Journal
NATURE CHEMICAL BIOLOGY
Volume 6, Issue 5, Pages 338-343Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio.338
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Funding
- US National Institute of Diabetes and Digestive and Kidney [NIH RO1 DK075069]
- Research Resource for Integrated Glycotechnology [NIH/NCRR P41R005351]
- National Cancer Institute of the US National Institutes of Health [NIH/NCI R01CA088986, NIH HL067464, HL079364]
- American Heart Association (Southeast Affiliation)
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Studies of post-translational modification by beta-N-acetyl-D-glucosamine (O-GlcNAc) are hampered by a lack of efficient tools such as O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization. We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology. Immunoprecipitation followed by large-scale shotgun proteomics led to the identification of more than 200 mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins. A substantial number of the glycoproteins were enriched by only one of the antibodies. This observation, combined with the results of inhibition ELISAs, suggests that the antibodies, in addition to their O-GlcNAc dependence, also appear to have different but overlapping local peptide determinants. The monoclonal antibodies made it possible to delineate differentially modified proteins of liver in response to trauma-hemorrhage and resuscitation in a rat model.
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