scholarly journals Heat shock response in archaea

2018 ◽  
Vol 2 (4) ◽  
pp. 581-593 ◽  
Author(s):  
Liesbeth Lemmens ◽  
Rani Baes ◽  
Eveline Peeters
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Molecular Mechanisms ◽  
Structural Response ◽  
Large Temperature ◽  
Cell Factories ◽  
Shock Response ◽  
Molecular Aspects ◽  
Shock Proteins ◽  
Response To Temperature

An adequate response to a sudden temperature rise is crucial for cellular fitness and survival. While heat shock response (HSR) is well described in bacteria and eukaryotes, much less information is available for archaea, of which many characterized species are extremophiles thriving in habitats typified by large temperature gradients. Here, we describe known molecular aspects of archaeal heat shock proteins (HSPs) as key components of the protein homeostasis machinery and place this in a phylogenetic perspective with respect to bacterial and eukaryotic HSPs. Particular emphasis is placed on structure–function details of the archaeal thermosome, which is a major element of the HSR and of which subunit composition is altered in response to temperature changes. In contrast with the structural response, it is largely unclear how archaeal cells sense temperature fluctuations and which molecular mechanisms underlie the corresponding regulation. We frame this gap in knowledge by discussing emerging questions related to archaeal HSR and by proposing methodologies to address them. Additionally, as has been shown in bacteria and eukaryotes, HSR is expected to be relevant for the control of physiology and growth in various stress conditions beyond temperature stress. A better understanding of this essential cellular process in archaea will not only provide insights into the evolution of HSR and of its sensing and regulation, but also inspire the development of biotechnological applications, by enabling transfer of archaeal heat shock components to other biological systems and for the engineering of archaea as robust cell factories.

Urea sensitizes mIMCD3 cells to heat shock-induced apoptosis: protection by NaCl

2001 ◽  
Vol 280 (3) ◽  
pp. C614-C620 ◽  
Author(s):  
Chantal Colmont ◽  
Stéphanie Michelet ◽  
Dominique Guivarc'h ◽  
Germain Rousselet
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Heat Sensitivity ◽  
Osmotic Gradient ◽  
Water Reabsorption ◽  
Apoptotic Pathway ◽  
Shock Response ◽  
Induced Apoptosis ◽  
Shock Proteins ◽  
Dose Dependent

Urea, with NaCl, constitutes the osmotic gradient that allows water reabsorption in mammalian kidneys. Because NaCl induces heat shock proteins, we tested the responses to heat shock of mIMCD3 cells adapted to permissive urea and/or NaCl concentrations. We found that heat-induced cell death was stronger after adaptation to 250 mM urea. This effect was reversible, dose dependent, and, interestingly, blunted by 125 mM NaCl. Moreover, we have shown that urea-adapted cells engaged in an apoptotic pathway upon heat shock, as shown by DNA laddering. This sensitization is not linked to a defect in the heat shock response, because the induction of HSP70 was similar in isotonic and urea-adapted cells. Moreover, it is not linked to the presence of urea inside cells, because washing urea away did not restore heat resistance and because applying urea and heat shock at the same time did not lead to heat sensitivity. Together, these results suggest that urea modifies the heat shock response, leading to facilitated apoptosis.

scholarly journals Se Alleviated Oxidative Stress-Mediated Complex Poisoning Mechanism in Pb-Treated Chicken Kidneys: Inflammation, Heat Shock Response, and Autophagy

2021 ◽  
Author(s):  
Zhiying Miao ◽  
Weikang Yu ◽  
Yueyang Wang ◽  
Xianhong Gu ◽  
Xiaohua Teng
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Protein Expression ◽  
Heat Shock Response ◽  
Potable Water ◽  
Histological Structure ◽  
Standard Diet ◽  
Shock Response ◽  
Mrna And Protein Expression ◽  
Shock Proteins

Abstract Background: Lead (Pb) is a toxic environmental pollutant and can exerts toxicity in kidneys. It is known that selenium (Se) has an antagonistic effect on Pb poisoning. However, biological events during the process were not well understood in chicken kidneys.Methods: One hundred and eighty male Hyline chickens (7-day-old) were randomly divided into the control group (offering standard diet and potable water), the Se group (offering Na2SeO3-added standard diet and potable water), the Pb group (offering standard diet and (CH3OO)2Pb-added potable water), and the Pb+Se group (offering Na2SeO3-added standard diet and (CH3OO)2Pb-added potable water). On 30th, 60th, and 90th days, kidneys were removed to perform the studies of histological structure, oxidative stress indicators, cytokines, heat shock proteins, and autophagy in the chicken kidneys.Results: The experimental results indicated that Pb poisoning changed renal histological structure; decreased catalase, glutathione-s-transferase, and total antioxidative capacity activities; increased hydrogen peroxide content; induced mRNA and protein expression of heat shock proteins; inhibited interleukin (IL)-2 mRNA expression, and induced IL-4 and IL-12β mRNA expression; inhibited mammalian target of rapamycin mRNA and protein expression, and induced autophagy-related gene mRNA and protein expression in the chicken kidneys. Supplement of Se mitigated the above changes caused by Pb.Conclusion: Our research strengthens the evidence that Pb induced oxidative stress, inflammation, heat shock response, and autophagy and Se administration alleviated Pb poisoning through mitigating oxidative stress in the chicken kidneys.

