STATE-OF-THE-ART PAPER
Potential Role of the Ubiquitin-Proteasome System in AtherosclerosisAspects of a Protein Quality Disease
Joerg Herrmann, MD*,
Sandra M. Soares, MD,
Lilach O. Lerman, MD, PhD and
Amir Lerman, MD
Department of Internal Medicine, Mayo Clinic, Rochester, Minnesota.
Manuscript received November 7, 2007;
revised manuscript received January 28, 2008,
accepted February 12, 2008.
*
Reprint requests and correspondence: Dr. Joerg Herrmann, Department of Internal Medicine, Mayo Clinic Rochester, 200 First Street Southwest, Rochester, Minnesota 55905. (Email: herrmann.joerg{at}mayo.edu).
Misfolded or damaged proteins are recognized intracellularly by protein quality mechanisms. These include chaperones and the ubiquitin-proteasome system, which aim at restoration of protein function and protein removal, respectively. A number of studies have outlined the functional significance of the ubiquitin-proteasome system for the heart and, as of recently, for the vascular system. This review summarizes these recent findings with a focus on atherosclerosis. In particular, this paper reflects on the viewpoint of atherosclerosis as a protein quality disease.
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Abbreviations and Acronyms
| | Abeta = amyloid beta protein | | APP = amyloid precursor protein | | ER = endoplasmic reticulum | | ERAD = endoplasmic reticulum-associated protein degradation | | HSP = heat shock protein | | LDL = low-density lipoprotein | | ROS = reactive oxygen species | | TIA = transient ischemic attack | | UPS = ubiquitin-proteasome system |
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