Pathway
9.0K
Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...
9.0K


