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Diathermy therapy
Published in Riadh Habash, BioElectroMagnetics, 2020
Cellular stress can be caused by a number of physical and/or chemical factors. These include nonphysiological temperatures (heat, cold), oxygen deficits, acid–base imbalances, toxic compounds, ionizing radiation, etc. [16]. Heat stress has been extensively investigated for decades. If the temperature is high enough, cells respond with a heat stress response trying to protect the cell from undergoing apoptosis and/or necrosis [17]. A number of cellular processes are affected, leading to the survival of the cell. Prior to this event, the cell is increasing the expression of genes encoding the so-called heat shock proteins (HSP), which execute the necessary functional adjustments. It is important to observe that if a so-called mild heat stress (39–43°C) at a level below a lethal temperature (44–45°C) occurs, the cellular response is somewhat different [18]. This is reflected in both the gene expression pattern and the physiological responses within the cell [19,20].
Oryza sativa) during arsenic toxicity amelioration by a potential microbial consortium
Published in Yong-Guan Zhu, Huaming Guo, Prosun Bhattacharya, Jochen Bundschuh, Arslan Ahmad, Ravi Naidu, Environmental Arsenic in a Changing World, 2019
S. Awasthi, R. Chauhan, S. Srivastava, R.D. Tripathi
The present study indicates a practical potential for microbial application as an intervention strategy in mitigating As toxicity and reducing As uptake and translocation in rice plants. Supplementation of P. putida and C. vulgaris with 50µM As(V) significantly alleviated As induced growth inhibition in rice seedlings (Fig. 1), improved photosynthetic and antioxidant machinery and significantly decreased rice As concentration. Many proteins were differentially induced in rice seedlings by P. putida and C. vulgaris under As stress. The differentially expressed proteins were mainly involved to regulate defense system, photosynthesis, detoxification, plant hormones and energy metabolism. Heat shock protein are also found to be accumulated, which were a class of functionally related proteins involved in repair and aid in the renaturation of stress-damaged proteins, and reestablish cellular homeostasis, protect cells against the damage of stress (Ahsan et al., 2009). This study also revealed the expression of IAP100 (Inhibitor of Apoptosis) in the presence of consortium under As stress; IAP100 has ability to regulate caspases and also influence ubiquitin (Ub)-dependent pathways that modulate innate immune signaling. In conclusion, results provide new insights about the proteins and mechanisms involved in microbial consortium mediated As toxicity amelioration in rice.
Cellular Biology in Tissue Engineering
Published in Joseph W. Freeman, Debabrata Banerjee, Building Tissues, 2018
Joseph W. Freeman, Debabrata Banerjee
The final type of physical stimulation that we will discuss is thermal stimulation. Just as the name implies, thermal stimulation involves the use of heat to induce specific behaviors in targeted cells. After many studies, it has been concluded that during a stress response, the cell expresses a set of proteins known as heat shock proteins. These proteins respond to the stress signal by performing various types of physiologic functions, such as repairing damage and translocation assistance of proteins.87 These functions can be harnessed and guided to stimulate the proliferation of MSCs. Therefore, heat shock proteins have an important influence on stem cells. In fact, studies have shown that there are some heat shock proteins that physically interact with a number of transcription factors.87 This interaction allows the protein to have a direct influence on the cell. Alternatively, changes in the heat shock protein expression have exhibited changes in cell behavior, self-renewal potential, and differentiation.
The influence of climate change on human cardiovascular function
Published in Archives of Environmental & Occupational Health, 2020
Milos Gostimirovic, Radmila Novakovic, Jovana Rajkovic, Vladimir Djokic, Dusko Terzic, Svetozar Putnik, Ljiljana Gojkovic-Bukarica
What happens to subcellular structures after being exposed to a severe thermal stress? Probably the most important protective superfamily of proteins that play key role in the protein preservation and prevention of its degradation after acute or prolonged stress are called heat shock proteins (HSP).7 HSP represent highly conserved and ubiquitously expressed family of proteins that have crucial role in cell protection after exposure to severe stress. Upregulation of HSP synthesis is considered a powerful, physiological mechanism for protecting major cell structures against disturbing factors.7,8 As their concentration is increased many fold after acute or prolonged stress stimuli, they are also considered a part of the systemic stress response. Specific HSPs have a great role in thermo-tolerance and represent an important factor for survival in high temperatures.7
Benzo[a]pyrene constrains embryo development via oxidative stress induction and modulates the transcriptional responses of molecular biomarkers in the marine medaka Oryzias javanicus
Published in Journal of Environmental Science and Health, Part A, 2020
Sang-Eun Nam, Manoharan Saravanan, Jae-Sung Rhee
The major BaP mode of action is genotoxicity via the activation of a ligand-activated transcription factor, the aryl hydrocarbon receptor (AhR).[10] The direct binding of BaP to AhR in fish can trigger phase I and II biotransformations.[11] In fish, it has been suggested that BaP detrimentally affects the modulation of hormone receptor signaling pathways, induces oxidative stress, and causes DNA damage, apoptosis, and immunosuppression.[4,12–16] CYP1A is one of the main enzymes involved in the metabolism of PAHs and its induction has been used as a promising biomarker in ecotoxicological studies. Heat shock proteins are typically expressed in cells when they respond to various stressors and enhance survival by protecting vital cellular functions.[17] Acetylcholinesterase (AChE) is mainly responsible for modulating the neurotransmitter acetylcholine (ACh) in the nerve system, which is vital for the normal functioning of sensory and neuromuscular systems.[18] Furthermore, AChE plays important roles in the neuronal and muscular development of fish embryos and has been used as an important neurotoxicity indicator.[19]
Expression of genes related to antioxidant activity in Nile tilapia kept under salinity stress and fed diets containing different levels of vitamin C
Published in Journal of Toxicology and Environmental Health, Part A, 2018
Caio Alexandre Santos Caxico Vieira, Jodnes Sobreira Vieira, Marisa Silva Bastos, Vittor Zancanela, Leandro Teixeira Barbosa, Eliane Gasparino, Ana Paula Del Vesco
In contrast to antioxidant enzymes, after only 24 h, tilapia maintained in 21‰ salinity presented higher HSP70 gene expression. Heat shock proteins (HSPs) act as molecular chaperones under normal conditions, playing a crucial role in protein folding and dealing with damaged proteins. However, these proteins are largely produced as a consequence of stress situations reacting to a broad range of stressors including temperature, UV radiation, hypoxia, inflammation, infections, chemical pollutants, and salinity. In these situations, HSPs play a role in repair and protection as well as in the degradation of poorly enveloped proteins whose damage is not reversible (Pirkkala and Sistonen 2006; Varasteh et al. 2015). Thus, exposure to any of these factors induces HSP synthesis and increases cell protection (Di Giulio and Hinton 2008). In addition, Deane et al. (2002) noted that salinity stress by itself may determine whether the heat shock response of an organism is augmented or attenuated during exposure to other stressors. Indeed, under salinity stress, HSPs may be associated with other factors since a positive correlation between HSP70 and Na+,K+/ATPase gene expression was found in the gill of black-chinned tilapia (Sarotherodon melanotheron) exposed to salinity conditions (Tine et al. 2010). Tine et al. (2010) also observed that the highest HSP70 and Na+,K+/ATPase mRNA levels were present in the poorest CF situations at 21‰ salinity without vitamin C supplementation. This treatment also had the highest expression of HSP70 gene levels after 24 h.