Related Experiment Video
Updated: Jun 14, 2026

11:36
Glycan Node Analysis: A Bottom-up Approach to Glycomics
Published on: May 22, 2016
Common aberrations from the normal human plasma N-glycan profile.
Maja Pucic1, Sofia Pinto, Mislav Novokmet
1Genos Ltd., Glycobiology Division, Planinska 1, 10000 Zagreb, Croatia.
Glycobiology
|April 10, 2010
Summary
Researchers identified distinct N-glycan profiles in plasma, revealing specific glyco-phenotypes. Some altered patterns, like A2G2S1, are linked to health issues, while others show no adverse effects.
Area of Science:
- Biochemistry
- Human Genetics
- Clinical Chemistry
Background:
- N-glycans are crucial glycans involved in various biological processes.
- Altered N-glycan profiles in plasma can indicate underlying health conditions.
Purpose of the Study:
- To identify and characterize distinct N-glycan profiles in human plasma.
- To investigate the association between specific N-glycan patterns and clinical conditions.
Main Methods:
- Hydrophilic interaction and weak anion exchange high-performance liquid chromatography (HILIC-WAX-HPLC) were used to analyze plasma N-glycans.
- Consensus scoring of pairwise distances was applied to group individuals based on glycan profiles.
Main Results:
- Six distinct glyco-phenotype groups were identified among 1991 individuals.
- An increase in monosialylated biantennary glycans (A2G2S1) was associated with renal problems.
- Significant alterations, including the absence of neutral glycans or fucosylated glycans, were not linked to adverse health outcomes.
Conclusions:
- Specific altered glyco-phenotypes exist in the human population.
- Certain glyco-phenotypes may serve as risk factors for developing specific diseases.
Related Concept Videos
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,...
Membrane Carbohydrates
The plasma membrane is a dynamic barrier composed of lipids, proteins, and carbohydrates. It is the epicenter of many cellular processes required for cell growth and survival. Carbohydrates have unique structural and chemical properties that help the plasma membrane to carry out its functions effectively.
Membrane carbohydrates do not have any hydrophobic region and are exclusively located on the cell's outer surface. The addition of sugar molecules or glycosylation of proteins happens in...
Membrane carbohydrates do not have any hydrophobic region and are exclusively located on the cell's outer surface. The addition of sugar molecules or glycosylation of proteins happens in...
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...
Glycocalyx 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...
Components of...
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...
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...
