蛋白质氨酸酸酶通过反应性氧物种的调节
Colin L Welsh1, Lalima K Madan2
1Department of Cell and Molecular Pharmacology & Experimental Therapeutics, College of Medicine, Medical University of South Carolina, Charleston, SC, United States.
Advances in cancer research
|July 28, 2024
概括
蛋白氨酸酸酶 (PTPs) 对于细胞信号传递至关重要,对氧化应激敏感. 本综述详细介绍了活性氧物种 (ROS) 如何可逆和不可逆地氧化PTP,影响其功能.
科学领域:
- 生物化学 生物化学
- 细胞生物学 细胞生物学
- 酶学 是一种酶学.
背景情况:
- 蛋白氨酸酸酶 (PTPs) 通过控制蛋白质酸化来调节重要的细胞过程,如分裂,增殖和分化.
- PTPs具有基于氨酸的催化机制,使其易受氧化还原调节和氧化应激反应的影响.
- 反应性氧物种 (ROS),特别是过氧化 (H2O2),可以显著改变PTP活性.
研究的目的:
- 审查PTP活体地点的结构和化学特性,以了解它们对ROS的脆弱性.
- 为了阐明 PTP 氧化和 H2O2.2 无活化的机制.
- 探索ROS介导信号与PTP控制的酸化信号之间的相互作用.
主要方法:
- 文献综述侧重于PTP的结构特征和活性部位化学.
- 分析已知的PTP氧化途径及其对其他氧化回收敏感蛋白质 (如Peroxiredoxins,Thioredoxins) 的依赖.
- 检查可逆 (硫酸,二硫化物,硫胺) 和不可逆 (硫酸,硫酸) 的氧化状态.
主要成果:
- PTPs可以被H2O2可逆地氧化成硫酸形式,这可能导致进一步的修改.
- 通过进一步氧化硫酸以硫酸或硫酸形式发生不可逆转的无活化.
- PTP氧化途径通常与其他细胞抗氧化系统协调.
结论:
- 了解PTP氧化动态对于针对这些酶的潜在治疗干预至关重要.
- 需要进一步的研究,以充分描述蛋白质氧化的精确动态,并确定PTP中的特定可向的氧化状态.
- 通过ROS介导的信号与PTP调节的酸化信号网络显著交叉.
相关概念视频
Protein Kinases and Phosphatases
13.1K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
13.1K
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
Phosphorylation
50.2K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
50.2K
Receptor Tyrosine Kinases
12.6K
Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
12.6K
Regulated Protein Degradation
7.2K
It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
7.2K
Regulation of the Unfolded Protein Response
2.4K
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.4K


