Heat shock response by EBV-immortalized B-lymphocytes from centenarians and control subjects: a model to study the relevance of stress response in longevity

2004 ◽  
Vol 39 (1) ◽  
pp. 83-90 ◽  
Author(s):  
Marina Marini ◽  
Rosa Lapalombella ◽  
Silvia Canaider ◽  
Antonio Farina ◽  
Daniela Monti ◽  
...  
Keyword(s):  
Stress Response ◽  
Heat Shock ◽  
B Lymphocytes ◽  
Heat Shock Response ◽  
Control Subjects ◽  
Shock Response ◽  
And Control

scholarly journals Molecular Basis of the Defective Heat Stress Response in Mycobacterium leprae

2007 ◽  
Vol 189 (24) ◽  
pp. 8818-8827 ◽  
Author(s):  
Diana L. Williams ◽  
Tana L. Pittman ◽  
Mike Deshotel ◽  
Sandra Oby-Robinson ◽  
Issar Smith ◽  
...  
Keyword(s):  
Heat Stress ◽  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Elevated Temperatures ◽  
Transcriptional Response ◽  
Mycobacterium Leprae ◽  
Heat Stress Response ◽  
Regulatory Circuits ◽  
Shock Response

ABSTRACT Mycobacterium leprae, a major human pathogen, grows poorly at 37°C. The basis for its inability to survive at elevated temperatures was investigated. We determined that M. leprae lacks a protective heat shock response as a result of the lack of transcriptional induction of the alternative sigma factor genes sigE and sigB and the major heat shock operons, HSP70 and HSP60, even though heat shock promoters and regulatory circuits for these genes appear to be intact. M. leprae sigE was found to be capable of complementing the defective heat shock response of mycobacterial sigE knockout mutants only in the presence of a functional mycobacterial sigH, which orchestrates the mycobacterial heat shock response. Since the sigH of M. leprae is a pseudogene, these data support the conclusion that a key aspect of the defective heat shock response in M. leprae is the absence of a functional sigH. In addition, 68% of the genes induced during heat shock in M. tuberculosis were shown to be either absent from the M. leprae genome or were present as pseudogenes. Among these is the hsp/acr2 gene, whose product is essential for M. tuberculosis survival during heat shock. Taken together, these results suggest that the reduced ability of M. leprae to survive at elevated temperatures results from the lack of a functional transcriptional response to heat shock and the absence of a full repertoire of heat stress response genes, including sigH.

Testing the hormetic nature of homeopathic interventions through stress response pathways

2010 ◽  
Vol 29 (7) ◽  
pp. 551-554 ◽  
Author(s):  
Suresh IS Rattan ◽  
Taru Deva
Keyword(s):  
Stress Response ◽  
Heat Shock ◽  
Dose Response ◽  
Heat Shock Response ◽  
Unfolded Protein ◽  
Shock Response ◽  
Protein Response ◽  
Homeopathic Remedies ◽  
Homeopathic Drugs ◽  
Biphasic Dose Response

The scientific foundations of hormesis are now well established and include various biochemical and molecular criteria for testing the hormetic nature of chemicals and other modulators. In order to claim homeopathy as being hormetic, it is essential that, in addition to the hormetic biphasic dose response, homeopathic remedies should fulfill one or more molecular criteria. Since stress response pathways, such as heat shock response, antioxidative response, autophagic response and unfolded protein response, are integral components of the physiological hormesis, it is important that homeopathic drugs be tested for these pathways if these are to be considered as hormetins and to cause hormesis.

scholarly journals Systemic activation coordinates the heat shock response of the insulin/IGF-1 pathway in Caenorhabditis elegans

2017 ◽  
Author(s):  
Ronen B Kopito ◽  
Kathie Watkins ◽  
Erel Levine
Keyword(s):  
Caenorhabditis Elegans ◽  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Cellular Response ◽  
Precise Control ◽  
Cellular Processes ◽  
Shock Response ◽  
Stressed Cells ◽  
Shock Proteins

