相关实验视频

Updated: Sep 17, 2025

Mass Spectrometric Analysis of Glycosphingolipid Antigens

Mass Spectrometric Analysis of Glycosphingolipid Antigens

Published on: April 16, 2013

在SLC35A2-CDG中,葡萄糖脂合成受损,并且通过补充银河糖改善

Andrea Jáñez Pedrayes^1,2,3, Sam De Craemer^1,2, Jakub Idkowiak⁴

¹Laboratory of Applied Mass Spectrometry, Department of Cellular and Molecular Medicine, KU Leuven, Leuven, 3000, Belgium.

Cellular and molecular life sciences : CMLS

|June 27, 2025

概括

血糖定制的先天性疾病 SLC35A2-CDG 损害了脂质,而不是蛋白质的血糖定制. 银河糖治疗改善了糖类脂 (GSL) 合成,这表明GSL可以作为神经症状的治疗标和生物标志物.

科学领域:

生物化学生化学
遗传学是一个遗传学.
代谢障碍代谢障碍代谢障碍

背景情况:

SLC35A2-CDG是一种X结合的血糖化 (CDG) 的先天性疾病,影响了UDP-银糖的运输.
这种缺陷导致甘氨酸的银河系氧化和神经症状不足.
确切的病理机制和治疗策略仍然不完全理解.

研究的目的:

调查SLC35A2缺乏对蛋白质和脂质糖化酶的影响.
为了评估银河糖补充剂对葡萄糖脂 (GSL) 合成和恒温的疗效.
为了确定SLC35A2-CDG的潜在生物标志物.

主要方法:

在患者纤维细胞中分析N和O相关蛋白质糖化.
评估脂质糖化,包括GLS和化物.
在补充银河糖后测量UDP-银河糖水平和运输.
对潜在疾病生物标志物的血清分析.

主要成果:

蛋白质糖化受影响很小,但脂质糖化在SLC35A2-CDG纤维细胞中显著受损.
银河糖补充恢复了UDP-银河糖运输,并纠正了缺陷的GLS合成.
氧化GLS,特别是GM3,被确定为患者血清中的潜在生物标志物.
在患者细胞和细胞模型中改善了GLL平衡.

结论:

SLC35A2-CDG主要破坏脂质糖化,特别是GLS,这可能导致神经症状.
口服银河糖补充剂有效地增强了GLS合成和恒常性.
准GSL新陈代谢为SLC35A2-CDG提供了一个有希望的治疗途径.
氧化GLS代表疾病诊断和监测的潜在生物标志物.

关键词:

这是CDG的CDG.在GSL中使用.团结体团结体团结体团结体葡萄糖脂类的葡萄糖脂类.在 SLC35A2-CDG 中.标志性物质的代谢学

更多相关视频

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

Ganglioside Extraction, Purification and Profiling

Ganglioside Extraction, Purification and Profiling

Published on: March 12, 2021

相关概念视频

Glucose Transporters

Glucose Transporters

Glucose transporters facilitate the transport of glucose across the cell membrane. In addition to glucose, some glucose transporters can also aid the movement of other hexoses such as fructose, mannose, and galactose.
Facilitated diffusion-glucose transporters (GLUTs) are encoded by the solute-linked carrier (SLC) family 2, subfamily A gene family, or SLC2A. The 14 GLUT protein members are distributed into three classes:

Oligosaccharide Assembly

Oligosaccharide Assembly

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...

Inborn Errors of Metabolism

Inborn Errors of Metabolism

Phenylketonuria (PKU) is a protein metabolism disorder characterized by high blood levels of the amino acid phenylalanine. This results from a mutation in the gene responsible for phenylalanine hydroxylase, an enzyme that converts phenylalanine into tyrosine. When this enzyme is deficient, phenylalanine builds up in the blood, leading to symptoms such as vomiting, rashes, seizures, growth deficiency, and severe mental retardation. An early diagnosis and a diet restricting phenylalanine intake...

Biosynthesis of Polysaccharides

Biosynthesis of Polysaccharides

Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...

Protein Glycosylation

Protein Glycosylation

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...

Lysosomal Hydrolases

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...