Related Experiment Video
Updated: Aug 8, 2026

05:57
Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining
Published on: February 25, 2021
[Glycosaminoglycans in syrinogomyelia]
Summary
Glycosaminoglycan (GAG) excretion is significantly reduced in syringomyelia patients, with altered GAG levels in skin, CSF, and brain tissues. This suggests a widespread connective tissue metabolism disorder in the condition.
Area of Science:
- Biochemistry
- Genetics
- Neurology
Context:
- Syringomyelia is a rare neurological disorder characterized by cyst formation within the spinal cord.
- Alterations in glycosaminoglycan (GAG) metabolism have been implicated in various connective tissue disorders.
Purpose:
- To investigate urinary glycosaminoglycan (GAG) excretion patterns in patients with syringomyelia.
- To determine the tissue-specific content of GAG in patients with syringomyelia and compare it with healthy individuals.
Summary:
- Urinary GAG excretion was 2.7-fold lower in syringomyelia patients compared to healthy controls.
- GAG content was reduced in skin (30%), cerebrospinal fluid (40%), and brain (20-40%), but increased by 80% in the affected spinal cord.
- The observed GAG excretion patterns are genetically determined and inherited in a dominant manner.
Impact:
- The findings indicate a significant impairment of connective tissue metabolism in syringomyelia.
- This study highlights the potential role of GAGs as biomarkers for syringomyelia.
- Understanding GAG metabolism alterations may open new avenues for therapeutic interventions in syringomyelia.
Related Concept Videos
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...
Glycosylation occurs in...
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...
Multiple sugar molecules that may or may...
Proteoglycans
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,...
Glycosaminoglycans
Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
Matrix Proteoglycans and Glycoproteins
Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
Connective Tissue Fibers and Ground Substance
One of the significant functions of connective tissue is connecting tissues and organs. Unlike epithelial tissue that is composed of cells closely packed with little or no extracellular space in between, connective tissue cells are dispersed in a matrix. The matrix usually includes a large amount of extracellular material produced by the connective tissue cells that are embedded within it. It plays a significant role in the functioning of this tissue. The major component of the matrix is a...