Exposure to high temperatures has an adverse effect on cellular processes and results in activation of the cellular heat shock response (HSR), a highly conserved program of inducible genes to maintain protein homeostasis1. The insulin/IGF-1 signaling (IIS) pathway, which has diverse roles from metabolism to stress response and longevity, is activated as part of the HSR2–4. Recent evidence suggest that the IIS pathway is able to affect proteostasis non-autonomously5,6, yet it is not known if it is activated autonomously in stressed cells or systemically as part of an organismic program. In Caenorhabditis elegans, the single forkhead box O (FOXO) homologue DAF-16 functions as the major target of the IIS pathway7 and, together with the heat-shock factor HSF-1, induce the expression of small heat shock proteins in response to heat shock8–10,3. Here we use a novel microfluidic device that allows precise control of the spatiotemporal temperature profile to show that cellular activation of DAF-16 integrates local temperature sensation with systemic signals. We demonstrate that DAF-16 activation in head sensory neurons is essential for DAF-16 activation in other tissues, but show that no known thermosensory neuron is individually required. Our findings demonstrate that systemic and cell-autonomous aspects of stress response act together to facilitate a coordinated cellular response at the organismic level.

scholarly journals The Heat Shock Response in the Western Honey Bee (Apis mellifera) is Antiviral

Viruses ◽  
2020 ◽  
Vol 12 (2) ◽  
pp. 245 ◽  
Author(s):  
Alexander J. McMenamin ◽  
Katie F. Daughenbaugh ◽  
Michelle L. Flenniken
Keyword(s):  
Apis Mellifera ◽  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Honey Bee ◽  
Heat Shock Response ◽  
Honey Bees ◽  
Immune Gene ◽  
Protein Encoding ◽  
Shock Response

Honey bees (Apis mellifera) are an agriculturally important pollinator species that live in easily managed social groups (i.e., colonies). Unfortunately, annual losses of honey bee colonies in many parts of the world have reached unsustainable levels. Multiple abiotic and biotic stressors, including viruses, are associated with individual honey bee and colony mortality. Honey bees have evolved several antiviral defense mechanisms including conserved immune pathways (e.g., Toll, Imd, JAK/STAT) and dsRNA-triggered responses including RNA interference and a non-sequence specific dsRNA-mediated response. In addition, transcriptome analyses of virus-infected honey bees implicate an antiviral role of stress response pathways, including the heat shock response. Herein, we demonstrate that the heat shock response is antiviral in honey bees. Specifically, heat-shocked honey bees (i.e., 42 °C for 4 h) had reduced levels of the model virus, Sindbis-GFP, compared with bees maintained at a constant temperature. Virus-infection and/or heat shock resulted in differential expression of six heat shock protein encoding genes and three immune genes, many of which are positively correlated. The heat shock protein encoding and immune gene transcriptional responses observed in virus-infected bees were not completely recapitulated by administration of double stranded RNA (dsRNA), a virus-associated molecular pattern, indicating that additional virus–host interactions are involved in triggering antiviral stress response pathways.

scholarly journals Urocortin 3 overexpression reduces ER stress and heat shock response in 3T3-L1 adipocytes

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Sina Kavalakatt ◽  
Abdelkrim Khadir ◽  
Dhanya Madhu ◽  
Heikki A. Koistinen ◽  
Fahd Al-Mulla ◽  
...  
Keyword(s):  
Stress Response ◽  
Heat Shock ◽  
Er Stress ◽  
Glucose Uptake ◽  
Heat Shock Response ◽  
Cellular Stress Response ◽  
Mrna Levels ◽  
Obesity And Diabetes ◽  
Shock Response ◽  
Urocortin 3

