Related Experiment Video
Updated: Jun 8, 2026
10:41
Using a GFP-tagged TMEM184A Construct for Confirmation of Heparin Receptor Identity
Published on: February 17, 2017
Applications of isotopes in advancing structural and functional heparanomics
Vy M Tran1, Thao K N Nguyen, Karthik Raman
1Department of Bioengineering, University of Utah, Salt Lake City, UT 84112, USA.
Analytical and Bioanalytical Chemistry
|September 15, 2010
Summary
This review explores using isotopes to decode the heparanome, aiding the structural elucidation of heparan sulfate and heparin oligosaccharides. These methods advance understanding of heparanomics and enzyme specificity.
Area of Science:
- Biochemistry and Glycobiology
- Analytical Chemistry
Background:
- Heparanomics, the study of biologically active oligosaccharide domains in the heparanome, faces significant challenges in structural elucidation.
- Understanding the structure-function relationships of heparan sulfate and heparin is crucial but hindered by complex analytical hurdles.
Purpose of the Study:
- To review the application of isotopes (radioisotopes and stable isotopes) in the structural elucidation of the heparanome.
- To highlight novel strategies and analytical tools for decoding complex oligosaccharide structures.
- To outline the utility of isotopes in determining the substrate specificity of biosynthetic enzymes.
Main Methods:
- Liquid chromatography (LC)
- Nuclear magnetic resonance (NMR) spectroscopy
- Mass spectrometry (MS)
- Isotope labeling (radioisotopes and stable isotopes)
Main Results:
- Isotopes significantly aid in the structural elucidation of heparan sulfate and heparin oligosaccharides at the disaccharide and oligosaccharide levels.
- LC-MS and LC-NMR, when combined with isotope labeling, provide powerful tools for decoding the heparanome.
- Isotopic analysis facilitates the determination of enzyme substrate specificity in oligosaccharide biosynthesis.
Conclusions:
- Isotope applications are pivotal for overcoming barriers in heparanome structural elucidation.
- Advancements in analytical techniques using isotopes are essential for progress in heparanomics.
- Understanding enzyme specificity through isotopic methods is key to controlling the emergence of biologically active oligosaccharides.
Related Concept Videos
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...
01:56Structural Protein Function
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
01:56Structural Protein Function
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
01:21Matrix 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...
01:30Anticoagulant Drugs: Low-Molecular-Weight Heparins
Hemostasis is a crucial process that prevents excessive blood loss from damaged blood vessels. It involves various mechanisms such as vasoconstriction, platelet adhesion and activation, and fibrin formation. The importance of each mechanism depends on the type of vessel injury. In contrast, thrombosis is the abnormal formation of a blood clot within the blood vessels, leading to potential complications if the clot obstructs blood flow. Thrombosis can be caused by increased coagulability of the...
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,...