探索败血症和戈尔吉器官功能障碍之间的关系:生物信息学的见解和诊断标记物的发现
Wanli Ma1, Xinyi Liu1, Ran Yu2
1Department of Anesthesiology, Municipal Hospital of Chifeng, Chifeng, Inner Mongolia, China.
Frontiers in genetics
|February 21, 2025
概括
这项研究揭示了Golgi关联基因作为毒症发病的关键参与者. 像B3GNT5和C1GALT1C1这样的新生物标志物显示出对败血症诊断的高准确性.
科学领域:
- 生物信息学是一种生物信息学.
- 分子生物学分子生物学
- 免疫学 免疫学 免疫学
背景情况:
- 败血症是一种危及生命的传染病,与细胞内戈尔吉器官功能障碍有关.
- 了解毒症和戈尔吉装置之间的分子机制对于改善诊断和治疗至关重要.
研究的目的:
- 用生物信息学方法研究高尔基相关基因在败血症中的作用.
- 根据Golgi相关基因表达,识别出新的败血症诊断生物标志物.
主要方法:
- 来自NCBI GEO数据库的mRNA表达特征分析.
- 鉴定差异表达基因 (DEGs) 和与戈尔吉相关基因和WGCNA模块的交叉,以找到戈尔吉相关差异表达基因 (GARGs).
- 功能丰富分析 (GO,KEGG,GSEA),PPI网络构建,免疫透分析和使用后勤回归的诊断模型的开发.
主要成果:
- 确定了53种GARG,主要涉及蛋白质糖化和戈尔吉膜过程.
- 他们确定了8个枢纽基因,包括B3GNT5,FUT11和ST6GAL1.
- 使用五个基因 (B3GNT5,FUT11,MAN1C1,ST6GAL1,C1GALT1C1) 的诊断模型显示出高预测精度 (AUC>0.96).
- 免疫透分析显示,败血症患者和健康对照人群之间的免疫细胞种群存在显著差异.
结论:
- 这项研究确立了败血症和戈尔吉器官功能障碍之间的联系.
- 鉴定到的GARG和枢纽基因提供了对败血症发病因子的洞察.
- 新的生物标志物,包括B3GNT5,C1GALT1C1和GALNT14,显示出精确的败血症诊断的潜力.
相关概念视频
Golgi Apparatus
89.9K
As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.
89.9K
Golgi Matrix Proteins
2.0K
Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
2.0K
Transport Across the Golgi
4.0K
While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
4.0K
ER Retrieval Pathway
3.7K
In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
3.7K
Vesicular Tubular Clusters
2.4K
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
With the help of motor proteins such...
2.4K
Protein Glycosylation
6.7K
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...
6.7K


