The time-profile of the PBMC HSP70 response to in vitro heat shock appears temperature-dependent

R Lovell, L Madden, Samantha Carroll, Lars McNaughton

Research output: Contribution to journalArticle

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Abstract

Heat shock proteins (HSPs) are synthesised by cells subsequent to a stress exposure and are known to confer protection to the cell in response to a second challenge. HSP induction and decay are correlated to thermotolerance and may therefore be used as a biomarker of thermal history. The current study tested the temperature-dependent nature of the heat shock response and characterised its time profile of induction. Whole blood from 6 healthy males (Age: 26 ± (SD) 2 yrs; Body mass 74.2 ± 3.8 kgs; VO2max: 49.1 ± 4.0 ml·kg−1·min−1) were isolated and exposed to in vitro heat shock (HS) at 37, 38, 39, 40, and 41 °C for a period of 90 min. After HS the temperature was returned to 37 °C and intracellular HSP70 was quantified from the leukocytes at 0, 2, 4, and 6 h after heat treatment. The concentration of HSP70 was not different between temperatures (P > 0.05), but the time-profile of HSP70 synthesis appeared temperature-dependent. At control (37 °C) and lower temperatures (38–39 °C) the mean HSP70 concentration increased up to 4 h post HS (P < 0.05) and then returned towards baseline values by 6 h post HS. With in vitro hyperthermic conditions (40–41 °C), the time-profile was characterised by a sharp rise in HSP70 levels immediately after treatment (P < 0.05 for 40 °C at 0 h), followed by a progressive decline over time. The results suggest a temperature-dependent time-profile of HSP70 synthesis. In addition, the temperature at which HSP70 is inducted might be lower than 37 °C.
Original languageEnglish
Pages (from-to)137-144
JournalAmino Acids
Volume33
Issue number1
DOIs
Publication statusPublished - 2007

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Shock
Hot Temperature
Temperature
Heat-Shock Proteins
Heat-Shock Response
Cytoprotection
Biomarkers
In Vitro Techniques
Leukocytes
Blood
Heat treatment

Cite this

Lovell, R ; Madden, L ; Carroll, Samantha ; McNaughton, Lars. / The time-profile of the PBMC HSP70 response to in vitro heat shock appears temperature-dependent. In: Amino Acids. 2007 ; Vol. 33, No. 1. pp. 137-144.
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The time-profile of the PBMC HSP70 response to in vitro heat shock appears temperature-dependent. / Lovell, R; Madden, L; Carroll, Samantha; McNaughton, Lars.

In: Amino Acids, Vol. 33, No. 1, 2007, p. 137-144.

Research output: Contribution to journalArticle

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AB - Heat shock proteins (HSPs) are synthesised by cells subsequent to a stress exposure and are known to confer protection to the cell in response to a second challenge. HSP induction and decay are correlated to thermotolerance and may therefore be used as a biomarker of thermal history. The current study tested the temperature-dependent nature of the heat shock response and characterised its time profile of induction. Whole blood from 6 healthy males (Age: 26 ± (SD) 2 yrs; Body mass 74.2 ± 3.8 kgs; VO2max: 49.1 ± 4.0 ml·kg−1·min−1) were isolated and exposed to in vitro heat shock (HS) at 37, 38, 39, 40, and 41 °C for a period of 90 min. After HS the temperature was returned to 37 °C and intracellular HSP70 was quantified from the leukocytes at 0, 2, 4, and 6 h after heat treatment. The concentration of HSP70 was not different between temperatures (P > 0.05), but the time-profile of HSP70 synthesis appeared temperature-dependent. At control (37 °C) and lower temperatures (38–39 °C) the mean HSP70 concentration increased up to 4 h post HS (P < 0.05) and then returned towards baseline values by 6 h post HS. With in vitro hyperthermic conditions (40–41 °C), the time-profile was characterised by a sharp rise in HSP70 levels immediately after treatment (P < 0.05 for 40 °C at 0 h), followed by a progressive decline over time. The results suggest a temperature-dependent time-profile of HSP70 synthesis. In addition, the temperature at which HSP70 is inducted might be lower than 37 °C.

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