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06:01
Standardized Methods for Measuring Induction of the Heat Shock Response in Caenorhabditis elegans
Published on: July 3, 2020
Thermotolerance and the heat shock proteins
1Department of Bioscience & Biotechnology, Todd Centre, University of Strathclyde, Glasgow, UK.
Symposia of the Society for Experimental Biology
|January 1, 1987
Summary
Mammalian cells develop thermotolerance after heat conditioning, potentially involving heat shock proteins (hsps) and protein synthesis regulation. Further research is needed to fully understand these protective mechanisms against thermal damage.
Area of Science:
- Cellular Biology
- Stress Response
- Molecular Biology
Background:
- Mammalian cells exhibit increased tolerance to thermal damage following prior heat conditioning.
- Thermotolerance is influenced by thermal history, heat fractionation intervals, and recovery conditions.
- Heat shock proteins (hsps) are hypothesized to mediate cellular protection against heat stress.
Purpose of the Study:
- To investigate the role of heat shock proteins (hsps) in the development and maintenance of thermotolerance in mammalian cells.
- To examine the correlation between hsps levels and thermotolerance.
- To explore the relationship between protein synthesis and thermal resistance.
Main Methods:
- Monitoring heat shock protein synthesis and degradation during thermotolerance development and decay.
- Assessing thermotolerance in cells with inhibited hsp induction (e.g., cycloheximide treatment, Ca2+ depletion).
- Measuring thermal resistance of total protein synthesis in HeLa cells under various heat treatments.
Main Results:
- While hsps levels correlate with thermotolerance in some cases, this correlation is not always consistent.
- Inhibition of hsp synthesis does not always block thermotolerance development.
- Thermotolerance in cell survival parallels the thermal resistance of total protein synthesis, suggesting a broader role beyond hsps.
- Actinomycin D reduces thermotolerance in protein synthesis, implicating the nucleolus.
Conclusions:
- Heat shock proteins, particularly hsp 70 and ubiquitin, may play roles in repairing heat-damaged nucleoli and degrading abnormal proteins, respectively.
- Thermotolerance involves complex mechanisms potentially including basal levels of hsps and regulation of overall protein synthesis.
- The nucleolus appears to be involved in the development of thermotolerance in protein synthesis.
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