Community Research and Development Information Service - CORDIS


Glycoproteomics Result In Brief

Project ID: 293847
Funded under: FP7-PEOPLE
Country: Germany

Advancing glycosylation monitoring

A deeper understanding of what goes on within a cell often requires the structural characterisation of some important biomolecules. This goes hand in hand with technological advancements in the field of biomedical sciences.
Advancing glycosylation monitoring
Glycoproteins are proteins that contain sugar residues and play an important role in cellular communication. They are primarily located on the membrane where they mediate interaction with other cells, or can be secreted and travel around the body via the bloodstream.

The process of sugar attachment onto proteins occurs after protein synthesis and is known as glycosylation. Accumulating evidence indicates that glycosylation alterations are associated with certain diseases and can thus serve as a diagnostic or therapeutic marker. Furthermore, sugar-recognising proteins (lectins) play a major role as control agents to prevent autoimmune reactions.

Despite the importance of these molecules, the available technology and tools to recognise and study glycoproteins are still at their infancy. Glycosylated peptides are chemically very different components and require specific analytical measures that cannot be fulfilled by existing methods. The scope of the EU-funded GLYCOPROTEOMICS (Quantitative glycomics and glycoproteomics for biomarker discovery) project is to advance existing methods and workflows for the systematic investigation of glycoproteins.

For this purpose, the consortium will develop a workflow based on the porous graphitised carbon liquid chromatography (PGC-LC) method coupled to a highly sensitive mass spectrometer. Apart from automated, high-throughput capacity this system is capable of quantifying fine structural features that cannot be distinguished by simple mass spectrometry methods. Using this system, researchers plan to analyse a large number of samples of inflammatory bowel disease to identify disease-related glycosylation profiles. This information will be correlated to the function of the respective glycoproteins.

Overall, the generated tools open up new avenues for studying and monitoring a diagnostically unexplored group of molecules. Glycosylation signatures associated with specific diseases could in the future be used for disease prediction and treatment monitoring.

Related information


Glycosylation, glycoproteins, mass spectrometry, inflammatory bowel disease
Record Number: 175027 / Last updated on: 2016-01-28
Domain: Biology, Medicine