Targeting the glycoproteome

Glycoconj J. 2013 Feb;30(2):119-36. doi: 10.1007/s10719-012-9438-6. Epub 2012 Aug 11.

Abstract

Despite numerous original publications describing the structural complexity of N- and O-linked glycans on glycoproteins, only very few answer the basic question of which particular glycans are linked to which amino acid residues along the polypeptide chain. Such structural information is of fundamental importance for understanding the biological roles of complex glycosylations as well as deciphering their non-template driven biosynthesis. This review focuses on presenting and commenting on recent strategies, specifically aimed at identifying the glycoproteome of cultured cells and biological samples, using targeted and global enrichment procedures and utilizing the high resolution power, high through-put capacity and complementary fragmentation techniques of tandem mass spectrometry. The goal is to give an update of this emerging field of protein and glyco-sciences and suggest routes to bridge the data gap between the two aspects of glycoprotein characteristics, i.e. glycan structures and their attachment sites.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cells, Cultured
  • Chromatography, Liquid / methods
  • Glycopeptides / analysis*
  • Glycopeptides / chemistry
  • Glycoproteins / analysis*
  • Glycoproteins / chemistry
  • Glycosylation
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Mass Spectrometry
  • Models, Biological
  • Proteome* / analysis
  • Proteome* / chemistry

Substances

  • Glycopeptides
  • Glycoproteins
  • Proteome