MITOCHONDRIAL HEAT SHOCK PROTEIN MORTALIN AS POTENTIAL TARGET FOR THERAPIES BASED ON OXIDATIVE STRESS

2021 ◽  
pp. 102256
Author(s):  
Ana Carolina Pagliarone ◽  
Edwin David Castañeda ◽  
Jhonne Pedro Pedott Santana ◽  
Caio Almeida Batista de Oliveira ◽  
Thaiane Alcarde Robeldo ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Potential Target ◽  
Mitochondrial Heat Shock Protein

Mortalin and DJ-1 coordinately regulate hematopoietic stem cell function through the control of oxidative stress

Blood ◽  
2014 ◽  
Vol 123 (1) ◽  
pp. 41-50 ◽  
Author(s):  
Ikue Tai-Nagara ◽  
Sahoko Matsuoka ◽  
Hiroyoshi Ariga ◽  
Toshio Suda
Keyword(s):  
Oxidative Stress ◽  
Stem Cell ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Hematopoietic Stem Cell ◽  
Cell Function ◽  
Hematopoietic Stem ◽  
Key Points ◽  
Mitochondrial Heat Shock Protein

Key Points Mitochondrial heat shock protein, mortalin, is essential for the maintenance of HSCs via the control of oxidative stress. Mortalin directly interact with DJ-1 to regulate ROS levels in the mitochondria of HSCs.

Heat Shock Protein HSP70 in Oxidative Stress in Apnea Patients

2020 ◽  
Vol 169 (5) ◽  
pp. 695-697
Author(s):  
I. M. Madaeva ◽  
N. A. Kurashova ◽  
N. V. Semenova ◽  
E. B. Ukhinov ◽  
S. I. Kolesnikov ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein Hsp70

scholarly journals Recombinant heat shock protein 27 (HSP27/HSPB1) protects against cadmium-induced oxidative stress and toxicity in human cervical cancer cells

2017 ◽  
Vol 22 (3) ◽  
pp. 357-369 ◽  
Author(s):  
Daiana G. Alvarez-Olmedo ◽  
Veronica S. Biaggio ◽  
Geremy A. Koumbadinga ◽  
Nidia N. Gómez ◽  
Chunhua Shi ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cervical Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Heat Shock Protein 27 ◽  
Cervical Cancer Cells ◽  
Human Cervical Cancer Cells ◽  
Human Cervical Cancer

Effects of ferulic acid on oxidative stress, heat shock protein 70, connexin 43, and monoamines in the hippocampus of pentylenetetrazole-kindled rats

2017 ◽  
Vol 95 (6) ◽  
pp. 732-742 ◽  
Author(s):  
Abdelaziz M. Hussein ◽  
Khaled M. Abbas ◽  
Osama A. Abulseoud ◽  
El-Hussainy M.A. El-Hussainy
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Ferulic Acid ◽  
Group Treatment ◽  
Heat Shock Protein 70 ◽  
Connexin 43 ◽  
Hsp70 Expression ◽  
Neuroprotective Effects ◽  
Cx43 Expression

The present study investigated the effects of ferulic acid (FA) on pentylenetetrazole (PTZ)-induced seizures, oxidative stress markers (malondialdehyde (MDA), catalase, and reduced glutathione (GSH)), connexin (Cx) 43, heat shock protein 70 (Hsp 70), and monoamines (serotonin (5-HT) and norepinephrine (NE)) levels in a rat model of PTZ-induced kindling. Sixty Sprague Dawley rats were divided into 5 equal groups: (a) normal group; (b) FA group: normal rats received FA at a dose of 40 mg/kg daily; (c) PTZ group: normal rats received PTZ at a dose of 50 mg/kg i.p. on alternate days for 15 days; (d) FA-before group: treatment was the same as for the PTZ group, except rats received FA; and (e) FA-after group: rats received FA from sixth dose of PTZ. PTZ caused a significant increase in MDA, Cx43, and Hsp70 along with a significant decrease in GSH, 5-HT, and NE levels and CAT activity in the hippocampus (p < 0.05). Pre- and post-treatment with FA caused significant improvement in behavioral parameters, MDA, CAT, GSH, 5-HT, NE, Cx43 expression, and Hsp70 expression in the hippocampal region (p < 0.05). We conclude that FA has neuroprotective effects in PTZ-induced epilepsy, which might be due to attenuation of oxidative stress and Cx43 expression and upregulation of neuroprotective Hsp70 and neurotransmitters (5-HT and NE).

scholarly journals The chloroplast small heat shock protein undergoes oxidation-dependent conformational changes and may protect plants from oxidative stress

1999 ◽  
Vol 4 (2) ◽  
pp. 129 ◽  
Author(s):  
Ulrika Härndahl ◽  
Roberta Buffoni Hall ◽  
Katherine W. Osteryoung ◽  
Elizabeth Vierling ◽  
Janet F. Bornman ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Conformational Changes ◽  
Small Heat Shock Protein

scholarly journals Exercise protects against doxorubicin-induced oxidative stress and proteolysis in skeletal muscle

2011 ◽  
Vol 110 (4) ◽  
pp. 935-942 ◽  
Author(s):  
Ashley J. Smuder ◽  
Andreas N. Kavazis ◽  
Kisuk Min ◽  
Scott K. Powers
Keyword(s):  
Oxidative Stress ◽  
Skeletal Muscle ◽  
Antioxidant Enzymes ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Oxidative Damage ◽  
Muscle Fibers ◽  
Muscular Exercise ◽  
Protease Activation ◽  
Exercise Induced

Doxorubicin (Dox) is a potent antitumor agent used in cancer treatment. Unfortunately, Dox is myotoxic and results in significant reductions in skeletal muscle mass and function. Complete knowledge of the mechanism(s) by which Dox induces toxicity in skeletal muscle is incomplete, but it is established that Dox-induced toxicity is associated with increased generation of reactive oxygen species and oxidative damage within muscle fibers. Since muscular exercise promotes the expression of numerous cytoprotective proteins (e.g., antioxidant enzymes, heat shock protein 72), we hypothesized that muscular exercise will attenuate Dox-induced damage in exercise-trained muscle fibers. To test this postulate, Sprague-Dawley rats were randomly assigned to the following groups: sedentary, exercise, sedentary with Dox, or exercise with Dox. Our results show increased oxidative stress and activation of cellular proteases (calpain and caspase-3) in skeletal muscle of animals treated with Dox. Importantly, our findings reveal that exercise can prevent the Dox-induced oxidative damage and protease activation in the trained muscle. This exercise-induced protection against Dox-induced toxicity may be due, at least in part, to an exercise-induced increase in muscle levels of antioxidant enzymes and heat shock protein 72. Together, these novel results demonstrate that muscular exercise is a useful countermeasure that can protect skeletal muscle against Dox treatment-induced oxidative stress and protease activation in skeletal muscles.

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