TY - JOUR
T1 - Chemical methods for glycoprotein discovery
AU - Bond, Michelle R.
AU - Kohler, Jennifer J.
N1 - Funding Information:
Thank you to Marguerite M Desko, Danielle H Dube, Ethan J Greenblatt, and Peter L Lee for their helpful comments. MRB thanks the National Science Foundation for a Graduate Research Fellowship. We acknowledge the support of the Camille and Henry Dreyfus Foundation.
PY - 2007/2
Y1 - 2007/2
N2 - 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.
AB - 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.
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U2 - 10.1016/j.cbpa.2006.11.032
DO - 10.1016/j.cbpa.2006.11.032
M3 - Review article
C2 - 17174139
AN - SCOPUS:33846818820
SN - 1367-5931
VL - 11
SP - 52
EP - 58
JO - Current Opinion in Chemical Biology
JF - Current Opinion in Chemical Biology
IS - 1
ER -