Article

Thermally induced injury and heat shock protein expression in cells and tissues

Department of Biomedical Engineering, The University of Texas at Austin, 1 University Station, C0800, Austin, TX 78712-1084, USA.
Annals of the New York Academy of Sciences (Impact Factor: 4.31). 01/2006; 1066(1):222-42. DOI: 10.1196/annals.1363.009
Source: PubMed

ABSTRACT Heat-shock proteins (HSPs) are critical components of a cell's defense mechanism against injury associated with adverse stresses. Initiating insults, such as elevated or depressed temperature, diminished oxygen, and pressure, increase HSP expression and can protect cells against subsequent, otherwise lethal, insults. Although HSPs are very beneficial to the normal cell, cancer cells can also use HSPs in response to stresses associated with various therapies (hyperthermia, chemotherapy, radiation), mitigating injury incurred by these treatments. Hyperthermia is a common treatment option for prostate cancer. HSPs can be induced in regions of the tumor where temperatures are insufficient to cause lethal thermal necrosis. Elevated HSP expression can enhance tumor cell viability and impart increased resistance to subsequent chemotherapy and radiation treatments, thereby promoting tumor recurrence. An understanding of the structure, function, and thermally stimulated HSP kinetics and cell injury for prostate cancer cells is essential to designing effective hyperthermia protocols. Measured thermally induced cellular HSP expression and injury data can be employed to develop a treatment planning model for optimization of the tissue response to therapy based on accurate prediction of the HSP expression and cell damage distribution.

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Available from: Yusheng Feng, Oct 28, 2014
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    • "When exposed to elevated temperatures, animal cells synthesize a small number of highly conserved proteins called heat-shock proteins (Hsps) (Lindquist 1986). Induction of Hsp expression has been reported to protect cells against subsequent temperature changes as well as diminished oxygen and pressure, and loss of Hsp expression may cause damage or be lethal (Marber et al. 1995; Ryan et al. 1992; Rylander et al. 2005; Villar et al. 1994; Wischmeyer 2002). For example, suppressed Hsp90 and Hsp27 expression resulted in increased endoplasmic reticulum stress (ER stress) and apoptosis (Lamoureux et al. 2013). "
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    • "HSPs are up-regulated in tumor cells and their protective effects confound thermal therapies, thus their expression should be controlled in order to achieve an optimal thermal therapy [29]. Laser treatments such as hyperthermia can be optimized by setting the optimum laser parameters (wavelength, power, pulse duration and delivery method) to satisfy the prescribed HSP expression distributions in tumor and healthy tissue required to minimize injury to healthy tissue and efficient tumor destruction [30]. "
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    • "Activation of proteotoxic stress pathways such as the HSR have been proposed to not only support tumour cell survival following a variety of insults but may also be a major factor in promoting tumour progression (Dai et al. 2007; Rylander et al. 2005). Activation of the transcription factor, HSF1, is synonymous with HSR induction; however, in addition to its ability to confer enhanced survival of cells, HSF1 can also regulate many other cellular processes. "
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