Heat Shock Proteins in Myocardial Protection
|
Edited By:Rakesh C. KukrejaVirginia Commonwealth University
Michael L. Hess Published: 2000-08-01 |
Myocardial ischemic syndromes pose a major medical problem and a significant economic health care concern. Reperfusion, although used in the clinical arena as essential to the survival of acutely ischemic heart muscle carries with it the risk of "reperfusion injury". Therefore the salvage of additional myocardium is highly desirable. Over a decade ago, it was shown that whole body heat shock activated a powerful endogenous protective mechanism that significantly improved myocardial salvage following prolonged ischemia and reperfusion injury in the heart. A characteristic feature of this heat shock response was the expression of a family of proteins known as heat shock proteins. Many of these proteins function as molecular chaperones, helping to refold proteins denatured as a consequence of lethal injuries and facilitating the synthesis of new proteins to replace those irreparably damaged. Altered expression of these proteins has been extensively documented in association with a diverse array of diseases such as ischemia and perfusion injury, cardiac hypertrophy, fever, inflammation, metabolic diseases, infection, cell and tissue trauma, aging, and cancer. Interestingly, some studies have now shown a direct correlation of the heat shock proteins produced and the degree of myocardial protection. This book is a thorough description of the current state of knowledge of the mechanisms of heat shock proteins induced cardiac protection at the cellular and molecular level, the controversies in this growing field and the potential of treating ischemic heart disease with overexpression of heat shock proteins in patients. The book will be especially useful for investigators interested in studying tissue injury and its protection with the overexpression of heat shock proteins.
Chapters available from this book
Ischemia/Reperfusion Injury and Heat Shock Proteins
Junichiro Nishizawa and Kazuhiro Nagata
Ischemic heart disease or myocardial infarction remains the most prevalent cause of death in developed countries despite advances in modern medicine. Recent advances in diagnosis and treatment have allowed at early stages, the rapid return of blood flow by surgical, interventional or pha...
Physiological Role of Heat Shock Protein 27
Dipak K. Das and Nilanjana Maulik
Heat shock protein 27 (Hsp27) is a stressinducible cytosolic protein that is ubiquitously present in many normal cells. The synthesis of Hsp27 is induced by heat shock and other environmental and pathophysiologic stresses such as UV radiation, hypoxia and ischemia.14<...
Stress Proteins in Myocardial Protection: Culture Shock Protein, Heme Oxygenase1 (Hsp32), Induced by Sublethal Stresses Protects the Heart Against Oxidative Stress
Shiro Hoshida
The formation of a stress protein comprises a mechanism of cell protection highly conserved in evolution. As the induction of stress proteins makes cells more tolerant towards a second, more toxic, and otherwise lethal stress, the stress protein response might be involved in cardiopro...
Antisense, Heat Shock Proteins and the Heart
A. A. Knowlton
Antisense technology provides a tool with which to dissect the components of the stress response. There are two known endogenous sets of protective proteins, the heat shock proteins (Hsps) and the antioxidants, such as superoxide dismutase;14 components of both sets of p...
Preconditioning of Cardiac Myocytes: Studies Using Cultured Neonatal
Jan A. Post, Chris T.W.M. Schneijdenberg and Arie J. Verkleij
The acquisition of tolerance towards myocardial ischemia and reperfusion can be acquired by several preconditioning procedures. The original preconditioning protocol described for myocardial tissue was reported by Murry et al1 and comprised a few short periods of ischemia o...
Hsp72 in the Regulation of TNFa Production:
Xianzhong Meng
Myocardial ischemia/reperfusion induces the production of the cardiac depressant cytokine tumor necrosis factora (TNFa). Macrophages (Mf) are the main sources of tissue TNFa, and nuclear fa...
Hsp70 and Ischemia Tolerance in the Compromised Heart Ger J. van der Vusse
Luc H.E.H. Snoeckx, Richard N.M. Cornelussen, Robert S. Reneman and
The discovery in eukaryotic and prokaryotic organisms of a prompt and specific response to heat shock, known as the heat shock response, has stimulated the development of a complete new research domain, in which the potential protective role of stress induced proteins in organisms, ti...
Role of Heat Shock Proteins, Protein Kinase C and ATP-Sensitive Potassium Channel in Delayed Myocardial Protection
Rakesh C. Kukreja, Yong-Zhen Qian and Jeffery B. Hoag
Heat shock proteins (Hsp's) are one of the highly conserved proteins in existence, found in every organism.1 These proteins are synthesized quickly and intensely in response to stressors and are known to protect the cells from the toxic effects of heat and other stresses....
Cardioprotection by Stress Proteins
Heat Shock Proteins in Myocardial Protection, edited by Rakesh C. Kukreja
Myocardial ischemia causes a series of changes at the intracellular level within the cardiomyocyte. These intracellular changes include changes in calcium levels, altered osmotic control, membrane damage, generation of free radicals, a decrease in intra-cellular pH, depressed intracellul...
Heat Stress Proteins: A Possible Route to Myocardial Protection
Mohamed Amrani, Caroline C. Gray and Magdi H. Yacoub
Heat stress proteins (hsp) are induced by a variety of stimuli including elevated temperature,1 ischemia,2 hypoxia,3 pressure overload4 and some chemicals. They help to maintain the metabolic and structural integrity of the cell, as a protec...
Stress Proteins in Myocardial Protection
Richard Carroll and Derek M. Yellon
In all organisms examined heat stress results in the synthesis of a specific group of proteins known as the heat shock or stress proteins (Hsps). Cells that accumulate these proteins adapt and become resistant to further heat stress, a protection that seems directlydependent on stress...

