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(Circulation Research. 2006;98:309.)
© 2006 American Heart Association, Inc.

Reviews

Proteomics of the Heart

Unraveling Disease

Emma McGregor, Michael J. Dunn

From the BioScience Communications (E.M.), London, UK; and Proteome Research Centre (M.J.D.), UCD Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Ireland.

Correspondence to Professor Michael J. Dunn, Proteome Research Centre, UCD Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland. E-mail michael.dunn{at}ucd.ie

This Review is part of a thematic series on Proteomics, which includes the following articles:

Cardiovascular Proteomics: Evolution and Potential

Applied Proteomics: Mitochondrial Proteins and Effect on Function

Organelle Proteomics: Implications for Subcellular Fractionation in Proteomics

Identification of Novel Signaling Complexes By Functional Proteomics

Proteomic Approaches to Analyze the Dynamic Relationships Between Nucleocytoplasmic Protein Glycosylation and Phosphorylation

Proteomics of the Heart: Unraveling Disease
Jennifer E. Van Eyk Guest Editor

Heart diseases resulting in heart failure are among the leading causes of morbidity and mortality in developed countries. Underlying molecular causes of cardiac dysfunction in most heart diseases are still largely unknown but are expected to result from causal alterations in gene and protein expression. Proteomic technology now allows us to examine global alterations in protein expression in the diseased heart and can provide new insights into cellular mechanisms involved in cardiac dysfunction. The majority of proteomic investigations still use 2D gel electrophoresis (2-DE) with immobilized pH gradients to separate the proteins in a sample and combine this with mass spectrometry (MS) technologies to identify proteins. In spite of the development of novel gel-free technologies, 2-DE remains the only technique that can be routinely applied to parallel quantitative expression profiling of large sets of complex protein mixtures such as whole cell lysates. It can resolve >5000 proteins simultaneously (2000 proteins routinely) and can detect <1 ng of protein per spot. Furthermore, 2-DE delivers a map of intact proteins, which reflects changes in protein expression level, isoforms, or post-translational modifications. The use of proteomics to investigate heart disease should result in the generation of new diagnostic and therapeutic markers. In this article, we review the current status of proteomic technologies, describing the 2-DE proteomics workflow, with an overview of protein identification by MS and how these technologies are being applied to studies of human heart disease.

Key Words: proteomics • two-dimensional gel electrophoresis • mass spectrometry • cardiomyopathy • heart failure

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