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Simulated diving after heat stress potentiates the induction of heat shock protein 70 and elevates glutathione in human endothelial cells

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Cell Stress and Chaperones Aims and scope

Abstract

Heat stress prior to diving has been shown to confer protection against endothelial damage due to decompression sickness. Several lines of evidence indicate a relation between such protection and the heat shock protein (HSP)70 and HSP90 and the major cellular red-ox determinant, glutathione (GSH). The present study has used human endothelial cells as a model system to investigate how heat stress and simulated diving affect these central cellular defense molecules. The results demonstrated for the first time that a simulated dive at 2.6 MPa (26 bar) had a potentiating effect on the heat-induced expression of HSP70, increasing the HSP70 concentration on average 54 times above control level. In contrast, a simulated dive had no significant potentiating effect on the HSP90 level, which might be due to the higher baseline level of HSP90. Both 2 and 24-h dive had similar effects on the HSP70 and HSP90, suggesting that the observed effects were independent of duration of the dive. The rapid HSP response following a 2-h dive with a decompression time of 5 min might suggest that the effects were due to compression or pressure per se rather than decompression and may involve posttranslational processing of HSP. The exposure order seemed to be critical for the HSP70 response supporting the suggestion that the potentiating effect of dive was not due to de novo synthesis of HSP70. Neither heat shock nor a simulated dive had any significant effect on the intracellular GSH level while a heat shock and a subsequent dive increased the total GSH level approximately 62%. Neither of these conditions seemed to have any effect on the GSH red-ox status.

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Acknowledgment

The authors would like to express their appreciation to Mrs. Torill Sage and Mr. Harald A. Sundland, both NUI AS, for excellent technical assistance in performing the cell culture work and exposure in pressure chambers. The authors are grateful for the careful analysis of glutathione performed by Mrs. Torunn Eide at Institute of Medicine, University of Bergen. This work was supported by StatoilHydro (formerly Statoil and Norsk Hydro) and Exxon Mobil, Norway.

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Correspondence to Rune Djurhuus.

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Djurhuus, R., Nossum, V., Lundsett, N. et al. Simulated diving after heat stress potentiates the induction of heat shock protein 70 and elevates glutathione in human endothelial cells. Cell Stress and Chaperones 15, 405–414 (2010). https://doi.org/10.1007/s12192-009-0156-3

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  • DOI: https://doi.org/10.1007/s12192-009-0156-3

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