Effect of Apnea-Induced Hypoxia on Cardiovascular Adaptation and Circulating Biomarkers of Oxidative Stress in Elite Breath-Hold Divers

Given the previous evidence that breath-hold diving is a cause of physiological stress, this study aimed to determine whether a combination static and dynamic apnea would affect total oxidant status, nitric oxide, heat shock proteins and cardiovascular parameters in elite freedivers. Thirteen finalists of the World and European championships in swimming pool breath-hold diving participated in the study. Whole-body plethysmography and electrocardiography was performed to determine the cardiorespiratory variables at baseline and during the simulation static apnea. An assessment of the heart rate, blood oxygen saturation and biochemical variables was performed before and in response to a combination of a static followed by a dynamic apnea. Static and dynamic breath-holding had a significant effect on oxidative stress, as evidenced by an increase in the total oxidant status/capacity (p < 0.001). The post apnea concentrations of heat shock proteins 27 (HSP27) were significantly elevated (p < 0.03, but total antioxidant status (TAS), HSP90, HSP70, and nitric oxide (NO) changes were not significant. levels under the influence of the static and dynamic breath-hold protocol. A significant positive correlation between HSPs and TAS (r = 0.63; p < 0.05) as well as NO levels was associated with beneficial cardiovascular adaptation. An increase in serum HSP27 levels mediated in nitric oxide levels could explain its important role in improving cardiovascular functions in elite freedivers. Further studies are necessary to explain the exact mechanisms of breath holds training of cardiovascular adaptation responsible for maintaining adequate oxygen supply in elite divers.

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HEAT SHOCK PROTEINS, FREE RADICALS, AND OXIDATIVE STRESS: INTEGRATING BASIC SCIENCE WITH EXERCISE STRESS

Medicine & Science in Sports & Exercise ◽

10.1097/00005768-199805001-01279 ◽

1998 ◽

Vol 30 (Supplement) ◽

pp. 225

Author(s):

P. L. Moseley ◽

K. C. Kregel ◽

G. R. Buettner ◽

P. M. Clarkson

Keyword(s):

Oxidative Stress ◽

Free Radicals ◽

Heat Shock ◽

Heat Shock Proteins ◽

Basic Science ◽

Exercise Stress ◽

Shock Proteins ◽

And Oxidative Stress

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Oxidative metabolism and heat shock-enhanced chemiluminescence in Dictyostelium discoideum

Journal of Cell Science ◽

10.1242/jcs.99.4.741 ◽

1991 ◽

Vol 99 (4) ◽

pp. 741-750

Author(s):

P. R. FISHER ◽

P. KARAMPETSOS ◽

Z. WILCZYNSKA ◽

L. T. ROSENBERG

Keyword(s):

Oxidative Stress ◽

Lipid Peroxidation ◽

Electron Transport ◽

Heat Shock ◽

Heat Shock Proteins ◽

Dictyostelium Discoideum ◽

Oxidative Metabolism ◽

Enhanced Chemiluminescence ◽

Shock Proteins ◽

Oxygen Metabolites

During early differentiation starving Dictyostelium discoideum amoebae produce a burst of light that is enhanced by heat shock at the beginning of development. We report here pharmacological, genetic and spectral evidence that the chemiluminescence results from lipid peroxidation reactions following oxygen reduction by leakage of electrons from ubiquinone in mitochondrial electron transport, and perhaps by peroxisomal oxidation of urate. Our results are consistent with the view that heat shock causes oxidative stress, which in turn induces heat shock proteins and production of reduced oxygen metabolites.

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Impact of Exercise and Metabolic Disorders on Heat Shock Proteins and Vascular Inflammation

Autoimmune Diseases ◽

10.1155/2012/836519 ◽

2012 ◽

Vol 2012 ◽

pp. 1-13 ◽

Cited By ~ 9

Author(s):

Earl G. Noble ◽

Garry X. Shen

Keyword(s):

Oxidative Stress ◽

Heat Shock ◽

Heat Shock Proteins ◽

Inflammatory Mediators ◽

Metabolic Disorders ◽

Cell Injury ◽

Vascular Inflammation ◽

Atherosclerotic Cardiovascular Disease ◽

Heat Shock Factor 1 ◽

Shock Proteins

Heat shock proteins (Hsp) play critical roles in the body’s self-defense under a variety of stresses, including heat shock, oxidative stress, radiation, and wounds, through the regulation of folding and functions of relevant cellular proteins. Exercise increases the levels of Hsp through elevated temperature, hormones, calcium fluxes, reactive oxygen species (ROS), or mechanical deformation of tissues. Isotonic contractions and endurance- type activities tend to increase Hsp60 and Hsp70. Eccentric muscle contractions lead to phosphorylation and translocation of Hsp25/27. Exercise-induced transient increases of Hsp inhibit the generation of inflammatory mediators and vascular inflammation. Metabolic disorders (hyperglycemia and dyslipidemia) are associated with type 1 diabetes (an autoimmune disease), type 2 diabetes (the common type of diabetes usually associated with obesity), and atherosclerotic cardiovascular disease. Metabolic disorders activate HSF/Hsp pathway, which was associated with oxidative stress, increased generation of inflammatory mediators, vascular inflammation, and cell injury. Knock down of heat shock factor-1 (HSF1) reduced the activation of key inflammatory mediators in vascular cells. Accumulating lines of evidence suggest that the activation of HSF/Hsp induced by exercise or metabolic disorders may play a dual role in inflammation. The benefits of exercise on inflammation and metabolism depend on the type, intensity, and duration of physical activity.

