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(Circulation Research. 2006;99:1315.)
© 2006 American Heart Association, Inc.

Reviews

Heart Failure and Protein Quality Control

Xuejun Wang, Jeffrey Robbins

From the Division of Basic Biomedical Sciences (X.W.), Sanford School of Medicine of the University of South Dakota, Vermillion, SD; and Children’s Hospital Research Foundation (J.R.), Cincinnati, Ohio.

Correspondence to Jeffrey Robbins, Division of Molecular Cardiovascular Biology, 3333 Burnet Ave, Cincinnati, OH 45229-3039. E-mail jeff.robbins{at}cchmc.org

This review is part of a thematic series on Ubiquitination, which includes the following articles:

Regulation of G Protein and Mitogen-Activated Protein Kinase Signaling by Ubiquitination: Insights From Model Organisms

Heart Failure and Protein Quality Control

Ubiquitin and Ubiquitin-Like Proteins in Protein Regulation

Seven-Transmembrane Receptors and Ubiquitination
Sudha K. Shenoy Guest Editor

The heart is constantly under mechanical, metabolic, and thermal stress, even at baseline physiological conditions, and cardiac stress may increase as a result of environmental or intrinsic pathological insults. Cardiomyocytes are continuously challenged to efficiently and properly fold nascent polypeptides, traffic them to their appropriate cellular locations, and keep them from denaturing in the face of normal and pathological stimuli. Because deployment of misfolded or unfolded proteins can be disastrous, cells, in general, and cardiomyocytes, in particular, have developed a multilayered protein quality control system for maintaining proper protein conformation and for reorganizing and removing misfolded or aggregated polypeptides. Here, we examine recent data pointing to the importance of protein quality control in cardiac homeostasis and disease.

Key Words: cardiac disease • cardiac failure • cardiac muscle • cardiomyocytes • cardiovascular disease • cardiovascular physiology

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