化保护糖蛋白免受氧化应激:关于酸氧化和结构稳定的机制见解
在PubMed上查看摘要
概括
此摘要是机器生成的。化保护蛋白质免受氧化应激. 这项研究揭示了酸如何抵抗损伤以及蛋白质化如何稳定结构以防止氧化展开,这对细胞健康至关重要.
科学领域
- 生物化学
- 化学生物学
- 结构生物学
背景情况
- 化是一种影响结构和功能的重要蛋白质修饰.
- 化对保护蛋白质免受氧化应激的作用尚不清楚.
研究的目的
- 研究化对氧化损伤的保护机制.
- 阐明酸的氧化途径及其对激素氧化的抵抗力.
- 证明在氧化应激下化对糖蛋白的稳定作用.
主要方法
- 控制氧化应激的微观低温等离子体.
- 高分辨率质谱和密度函数理论计算.
- 全离子展开离子移动性质谱对人类转移素.
主要成果
- 确定了前所未有的酸氧化途径,显示了逐步的侧链氧化.
- 与Neu5Ac相比,Neu5Gc的抗氧化能力更高.
- 人类转移素的化,防止氧化展开,具有增强稳定性的特定模式.
结论
- 通过稳定蛋白质结构,化对抗氧化应激起着关键的保护作用.
- 了解化抗性机制可以了解细胞应激下蛋白质的完整性.
- 这项工作强调了化作为在氧化环境中维持蛋白质构成和功能的关键因素.
相关概念视频
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...
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...
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,...
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

