Expression of heat shock protein 70 (hsp70) is stimulated during ischemia, but its proposed cytoprotective function during metabolic stress has remained conjectural. We introduced a human hsp70 gene into mouse 10T1/2 cells and assessed the susceptibility of these cells to injury in response to conditions that mimic ischemia. Transiently transfected cells, in the absence of stress, expressed human hsp70 to levels equal to or greater than those induced by heat shock, as assessed by RNAse protection, immunoblot, and immunohistochemical analyses. By comparison to cells transfected with a control plasmid, cells expressing the human hsp70 transgene were resistant to injury induced by glucose deprivation and inhibition of mitochondrial respiration. These results provide direct evidence for a cytoprotective function of hsp70 during metabolic stress.
R S Williams, J A Thomas, M Fina, Z German, I J Benjamin
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Drug Toxicity in Embryonic Development I
RJ Kavlock, GP Daston |
1997 | |
Heat Shock Proteins and the Cardiovascular System
AA Knowlton |
1997 | |
Heat Shock Proteins and Cytoprotection
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1997 | |
Specific induction of the 70-kD heat stress proteins by the tyrosine kinase inhibitor herbimycin-A protects rat neonatal cardiomyocytes. A new pharmacological route to stress protein expression?
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Annals of the New York Academy of Sciences | 1996 |
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