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The Stress Response and Stress Proteins
Published in John J. Lemasters, Constance Oliver, Cell Biology of Trauma, 2020
Martin E. Feder, Dawn A. Parsell, Susan L. Lindquist
The stress response, or heat shock response, is a fundamental molecular mechanism with which organisms compensate for environmentally induced perturbations of cellular function. Heat and a variety of other stresses induce a suite of stress or heat shock proteins. These proteins play diverse cellular roles in minimizing or repairing damage due to stress, or in inducing tolerance to subsequent stress. Even in the absence of stress, these proteins or their close relatives are essential for a variety of cellular processes. Due to the vital nature of stress protein function and the importance of their induction as a model for gene regulation, interest in the stress response has undergone explosive growth, averaging more than 800 publications in the primary literature per year during the past five years. More than 500 publications examine the relationships between the stress response and the other subjects in this volume (e.g., reactive oxygen species, ischemia-reperfusion injury, inflammation). Accordingly, here we can but touch upon a limited number of aspects of the stress response that are relevant to the cell biology of trauma, and so can provide only a general introduction to the field. We will, however, cite many of the excellent recent reviews that provide entree to the primary literature.
Heat Shock Proteins and Cell Thermotolerance
Published in Leopold J. Anghileri, Jacques Robert, Hyperthermia In Cancer Treatment, 2019
In human cells, the existence of such a protein whose activation would correspond to the first step in the heat-shock response is suggested by the work of Kao and Nevins.96,97 Induction of HSP by viral infection has been reported by several authors. Newcastle disease virus,98 herpes simplex virus,100 and simian virus 40 and Polyomavirus99 each induce an increased synthesis of at least the HSP70. Nevins96 demonstrated that upon adenovirus infection of HeLa cells, the HSP response was not due to a general stress response to the infection, but rather was the result of the specific action of the viral E1A gene product. By analogy with the known role of the E1A protein in the induction of the early viral mRNAs, they suggested that the viral protein was not a direct activator of transcription, but instead its action was indirect and involved its interaction with a protein factor of the host cell. The possibility that this factor is the same as that involved in the heat induction of HSP is further suggested by the observation (unpublished, reported in Reference 97) that some cells which support early viral transcription in the absence of E1A function also show a high level of heat-shock gene expression in the absence of hyperthermic treatment.
Basic Thermal Physiology: What Processes Lead to the Temperature Distribution on the Skin Surface
Published in Kurt Ammer, Francis Ring, The Thermal Human Body, 2019
Thermo tolerance or acquired cellular thermo tolerance describes the cellular adaptation accompanying systemic changes induced by successful heat adaptation [153]. This rapid, short acting molecular process is associated with the synthesis of several families of heat shock proteins (HSP) of different molecular weights resulting from acute short sub-lethal heat injury. It is thought to protect cells from noxious stimuli as well as to accelerate their repair. It is also defined as heat shock response (HSR). The time course of heat shock proteins varies in different cells but, on the average, heat shock proteins (HSP) in the intact body seem to operate several hours following the stress and retains its activity for a few days. The response is not heat-specific and can be elicited after subjection to several other stressors (e.g. ischemia, some chemicals, etc.) [2].
Biological modeling in thermoradiotherapy: present status and ongoing developments toward routine clinical use
Published in International Journal of Hyperthermia, 2022
H. P. Kok, G. C. van Rhoon, T. D. Herrera, J. Overgaard, J. Crezee
Mechanisms incorporated in the biological models so far were typically limited to DNA-damage repair inhibition and direct cell kill, as these are more easily determined in in vitro tumor models. Although these mechanisms are very important, the incorporation of other mechanisms is essential to realize higher accuracy and personalized treatment (planning). This also requires further research on understanding and quantifying the timing/dose-effect relationship of other relevant mechanisms, such as heat shock response, normal tissue response, vascular effects, blood flow, hypoxia and immunological effects. Dedicated in vivo studies are required to assess the contribution of each mechanism, depending on temperature/thermal dose and timing of hyperthermia. This should involve quantification of multiple clinically relevant end-points in several tumor sites, as well as in normal tissues. Some of this research is foreseen in the framework of Hyperboost.
Multipotent mesenchymal stromal cells are sensitive to thermic stress – potential implications for therapeutic hyperthermia
Published in International Journal of Hyperthermia, 2020
Alexander Rühle, Andreas Thomsen, Rainer Saffrich, Maren Voglstätter, Birgit Bieber, Tanja Sprave, Patrick Wuchter, Peter Vaupel, Peter E. Huber, Anca-Ligia Grosu, Nils H. Nicolay
As increased expression of heat shock proteins has been linked to cellular thermoresistance, we investigated the expression of several heat shock proteins and the heat shock transcription factor HSF1 before and after hyperthermia. In our analysis, MSCs exhibited slightly lower basal levels of HSP27, HSP60 and HSP70 compared to NHDFs which could partly explain the observed thermosensitive phenotype of MSCs, as these proteins play a major role in the heat shock response pathway. Especially MSC2 cells were found to have clearly reduced levels of HSF1 and HSP60, whereby MSC1 had similar levels compared with NHDFs. Heat shock proteins exhibit anti-apoptotic abilities by blocking both the intrinsic and extrinsic apoptotic pathways, and increased levels of HSF1 have been shown to inhibit autophagy induction after hyperthermia [62,63]. We observed only slightly increased levels of heat shock proteins at 24 h after hyperthermia. This marginal increase could be related to the short time interval, as in other studies, protein expression of HSP27, HSP70 and HSP90 reached its maximum in MSCs at 48 h after hyperthermia [64,65]. Although the levels of heat shock proteins were higher for NHDFs than for MSCs, it should be noticed that the expression of these proteins were markedly higher than the β-actin protein levels for all tested samples, which is consistent with previous reports showing a high expression of heat shock proteins in MSCs [50].
High altitude hypoxia on brain ultrastructure of rats and Hsp70 expression changes
Published in British Journal of Neurosurgery, 2019
Wen-Hua Li, Yu-Xiang Li, Jun Ren
Heat shock response is a kind of cellular level biological response to stress. Since heat shock response was found by Tissiéres et al.1 in the study on Drosophila larvae in 1974; heat shock response has become a hot research topic in various fields. The product of heat shock response was heat shock protein (HSP), while the first gene to be cloned and identified was HSP70. The human HSP70 gene is located in chromosome 1, 5, 6, 9, 11 and 14; and also considered to be present in chromosome 21.2,3 Their common code of a set of relative molecular mass from 66,000 to 78,000 was highly related to the protein. HSP70 gene family members can be used as a molecular chaperone to promote the correct folding, assembly and transport of new synthetic proteins, and promote the re-folding or degradation of proteins4,5. HSP70 protein plays an important protective role in the formation of heat tolerance or poison tolerance, as well as the prevention of oxidative damage. Heat stress protein is very important for the stability and adaptability of the intracellular environment. It is known that nucleotide substitution, deletion or insertion mutations can adjust the start of function or transcriptional activity6, while different HSP70 expression levels can modulate stress, or disease susceptibility or tolerance.7 Therefore, this study aimed to observe changes in brain tissue and HSP70 expression in high-altitude hypoxia rats, in order to clarify the mechanism of HSP70 in high-altitude hypoxia adaptation.