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Diathermy therapy
Published in Riadh Habash, BioElectroMagnetics, 2020
HSPs are the most abundant and ubiquitous soluble intracellular proteins. They are recognized as significant participants in immune reactions. Hyperthermia induces overexpression of HSP at the expense of inhibiting the synthesis of many other proteins, including cytoskeletal and regulatory proteins that may be crucial for normal cellular functions. For example, heat may alter the normal body immuno-response by altering thymocyte [109] and leukocyte [106] production as well as inducing T-lymphocyte propagation [110]. Ito et al. [111] suggested that HSP70 is an important modulator of tumor cell immunogenicity and that hyperthermic treatment of tumor cells can induce the host antitumor immunity via the expression of HSP70. These results may benefit further efforts on developing novel cancer immunotherapies based on hyperthermia. Other studies demonstrated a dual role of thermotolerance and immune stimulation of HSPs [112,113]. Ivarsson et al. [114] used an implantation model of colorectal liver metastases to identify increased expression and change in the localization of HSP70 at 10–15 h after laser ablation. It is postulated that increased HSP tumor petite complexes following focal hyperthermia are involved in tumor antigen presentation to macrophages and other antigen presenting cells. The immunological properties of HSPs enable them to be used in new immunotherapies of cancers and infections [115].
Molecular Approaches for Enhancing Abiotic Stress Tolerance in Plants
Published in Hasanuzzaman Mirza, Nahar Kamrun, Fujita Masayuki, Oku Hirosuke, Tofazzal M. Islam, Approaches for Enhancing Abiotic Stress Tolerance in Plants, 2019
Sushma Mishra, Dipinte Gupta, Rajiv Ranjan
Heat shock proteins (HSPs), which could be broadly divided into three classes – HSP90, HSP70 and low molecular weight (sHsps, 15–30 kDa), act as molecular chaperones that stabilize protein structures and membranes during high temperature and also assist in re-folding of the misfolded proteins under heat stress (Wahid et al., 2007). The different classes of HSPs/chaperones cooperate in cellular protection and play complementary and sometimes overlapping roles in the protection of proteins from stress (Wang et al., 2005). It has been reported that the sHsps stabilize the stress-denatured proteins (by preventing their aggregation) for subsequent refolding by members of the Hsp70/Hsp100 chaperone families (Veinger et al., 1998; Lee and Vierling, 2000).
Cellular Effects of Radio Frequency, Millimeter, and Terahertz Waves
Published in Ben Greenebaum, Frank Barnes, Biological and Medical Aspects of Electromagnetic Fields, 2018
Gene expression is a metabolic process in a cell in which the DNA sequence (genetic information) is transcribed into mRNA, and ultimately translated into protein. Research on the effect of RFW exposure on gene expression has focused on heat shock proteins (HSPs). Generally, increased expression of HSPs, including HSP70 and HSP27, is seen as a stress reaction to heat and cytotoxic chemical substances. The effect of RFW exposure on HSP has been investigated by various laboratories, and it has been observed that HSP expression is increased by the temperature rise due to high SARs of 20 W/kg or more. Another study investigated whether exposure to 2450 MHz RFWs could act as an environmental insult and evoke a stress response in A172 cells, using HSP70 and HSP27 as stress markers. The cells were exposed to 2450 MHz RFWs with a wide range of SAR values (5–200 W/kg) or sham conditions. Expression of HSP70 increased in a time- and dose-dependent manner at >50 W/kg SAR for 1–3 h. A similar effect was also observed in the corresponding heat controls. There was no significant change in HSP27 expression following exposure to RFWs at 5–200 W/kg or comparable heating for 1–3 h (Wang et al., 2006).
Green synthesis of silver nanoparticles using Macrolepiota procera extract and investigation of their HSP27, HSP70, and HSP90 inhibitory potentials in human cancer cells
Published in Particulate Science and Technology, 2023
Aykut Özgür, Özlem Kaplan, Nazan Gökşen Tosun, İbrahim Türkekul, İsa Gökçe
Cancer is a significant health problem that has a significant impact on society around the world. In 2020, about 19.3 million new cancer cases were diagnosed, and almost 10.0 million cancer patients died worldwide (Sung et al. 2021). Chemotherapy is the most common treatment option for cancer patients. Conventional chemotherapeutic agents are designed based on their antiproliferative ability against fast-growing cells such as cancer cells. However, side effects and drug resistance dramatically reduce the therapeutic efficiency of conventional drugs in cancer patients (Vasan, Baselga, and Hyman 2019). To minimize these limitations, targeted therapy is an important approach in cancer treatment (Bashraheel, Domling, and Goda 2020). HSPs have gained importance as a potential molecular target in cancer drug discovery due to their vital roles in the stabilization and activation of oncogenic signaling pathways to promote the survival of cancer cells (Tutar and Tutar 2010; Calderwood and Gong 2016; Olotu et al. 2018; Özgür 2021; Yang, Xiao, and Cao 2021). HSP27, HSP70, and HSP90 are overexpressed in cancer cells and play fundamental roles in cell proliferation, apoptosis, metastasis, angiogenesis, invasion, and drug resistance pathways. Therefore, inhibition of HSP27, HSP70, and HSP90 has been an effective strategy in cancer treatment. Numerous experimental studies reported that nanoparticle-based therapeutic systems might have the potential to inhibit chaperone activity of the HSP27, HSP70, and HSP90 in cancer cells (Tutar and Tutar 2010; Murphy 2013; Acunzo et al. 2014; Wang et al. 2014; Sherman and Gabai 2015; Gümus et al. 2016; Boudesco et al. 2018; Park et al. 2020; Yang, Xiao, and Cao 2021; Cyran and Zhitkovich 2022; Lampros et al. 2022). Herein, we aimed to investigate the HSP27, HSP70, and HSP90 inhibition potentials of MP-AgNPs in MCF-7, A549, Saos-2, and HT-29 cell lines.