Modulation of inflammation in vivo through induction of the heat shock response, effects on NF-κB activation

2002 ◽  
Vol 51 (2) ◽  
pp. 108-109 ◽  
Author(s):  
T. Lawrence
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Shock Response

scholarly journals Induction of Heat Shock Protein 70 in Mouse RPE as an In Vivo Model of Transpupillary Thermal Stimulation

2020 ◽  
Vol 21 (6) ◽  
pp. 2063
Author(s):  
Mooud Amirkavei ◽  
Marja Pitkänen ◽  
Ossi Kaikkonen ◽  
Kai Kaarniranta ◽  
Helder André ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Response ◽  
Pigment Epithelium ◽  
Retinal Pigment ◽  
In Vivo Model ◽  
Tunel Staining ◽  
Long Duration ◽  
Shock Response

The induction of heat shock response in the macula has been proposed as a useful therapeutic strategy for retinal neurodegenerative diseases by promoting proteostasis and enhancing protective chaperone mechanisms. We applied transpupillary 1064 nm long-duration laser heating to the mouse (C57Bl/6J) fundus to examine the heat shock response in vivo. The intensity and spatial distribution of heat shock protein (HSP) 70 expression along with the concomitant probability for damage were measured 24 h after laser irradiation in the mouse retinal pigment epithelium (RPE) as a function of laser power. Our results show that the range of heating powers for producing heat shock response while avoiding damage in the mouse RPE is narrow. At powers of 64 and 70 mW, HSP70 immunostaining indicates 90 and 100% probability for clearly elevated HSP expression while the corresponding probability for damage is 20 and 33%, respectively. Tunel staining identified the apoptotic regions, and the estimated 50% damaging threshold probability for the heating (ED50) was ~72 mW. The staining with Bestrophin1 (BEST1) demonstrated RPE cell atrophy with the most intense powers. Consequently, fundus heating with a long-duration laser provides an approachable method to develop heat shock-based therapies for the RPE of retinal disease model mice.

In vivo heat-shock response in the brain: signalling pathway and transcription factor activation

2003 ◽  
Vol 119 (1) ◽  
pp. 90-99 ◽  
Author(s):  
Paola Maroni ◽  
Paola Bendinelli ◽  
Laura Tiberio ◽  
Francesca Rovetta ◽  
Roberta Piccoletti ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Signalling Pathway ◽  
Transcription Factor Activation ◽  
Shock Response ◽  
The Brain

scholarly journals HSF1-dependent and -independent regulation of the mammalian in vivo heat shock response and its impairment in Huntington's disease mouse models

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Andreas Neueder ◽  
Theresa A. Gipson ◽  
Sophie Batterton ◽  
Hayley J. Lazell ◽  
Pamela P. Farshim ◽  
...  
Keyword(s):  
Heat Shock ◽  
Huntington's Disease ◽  
Huntington’S Disease ◽  
Mouse Models ◽  
Heat Shock Response ◽  
Shock Response

scholarly journals Heat-shock protein expression is absent in the antarctic fish Trematomus bernacchii (family Nototheniidae)

2000 ◽  
Vol 203 (15) ◽  
pp. 2331-2339 ◽  
Author(s):  
G.E. Hofmann ◽  
B.A. Buckley ◽  
S. Airaksinen ◽  
J.E. Keen ◽  
G.N. Somero
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Response ◽  
Solid Phase ◽  
Antarctic Fish ◽  
Shock Response ◽  
Enhanced Expression ◽  
Trematomus Bernacchii

The heat-shock response, the enhanced expression of one or more classes of molecular chaperones termed heat-shock proteins (hsps) in response to stress induced by high temperatures, is commonly viewed as a ‘universal’ characteristic of organisms. We examined the occurrence of the heat-shock response in a highly cold-adapted, stenothermal Antarctic teleost fish, Trematomus bernacchii, to determine whether this response has persisted in a lineage that has encountered very low and stable temperatures for at least the past 14–25 million years. The patterns of protein synthesis observed in in vivo metabolic labelling experiments that involved injection of (35)S-labelled methionine and cysteine into whole fish previously subjected to a heat stress of 10 degrees C yielded no evidence for synthesis of any size class of heat-shock protein. Parallel in vivo labelling experiments with isolated hepatocytes similarly showed significant amounts of protein synthesis, but no indication of enhanced expression of any class of hsp. The heavy metal cadmium, which is known to induce synthesis of hsps, also failed to alter the pattern of proteins synthesized in hepatocytes. Although stress-induced chaperones could not be detected under any of the experimental condition used, solid-phase antibody (western) analysis revealed that a constitutively expressed 70 kDa chaperone was present in this species, as predicted on the basis of requirements for chaperoning during protein synthesis. Amounts of the constitutively expressed 70 kDa chaperone increased in brain, but not in gill, during 22 days of acclimation to 5 degrees C. The apparent absence of a heat-shock response in this highly stenothermal species is interpreted as an indication that a physiological capacity observed in almost all other organisms has been lost as a result of the absence of positive selection during evolution at stable sub-zero temperatures. Whether the loss of the heat-shock response is due to dysfunctional genes for inducible hsps (loss of open reading frames or functional regulatory regions), unstable messenger RNAs, the absence of a functional heat-shock factor or some other lesion remains to be determined.

