The aim of this study was to identify whether more and less adapted Angus and Simmental cattle differed in physiological responses and expression of the heat shock factor 1 (HSF1) and the heat shock 70 kDa protein 6 (HSPA6), when subjected to heat stress. Thirty bulls (n = 15 ANG; n = 15 SIM), extremes "more adapted" and "less adapted" within each breed were selected to the heat tolerance test. They were selected according to an index based on the average of the respiratory rate obtained on two hot summer days from one hundred bulls. Before the heat tolerance test day, animals were taken to a paddock with water, grass and shade until 7 a.m. of the following day for morning measurements. They were kept in the barn without access to water and shade until 1 p.m. for the afternoon measurements. Respiratory rate in the morning (MRR) and afternoon (ARR), hair coat surface temperature in the morning (MST) and afternoon (AST), rectal temperature in the morning (MRT) and afternoon (ART) were measured and blood samples were collected for expression analysis of the HSF1 and HSPA6 genes. The MIXED procedure of SAS was used for all statistical analysis. The more adapted Simmental group had lesser values of MRR (P = 0.023) and MRT (P = 0.095), but there was no difference within Angus breed. The ARR was greater (P = 0.004) in less adapted animals for both breeds. The ART was lower in the Simmental breed (P < 0.001). Less adapted had greater levels of mRNA of HSF1 (P = 0.06) and HSPA6 (P = 0.09). In conclusion, respiratory rate, rectal temperature and expression of the HSF1 and HSPA6 genes can be indicators of thermotolerance in taurine cattle. Both breeds show physiologically similar responses under heat stress conditions.
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http://dx.doi.org/10.1016/j.jtherbio.2019.06.002 | DOI Listing |
Cell Mol Life Sci
September 2024
Department of Biology, University of Rome Tor Vergata, Rome, Italy.
Organisms respond to proteotoxic-stress by activating the heat-shock response, a cellular defense mechanism regulated by a family of heat-shock factors (HSFs); among six human HSFs, HSF1 acts as a proteostasis guardian regulating severe stress-driven transcriptional responses. Herein we show that human coronaviruses (HCoV), both low-pathogenic seasonal-HCoVs and highly-pathogenic SARS-CoV-2 variants, are potent inducers of HSF1, promoting HSF1 serine-326 phosphorylation and triggering a powerful and distinct HSF1-driven transcriptional-translational response in infected cells. Despite the coronavirus-mediated shut-down of the host translational machinery, selected HSF1-target gene products, including HSP70, HSPA6 and AIRAP, are highly expressed in HCoV-infected cells.
View Article and Find Full Text PDFCells
June 2021
Center for Translational Research and Molecular Biology of Cancer, Maria Sklodowska-Curie National Research Institute of Oncology Gliwice Branch, 44-102 Gliwice, Poland.
Manumycin A (MA) is a well-tolerated natural antibiotic showing pleiotropic anticancer effects in various preclinical in vitro and in vivo models. Anticancer drugs may themselves act as stressors to induce the cellular adaptive mechanism that can minimize their cytotoxicity. Heat shock proteins (HSPs) as cytoprotective factors can counteract the deleterious effects of various stressful stimuli.
View Article and Find Full Text PDFHeredity (Edinb)
March 2021
Department of Evolution, Ecology, and Behavior, University of Illinois, Urbana-Champaign, IL, 61801, USA.
Confined within the cold-stable Southern Ocean, Antarctic notothenioid fishes have undergone an evolutionary loss of the inducible heat shock response (HSR), while facing perpetual low-temperature challenges to cellular proteostasis. This study examines how evolution in chronic cold has affected the shared cellular apparatus that mediates proteostasis under normal and heat stressed states. To deduce Antarctic-specific changes, we compared native expression levels across the full suite of chaperome genes and assessed the structural integrity of two crucial HSR regulators - Heat Shock Factor 1 (HSF1) that activates HSR, and heat shock elements (HSEs), the binding sites for HSF1 - between Antarctic fishes and the basal temperate notothenioid Eleginops maclovinus.
View Article and Find Full Text PDFJ Therm Biol
August 2019
Universidade Federal de Lavras, Department of Animal Science, University Campus, Postal Code 3037, Downtown, Zip code 37200-000, Lavras, MG, Brazil. Electronic address:
The aim of this study was to identify whether more and less adapted Angus and Simmental cattle differed in physiological responses and expression of the heat shock factor 1 (HSF1) and the heat shock 70 kDa protein 6 (HSPA6), when subjected to heat stress. Thirty bulls (n = 15 ANG; n = 15 SIM), extremes "more adapted" and "less adapted" within each breed were selected to the heat tolerance test. They were selected according to an index based on the average of the respiratory rate obtained on two hot summer days from one hundred bulls.
View Article and Find Full Text PDFFree Radic Biol Med
March 2017
Faculty of Medicine, University of Tsukuba, Tsukuba, Ibaraki 305-8575, Japan; Doctoral Program in Biomedical Sciences, Graduate School of Comprehensive Human Sciences, University of Tsukuba, Tsukuba, Ibaraki 305-8575, Japan; Leading Graduate School Doctoral Program, Ph.D. Program in Human Biology, University of Tsukuba, Tsukuba, Ibaraki 305-8575, Japan. Electronic address:
The current consensus is that environmental electrophiles activate redox signal transduction pathways through covalent modification of sensor proteins with reactive thiol groups at low concentrations, while they cause cell damage at higher concentrations. We previously exposed human carcinoma A431 cells to the atmospheric electrophile 1,4-naphthoquinone (1,4-NQ) and found that heat shock protein 90 (HSP90), a negative regulator of heat shock factor 1 (HSF1), was a target of 1,4-NQ. In the study presented here, we determined whether 1,4-NQ activates HSF1.
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