Vaginal Immunology
William J. Ledger, Steven S. Witkin in Vulvovaginal Infections, 2017
Heat shock proteins, or stress proteins, comprise several protein families that are essential to life and are present in every known organism from bacteria to plants to man. When a cell finds itself under nonphysiological stressed conditions, such as elevated temperature (heat shock) or invasion by microorganisms, the biosynthesis of heat shock proteins is greatly upregulated. The release of heat shock proteins from infected cells serves as an initial warning to the immune system that cells are in danger and that immune cells should migrate and concentrate in the region of heat shock protein release.9 Several members of the heat shock protein family bind to specific receptors on the surface of phagocytic cells. This results in the release of cytokines and chemokines from these cells and the initiation of acquired immune system activation. The complement system is also activated by cell-free heat shock protein. The deposition of activated complement components on the surface of bacterial cells results in cell lysis or phagocytosis by cells possessing complement receptors. Cell-free heat shock proteins have been identified in the vaginal lumen of women with a history of recurrent vulvovaginal candidiasis.
The Stress Response and Stress Proteins
John J. Lemasters, Constance Oliver in Cell Biology of Trauma, 2020
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.
Two-Dimensional Nanomaterials for Drug Delivery in Regenerative Medicine
Harishkumar Madhyastha, Durgesh Nandini Chauhan in Nanopharmaceuticals in Regenerative Medicine, 2022
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).
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.
Nanoparticles as a potential teratogen: a lesson learnt from fruit fly
Published in Nanotoxicology, 2019
Bedanta Kumar Barik, Monalisa Mishra
NPs affect some of the proteins which are expressed under adverse conditions. Thus, expression of those proteins or related genes is checked as an outcome of NP toxicity. The activity of antioxidant enzymes such as SOD, catalase, glutathione assay is also used as a marker for detection of ROS production (Ahamed, Posgai et al. 2010). Lipid peroxidation assay with the help of malondialdehyde (MDA) marker depicts the extent of oxidative damage to cells (Carmona, Inostroza-Blancheteau et al. 2015). Further, upregulated heat shock protein activity mainly hsp70 is used as a marker. Overexpressed apoptotic protein levels such as p53, p38, caspase-3, caspase-9 are assessed to confirm apoptotic activity in NP-treated Drosophila (Ahamed, Posgai et al. 2010). Alteration in total amount of protein is also checked as a parameter to detect NP-induced stress.
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).
Related Knowledge Centers
- Bacteria
- Chaperonin
- Downregulation & Upregulation
- Hsp70
- Protein
- Stress
- Cell
- Chaperone
- Transcription
- Downregulation & Upregulation
- Heat Shock Factor