Department of Anatomy, BK21 Project for Medical Science, Yonsei University College of Medicine, Seoul, Korea
ABSTRACT
The phenomenon of ischemic tolerance (also referred to as ischemic preconditioning) is associated with the upregulation of a variety of genes and their proteins. One of highly upregulated proteins is the heat shock proteins (HSPs), which can be induced by exposure to an array of stresses including hyperthermia, excitotoxins, heavy metals, and pharmacologic agents, as well as ischemia. The major eukaryotic HSPs form a super-family consisting of several ubfamilies. Subfamilies are identified by molecular weight, which ranges from 10-170 kD, and are further sub-divided according to cellular localization, expression pattern, and function. They function as molecular chaperones, helping polypeptides assume their proper conformation by binding to nascent proteins via their C terminal domain. HSPs are also involved in antigen presentation, steroid receptor function, intracellular trafficking, nuclear receptor binding, and apoptosis. HSPs are increased following cerebral ischemic insults. While HSPs involved in direct protection of brain cells and other cells from arious stresses, it may not be required in the phenomenon of ischemic tolerance. It is likely that the cell protects itself through multiple echanisms depends on the nature of the tolerizing stress. Regardless, the exercise of isolating and characterizing upregulated genes in these experimental scenarios has led to the identification of a cytoprotective protein that may someday be applied at the clinical level.
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