蛋白O-GlcNAcylation:从 (病理) 生理学的角度来看,肝脏代谢灵活性中的甜蜜中心
Ya-Jie Hu1, Xu Zhang1, Hong-Ming Lv1
1Key Laboratory of Bovine Disease Control in Northeast China of Ministry of Agriculture and Rural affairs of the People's Republic of China, College of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, China.
概括
O-GlcNAcylation是一种对营养敏感的过程,调节细胞功能和葡萄糖平衡,特别是在肝脏中. 异常的O-GlcNAcylation有助于肝脏疾病和癌症的进展.
科学领域:
- 生物化学 生物化学
- 细胞生物学 细胞生物学
- 代谢调节 代谢调节 代谢调节
背景情况:
- O-GlcNAcylation是一种动态的翻译后修饰,调节蛋白质功能.
- 它是由O-GlcNAc转移酶和O-GlcNAcase控制的,对营养的可用性敏感.
- 肝脏O-GlcNAcylation对于葡萄糖平衡和胰岛素信号传递至关重要.
研究的目的:
- 审查O-GlcNAcylation的特征和稳态.
- 解释其营养敏感性和胰岛素信号的调节.
- 讨论其在肝脏疾病和癌症中的作用.
主要方法:
- 关于O-GlcNAcylation的文学评论.
- 分析其在代谢途径中的作用.
- 检查其参与肝脏病理生理学的研究.
主要成果:
- O-GlcNAcylation 作为营养传感器,影响碳水化合物,氨基酸,脂质和核酸代谢.
- 在禁食和食期间,它精确调节胰岛素信号传递和肝脏代谢平衡.
- 失调的O-GlcNAcylation与非酒精性脂肪肝疾病,脂肪肝炎,纤维化和肝癌有关.
结论:
- O-GlcNAcylation 是细胞代谢和全身葡萄糖平衡的关键调节剂.
- 它的失调对肝脏疾病具有显著的病理生理学影响.
- 向O-GlcNAcylation可能为肝脏病理和癌症提供治疗策略.
相关概念视频
Cell Specific Gene Expression
13.6K
Multicellular organisms contain a variety of structurally and functionally distinct cell types, but the DNA in all the cells originated from the same parent cells. The differences in the cells can be attributed to the differential gene expression. Liver cells, whose functions include detoxification of blood, production of bile to metabolize fats, and synthesis of proteins essential for metabolism, must express a specific set of genes to perform their functions. Gene expression also varies with...
13.6K
Regulation of Metabolism
9.5K
Cellular needs and conditions vary from cell to cell and change within individual cells over time. For example, the required enzymes and energetic demands of stomach cells are different from those of fat storage cells, skin cells, blood cells, and nerve cells. Furthermore, a digestive cell works much harder to process and break down nutrients during the time that closely follows a meal compared with many hours after a meal. As these cellular demands and conditions vary, so do the amounts and...
9.5K
Covalently Linked Protein Regulators
6.8K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
6.8K
Liver Physiology
567
The liver, an essential organ in the human body, performs over 200 vital functions that can be broadly categorized into metabolic, hematological, endocrine regulation, and bile production.
Metabolic Regulation:
The liver is the central organ involved in regulating blood composition. It stabilizes blood glucose levels, maintaining them within the range of 70–110 mg/dL. When these levels drop, the liver breaks down glycogen reserves and releases glucose into the bloodstream. It can...
Metabolic Regulation:
The liver is the central organ involved in regulating blood composition. It stabilizes blood glucose levels, maintaining them within the range of 70–110 mg/dL. When these levels drop, the liver breaks down glycogen reserves and releases glucose into the bloodstream. It can...
567
Protein Glycosylation
6.9K
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...
6.9K
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


