W. Morelle and J- C. Michalski Pages 2615 - 2645 ( 31 )
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 posttranslational 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.
genome,probe,posttranslational modifications,glycosylation,glycoforms,maldi-tof ms,time-of-flight
, Unite Mixte de Recherche CNRS/USTL 8576, Glycobiologie Structurale et Fonctionnelle , IFR118, Universite des Sciences et Technologies de Lille 1, 59655 Villeneuve d'Ascq Cedex, France.