AbstractThe neuropeptide urocortin 3 (UCN3) has a beneficial effect on metabolic disorders, such as obesity, diabetes, and cardiovascular disease. It has been reported that UCN3 regulates insulin secretion and is dysregulated with increasing severity of obesity and diabetes. However, its function in the adipose tissue is unclear. We investigated the overexpression of UCN3 in 3T3-L1 preadipocytes and differentiated adipocytes and its effects on heat shock response, ER stress, inflammatory markers, and glucose uptake in the presence of stress-inducing concentrations of palmitic acid (PA). UCN3 overexpression significantly downregulated heat shock proteins (HSP60, HSP72 and HSP90) and ER stress response markers (GRP78, PERK, ATF6, and IRE1α) and attenuated inflammation (TNFα) and apoptosis (CHOP). Moreover, enhanced glucose uptake was observed in both preadipocytes and mature adipocytes, which is associated with upregulated phosphorylation of AKT and ERK but reduced p-JNK. Moderate effects of UCN3 overexpression were also observed in the presence of 400 μM of PA, and macrophage conditioned medium dramatically decreased the UCN3 mRNA levels in differentiated 3T3-L1 cells. In conclusion, the beneficial effects of UCN3 in adipocytes are reflected, at least partially, by the improvement in cellular stress response and glucose uptake and attenuation of inflammation and apoptosis.

Inhibition of Interleukin-6 Signaling with CNTO328 Sensitizes Multiple Myeloma Cells to Bortezomib and Attenuates Proteasome Inhibitor-Mediated Induction of the Anti-Apoptotic Heat Shock Protein Response.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 1574-1574
Author(s):  
Peter M. Voorhees ◽  
Deborah J. Kuhn ◽  
George W. Small ◽  
John S. Strader ◽  
Robert Corringham ◽  
...  
Keyword(s):  
Multiple Myeloma ◽  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Response ◽  
Proteasome Inhibitor ◽  
Myeloma Cell ◽  
Significant Advance ◽  
Hsp 70 ◽  
Shock Response

Abstract The proteasome inhibitor bortezomib represents a significant advance in the treatment of multiple myeloma, but its efficacy is limited by a number of resistance mechanisms. One of the most important is the heat shock protein (HSP) and stress response pathways which, through members such as HSP-70 and mitogen-activated protein kinase (MAPK) phosphatase (MKP)-1, oppose the pro-apoptotic activities of bortezomib. Because interleukin (IL)-6 signaling augments the heat shock response through signal transducer and activator of transcription (STAT)-1 and heat shock transcription factor (HSF)-1, we hypothesized that downregulation of IL-6 signaling would attenuate HSP induction by bortezomib, thereby enhancing its anti-myeloma activity. Treatment of the IL-6-dependent multiple myeloma cell lines KAS-6 and ANBL-6 with the combination of bortezomib and CNTO328, a chimeric monoclonal IL-6 neutralizing antibody, resulted in greater reduction of cell viability than with either drug alone in a time- and concentration-dependent manner. This was associated with an enhanced induction of apoptosis which, under some conditions, was greater than the sum of the two individual agents alone, suggesting a synergistic interaction. Similar findings were not seen when using isotype control antibodies, and in studies of the IL-6-independent RPMI 8226 myeloma cell line. Increased activity was seen when cells were pre-treated with CNTO328 followed by bortezomib, or when they were treated with both agents concurrently, compared to treatment with bortezomib followed by CNTO328. Treatment with CNTO328 potently inhibited IL-6-mediated downstream signaling pathways, as demonstrated by marked blockade of STAT-3 and p44/42 MAPK phosphorylation. Enhanced activity of the combination regimen correlated with attenuated induction by bortezomib of the heat shock and stress response proteins HSP-70 and MKP-1 by up to 45% and 90%, respectively. Notably, CNTO328 markedly reduced levels of transcriptionally active phospho-STAT-1 and hyperphosphorylated HSF-1. Other strategies to suppress the heat shock response, including the use of the pharmacologic inhibitor KNK437, also yielded evidence for a synergistic anti-myeloma effect in combination with bortezomib. The synergistic activity of KNK437 and bortezomib was reproduced in normal mouse embryo fibroblasts (MEFs), but blunted in HSF-1 knockout MEFs. Taken together, the above data demonstrate that inhibition of IL-6 signaling enhances the anti-myeloma activity of bortezomib. They also support the hypothesis that this occurs, at least in part, by attenuating proteasome inhibitor-mediated induction of the heat shock response through downregulation of transcriptionally active STAT-1 and HSF-1. These findings provide a strong rationale for future translation of the CNTO328/bortezomib combination into the clinic.

