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BioMS

Swedish national infrastructure for biological mass spectrometry

Glycoproteomics and Glycomics


Glycosylation is among the most complex and diverse modification of proteins and lipids found in all forms of biological life and advanced mass spectrometry is central in the analysis of these structures.

Every living cell is composed of nucleic acids, proteins, lipids, low molecular weight metabolites and glycans. The basic exploration and our understanding of nucleic acids and proteins as well as the subsequent technical revolution in molecular biology has advanced those fields tremendously during the last decades. The study of glycans and glycoconjugates has been left behind, partly, this may be explained by the greater structural complexity and diversity of this class of molecules. Glycosylation demands a complex nomenclature and a need for multiple advanced technologies for preparation and analysis of glycoconjugates, and an in-depth knowledge of systems biology and medicine.

Analogous to proteomics, glycoproteomics is based on advanced mass spectrometry technologies that has evolved as the method of choice for global or directed analysis of glycoproteins and proteoglycans in biological tissue. The concept is to characterize the glycans as well as their exact attachment sites on specific peptides, identified by their unique amino acid sequences. To accomplish this a series of enrichment strategies, ionization techniques as well as bioinformatic tools have now become available.

Support within glycoproteomics at BioMS include:

  • Global identification of glycopeptides
  • Structural characterization of N- and O-linked glycopeptides
  • Relative quantification of glycopeptides


Changes of a cell’s glycosylation is one of the first signs of an altered environment for the cells. Hence, diseases such as cancer and inflammation manifest themselves by an altered glycosylation and suggest that glycoconjugates can be used as biomarkers for early stage diseases. The carbohydrate rich glycocalyx of a cell is also the way cells are presenting themselves to the outside word and specific carbohydrates are the transmitters for cellular communication. We believe that all extracellular biological events would involve glycoconjugates, and we have developed workflows that allows characterization of a variety of mammalian type glycoconjugates.

 HPLC and MS is currently the state-of-the-art providers of glycomic data N-linked, O-linked and glycosphingolipids). Our instrumentation has been shown to successfully address glycobiological questions in clinical, transgenic and small-scale cell culture.

The LC-MS methodology for analyses of O-linked and N-linked released oligosaccharides by negative ion graphitized carbon LC-MS has been validated in the HUPO glycomic committee. The same approach has also been adopted for glycosphingolipds. LC on graphitized carbon column giving excellent separation of structural isomers providing informative MS/MS of individual isomers. If the ceramide composition is of interest isolated native glycosphingolipids are analyzed by LC-MS using HILIC columns. We are continuously updating the freely available MS/MS spectral library UniCarb-DB (unicarb-db.com) to aid in assignment. The database is hosted by BioMS.

The HPLC methodology for N-linked glycans are well-established in both academic and pharma-industry and together with exoglycosidase digestion and MS, this provide detailed characterization of glycans in a high throughput platform. We are using the validated database GlycoBase (glycobase.nibrt.ie) to aid in assignment of structures.

Support within glycomics at BioMS include:

  • Screening of released N-linked and O-linked oligosaccharides and liberated glycans from glycolipids for comparative glycomics.
  • Detailed characterization of N-linked and O-linked oligosaccharides and liberated glycans from glycolipids using exoglycosidases and HPLC and/or LC-MSn

 

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Contact Information

Proteomics Core Facility

Box 413, 405 30 Göteborg, For questions regarding proteomics analyses, please use the contact form.

Visiting Address:
Medicinaregatan 7A, 413 90 Göteborg

Page Manager: Core Facilities web edito|Last update: 2/3/2020
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