scholarly journals Response of Heat Shock Protein 72 to Repeated Bouts of Hyperthermia in Rat Skeletal Muscle

2015 ◽  
pp. 935-938
Author(s):  
J. LEE ◽  
K. HIMORI ◽  
D. TATEBAYASHI ◽  
M. ABE ◽  
T. YAMADA
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Response ◽  
Extensor Digitorum Longus ◽  
Differential Regulation ◽  
Rat Skeletal Muscle ◽  
Single Bout ◽  
Shock Response ◽  
Muscle Types

We investigated the effects of repeated hyperthermic bouts on the heat shock response of heat shock protein (HSP) 72 in skeletal muscle. Rats were assigned to control and hyperthermia groups which were exposed to heated water at 42 °C. The hyperthermia group was further divided into sub-groups: a single bout (H30) or four bouts of hyperthermia for 30 min (H30x4). There was an increase in HSP72 protein content of the H30 groups in both extensor digitorum longus (EDL) and soleus muscles. Moreover, HSP72 protein expression in H30x4 group was significantly higher than in H30 group in both EDL and soleus muscles. The HSP72 mRNA was markedly increased from control levels in the H30 and H30x4 group in both types of muscles. However, HSP72 mRNA of the H30x4 group was lower than that of the H30 group in soleus muscles. Heat shock response of HSP72 is activated even after repeated bouts of hyperthermia, with a differential regulation between muscle types.

C-terminal heat shock protein 90 modulators produce desirable oncogenic properties

2015 ◽  
Vol 13 (16) ◽  
pp. 4627-4631 ◽  
Author(s):  
Y. Wang ◽  
S. R. McAlpine
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Response ◽  
Heat Shock Protein 90 ◽  
Cellular Protection ◽  
Protection Mechanism ◽  
C Terminus ◽  
N Terminus ◽  
Shock Response

The cellular protection mechanism, the heat shock response, is only activated by classical heat shock 90 inhibitors (Hsp90) that “target” the N-terminus of the protein, but not by those that modulate the C-terminus.

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.

Induction of the heat shock response in Arabidopsis by heat shock protein 70 inhibitor VER-155008

2019 ◽  
Vol 46 (10) ◽  
pp. 925
Author(s):  
Erina Matsuoka ◽  
Naoki Kato ◽  
Masakazu Hara
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Response ◽  
Wheat Germ ◽  
Heat Shock Protein 90 ◽  
Hsp90 Inhibitor ◽  
Wheat Germ Extract ◽  
Chlorophyll Contents ◽  
Shock Response ◽  
Human Hsp70

The heat shock protein 90 (HSP90) inhibitor, geldanamycin, is a chemical inducer of the heat shock response (HSR) in Arabidopsis. Geldanamycin is thought to activate the heat shock signal by dissociating the HSP90-heat shock factor (HSF) complex. Recent studies have indicated that plant HSP70 is also associated with HSF, suggesting that inhibition of HSP70 may induce the HSR. However, no studies have been conducted to test this hypothesis. Here, we found that a specific HSP70 inhibitor VER-155008 activated the promoter of a small HSP gene (At1 g53540, HSP17.6C-CI) of Arabidopsis, which was shown to be activated by geldanamycin and other HSP90 inhibitors. The production of HSP17.6C-CI, HSP70 and HSP90.1 proteins in Arabidopsis was enhanced by the addition of VER-155008. The reduction of chlorophyll contents by heat shock was ameliorated by VER-155008. Chaperone analyses indicated that VER-155008 inhibited the chaperone activities of wheat germ extract and human HSP70/HSP40, respectively. These results suggest that the inhibition of HSP70 by VER-155008 enhanced the heat tolerance of Arabidopsis by inducing the HSR in the plant.

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