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. 1993 Jul;92(1):503–508. doi: 10.1172/JCI116594

Human heat shock protein 70 (hsp70) protects murine cells from injury during metabolic stress.

R S Williams 1, J A Thomas 1, M Fina 1, Z German 1, I J Benjamin 1
PMCID: PMC293638  PMID: 8326014

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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