Induction of human endothelial cell apoptosis requires both heat shock and oxidative stress responses

1997 ◽  
Vol 272 (5) ◽  
pp. C1543-C1551 ◽  
Author(s):  
J. H. Wang ◽  
H. P. Redmond ◽  
R. W. Watson ◽  
D. Bouchier-Hayes
Keyword(s):  
Oxidative Stress ◽  
Endothelial Cell ◽  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Sodium Arsenite ◽  
Oxidative Stress Response ◽  
Tnf Alpha ◽  
Shock Response ◽  
Hsp72 Expression

Endothelial cell (EC) death may play an important role in the development of increased vascular permeability and capillary leak syndrome during systemic inflammatory response syndrome. However, the mode of EC death and the mechanisms involved remain unclear. In this study we employed the proinflammatory mediators lipopolysaccharide (LPS) and tumor necrosis factor-alpha (TNF-alpha), the chemical reagent sodium arsenite, and heat shock to trigger the stress gene responses. Human ECs were used as surrogates of the microvasculature to test the hypothesis that the induction of the heat shock response and the oxidative stress response might combine to induce apoptosis rather than necrosis in human ECs. Sodium arsenite at 80-320 microM, which induced heat shock protein 72 (HSP72) expression and reactive oxygen intermediate (ROI) generation in ECs, resulted in EC apoptosis. TNF-alpha alone (5-75 ng/ml) increased EC ROI generation but did not induce EC apoptosis. Heat shock alone (42 degrees C, 45 min) or sodium arsenite (40 microM) alone, each of which induced HSP72 expression, did not result in EC apoptosis. However, the combination of TNF-alpha with heat shock or 40 microM sodium arsenite led to EC apoptosis as HSP72 expression and ROI were induced. Furthermore, sodium arsenite (80 microM) in the presence of antioxidants failed to induce EC apoptosis. Apoptotic ECs also exhibited functional disturbances as represented by the depression of intercellular adhesion molecule-1 expression as well as the disruption of EC monolayer integrity. These results indicate that the simultaneous induction of a heat shock response and an oxidative stress response is responsible for human EC apoptosis.

Effect of Heat Shock on the Thermotolerance and Protein Composition of Yersinia enterocolitica in Brain Heart Infusion Broth and Ground Pork

1996 ◽  
Vol 59 (4) ◽  
pp. 360-364 ◽  
Author(s):  
KALPANA SHENOY ◽  
ELSA A. MURANO
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Yersinia Enterocolitica ◽  
Heat Shock Response ◽  
Control Cell ◽  
Brain Heart Infusion ◽  
Ground Pork ◽  
Shock Response ◽  
Shock Proteins ◽  
And Control

The optimum conditions required to induce a heat-shock response in Yersinia enterocolitica in brain heart infusion (BHI) broth were determined. The production of heat-shock proteins and the increased thermotolerance of heat-shocked Yersinia cells in ground pork when exposed to higher temperatures was also examined. Heat shocking Y. enterocolitica cells at 45°C for 60 min consistently resulted in an increased number of survivors to a subsequent treatment of 55 or 60°C in BHI broth when compared with non-heat-shocked controls. D values at 55°C were calculated as 7.7 and 2.0 min and at 60°C as 1.6 and 1.2 min for heat-shocked and control cells, respectively. After examination of heat-shocked cells by sodium dodecyl sulfate-polyacrilamide gel electrophoresis (SDS-PAGE), two distinct heat-shock proteins with molecular masses of 70.5 and 58.0 kDa were observed that were not present in the control. Evaluation of heat-shocked and control cell survival in ground pork revealed D55 values of 15.6 and 6.5 min and D60 values of 6.7 and 1.7 min, respectively. The results indicate that prior heat shock can induce increased resistance in Y. enterocolitica in ground pork to higher heat treatments. Survival of Yersinia enterocolitica in cooked meat due to the phenomenon of the heat-shock response can become a cause of concern regarding microbiological food safety.

scholarly journals Heat shock response and autophagy—cooperation and control

Autophagy ◽  
2015 ◽  
Vol 11 (2) ◽  
pp. 200-213 ◽  
Author(s):  
Karol Dokladny ◽  
Orrin B Myers ◽  
Pope L Moseley
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Shock Response ◽  
And Control
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