Copyright © 2007, European Society of Cardiology
S100 proteins: A missing piece in the puzzle of heart failure?
aMedizinische Universitätsklinik und Poliklinik III, Otto-Meyerhof-Zentrum, Ruprecht-Karls Universität Heidelberg, Heidelberg, Germany
bCenter for Translational Medicine, Thomas Jefferson University, 1025 Walnut Street, Philadelphia, PA 19107, USA
* Corresponding author. hugo_katus@med.uni-heidelberg.de
Received 2 May 2007; accepted 4 May 2007
| The first 10% of the full text of this article appears below. |
See article by Schneider et al. [13] (pages 40–50) in this issue.
Heart failure (HF) represents the common endpoint of many different kinds of cardiopulmonary diseases. Essentially, loss of myocardium triggers a sequence of molecular, cellular and physiological responses leading to ventricular remodelling and the inability of the ventricle to maintain an output sufficient for the metabolic requirements of the tissues of the body [1]. Although these responses may be viewed as compensatory in nature, many of them are or become counterregulatory and lead to long-term adverse effects [1]. Thus, novel insight into the regulatory mechanisms that contribute to the
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B. L. Prosser, N. T. Wright, E. O. Hernandez-Ochoa, K. M. Varney, Y. Liu, R. O. Olojo, D. B. Zimmer, D. J. Weber, and M. F. Schneider S100A1 Binds to the Calmodulin-binding Site of Ryanodine Receptor and Modulates Skeletal Muscle Excitation-Contraction Coupling J. Biol. Chem., February 22, 2008; 283(8): 5046 - 5057. [Abstract] [Full Text] [PDF] |
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