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.

Surgical stress and the heat shock response: In vivo models of stress conditioning

1998 ◽  
Vol 5 ◽  
pp. 34
Author(s):  
G.A. Perdrizet ◽  
J.C. Garcia ◽  
C.J. Lena ◽  
D.S. Shapiro ◽  
M.J. Rewinski
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Surgical Stress ◽  
In Vivo Models ◽  
Shock Response ◽  
Stress Conditioning

scholarly journals The heat shock response, determined by QuantiGene multiplex, is impaired in HD mouse models and not caused by HSF1 reduction

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Casandra Gomez-Paredes ◽  
Michael A. Mason ◽  
Bridget A. Taxy ◽  
Aikaterini S. Papadopoulou ◽  
Paolo Paganetti ◽  
...  
Keyword(s):  
Heat Shock ◽  
Mouse Models ◽  
Heat Shock Response ◽  
Inclusion Bodies ◽  
Neurodegenerative Disorder ◽  
Comprehensive Analysis ◽  
Mouse Tissue ◽  
Brain Hemispheres ◽  
Shock Response

AbstractHuntington’s disease (HD) is a devastating neurodegenerative disorder, caused by a CAG/polyglutamine repeat expansion, that results in the aggregation of the huntingtin protein, culminating in the deposition of inclusion bodies in HD patient brains. We have previously shown that the heat shock response becomes impaired with disease progression in mouse models of HD. The disruption of this inducible arm of the proteostasis network is likely to exacerbate the pathogenesis of this protein-folding disease. To allow a rapid and more comprehensive analysis of the heat shock response, we have developed, and validated, a 16-plex QuantiGene assay that allows the expression of Hsf1 and nine heat shock genes, to be measured directly, and simultaneously, from mouse tissue. We used this QuantiGene assay to show that, following pharmacological activation in vivo, the heat shock response impairment in tibialis anterior, brain hemispheres and striatum was comparable between zQ175 and R6/2 mice. In contrast, although a heat shock impairment could be detected in R6/2 cortex, this was not apparent in the cortex from zQ175 mice. Whilst the mechanism underlying this impairment remains unknown, our data indicated that it is not caused by a reduction in HSF1 levels, as had been reported.

scholarly journals Caloric restriction induces heat shock response and inhibits B16F10 cell tumorigenesis both in vitro and in vivo

Aging ◽  
2015 ◽  
Vol 7 (4) ◽  
pp. 233-240 ◽  
Author(s):  
Marta G. Novelle ◽  
Ashley Davis ◽  
Nathan L. Price ◽  
Ahmed Ali ◽  
Stefanie Fürer-Galvan ◽  
...  
Keyword(s):  
Heat Shock ◽  
Caloric Restriction ◽  
Heat Shock Response ◽  
B16f10 Cell ◽  
Shock Response

Surgical Stress and the Heat Shock Response: In Vivo Models of Stress Conditioning

1999 ◽  
Vol 874 (1 HEART IN STRE) ◽  
pp. 320-325 ◽  
Author(s):  
G. A. PERDRIZET ◽  
D. S. SHAPIRO ◽  
M. J. REWINSKI
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Surgical Stress ◽  
In Vivo Models ◽  
Shock Response ◽  
Stress Conditioning

scholarly journals The Heat Shock Response ofMycobacterium tuberculosis: Linking Gene Expression, Immunology and Pathogenesis

2002 ◽  
Vol 3 (4) ◽  
pp. 348-351 ◽  
Author(s):  
Graham R. Stewart ◽  
Lorenz Wernisch ◽  
Richard Stabler ◽  
Joseph A. Mangan ◽  
Jason Hinds ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Drug Targets ◽  
Expression Patterns ◽  
Transcriptional Regulators ◽  
Deletion Mutants ◽  
Immune Recognition ◽  
Physiological Conditions ◽  
Shock Response

The regulation of heat shock protein (HSP) expression is critically important to pathogens such asMycobacterium tuberculosisand dysregulation of the heat shock response results in increased immune recognition of the bacterium and reduced survival during chronic infection. In this study we use a whole genome spotted microarray to characterize the heat shock response ofM. tuberculosis. We also begin a dissection of this important stress response by generating deletion mutants that lack specific transcriptional regulators and examining their transcriptional profiles under different stresses. Understanding the stimuli and mechanisms that govern heat shock in mycobacteria will allow us to relate observedin vivoexpression patterns of HSPs to particular stresses and physiological conditions. The mechanisms controlling HSP expression also make attractive drug targets as part of a strategy designed to enhance immune recognition of the bacterium.

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