title: Integrated glycoprotein immobilization method for glycopeptide and glycan analysis of cardiac hypertrophy.
abstract: 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.
authors.affiliation: Department of Pathology, and ‡Department of Pediatrics, Johns Hopkins University , Baltimore, Maryland 21287, United States.
authors.forename: Shuang
authors.initials: S
authors.lastname: Yang
authors.affiliation: Department of Pathology, and ‡Department of Pediatrics, Johns Hopkins University , Baltimore, Maryland 21287, United States.
authors.forename: Sumita
authors.initials: S
authors.lastname: Mishra
authors.affiliation: Department of Pathology, and ‡Department of Pediatrics, Johns Hopkins University , Baltimore, Maryland 21287, United States.
authors.forename: Lijun
authors.initials: L
authors.lastname: Chen
authors.affiliation: Department of Pathology, and ‡Department of Pediatrics, Johns Hopkins University , Baltimore, Maryland 21287, United States.
authors.forename: Jian-Ying
authors.initials: JY
authors.lastname: Zhou
authors.affiliation: Department of Pathology, and ‡Department of Pediatrics, Johns Hopkins University , Baltimore, Maryland 21287, United States.
authors.forename: Daniel W
authors.initials: DW
authors.lastname: Chan
authors.affiliation: Department of Pathology, and ‡Department of Pediatrics, Johns Hopkins University , Baltimore, Maryland 21287, United States.
authors.forename: Subroto
authors.initials: S
authors.lastname: Chatterjee
authors.affiliation: Department of Pathology, and ‡Department of Pediatrics, Johns Hopkins University , Baltimore, Maryland 21287, United States.
authors.forename: Hui
authors.initials: H
authors.lastname: Zhang
mesh_terms: D000818:Animals; D006332:Cardiomegaly / Q000378:metabolism*; D004734:Energy Metabolism; D006020:Glycopeptides / Q000032:analysis* / Q000378:metabolism; D006023:Glycoproteins / Q000737:chemistry*; D008297:Male; D051379:Mice; D011134:Polysaccharides / Q000032:analysis* / Q000378:metabolism
chemical_list: D006020:Glycopeptides; D006023:Glycoproteins; D011134:Polysaccharides