Heat Shock Proteins

Following IEG expression, several stress-response genes are upregulated (93-95). Heat-shock proteins (HSPs), among the most studied in the setting of brain ischemia, are a family of chaperone proteins thought to function as the cell's endogenous, self-protecting response to stresses and lethal insults. The inducible HSP70, especially increased following brain ischemia, is a useful marker of stress and correlates to brain regions relatively resistant to injury. In some settings, HSP70 is thought to protect the brain from injury through its chaperone functions by preventing protein malfolding and aggregation (93). However, recent studies suggest that HSP70 might also interfere with cell death pathways, such as apoptosis (96-99), and inhibit expression of damaging proteins, such as the matrix metalloproteinases (MMPs) (100). Whether HSPs can someday be used as a cytoprotective therapy is unclear, but some laboratory data indicate that administration of geldanamycin, a benzoquinone ansamycin that induces HSPs by binding HSP90 and releasing heat-shock factor (HSF) to induce HSP70, ameliorates injury from experimental stroke (101 ).

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