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Updated: May 8, 2026
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Profiling of Permethylated Mucin O-glycans Using Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry
Published on: June 20, 2025
Glycan-based biomarkers for mucopolysaccharidoses
Roger Lawrence1, Jillian R Brown2, Fred Lorey3
1Department of Cellular and Molecular Medicine, Glycobiology Research and Training Center, University of California San Diego, La Jolla, CA 92093, USA.
Molecular Genetics and Metabolism
|August 21, 2013
Summary
Mucopolysaccharidoses (MPS) involve enzyme deficiencies affecting glycosaminoglycan breakdown. New glycan biomarker analysis offers rapid diagnosis and therapy monitoring for MPS patients.
Area of Science:
- Biochemistry
- Genetics
- Biomarker Discovery
Background:
- Mucopolysaccharidoses (MPS) are genetic disorders caused by deficiencies in lysosomal enzymes responsible for glycosaminoglycan (GAG) degradation.
- Accumulation of GAGs like hyaluronan, heparan sulfate, and keratan sulfate leads to cellular dysfunction and disease manifestations.
- Current diagnostic and monitoring strategies for MPS can be complex and time-consuming.
Purpose of the Study:
- To review the utility of glycan biomarkers for characterizing MPS animal models.
- To summarize diagnostic applications of glycan biomarkers in MPS patients.
- To highlight the role of glycan biomarkers in monitoring MPS therapies, including hematopoietic stem cell transplantation and enzyme replacement therapy.
Main Methods:
- Focus on analyzing the non-reducing termini of accumulating GAGs as biomarkers.
- Utilizes enzymatic digestion with bacterial enzymes.
- Employs quantitative liquid chromatography/mass spectrometry (LC-MS) for precise glycan analysis.
Main Results:
- New methods enable simple, rapid diagnostic strategies for MPS.
- Analysis is applicable to various biological samples, including urine, blood, CSF, cells, and dried blood spots.
- These glycan analyses facilitate monitoring of enzyme replacement and substrate reduction therapies.
Conclusions:
- Analysis of non-reducing end glycans represents a significant advancement in MPS diagnostics.
- This approach offers a powerful tool for monitoring therapeutic efficacy in MPS.
- It also serves as a discovery platform for novel MPS biomarkers and potentially new MPS subtypes.
Related Concept Videos
01:05Proteoglycans
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,...
01:23Glycosaminoglycans
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...
01:24Oligosaccharide 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...
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01:25Protein 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...
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01:14Glycocalyx and its Functions
The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
Components of...
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