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Chapter category: Heat Shock Proteins

Role of Heat Shock Proteins, Protein Kinase C and ATP-Sensitive Potassium Channel in Delayed Myocardial Protection

This chapter appears in the following book:

Heat Shock Proteins in Myocardial Protection

Edited by: Rakesh C. Kukreja
ISBN: 1-58706-021-3
» Get more information about this book at landesbioscience.com «

Chapter authors:
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.2 There has been a tremendous interest in the role of Hsp's to understand their function under stress conditions as well as homeostatic states. Exactly how Hsp's protect cells is unclear; however, several explanations have been offered. These include the renaturation of damaged proteins, or facilitation of the folding and targeting of newly synthesized proteins to organelles.2,3 Hsp's may also maintain newly synthesized proteins in a translocational configuration (linear or unfolded).4 After heat stress the cytoplasmic Hsp 72 is found to localize in and around the nucleus but move back out to the cytoplasm during the recovery phase. Hsp 72 and 73 bind transiently to nascent proteins acting as intracellular chaperones and help stabilize these proteins until they achieve their final conformation.5

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