Journal of Cell Science, Vol 104, Issue 1 11-17, Copyright © 1993 by Company of Biologists

JOURNAL ARTICLES

Thermotolerance in mammalian cells. Protein denaturation and aggregation, and stress proteins

HH Kampinga
Department of Radiobiology, Faculty of Medicine, University of Groningen, The Netherlands.

Cells that have been pre-exposed to thermal stress can acquire a transient resistance against the killing effect of a subsequent thermal stress. The cause for this phenomenon, called thermotolerance, seems to be an enhanced resistance of proteins against thermal denaturation and aggregation. This resistance can be expressed as an attenuation of damage formation (less initial damage) or as a better repair of the protein damage (facilitated recovery). Heat Shock (or better, Stress) Proteins (HSPs) may play a role in and even be required for thermal resistance. However, rather than stress-induced enhanced synthesis and elevated total levels of HSPs per se, the concentration of, both constitutive and inducible, HSPs at and/or (re)distributed to specific subcellular sites may be the most important factor for the acquisition of thermotolerance. Specific HSPs may be involved either in damage protection or in damage repair.
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