Chemical methods for glycoprotein discovery

Michelle R. Bond, Jennifer J. Kohler

Research output: Contribution to journalReview articlepeer-review

63 Scopus citations

Abstract

An important frontier in glycoproteomics is the discovery of proteins with post-translational glycan modifications. The first step in glycoprotein identification is the isolation of glycosylated proteins from the remainder of the proteome. New enzymatic and metabolic methods are being used to chemically tag proteins to enable their isolation. Once isolated, glycoproteins can be identified by mass spectrometry. Additional information can be obtained by using either enzymatic or chemoselective reactions to incorporate isotope labels at specific sites of glycosylation. Isotopic labeling facilitates mass spectrometry-based confirmation of glycoprotein identity, identification of glycosylation sites, and quantification of the extent of modification. By combining chemical tagging for isolation and isotope labeling for mass spectrometry analysis, researchers are developing highly effective strategies for glycoproteomics. These techniques are enabling cancer biologists to identify biomarkers whose glycosylation state correlates with disease states, and developmental biologists to characterize stage-specific changes in glycoprotein expression. Next-generation methods will make functional analyses of the glycoproteome possible, including the discovery of glycoprotein interaction partners and the identification of enzymes responsible for synthesis of particular glycan structures.

Original languageEnglish (US)
Pages (from-to)52-58
Number of pages7
JournalCurrent Opinion in Chemical Biology
Volume11
Issue number1
DOIs
StatePublished - Feb 1 2007

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry

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