MOJ ISSN: 2374-6920MOJPB

Proteomics & Bioinformatics
Volume 1 Issue 3 - 2014
The Promise of Glycoproteomics for Studying Cardiovascular Disease
Merry L Lindsey1,2,3 and Yuan Tian1,2*
1Department of Physiology and Biophysics, University of Mississippi Medical Center, USA
2San Antonio Cardiovascular Proteomics Center, USA
3Research Service, G.V. (Sonny) Montgomery Veterans Affairs Medical Center, USA
Received: June 26, 2014 | Published: July 01, 2014
*Corresponding author: Yuan Tian, Department of Physiology and Biophysics, University of Mississippi Medical Center, 2500 North State St. Jackson, MS 39216-4505, USA, Tel: 601-984-4795; Fax: 601-984-1833; Email:
Citation: Lindsey ML, Tian Y (2014) The Promise of Glycoproteomics for Studying Cardiovascular Disease. MOJ Proteomics Bioinform 1(3): 00011. DOI: 10.15406/mojpb.2014.01.00011


The potential of glycoproteomics for analyzing proteins associated with cardiovascular diseases are discussed.
Keywords: Glycoproteomics; Extracellular matrix; Myocardial infarction

Protein glycosylation, an enzyme-directed site-specific process, is one of the most common co-translational and post-translational modifications [1]. Glycoproteins modulate multiple biological processes, including cell adhesion and migration, signal transduction, and cell-cell communication [2,3]. Despite its widespread importance, glycoproteomics is not commonly used for studying cardiovascular disease compared to other diseases, such as cancers and diabetes. Glycoproteomics has the potential to be a powerful tool for analyzing proteins associated with cardiovascular diseases, as discussed below.
i. Glycosylation alters protein function by influencing protein folding, activity, stability, and distribution [4]. Glycosylation is increasingly recognized for its importance in modulating cardiomyocyte function and survival [5].
ii. Glycoproteins are the major components of the cardiac extracellular matrix, including structural and non-structural proteins that play key roles in cardiovascular disease development [6]. For example, thrombospondin, tenascin-C, and periostin are 3 nonstructural extracellular matrix glycoproteins that modulate cardiac remodeling after myocardial infarction [7-9].
iii. Since most cell surface and secreted proteins, including extracellular matrix proteins, are glycosylated, glycoproteomics is a useful enrichment strategy for the study of extracellular proteins [10-12]. Due to the extracellular location, these proteins are readily detected on cell surface or released into circulation, allowing them to serve as potential biomarkers and logical drug targets [13]. Therefore, glycoproteomics is a good approach for biomarker discovery.
iv. Glycoproteomics greatly reduces the sample complexity by focusing on glycosylated peptides instead of all protein peptides, which greatly improves the odds of the detecting low abundant proteins [14,15]. Glycoproteome enrichment coupled with targeted mass spectrometry analysis, such as selected reaction monitoring (SRM), further improves the sensitivity of mass spectrometry-based assays [16].
Glycosylation is a highly abundant modification crucial for the regulation of protein function, including proteolytic cleavage by enzymes and intra-protein interaction. Glycoproteomics is a logical approach to target specific subproteome with improved sensitivity for low abundant proteins. Therefore, glycoproteomics presents a new direction in methods that allow proteins associated with cardiovascular disease to be assessed for potential use as biomarkers or drug targets.


  1. Furukawa K, Kobata A (1992) Protein glycosylation. Curr Opin Biotechnol 3(5): 554-559.
  2. Isaji T, Gu J, Nishiuchi R, Zhao Y, Takahashi M, et al. (2004) Introduction of bisecting GlcNAc into integrin alpha5beta1 reduces ligand binding and down-regulates cell adhesion and cell migration. J Biol Chem 279(19): 19747-19754.
  3. Rudd PM, Elliott T, Cresswell P, Wilson IA, Dwek RA (2001) Glycosylation and the immune system. Science 291(5512): 2370-2376.
  4. Spiro RG (2002) Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 12(4): 43R-56R.
  5. Parker BL, Palmisano G, Edwards AV, White MY, Engholm-Keller K, et al. (2011) Quantitative N-linked glycoproteomics of myocardial ischemia and reperfusion injury reveals early remodeling in the extracellular environment. Mol Cell Proteomics 10(8): M110.006833.
  6. Rienks M, Papageorgiou AP, Frangogiannis NG, Heymans S (2014) Myocardial extracellular matrix: an ever-changing and diverse entity. Circ Res 114(5): 872-888.
  7. Xia Y, Dobaczewski M, Gonzalez-Quesada C, Chen W, Biernacka A, et al. (2011) Endogenous thrombospondin 1 protects the pressure-overloaded myocardium by modulating fibroblast phenotype and matrix metabolism. Hypertension 58(5): 902-911.
  8. Nishioka T, Onishi K, Shimojo N, Nagano Y, Matsusaka H, et al. (2010) Tenascin-C may aggravate left ventricular remodeling and function after myocardial infarction in mice. Am J Physiol Heart Circ Physiol 298(3): H1072-H1078.
  9. Oka T, Xu J, Kaiser RA, Melendez J, Hambleton M, et al. (2007) Genetic manipulation of periostin expression reveals a role in cardiac hypertrophy and ventricular remodeling. Circ Res 101(3): 313-321.
  10. Tian Y, Kelly-Spratt KS, Kemp CJ, Zhang H (2010) Mapping tissue-specific expression of extracellular proteins using systematic glycoproteomic analysis of different mouse tissues. J Proteome Res 9(11): 5837-5847.
  11. Tian Y, Koganti T, Yao Z, Cannon P, Shah P, et al. (2014) Characterization of cardiac extracellular proteome and membrane topology using glycoproteomics. Proteomics Clin Appl doi: 10.1002/prca.201400009.
  12. Lee MC, Sun B (2014) Glycopeptide capture for cell surface proteomics. J Vis Exp 9(87): doi: 10.3791/51349.
  13. Collins BE, Paulson JC (2004) Cell surface biology mediated by low affinity multivalent protein-glycan interactions. Curr Opin Chem Biol 8(6): 617-625.
  14. Zhang H, Liu AY, Loriaux P, Wollscheid B, Zhou Y, et al. (2007) Mass spectrometric detection of tissue proteins in plasma. Mol Cell Proteomics 6(1): 64-71.
  15. Tian Y, Kelly-Spratt KS, Kemp CJ, Zhang H (2008) Identification of glycoproteins from mouse skin tumors and plasma. Clin Proteomics 4(3-4): 117-136.
  16. Schiess R, Wollscheid B, Aebersold R (2009) Targeted proteomic strategy for clinical biomarker discovery. Mol Oncol 3(1): 33-44.
© 2014-2018 MedCrave Group, All rights reserved. No part of this content may be reproduced or transmitted in any form or by any means as per the standard guidelines of fair use.
Creative Commons License Open Access by MedCrave Group is licensed under a Creative Commons Attribution 4.0 International License.
Based on a work at
Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version | Opera |Privacy Policy