scholarly journals Activation of the heat shock response in a primary cellular model of motoneuron neurodegeneration-evidence for neuroprotective and neurotoxic effects

2009 ◽  
Vol 14 (2) ◽  
Author(s):  
Bernadett Kalmar ◽  
Linda Greensmith
Keyword(s):  
Cell Death ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Apoptotic Cell ◽  
Experimental Conditions ◽  
Pharmacological Agents ◽  
Shock Response ◽  
Induced Apoptosis ◽  
Shock Proteins ◽  
The Relationship

AbstractPharmacological up-regulation of heat shock proteins (hsps) rescues motoneurons from cell death in a mouse model of amyotrophic lateral sclerosis. However, the relationship between increased hsp expression and neuronal survival is not straightforward. Here we examined the effects of two pharmacological agents that induce the heat shock response via activation of HSF-1, on stressed primary motoneurons in culture. Although both arimoclomol and celastrol induced the expression of Hsp70, their effects on primary motoneurons in culture were significantly different. Whereas arimoclomol had survival-promoting effects, rescuing motoneurons from staurosporin and H2O2 induced apoptosis, celastrol not only failed to protect stressed motoneurons from apoptosis under same experimental conditions, but was neurotoxic and induced neuronal death. Immunostaining of celastrol-treated cultures for hsp70 and activated caspase-3 revealed that celastrol treatment activates both the heat shock response and the apoptotic cell death cascade. These results indicate that not all agents that activate the heat shock response will necessarily be neuroprotective.

scholarly journals Disruption of the three cytoskeletal networks in mammalian cells does not affect transcription, translation, or protein translocation changes induced by heat shock.

1985 ◽  
Vol 5 (7) ◽  
pp. 1571-1581 ◽  
Author(s):  
W J Welch ◽  
J R Feramisco
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Mammalian Cells ◽  
Stress Proteins ◽  
Protein Translocation ◽  
Shock Response ◽  
Cytochalasin E ◽  
Cytoskeletal Networks ◽  
Shock Proteins ◽  
Cytoskeletal Elements

Mammalian cells show a complex series of transcriptional and translational switching events in response to heat shock treatment which ultimately lead to the production and accumulation of a small number of proteins, the so-called heat shock (or stress) proteins. We investigated the heat shock response in both qualitative and quantitative ways in cells that were pretreated with drugs that specifically disrupt one or more of the three major cytoskeletal networks. (These drugs alone, cytochalasin E and colcemid, do not result in induction of the heat shock response.) Our results indicated that disruption of the actin microfilaments, the vimentin-containing intermediate filaments, or the microtubules in living cells does not hinder the ability of the cell to undergo an apparently normal heat shock response. Even when all three networks were simultaneously disrupted (resulting in a loose, baglike appearance of the cells), the cells still underwent a complete heat shock response as assayed by the appearance of the heat shock proteins. In addition, the major induced 72-kilodalton heat shock protein was efficiently translocated from the cytoplasm into its proper location in the nucleus and nucleolus irrespective of the condition of the three cytoskeletal elements.

The heat-shock response of developing barley aleurone layers

2003 ◽  
Vol 13 (3) ◽  
pp. 229-238 ◽  
Author(s):  
Melissa A. Harju ◽  
Sunita deSouza ◽  
Mark R. Brodl
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Developmental Stages ◽  
Lipid Transfer Protein ◽  
Secretory Proteins ◽  
Lipid Transfer ◽  
Developmentally Regulated ◽  
Shock Response ◽  
Barley Grains ◽  
Shock Proteins

AbstractAleurone layers of mature germinating barley (Hordeum vulgare, cv. Himalaya) grains respond to heat shock by synthesizing heat-shock proteins (HSPs) and by selectively suppressing the synthesis of proteins normally translated by endoplasmic reticulum (ER)-bound ribosomes. To determine if this also was the case during seed development, we investigated the synthesis of proteins translated by ER-bound ribosomes in heat-shocked aleurone layers isolated from developing barley grains. The optimal induction temperature for the heat shock response in developing aleurone layers was 37.5°C, and temperatures above 42°C inhibited translation. HSPs with apparent molecular masses of 71.1, 66.2, 57.8, 19.1 and 18.8 kDa were induced. Other studies have shown that, in gibberellic acid (GA)-induced aleurone layers from mature barley grains, these temperatures were 40°C and 45°C, respectively. Furthermore, in developing aleurone layers, mRNAs encoding proteins translated by ER-bound ribosomes (mRNAs for a lipid transfer protein and a putative amylase/protease inhibitor) remained stable during heat shock. The ER membranes themselves remained in stacks, but the lumen became distended with electron-dense material. Heat shock prevented the movement of proteins from the ER into the rest of the endomembrane pathway. In contrast, other studies show that in mature, GA-induced aleurone layers, heat shock dissociates ER stacks and blocks translation, but the processing of secretory proteins in the endomembrane pathway is not inhibited. The observation that the same tissue at different developmental stages may respond differently to heat shock indicates that components of the heat-shock response are developmentally regulated. This system provides an opportunity to better understand the nuances of the heat-shock response, especially the post-transcriptional gene regulatory mechanisms that occur.

scholarly journals Genetic differences in the duration of the lymphocyte heat shock response in mice.

