scholarly journals Domain Mapping of Heat Shock Protein 70 Reveals That Glutamic Acid 446 and Arginine 447 Are Critical for Regulating Superoxide Dismutase 2 Function

2016 ◽  
Vol 292 (6) ◽  
pp. 2369-2378 ◽  
Author(s):  
Adeleye J. Afolayan ◽  
Maxwell Alexander ◽  
Rebecca L. Holme ◽  
Teresa Michalkiewicz ◽  
Ujala Rana ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Glutamic Acid ◽  
Heat Shock Protein 70 ◽  
Domain Mapping ◽  
Superoxide Dismutase 2

Oxidant stress increases heat shock protein 70 mRNA in isolated perfused rat heart

1994 ◽  
Vol 267 (6) ◽  
pp. H2213-H2219 ◽  
Author(s):  
R. C. Kukreja ◽  
M. C. Kontos ◽  
K. E. Loesser ◽  
S. K. Batra ◽  
Y. Z. Qian ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Rat Heart ◽  
Heat Shock Protein 70 ◽  
Coronary Flow ◽  
Oxidant Stress ◽  
Recovery Period ◽  
Hsp 70 ◽  
Developed Pressure

Ischemia/reperfusion (I/R) and preconditioning of the heart by coronary artery occlusions increase expression of heat shock protein 70 (HSP 70). Because free radicals are generated during I/R, we hypothesized that the oxidant stress might contribute to an increased expression of HSP 70. Isolated rat hearts were perfused with free radical-generating systems such as xanthine/xanthine oxidase (X/XO), irradiated rose bengal (RB) generating singlet oxygen, and H2O2 for 15 min followed by 30 min of recovery period. Significant decrease in developed pressure and coronary flow occurred after perfusion with X/XO, H2O2, and RB. During I/R, the developed pressure and coronary flow were 60 +/- 8 and 80 +/- 5%, respectively, of control, which improved significantly with superoxide dismutase. The expression of HSP 70 mRNA increased over 13-fold in hearts perfused with X/XO, 6- to 7-fold with RB, and over 5-fold with H2O2. With I/R, an over 10-fold increase in HSP 70 mRNA was observed, which decreased significantly in the presence of superoxide dismutase. These results demonstrate that oxidant stress directly increases HSP 70 mRNA in the rat heart. It is concluded that one of the potential mechanisms of expression of HSP 70 by I/R may be oxygen radicals.

Heat shock protein 70 and cellular disturbances in cochlear cisplatin ototoxicity model

2010 ◽  
Vol 124 (6) ◽  
pp. 599-609 ◽  
Author(s):  
J R García-Berrocal ◽  
J Nevado ◽  
J Á González-García ◽  
C Sánchez-Rodríguez ◽  
R Sanz ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Auditory Brainstem ◽  
State Response ◽  
Auditory Steady State Response ◽  
Brainstem Response ◽  
Response Thresholds ◽  
Total Superoxide Dismutase

AbstractBackground:Exposure to cisplatin leads to cochlear cell death by apoptosis; these changes are most marked on the seventh day after exposure. Heat shock proteins are induced in inner ear cells in response to a variety of stimuli. This study examined the role of heat shock protein 70 in cisplatin-induced cochlear cell death.Methods:Fifty-six Sprague–Dawley rats were involved. Some were injected with cisplatin (5 mg/kg body weight), some with cisplatin plus the caspase inhibitor Z-Asp(OMe)-Glu(OMe)-Val-Asp(OME)-fluoromethylketone (5 mg/kg body weight) and others were left as controls (being injected only with saline). Seven days later, we examined the expression of heat shock protein 70 and several other apoptosis-related proteins within the rat cochlear cells; we also assessed total superoxide dismutase activity, auditory brainstem response and auditory steady state response.Results:Seven days after cisplatin injection, significantly increased expression of heat shock protein 70 was found within the rat cochleae. This correlated with increased executioner caspase levels, total superoxide dismutase activity and auditory brainstem response thresholds, and a significant elevation in auditory steady state response thresholds. Inhibition of caspase-3 activity significantly reduced cochlear heat shock protein 70 expression and total superoxide dismutase activity, and improved auditory brainstem response and auditory steady state response thresholds.Conclusions:Seven days after cisplatin exposure, we found disturbances of the cochlear cellular machinery involving heat shock protein 70, other apoptotic proteins and total superoxide dismutase.

scholarly journals Characterization of Heat Shock Protein 60 as an Interacting Partner of Superoxide Dismutase 2 in the Silkworm, Bombyx mori, and Its Response to the Molting Hormone, 20-Hydroxyecdysone

Antioxidants ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 1385
Author(s):  
Yosui Nojima
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Bombyx Mori ◽  
Molecular Mechanisms ◽  
Heat Shock Protein 60 ◽  
Molting Hormone ◽  
Superoxide Dismutase 2 ◽  
Silkworm Bombyx Mori

Oxidative stress promotes pupation in some holometabolous insects. The levels of superoxide, a reactive oxygen species (ROS), are increased and superoxide dismutase 1 (BmSod1) and superoxide dismutase 2 (BmSod2) are decreased during metamorphic events in silkworm (Bombyx mori). These observations strongly suggest that pupation is initiated by oxidative stress via the down-regulation of BmSod1 and BmSod2. However, the molecular mechanisms underlying ROS production during metamorphic events in silkworm remain unknown. To investigate these molecular mechanisms, the peripheral proteins of BmSod1 and BmSod2 were identified and characterized using dry and wet approaches in this study. Based on the results, silkworm heat shock protein 60 (BmHsp60) was identified as an interacting partner of BmSod2, which belongs to the Fe/MnSOD family. Furthermore, the present study results showed that BmHsp60 mRNA expression levels were increased in response to oxidative stress caused by ultraviolet radiation and that BmHsp60 protein levels (but not mRNA levels) were decreased during metamorphic events, which are regulated by the molting hormone 20-hydroxyecdysone. These findings improve our understanding of the mechanisms by which holometabolous insects control ROS during metamorphosis.

Ammonia aggravates emotional stress-induced gastric mucosal oxidative injury through the cancellation of heat shock protein 70 (HSP70)

2001 ◽  
Vol 120 (5) ◽  
pp. A152-A152
Author(s):  
H SUZUKI ◽  
S NAGAHASHI ◽  
M MIYAZAWA ◽  
M MORI ◽  
H NAGATA ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Emotional Stress ◽  
Heat Shock Protein 70 ◽  
Oxidative Injury
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