Journal
ANALYTICAL CHEMISTRY
Volume 87, Issue 19, Pages 9671-9678Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.5b01663
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Funding
- National Institutes of Health
- National Cancer Institute, Clinical Proteomics Tumor Analysis Consortium [U24CA160036]
- Early Detection Research Network (EDRN) [U0ICA152813, U24CA115102, R01CA112314]
- National Heart Lung Blood Institute, Programs Excellence in Glycosciences [P01HL107153]
- NHLBI Proteomic Center [N01-HV-00240]
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Post-translational modifications of proteins can have a major role in disease initiation and progression. Incredible efforts have recently been made to study the regulation of glycoproteins for disease prognosis and diagnosis. It is essential to elucidate glycans and intact glycoproteins to understand the role of glycosylation in diseases. Sialylated N-glycans play crucial roles in physiological and pathological processes; however, it is laborious to study sialylated glycoproteins due to the labile nature of sialic acid residues. In this study, an integrated platform is developed for the analysis of intact glycoproteins and glycans using a chemoenzymatic approach for immobilization and derivatization of sialic acids. N-Glycans, deglycosylated proteins, and intact glycoproteins from heart tissues of wild type (WT) and transverse aortic constriction (TAC) mouse models were analyzed. We identified 291 unique glycopeptides from 195 glycoproteins; the comparative studies between WT and TAC mice indicate the overexpression of extracellular proteins for heart matrix remodeling and the down-regulation of proteins associated with energy metabolism in cardiac hypertrophy. The integrated platform is a powerful tool for the analysis of glycans and glycoproteins in the discovery of potential cardiac hypertrophy biomarkers.
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