The use of mass spectrometry for the proteomic analysis of glycosylation.
Of all protein PTMs, glycosylation is by far the most common, and is a target for proteomic research. Glycosylation plays key roles in controlling various cellular processes and the modifications of the glycan structures in diseases highlight the clinical importance of this PTM. Glycosylation analysis remains a difficult task. MS, in combination with modern separation methodologies, is one of the most powerful and versatile techniques for the structural analysis of glycoconjugates. This review describes methodologies based on MS for detailed characterization of glycoconjugates in complex biological samples at the sensitivity required for proteomic work.
Morelle
Willy
W
Unité Mixte de Recherche CNRS/USTL 8576, Université des Sciences et Technologies de Lille 1, Villeneuve d'Ascq Cedex, France. willy.morelle@univ-lille1.fr
Canis
Kévin
K
Chirat
Frédéric
F
Faid
Valegh
V
Michalski
Jean-Claude
JC
D015415:Biomarkers / Q000737:chemistry; D006020:Glycopeptides / Q000737:chemistry*; D006023:Glycoproteins / Q000737:chemistry*; D006031:Glycosylation; D006801:Humans; D013058:Mass Spectrometry; D011134:Polysaccharides / Q000737:chemistry; D040901:Proteomics / Q000295:instrumentation; D012680:Sensitivity and Specificity
D015415:Biomarkers; D006020:Glycopeptides; D006023:Glycoproteins; D011134:Polysaccharides