Oxidative metabolism and heat shock-enhanced chemiluminescence in Dictyostelium discoideum

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.

Short-term exercise training can improve myocardial tolerance to I/R without elevation in heat shock proteins

2001 ◽  
Vol 281 (3) ◽  
pp. H1346-H1352 ◽  
Author(s):  
Karyn L. Hamilton ◽  
Scott K. Powers ◽  
Takao Sugiura ◽  
Sunjoo Kim ◽  
Shannon Lennon ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Ischemia Reperfusion ◽  
Left Ventricular ◽  
Antioxidant Defenses ◽  
Control Group ◽  
Shock Proteins ◽  
Mnsod Activity ◽  
Over Time

We examined the effects of 3 days of exercise in a cold environment on the expression of left ventricular (LV) heat shock proteins (HSPs) and contractile performance during in vivo ischemia-reperfusion (I/R). Sprague-Dawley rats were divided into the following three groups ( n = 12/group): 1) control, 2) exercise (60 min/day) at 4°C (E-Cold), and 3) exercise (60 min/day) at 25°C (E-Warm). Left anterior descending coronary occlusion was maintained for 20 min, followed by 30 min of reperfusion. Compared with the control group, both the E-Cold and E-Warm groups maintained higher ( P < 0.05) LV developed pressure, first derivative of pressure development over time (+dP/d t), and pressure relaxation over time (−dP/d t) throughout I/R. Relative levels of HSP90, HSP72, and HSP40 were higher ( P < 0.05) in E-Warm animals compared with both control and E-Cold. HSP10, HSP60, and HSP73 did not differ between groups. Exercise increased manganese superoxide dismutase (MnSOD) activity in both E-Warm and E-Cold hearts ( P < 0.05). Protection against I/R-induced lipid peroxidation in the LV paralleled the increase in MnSOD activity whereas lower levels of lipid peroxidation were observed in both E-Warm and E-Cold groups compared with control. We conclude that exercise-induced myocardial protection against a moderate duration I/R insult is not dependent on increases in myocardial HSPs. We postulate that exercise-associated cardioprotection may depend, in part, on increases in myocardial antioxidant defenses.

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

2012 ◽  
Vol 2012 ◽  
pp. 1-13 ◽  
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.

In vivo evidence from an Agrostis stolonifera selection genotype that chloroplast small heat-shock proteins can protect photosystem II during heat stress

2002 ◽  
Vol 29 (8) ◽  
pp. 935 ◽  
Author(s):  
Scott A. Heckathorn ◽  
Samantha L. Ryan ◽  
Joanne A. Baylis ◽  
Dongfang Wang ◽  
E. William Hamilton III ◽  
...  
Keyword(s):  
Heat Stress ◽  
Electron Transport ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Agrostis Stolonifera ◽  
Small Heat Shock Proteins ◽  
O2 Evolution ◽  
Shock Proteins ◽  
Tolerant Genotype

Previous in vitro experiments indicated that chloroplast small heat-shock proteins (sHsp) could associate with thylakoids and protect PSII during heat and other stresses, possibly by stabilizing the O2-evolving complex (OEC). However, in vivo evidence of sHsp protection of PSII is equivocal at present. Using previously characterized selection genotypes of Agrostis stolonifera Huds. that differ in thermotolerance and production of chloroplast sHsps, we show that both genotypes contain thylakoid-associating sHsps, but the heat-tolerant genotype, which produces an additional sHsp isoform not made by the sensitive genotype, produces a greater quantity of chloroplast and thylakoid sHsp. Following a pre-heat stress to induce sHsps, in vivo PSII function decreased less at high temperatures in the tolerant genotype. Differences in PSII thermotolerance in vivo were associated with increased thermotolerance of the OEC proteins and O2-evolving function of PSII, and not with other PSII proteins or functions examined. In vivo cross-linking experiments indicated that a greater amount of sHsp associated with PSII proteins during heat stress in the tolerant genotype. PSII was the most thermosensitive component of photosynthetic electron transport, and no differences between genotypes in the thermotolerance of other electron transport components were observed. These results indicate that in vivo chloroplast sHsps can protect O2 evolution and the OEC proteins of PSII during heat stress.

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

1987 ◽  
Vol 33 (2) ◽  
pp. 162-168 ◽  
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.

4 P Expression of heat shock proteins in response to the oxidative stress in patients with chronic liver diseases

2002 ◽  
Vol 34 ◽  
pp. A137
Author(s):  
F. Terraciano ◽  
A. Federico ◽  
T. De Simone ◽  
C. Tuccillo ◽  
E. Finamore ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Liver Diseases ◽  
Chronic Liver ◽  
Chronic Liver Diseases ◽  
Shock Proteins
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