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

scholarly journals Histamine Is an Inducer of the Heat Shock Response in SOD1-G93A Models of ALS

2019 ◽  
Vol 20 (15) ◽  
pp. 3793 ◽  
Author(s):  
Savina Apolloni ◽  
Francesca Caputi ◽  
Annabella Pignataro ◽  
Susanna Amadio ◽  
Paola Fabbrizio ◽  
...  
Keyword(s):  
Heat Shock ◽  
Motor Neuron ◽  
Motor Neurons ◽  
Heat Shock Response ◽  
Type I ◽  
Spine Density ◽  
Shock Response ◽  
Anti Inflammatory

(1) Background: Amyotrophic lateral sclerosis (ALS) is a multifactorial non-cell autonomous disease where activation of microglia and astrocytes largely contributes to motor neurons death. Heat shock proteins have been demonstrated to promote neuronal survival and exert a strong anti-inflammatory action in glia. Having previously shown that the pharmacological increase of the histamine content in the central nervous system (CNS) of SOD1-G93A mice decreases neuroinflammation, reduces motor neuron death, and increases mice life span, here we examined whether this effect could be mediated by an enhancement of the heat shock response. (2) Methods: Heat shock protein expression was analyzed in vitro and in vivo. Histamine was provided to primary microglia and NSC-34 motor neurons expressing the SOD1-G93A mutation. The brain permeable histamine precursor histidine was chronically administered to symptomatic SOD1-G93A mice. Spine density was measured by Golgi-staining in motor cortex of histidine-treated SOD1-G93A mice. (3) Results: We demonstrate that histamine activates the heat shock response in cultured SOD1-G93A microglia and motor neurons. In SOD1-G93A mice, histidine augments the protein content of GRP78 and Hsp70 in spinal cord and cortex, where the treatment also rescues type I motor neuron dendritic spine loss. (4) Conclusion: Besides the established histaminergic neuroprotective and anti-inflammatory effects, the induction of the heat shock response in the SOD1-G93A model by histamine confirms the importance of this pathway in the search for successful therapeutic solutions to treat ALS.

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

p38β-regulated induction of the heat shock response by carbon monoxide releasing molecule CORM-2 mediates cytoprotection in lung cells in vitro

2011 ◽  
Vol 670 (1) ◽  
pp. 58-66 ◽  
Author(s):  
Nils Schallner ◽  
Sven Schwemmers ◽  
Christian I. Schwer ◽  
Christian Froehlich ◽  
Patrick Stoll ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Lung Cells ◽  
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
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