Integrated Glycoprotein Immobilization Method for Glycopeptide and Glycan Analysis of Cardiac Hypertrophy

Shuang Yang, Sumita Mishra, Lijun Chen, Jian Ying Zhou, Daniel W. Chan, Subroto Chatterjee, Hui Zhang

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)9671-9678
Number of pages8
JournalAnalytical Chemistry
Issue number19
StatePublished - Oct 6 2015

ASJC Scopus subject areas

  • Analytical Chemistry


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