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 The long noncoding RNA NEAT1 and nuclear paraspeckles are up-regulated by the transcription factor HSF1 in the heat shock response

2018 ◽  
Vol 293 (49) ◽  
pp. 18965-18976 ◽  
Author(s):  
S. Mohammad Lellahi ◽  
Ingrid Arctander Rosenlund ◽  
Annica Hedberg ◽  
Liv Torill Kiær ◽  
Ingvild Mikkola ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Long Noncoding Rna ◽  
Noncoding Rna ◽  
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.

Heat Shock Response, Heat Shock Transcription Factor and Cell Aging

Neurosignals ◽  
1996 ◽  
Vol 5 (3) ◽  
pp. 180-191 ◽  
Author(s):  
Yoon-Kwang Lee ◽  
Dominador Manalo ◽  
Alice Y.-C. Liu
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Heat Shock Transcription Factor ◽  
Cell Aging ◽  
Shock Response

HSF Transcription Factor Family, Heat Shock Response, and Protein Intrinsic Disorder

2012 ◽  
Vol 13 (1) ◽  
pp. 86-103 ◽  
Author(s):  
Sandy D. Westerheide ◽  
Rachel Raynes ◽  
Chase Powell ◽  
Bin Xue ◽  
Vladimir N. Uversky
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Intrinsic Disorder ◽  
Transcription Factor Family ◽  
Shock Response ◽  
Protein Intrinsic Disorder

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 New inhibitor targeting human transcription factor HSF1: effects on the heat shock response and tumor cell survival

2017 ◽  
Vol 45 (10) ◽  
pp. 5797-5817 ◽  
Author(s):  
Nuria Vilaboa ◽  
Alba Boré ◽  
Francisco Martin-Saavedra ◽  
Melanie Bayford ◽  
Natalie Winfield ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Tumor Cell ◽  
Cell Survival ◽  
Heat Shock Response ◽  
Shock Response ◽  
Tumor Cell Survival ◽  
Human Transcription Factor

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.

scholarly journals Sis1 delivers the State of the Union

2020 ◽  
Vol 220 (1) ◽  
Author(s):  
Danish Khan ◽  
Onn Brandman
Keyword(s):  
Gene Expression ◽  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Response ◽  
The State ◽  
Gene Expression Program ◽  
State Of The Union ◽  
Shock Response ◽  
Expression Program

The heat shock response (HSR) is a gene expression program that protects cells from heat and proteotoxic stressors. In this issue, Feder et al. (2020. J. Cell Biol.https://doi.org/10.1083/jcb.202005165) show that subcellular relocalization of the cochaperone Sis1 drives the HSR by de-suppressing the transcription factor Hsf1.

Sign in / Sign up

Export Citation Format

Share Document