Nitric oxide-heat shock protein axis in menopausal hot flushes: neglected metabolic issues of chronic inflammatory diseases associated with deranged heat 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.

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KPNA3-knockdown eliminates the second heat shock protein peak associated with the heat shock response of male silkworm pupae ( Bombyx mori ) by reducing heat shock factor transport into the nucleus

Gene ◽

10.1016/j.gene.2015.09.018 ◽

2016 ◽

Vol 575 (2) ◽

pp. 452-457

Author(s):

Jun Li ◽

Guoqing Wei ◽

Lei Wang ◽

Cen Qian ◽

Kedong Li ◽

...

Keyword(s):

Heat Shock ◽

Heat Shock Protein ◽

Bombyx Mori ◽

Heat Shock Response ◽

Heat Shock Factor ◽

Protein Peak ◽

Silkworm Pupae ◽

Shock Response

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Thermal acclimation alters both basal heat shock protein gene expression and the heat shock response in juvenile lake whitefish (Coregonus clupeaformis)

Journal of Thermal Biology ◽

10.1016/j.jtherbio.2021.103185 ◽

2022 ◽

pp. 103185

Author(s):

Lori A. Manzon ◽

Megan A. Zak ◽

Matthew Agee ◽

Douglas R. Boreham ◽

Joanna Y. Wilson ◽

...

Keyword(s):

Gene Expression ◽

Heat Shock ◽

Heat Shock Protein ◽

Heat Shock Response ◽

Protein Gene ◽

Thermal Acclimation ◽

Coregonus Clupeaformis ◽

Lake Whitefish ◽

Heat Shock Protein Gene ◽

Shock Response

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The heat shock response in hydra: immunological relationship of hsp60, the major heat shock protein of Hydra vulgaris, to the ubiquitous hsp70 family

Coelenterate Biology: Recent Research on Cnidaria and Ctenophora ◽

10.1007/978-94-011-3240-4_72 ◽

1991 ◽

pp. 513-517 ◽

Cited By ~ 1

Author(s):

Thomas C. G. Bosch ◽

Gabriele Praetzel

Keyword(s):

Heat Shock ◽

Heat Shock Protein ◽

Heat Shock Response ◽

Hydra Vulgaris ◽

Hsp70 Family ◽

Shock Response ◽

Immunological Relationship ◽

Relationship Of

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

International Journal of Molecular Sciences ◽

10.3390/ijms21062063 ◽

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.

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

Functional Plant Biology ◽

10.1071/fp18259 ◽

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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