Journal
NATURE METHODS
Volume 13, Issue 1, Pages 81-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.3675
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Funding
- US National Institutes of Health [U01CA168930, P41GM103694]
- Georgia Research Alliance (GRA)
- Biotechnology and Biological Sciences Research Council [BB/K016164/1]
- Wellcome Trust
- Emory Integrated Proteomics Core
- NATIONAL CANCER INSTITUTE [U01CA168930] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P41GM103694, T32GM008169] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [P30NS055077] Funding Source: NIH RePORTER
- BBSRC [BB/K016164/1] Funding Source: UKRI
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Protein O-glycosylation has key roles in many biological processes, but the repertoire of O-glycans synthesized by cells is difficult to determine. Here we describe an approach termed Cellular O-Glycome Reporter/Amplification (CORA), a sensitive method used to amplify and profile mucin-type O-glycans synthesized by living cells. Cells convert added peracetylated benzyl-alpha-N-acetylgalactosamine to a large variety of modified O-glycan derivatives that are secreted from cells, allowing for easy purification for analysis by HPLCLC and mass spectrometry (MS). Relative to conventional O-glycan analyses, CORA resulted in an similar to 100-1,000-fold increase in sensitivity and identified a more complex repertoire of O-glycans in more than a dozen cell types from Homo sapiens and Mus musculus. Furthermore, when coupled with computational modeling, CORA can be used for predictions about the diversity of the human O-glycome and offers new opportunities to identify novel glycan biomarkers for human diseases.
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