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Myofilament proteins: From cardiac disorders to proteomic changes

  1. Chao Yuan,
  2. R. John Solaro Dr.*

Article first published online: 12 JUN 2008

DOI: 10.1002/prca.200780076

Issue

PROTEOMICS - Clinical Applications

PROTEOMICS - Clinical Applications

Special Issue: CARDIOVASCULAR PROTEOMICS

Volume 2, Issue 6, pages 788–799, No. 6 June 2008

Additional Information

How to Cite

Yuan, C. and Solaro, R. J. (2008), Myofilament proteins: From cardiac disorders to proteomic changes. Prot. Clin. Appl., 2: 788–799. doi: 10.1002/prca.200780076

Author Information

  1. Department of Physiology and Biophysics and Center for Cardiovascular Research, University of Illinois at Chicago, Chicago, IL, USA

*Department of Physiology and Biophysics (M/C 901), University of Illinois at Chicago, College of Medicine, 835 South Wolcott Avenue, Chicago, IL 60612, USA Fax: +1-312-996-1414

Publication History

  1. Issue published online: 12 JUN 2008
  2. Article first published online: 12 JUN 2008
  3. Manuscript Received: 6 OCT 2007

Funded by

  • NIH. Grant Numbers: R37/R01 HL 22231, RO1 HL 64035, PO1 HL 62426, T32 007692
  • Chicago Biomedical Consortium

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Keywords:

  • Heart;
  • Oxidative stress;
  • Phosphorylation;
  • Protein isoforms;
  • Sarcomere

Abstract

Myofilament proteins of the cardiac sarcomere house the molecular machinery responsible for generating tension and pressure. Release of intracellular Ca2+ triggers myofilament tension generation and shortening, but the response to Ca2+ is modulated by changes in key regulatory proteins. We review how these proteomic changes are essential to adaptive physiological regulation of cardiac output and become maladaptive in cardiac disorders. We also review the essentials of proteomic techniques used to study myofilament protein changes, including degradation, isoform expression, phosphorylation and oxidation. Selected proteomic studies illustrate the applications of these approaches.

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