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Two-Dimensional Nanomaterials for Drug Delivery in Regenerative Medicine
Published in Harishkumar Madhyastha, Durgesh Nandini Chauhan, Nanopharmaceuticals in Regenerative Medicine, 2022
Zahra Mohammadpour, Seyed Morteza Naghib
Black phosphorous (BP) nanosheets with unique optical properties and biodegradation into harmless compounds have garnered considerable interest in biomedicine. Hou et al. used BP nanosheets for the treatment of acute kidney injury (Hou et al. 2020). Through scavenging the reactive oxygen species (ROSs), BP nanosheets could alleviate the cellular apoptosis associated with oxidative stress. The authors stated that the flake-like morphology, antioxidative property, and minimal cytotoxicity make BP nanosheets intriguing candidates for the treatment of acute kidney injury and other ROS-related diseases. Another well-known property of BP nanosheets is their ability to convert NIR light into heat. This characteristic has been widely used in biomedicine (Mohammadpour and Majidzadeh-A 2020). In a study by Tong et al., highly efficient bone regeneration was induced on an osteoimplant (BPs@poly(lactic-co-glycolic acid) (PLGA)) (Tong et al. 2019). The mild heat generated by the photothermal conversion property of BP nanosheets led to in vitro and in vivo osteogenesis under remote control. The expression of cellular heat shock proteins played an important role. The photothermal conversion of BP nanosheets can also be used to on-demand light-controlled drug delivery for the regeneration of bone (Wang et al. 2018) and fighting bacterial infection (Guo et al. 2020).
Recent Progress in Cancer Thermal Therapy Using Gold Nanoparticles *
Published in Valerio Voliani, Nanomaterials and Neoplasms, 2021
Nardine S. Abadeer, Catherine J. Murphy
It is thought that tumor tissue is more hypoxic, is more acidic, and is nutrient-deficient compared to normal tissues [28]. These traits may render some cancer cells more sensitive to heat. However, the overexpression of heat shock proteins has also been observed in some cancers [29]. These proteins may then make cancer cells more resistant than expected to heat-based therapies, so the effects of thermal therapy are not universal in all types of cancer [30].
Human Responses to Endotoxin: Role of the Genetic Background
Published in Helmut Brade, Steven M. Opal, Stefanie N. Vogel, David C. Morrison, Endotoxin in Health and Disease, 2020
Heat-shock proteins represent a physiological response to cellular stress, which is highly conserved in evolution. Expression of heat-shock proteins as molecular chaperones facilitates intracellular folding of synthesized proteins (45). Inhibition of the heat-shock response exacerbates septic shock in animal models. On the other hand, induction of heat-shock proteins prior to lethal endotoxin challenges reduces the lethality of septic shock (45).
Acute exposure of glyphosate-based herbicide induced damages on common carp organs via heat shock proteins-related immune response and oxidative stress
Published in Toxin Reviews, 2021
Yuanyuan Li, Weikai Ding, Xiaoyu Li
Heat shock proteins (HSPs) are a family of highly conserved proteins including the small HSPs (sHSPs), the HSP70 superfamily, and HSP90 (Heikkila 2010). The HSP70 family is the most frequently studied HSPs, which are mainly encoded by two genes, a constitutive (HSC70) and stress-inducible (HSP70) genes (Xing et al.2013). These two HSP70s play crucial roles in synergetic immunity, antioxidant, molecular chaperone, and other biological functions (Basu 2002), and HSP90 also has many biological functions, such as protein folding, unfolding, degradation, aggregation, and remodeling of protein complexes, and cells defending against exogenous stresses (Sørensen et al.2003). Therefore, they are commonly used by environmental toxicologists as indicators or biomarkers for early warning of stress condition of exposure to various physical, chemical, and biological stressors, such as metals, pesticides, and pathogen infection (Lindquist and Craig 1988, Bhargav et al.2008, Jing et al.2013, Mrdaković et al.2016, Ma et al.2018a).
Hsp70 modulates immune response in pancreatic cancer through dendritic cells
Published in OncoImmunology, 2021
Bhuwan Giri, Prateek Sharma, Tejeshwar Jain, Anthony Ferrantella, Utpreksha Vaish, Siddharth Mehra, Bharti Garg, Srikanth Iyer, Vrishketan Sethi, Zoe Malchiodi, Rossana Signorelli, Harrys K.C Jacob, John George, Preeti Sahay, Ejas P. Bava, Rajinder Dawra, Sundaram Ramakrishnan, Ashok Saluja, Vikas Dudeja
Heat shock proteins are part of an evolutionarily conserved cellular machinery, which are geared toward protecting cells and tissues from various stresses, including thermal distress.11 Heat Shock Protein 70, or Hsp70, is a member of heat shock protein family, which is ubiquitously expressed in a variety of cell types.12 We have previously demonstrated that Hsp70 is overexpressed in pancreatic cancer cells and that it plays a prosurvival and antiapoptotic role in pancreatic cancer epithelial cells. However, the role of Hsp70 in the TME is unknown.13 In the current study, we have investigated the role of Hsp70 in TME in the progression of cancer. Our results suggest that selective genetic deletion of Hsp70 in the TME significantly attenuates tumor growth. Our results also suggest that this effect is due to the deletion of Hsp70 in immune cellsand not due to depletion of Hsp70 in CAFs. Using a combination of in vitro and in vivo approaches, we demonstrate that lack of Hsp70 in dendritic cells energizes the antigen presentation machinery, which, in turn, leads to the development of a robust anticancer immune response. These findings pave the way for a more complete understanding in modulating and designing effective therapeutic approaches that can complement immunotherapy and dendritic cell vaccination against pancreatic cancer.
Exosomes released by breast cancer cells under mild hyperthermic stress possess immunogenic potential and modulate polarization in vitro in macrophages
Published in International Journal of Hyperthermia, 2020
Kacoli Sen, Austin E. F. Sheppe, Ishita Singh, Winnie W. Hui, Mariola J. Edelmann, Carlos Rinaldi
Heat shock protein 70 (Hsp70) is a component of the intracellular heat shock protein family, which is expressed in both prokaryotes and eukaryotes [43]. The heat shock proteins maintain cellular homeostasis and promote cell survival in response to temperature-induced stress while also playing a significant role in immune reactions. Previous studies have suggested that hyperthermia treatment of tumor cells leads to the expression of Hsp70, which can elicit host antitumor immunity [44,45]. In our study, we found that exosomes secreted by breast cancer cells in stress-induced (heat shock at 43 °C at CEM TD50) conditions had increased Hsp70 content. Specifically, exosomal Hsp70 was significantly increased after exposure to heat stress for murine breast cancer cell lines [p = 0.0415, 0.0184 for EMT6 and 4T1, respectively] (Figure 6(a,b)). Since exosomal membranes are abundant in the endosome-specific tetraspanins (CD9 and CD63), these two proteins were also analyzed as exosomal markers (Figure 6(c,d)).