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Copper and arsenic-induced oxidative stress and immune imbalance are associated with activation of heat shock proteins in chicken intestines

International Immunopharmacology ◽

10.1016/j.intimp.2018.04.038 ◽

2018 ◽

Vol 60 ◽

pp. 64-75 ◽

Cited By ~ 46

Author(s):

Yu Wang ◽

Hongjing Zhao ◽

Juanjuan Liu ◽

Yizhi Shao ◽

Jinglun Li ◽

...

Keyword(s):

Oxidative Stress ◽

Heat Shock ◽

Heat Shock Proteins ◽

Immune Imbalance ◽

Shock Proteins

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The Major Heat Shock Proteins, Hsp70 and Hsp90, in 2-Methoxyestradiol-Mediated Osteosarcoma Cell Death Model

International Journal of Molecular Sciences ◽

10.3390/ijms21020616 ◽

2020 ◽

Vol 21 (2) ◽

pp. 616

Author(s):

Magdalena Gorska-Ponikowska ◽

Alicja Kuban-Jankowska ◽

Antonella Marino Gammazza ◽

Agnieszka Daca ◽

Justyna M. Wierzbicka ◽

...

Keyword(s):

Nitric Oxide ◽

Heat Shock ◽

Nitric Oxide Synthase ◽

Heat Shock Proteins ◽

Nuclear Translocation ◽

Neuronal Nitric Oxide Synthase ◽

Osteosarcoma Cell ◽

Anticancer Efficacy ◽

Shock Proteins ◽

Oxide Synthase

2-Methoxyestradiol is one of the natural 17β-estradiol derivatives and a potential novel anticancer agent currently being under evaluation in advanced phases of clinical trials. However, the mechanism of anticancer action of 2-methoxyestradiol has not been yet fully established. In our previous studies we have demonstrated that 2-methoxyestradiol selectively induces the expression and nuclear translocation of neuronal nitric oxide synthase in osteosarcoma 143B cells. Heat shock proteins (Hsps) are factors involved in the regulation of expression and activity of nitric oxide synthases. Herein, we chose osteosarcoma cell lines differed in metastatic potential, metastatic 143B and highly metastatic MG63.2 cells, in order to further investigate the anticancer mechanism of 2-methoxyestradiol. The current study aimed to determine the role of major heat shock proteins, Hsp90 and Hsp70 in 2-methoxyestradiol-induced osteosarcoma cell death. We focused on the implication of Hsp90 and Hsp70 in control under expression of neuronal nitric oxide synthase, localization of the enzyme, and further generation of nitro-oxidative stress. To give the insight into the role of Hsp90 in regulation of anticancer efficacy of 2-methoxyestradiol, we used geldanamycin as a potent Hsp90 inhibitor. Herein, we evidenced that inhibition of Hsp90 controls the protein expression of 2-methoxyestradiol-induced neuronal nitric oxide synthase and inhibits enzyme nuclear translocation. We propose that decreased level of neuronal nitric oxide synthase protein after a combined treatment with 2-methoxyestradiol and geldanamycin is directly associated with the accompanying upregulation of Hsp70 and downregulation of Hsp90. This interaction resulted in abrogation of anticancer efficacy of 2-methoxyestradiol by geldanamycin.

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Alteration of the protein synthesis pattern in Neurospora crassa cells by hyperthermal and oxidative stress

Canadian Journal of Microbiology ◽

10.1139/m87-028 ◽

1987 ◽

Vol 33 (2) ◽

pp. 162-168 ◽

Cited By ~ 22

Author(s):

M. Kapoor ◽

J. Lewis

Keyword(s):

Oxidative Stress ◽

Heat Shock ◽

Heat Shock Proteins ◽

Neurospora Crassa ◽

Sodium Arsenite ◽

Dna Binding Protein ◽

Specific Protein ◽

One Dimensional ◽

Shock Proteins ◽

And Oxidative Stress

Neurospora crassa cells, grown at 28 °C for 14 h and heat shocked at 48 °C for 45 min, showed the synthesis of 11 heat-shock proteins (nHSPs) in one-dimensional electrophoretic profiles. Treatment with sodium arsenite induced the synthesis of two heat-shock proteins, nHSP70 and nHSP80, and a third, arsenite-specific protein, not induced by hyperthermia. Exposure to 0.5 or 1.0 mM H2O2 led to the induction of two of the heat-inducible nHSP70 family polypeptides. Sodium selenite, used in concert with H2O2, and arsenite were observed to modulate that heat-shock response. In addition, H2O2, menadione, and the glutathione depleters diamide and diethyl maleate promoted the synthesis of another protein, designated oxidative stress-responsive protein (OSP). A DNA-binding protein, specific for Neurospora DNA, was also demonstrated in extracts of heat-shocked cells.

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