在末期脏疾病中对人类转移素的糖化和表征
Goran Miljuš1, Ana Penezić1, Lucia Pažitná2
1Institute for the Application of Nuclear Energy (INEP), Department for Metabolism, University of Belgrade, 11000 Belgrade, Serbia.
International journal of molecular sciences
|May 11, 2024
概括
末期脏病 (ESKD) 患者的转移林 (Tf) 糖化发生变化,接受腹腔透析 (PD) 的患者不会损害铁运输功能. 保持结构完整性和Tf-TfR相互作用建议针对PD患者贫血的向治疗.
科学领域:
- 腎臟病學 (nephrology) 是一種醫學.
- 生物化学 生物化学
- 血液学 血液学 血液学
背景情况:
- 慢性病 (CKD) 影响全球超过10亿人.
- 末期脏病 (ESKD) 患者经常患有贫血,这是一种由腹腔透析 (PD) 加剧的并发症.
- 患PD的治疗可能导致蛋白质损失,包括转移素 (Tf),这对铁运输至关重要.
研究的目的:
- 在接受PD的ESKD患者中研究转激素 (Tf) 的特征.
- 在ESKD患者和健康个体之间比较Tf糖化,结构和功能.
- 评估Tf和转激素受体 (TfRs) 在PD患者之间的相互作用.
主要方法:
- 莱克微阵列分析以检测Tf糖化中的变化.
- 光谱技术和免疫细胞化学分析用于结构和功能评估.
- 在PD患者中对Tf-TfR相互作用的比较分析与健康对照.
主要成果:
- 与健康对照组相比,在PD中的ESKD患者表现出显著改变的Tf糖化模式.
- 两组之间Tf的二级或三级结构没有显著差异.
- 在PD患者和健康人群中,Tf-TfR相互作用保持了可比性,表明功能得到保留.
结论:
- 尽管发生了改变的糖化,但Tf 保持了其结构完整性和功能能力,能够与 PD 患者的 TfR 相互作用.
- 在Tf中的糖化变化可能会影响铁代谢,但不会影响Tf功能.
- 这项研究表明,无葡萄糖透析溶液可能有利于治疗PD患者的贫血,可能改善患者的治疗结果.
更多相关视频
10:37Comparative Proteomic Analysis of Whole Kidney, Medulla, and Cortical Tubules in Diabetic Pathogenesis of Kidney Injury in Mice
Published on: May 2, 2025
141
09:54Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
Published on: December 26, 2011
36.6K
相关概念视频
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
2.8K
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...
2.8K
Proteoglycans
3.9K
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,...
3.9K
