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Cardiac Extracellular Proteome Profiling and Membrane Topology Analysis Using Glycoproteomics
Proteomics - Clinical Applications
  • Yuan Tian, San Antonio Cardiovascular Proteomics Center
  • Tejaswi Koganti, Cancer Bioinformatics Core
  • Zhihao Yao, San Antonio Cardiovascular Proteomics Center
  • Presley Cannon, San Antonio Cardiovascular Proteomics Center
  • Punit Shah, Johns Hopkins School of Medicine
  • Laura Pietrovito, Università degli Studi di Firenze
  • Alessandra Modesti, Università degli Studi di Firenze
  • Paul Aiyetan, Johns Hopkins School of Medicine
  • Kristine Deleon-Pennell, San Antonio Cardiovascular Proteomics Center
  • Yonggang Ma, San Antonio Cardiovascular Proteomics Center
  • Ganesh V. Halade, San Antonio Cardiovascular Proteomics Center
  • Chindo Hicks, Cancer Bioinformatics Core
  • Hui Zhang, Johns Hopkins School of Medicine
  • Merry L. Lindsey, San Antonio Cardiovascular Proteomics Center
Document Type
Article
Publication Date
1-1-2014
Keywords
  • Extracellular matridome,
  • Glycoprotein,
  • Left ventricle,
  • Matrix metalloproteinase,
  • Membrane orientation,
  • Myocardial infarction
Digital Object Identifier (DOI)
https://doi.org/10.1002/prca.201400009
Abstract

Purpose: Extracellular proteins are easily accessible, which presents a subproteome of molecular targets that have high diagnostic and therapeutic potential. Efforts have been made to catalog the cardiac extracellular matridome and analyze the topology of identified proteins for the design of therapeutic targets. Although many bioinformatics tools have been developed to predict protein topology, topology has been experimentally validated for only a very small portion of membrane proteins. The aim of this study was to use a glycoproteomics and MS approach to identify glycoproteins in the extracellular matridome of the infarcted left ventricle (LV) and provide experimental evidence for topological determination. Experimental design: Glycoproteomics analysis was performed on eight biological replicates of LV samples from wild-type mice at 7 days following myocardial infarction using SPE of glycopeptides, followed by mass spectrometric identification of N-linked glycosylation sites for topology assessment. Results: We identified hundreds of glycoproteins, and the identified N-glycosylation sites provide novel information on the correct topology for membrane proteins present in the infarct setting. Conclusions and clinical relevance: Our data provide the foundation for future studies of the LV infarct extracellular matridome, which may facilitate the discovery of drug targets and biomarkers.

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Citation / Publisher Attribution

Proteomics - Clinical Applications, v. 8, issue 7-8, p. 595-602

This is the peer reviewed version of the following article: Tian, Y., Koganti, T., Yao, Z., Cannon, P., Shah, P., Pietrovito, L., Modesti, A., Aiyetan, P., DeLeon‐Pennell, K., Ma, Y., Halade, G.V., Hicks, C., Zhang, H. and Lindsey, M.L. (2014), Cardiac extracellular proteome profiling and membrane topology analysis using glycoproteomics. Prot. Clin. Appl., 8: 595-602., which has been published in final form at 10.1002/prca.201400009. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.

Citation Information
Yuan Tian, Tejaswi Koganti, Zhihao Yao, Presley Cannon, et al.. "Cardiac Extracellular Proteome Profiling and Membrane Topology Analysis Using Glycoproteomics" Proteomics - Clinical Applications Vol. 8 Iss. 7-8 (2014) p. 595 - 602
Available at: http://works.bepress.com/ganesh-halade/22/