氧化物和翻译后修改对调节α-晶素的陪伴功能的影响
Khuraijam Surjalal Singh1, Snigdha Krishna1, Akshita Gupta1
1Dr. B. R. Ambedkar Center for Biomedical Research, University of Delhi, Delhi, India.
Progress in molecular biology and translational science
|February 13, 2025
概括
阿尔法晶体素是一种内在无序的蛋白质,通过防止蛋白质聚合来保持透镜的透明度. 糖化会损害其陪伴功能,增加糖尿病患者白内障的风险.
科学领域:
- 生物化学 生物化学
- 眼科医生 眼科 眼科
- 蛋白质科学 蛋白质科学
背景情况:
- 阿尔法晶体是眼镜中的一个关键蛋白质,作为分子陪伴者.
- 它是一种内在无序的蛋白质 (IDP),缺乏固定的3D结构,这有助于其功能.
- 它的动态结构和与各种蛋白质相互作用的能力对于保持透镜透明度至关重要.
研究的目的:
- 探索alpha-crystallin作为分子陪伴者的作用.
- 了解固有无序蛋白质如何在细胞过程中起作用.
- 调查翻译后修改,特别是糖化对α-晶体蛋白功能及其与白内障的联系的影响.
主要方法:
- 对有关α-晶体结构和功能的现有文献的审查.
- 分析固有无序蛋白质特征对伴侣活动的影响.
- 检查化物和翻译后修饰 (PTMs) 的作用,如糖化.
主要成果:
- 阿尔法晶的无序性质和动态的四级结构增强了它的伴侣活动.
- 奥斯莫利特稳定了α-晶体,而PTM如糖化会损害其功能.
- 糖化导致先进的糖化最终产品 (AGEs),导致结构变化和减少伴侣作用.
结论:
- 了解alpha-crystallin的结构灵活性和PTM对于镜片健康至关重要.
- 糖化诱导的α-晶功能障碍有助于白内障的形成,特别是在糖尿病患者中.
- 对PTM的进一步研究可以为预防与年龄相关和代谢障碍相关的白内障的策略提供信息.
相关概念视频
Molecular Chaperones and Protein Folding
17.7K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
17.7K
Protein Folding
7.7K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
7.7K
Protein Modifications in the RER
5.0K
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...
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...
5.0K
Amyloid Fibrils
9.2K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
9.2K
Protein Denaturation
3.8K
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
3.8K
Protein Folding Quality Check in the RER
3.7K
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...
3.7K