Genetics ◽  
1990 ◽  
Vol 124 (4) ◽  
pp. 949-955
Author(s):  
V K Mohl ◽  
G D Bennett ◽  
R H Finnell
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Mouse Strains ◽  
Adult Mice ◽  
Shock Response ◽  
Increased Sensitivity ◽  
Shock Proteins ◽  
The Relationship

Abstract Lymphocytes from adult mice bearing a known difference in genetic susceptibility to teratogen-induced exencephaly (SWV/SD, and DBA/2J) were evaluated for changes in protein synthesis following an in vivo heat treatment. Particular attention was paid to changes indicative of the heat shock response, a highly conserved response to environmental insult consisting of induction of a few, highly conserved proteins with simultaneous decreases in normal protein synthesis. The duration of heat shock protein induction in lymphocytes was found to be increased by 1 hr in the teratogen-sensitive SWV/SD strain as compared to the resistant DBA/2J strain. Densitometric analysis revealed a significant decrease in the relative synthesis of at least two non-heat shock proteins (36 kD and 45 kD) in the SWV/SD lymphocytes as compared to DBA/2J cells. The increased sensitivity of protein synthesis to hyperthermia in the SWV/SD lymphocytes were lost in the F1 progeny of reciprocal crosses between SWV/SD and DBA/2J mouse strains. Sensitivity to hyperthermia-induced exencephaly is recessive to resistance in these crosses. The relationship between altered protein synthesis and teratogen susceptibility is discussed.

scholarly journals Characterizing Gene Copy Number of Heat Shock Protein Gene Families in the Emerald Rockcod, Trematomus bernacchii

Genes ◽  
2020 ◽  
Vol 11 (8) ◽  
pp. 867
Author(s):  
Anthony D. Tercero ◽  
Sean P. Place
Keyword(s):  
Heat Shock ◽  
Gene Duplication ◽  
Heat Shock Proteins ◽  
Heat Shock Response ◽  
Copy Number ◽  
Gene Families ◽  
Gene Copy ◽  
Shock Response ◽  
Trematomus Bernacchii ◽  
Shock Proteins

The suborder Notothenioidae is comprised of Antarctic fishes, several of which have lost their ability to rapidly upregulate heat shock proteins in response to thermal stress, instead adopting a pattern of expression resembling constitutive genes. Given the cold-denaturing effect that sub-zero waters have on proteins, evolution in the Southern Ocean has likely selected for increased expression of molecular chaperones. These selective pressures may have also enabled retention of gene duplicates, bolstering quantitative output of cytosolic heat shock proteins (HSPs). Given that newly duplicated genes are under more relaxed selection, it is plausible that gene duplication enabled altered regulation of such highly conserved genes. To test for evidence of gene duplication, copy number of various isoforms within major heat shock gene families were characterized via qPCR and compared between the Antarctic notothen, Trematomus bernacchii, which lost the inducible heat shock response, and the non-Antarctic notothen, Notothenia angustata, which maintains an inducible heat shock response. The results indicate duplication of isoforms within the hsp70 and hsp40 super families have occurred in the genome of T. bernacchii. The findings suggest gene duplications may have been critical in maintaining protein folding efficiency in the sub-zero waters and provided an evolutionary mechanism of alternative regulation of these conserved gene families.

Physical Activity, Muscle, and the HSP70 Response

1998 ◽  
Vol 23 (3) ◽  
pp. 245-260 ◽  
Author(s):  
J. Lon Kilgore ◽  
Timothy I. Musch ◽  
Christopher R. Ross
Keyword(s):  
Physical Activity ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Heat Shock Response ◽  
Shock Response ◽  
Potential Applications ◽  
Shock Proteins ◽  
External Stimuli ◽  
Exercise And Training

Selye (1936) described how organisms react to various external stimuli (i.e., stressors). These reactions generally follow a programmed series of events and help the organism adapt to the imposed stress. The heat shock response is a common cellular reaction to external stressors, including physical activity. A characteristic set of proteins is synthesised shortly after the organism is exposed to stress. Researchers have not determined how heat shock proteins affect the exercise response. However, their role in adaptation to exercise and training might he inferred, since the synthetic patterns correlate well with the stress adaptation syndrome that Selye described. This review addresses the 70 kilodalton heat shock protein family (HSP70), the most strongly induced heat shock proteins. This paper provides an overview of the general heat shock response and a brief review of literature on HSP70 function, structure, regulation, and potential applications. Potential applications in health, exercise, and medicine are provided. Key words: heat shock, protein, exercise

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