Glycomics and Mass Spectrometry

Abstract

Proteomics is closely associated with the modifications of the gene product such as the post-translational events that yield functionally active gene products. Among these, glycosylation represents a critically important post-translational modification and is a target for proteomic research. Glycan moieties are involved in a wide variety of intracellular, cell-cell and cell-matrix recognition events. This is why understanding how glycosylation affects the activities and functions of proteins in health and disease represents a major challenge. The study of the glycome--the whole set of glycans produced in a single organism--is therefore essential to determine the functions of all genes. Mass spectrometry, in combination with modern separation methodologies, is one of the most powerful and versatile techniques for the structural analysis of oligosaccharides. This review provides a summary of the current knowledge for the mass spectrometric analysis of glycoproteins and their glycan structures.

Advances on the compositional analysis of glycosphingolipids combining thin-layer chromatography with mass spectrometry

“…It is predicted that both naturally occurring GSLs and synthetic neoglycolipids will be required for the fabrication of microarrays that are sufficiently comprehensive and representative of entire glycomes . The new field of functional glycomics is now being explored through glycan array technology to decipher the information content of the glycome (Feizi, 2000a;Feizi & Mulloy, 2003;Morelle & Michalski, 2005;Pilobello & Mahal, 2007). Such new glycomic approaches, which are currently being developed and are entering clinical applications (Miyamoto, 2006), are contributing to our increased understanding of the underlying biology that is responsible for the development of cancer and other diseases.…”

Comparison of HPLC/ESI-FTICR MS versus MALDI-TOF/TOF MS for glycopeptide analysis of a highly glycosylated HIV envelope glycoprotein

“…These studies are important because glycosylation is the most common post-translational modification present in both eukaryotic and prokaryotic proteins [1,2], and this modification effects proteins' biological and cellular processes and influences their physiochemical properties [3][4][5]. Additionally, glycans have been shown to play a vital role in various parasitic, bacterial, and viral disease infections [6].…”

“…To obviate these obstacles, it is often necessary to perform an enrichment or chromatographic separation before MS analysis. Several studies have addressed this issue and proposed effective enrichment or/and chromatographic methods that can be utilized before MS analysis of glycopeptides [3,20].…”

Liquid Chromatography – Mass Spectrometry of Carbohydrates Derivatized with Biotinamidocaproyl Hydrazide

“…A common obstacle in the mass spectrometry of saccharides is the characterization of the stereochemistry of the glycosidic bond (Zhu et al, 2009;Morelle & Michalski, 2005). Isomers usually have very similar MS 2 -or MS 3 -fragmentation and are difficult to differentiate without a previous separation.…”