Climate change has intensified the occurrence of heat waves, resulting in organisms being exposed to thermal and chemical stress at the same time. The effects of mild heat shock combined with sublethal concentrations of phenanthrene (PHE) on defense mechanisms in springtails Folsomia candida were investigated. The transcription of Heat Shock Protein 70 (HSP70) was significantly upregulated by heat shock but tended to reach the control levels after 42 h of recovery. The transcription of cytochrome P450 3A13 (CYP3A13) was upregulated 3-13 fold by PHE but suppressed by heat shock. The suppression by heat shock might contribute to the reduced detoxification of PHE during high-temperature exposure. In line with this, we found that the internal PHE concentration was approximately 70% higher in heat-shocked springtails than in animals kept at control temperature. In general, the transcription of genes encoding enzymes of detoxification phase Ⅱ (glutathione S-transferase 3) and phase Ⅲ (ABC transporter 1) and the activity of antioxidant defense enzymes (superoxide dismutase and catalase) were less influenced than genes encoding phase I detoxification mechanisms (CYP3A13). These results indicate that heat shock delays the detoxification of PHE in springtails.
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http://dx.doi.org/10.1016/j.chemosphere.2022.137119 | DOI Listing |
Biol Chem
January 2025
Cell Biology Center, Institute of Integrated Research, Institute of Science Tokyo (Formerly Tokyo Institute of Technology), S2-19, Nagatsuta 4259, Midori-ku, Yokohama, 226-8501, Japan.
The heat stress response is an essential defense mechanism in all organisms. Heat shock proteins (Hsps) are produced in response to thermal stress, with their expression levels regulated by heat shock transcription factors. In the key transcription factor σ positively regulates Hsp expression.
View Article and Find Full Text PDFFASEB J
January 2025
Department of Biochemistry and Molecular Biology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Molecular chaperones play critical roles in post-translational maintenance in protein homeostasis. Previous studies have shown that loss of Smyd1b function results in defective myofibril organization and dramatic upregulation of heat shock protein gene (hsp) expression in muscle cells of zebrafish embryos. To investigate the molecular mechanisms and functional importance of this stress response, we characterized changes of gene expression in smyd1b knockdown and knockout embryos using RNA-seq.
View Article and Find Full Text PDFiScience
November 2024
Department of Drug Discovery and Development, Harrison College of Pharmacy, Auburn University, 720 S. Donahue Dr., Auburn, AL, USA.
Bruton's tyrosine kinase (BTK) inhibitor, ibrutinib, has been shown to synergize with proteasome inhibitors (PIs) in reducing the viability of cells derived from B cell malignancies, but the mechanism is not known. We report here that an off-target effect of ibrutinib causes synergy because not all BTK inhibitors exhibited the synergistic effect, and those that synergized did so even in cells that do not express BTK. The allosteric BTK inhibitor CGI-1746 showed the strongest synergy.
View Article and Find Full Text PDFComp Biochem Physiol A Mol Integr Physiol
January 2025
Beijing Normal University, Beijing 100875, China; State Key Laboratory of Environmental Criteria and Risk Assessment, Chinese Research Academy of Environmental Science, Beijing 100012, China.
The prevalence of heatwave and hypoxia events and their devastating impacts on aquatic ecosystems and fishery resources reinforces the priority of research to address the resilience and adaption mechanisms to these two stressors in important fish species. However, our understanding of the development of cross-tolerance of these two stressors in fish still limited. Here, we investigated the impacts of prior heatwave exposure on hypoxia tolerance and the underlying mechanisms in silver carp (Hypophthalmichthys molitrix), a species of considerable ecological and commercial importance.
View Article and Find Full Text PDFDrug Discov Today
January 2025
Key Laboratory of Study and Discovery of Small Targeted Molecules of Hunan Province, School of Pharmaceutical Sciences, Hunan Normal University, Changsha 410013, Hunan, China. Electronic address:
The heat shock protein (HSP) 110 family has a key role as a unique class of molecular chaperones maintaining cellular proteostasis in eukaryotes. Abnormal activation of Hsp110 has been implicated in several diseases. Given its important role in pathogenesis, Hsp110 has become a novel drug target for disease diagnosis and targeted therapy.
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