Table of Contents
International Journal of Proteomics
Volume 2012 (2012), Article ID 342659, 17 pages
http://dx.doi.org/10.1155/2012/342659
Research Article

Human Myocardial Protein Pattern Reveals Cardiac Diseases

1Analytical Chemistry, Department of Chemistry, Biomedical Center and SciLife Lab, Uppsala University, P.O. Box 599, 751 24 Uppsala, Sweden
2Bruker Daltonik GmbH, 28359 Bremen, Germany
3Department of Medical Sciences, Hedenstierna Laboratory, Uppsala University, 75185 Uppsala, Sweden
4Institute of Biophysics, University of Frankfurt, 60438 Frankfurt/M, Germany

Received 13 January 2012; Accepted 28 March 2012

Academic Editor: Ákos Végvári

Copyright © 2012 Jonas Bergquist et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Proteomic profiles of myocardial tissue in two different etiologies of heart failure were investigated using high performance liquid chromatography (HPLC)/Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS). Right atrial appendages from 10 patients with hemodynamically significant isolated aortic valve disease and from 10 patients with isolated symptomatic coronary heart disease were collected during elective cardiac surgery. As presented in an earlier study by our group (Baykut et al., 2006), both disease forms showed clearly different pattern distribution characteristics. Interesting enough, the classification patterns could be used for correctly sorting unknown test samples in their correct categories. However, in order to fully exploit and also validate these findings there is a definite need for unambiguous identification of the differences between different etiologies at molecular level. In this study, samples representative for the aortic valve disease and coronary heart disease were prepared, tryptically digested, and analyzed using an FT-ICR MS that allowed collision-induced dissociation (CID) of selected classifier masses. By using the fragment spectra, proteins were identified by database searches. For comparison and further validation, classifier masses were also fragmented and analyzed using HPLC-/Matrix-assisted laser desorption ionization (MALDI) time-of-flight/time-of-flight (TOF/TOF) mass spectrometry. Desmin and lumican precursor were examples of proteins found in aortic samples at higher abundances than in coronary samples. Similarly, adenylate kinase isoenzyme was found in coronary samples at a higher abundance. The described methodology could also be feasible in search for specific biomarkers in plasma or serum for diagnostic purposes.