scholarly journals Superoxide Dismutase 1 Loss Disturbs Intracellular Redox Signaling, Resulting in Global Age-Related Pathological Changes

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Kenji Watanabe ◽  
Shuichi Shibuya ◽  
Yusuke Ozawa ◽  
Hidetoshi Nojiri ◽  
Naotaka Izuo ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Oxidative Damage ◽  
Molecular Mechanisms ◽  
The Body ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Age Related ◽  
Tissue Changes ◽  
Copper Zinc

Aging is characterized by increased oxidative stress, chronic inflammation, and organ dysfunction, which occur in a progressive and irreversible manner. Superoxide dismutase (SOD) serves as a major antioxidant and neutralizes superoxide radicals throughout the body.In vivostudies have demonstrated that copper/zinc superoxide dismutase-deficient (Sod1−/−) mice show various aging-like pathologies, accompanied by augmentation of oxidative damage in organs. We found that antioxidant treatment significantly attenuated the age-related tissue changes and oxidative damage-associated p53 upregulation inSod1−/−mice. This review will focus on various age-related pathologies caused by the loss ofSod1and will discuss the molecular mechanisms underlying the pathogenesis inSod1−/−mice.

scholarly journals A Superoxide Dismutase C Mutant of Haemophilus ducreyi Is Virulent in Human Volunteers

2002 ◽  
Vol 70 (3) ◽  
pp. 1367-1371 ◽  
Author(s):  
Cliffton T. H. Bong ◽  
Kate R. Fortney ◽  
Barry P. Katz ◽  
Antoinette F. Hood ◽  
Lani R. San Mateo ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Haemophilus Ducreyi ◽  
Swine Model ◽  
Bacterial Survival ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Human Volunteers ◽  
Significant Difference ◽  
Copper Zinc

ABSTRACT Haemophilus ducreyi produces a periplasmic copper-zinc superoxide dismutase (Cu-Zn SOD), which is thought to protect the organism from exogenous reactive oxygen species generated by neutrophils during an inflammatory response. We had previously identified the gene, sodC, responsible for the production and secretion of Cu-Zn SOD and constructed an isogenic H. ducreyi strain with a mutation in the sodC gene (35000HP-sodC-cat). Compared to the parent, the mutant does not survive in the presence of exogenous superoxide (L. R. San Mateo, M. Hobbs, and T. H. Kawula, Mol. Microbiol. 27:391-404, 1998) and is impaired in the swine model of H. ducreyi infection (L. R. San Mateo, K. L. Toffer, P. E. Orndorff, and T. H. Kawula, Infect. Immun. 67:5345-5351, 1999). To test whether Cu-Zn SOD is important for bacterial survival in vivo, six human volunteers were experimentally infected with 35000HP and 35000HP-sodC-cat and observed for papule and pustule formation. Papules developed at similar rates at sites inoculated with the mutant or parent. The pustule formation rates were 75% (95% confidence intervals [CI], 43 to 95%) at 12 parent-inoculated sites and 67% (95% CI, 41 to 88%) at 18 mutant-inoculated sites (P = 0.47). There was no significant difference in levels of H. ducreyi recovery from mutant- and parent-inoculated biopsy sites. These results suggest that expression of Cu-Zn SOD does not play a major role in the survival of this pathogen in the initial stages of experimental infection of humans.

Age-Correlated Modifications of Copper-Zinc Superoxide Dismutase and Glutathione-Related Enzyme Activities in Human Erythrocytes

1992 ◽  
Vol 38 (1) ◽  
pp. 66-70 ◽  
Author(s):  
Iréne Ceballos-Picot ◽  
Jean-Marc Trivier ◽  
Annie Nicole ◽  
Pierre-Marie Sinet ◽  
Marc Thevenin
Keyword(s):  
Superoxide Dismutase ◽  
Enzyme Activities ◽  
Human Erythrocytes ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Age Related ◽  
Copper Zinc ◽  
Group 3 ◽  
Group 5 ◽  
Group 2

Abstract To obtain a comprehensive profile of the erythrocyte antioxidant defense potential during aging, we investigated copper-zinc superoxide dismutase (CuZn-SOD), seleno-dependent glutathione peroxidase (GSH-Px), glutathione reductase (GSSG-RD), and glutathione-S-transferase (GSH-S-T) activities in human erythrocytes from 167 apparently healthy subjects, ages one month to 63 years (102 females, 65 males). We found a negative correlation between age and activities of CuZn-SOD (r = 0.362, P less than 0.001), GSSG-RD (r = 0.549, P less than 0.001), and GSH-S-T (r = 0.575, P less than 0.001). In contrast, we found a positive correlation between age and GSH-Px activity (r = 0.401, P less than 0.001). To evaluate aging changes, we divided the subjects into five groups: Group 1 (newborn-age one year), Group 2 (1-11 years), Group 3 (11-25 years), Group 4 (25-40 years), and Group 5 (40-63 years). Significant age-related modifications in erythrocyte enzyme activities appeared in Group 3 for CuZn-SOD, GSSG-RD, and GSH-Px activity, whereas for GSH-S-T activity age-related modifications appeared in Group 2. We found no sex-related differences in erythrocyte CuZn-SOD, GSSG-RD, GSH-Px, and GSH-S-T activities.

Intermittent hyperthermia enhances skeletal muscle regrowth and attenuates oxidative damage following reloading

2007 ◽  
Vol 102 (4) ◽  
pp. 1702-1707 ◽  
Author(s):  
J. T. Selsby ◽  
S. Rother ◽  
S. Tsuda ◽  
O. Pracash ◽  
J. Quindry ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Superoxide Dismutase ◽  
Oxidative Damage ◽  
Manganese Superoxide Dismutase ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Manganese Superoxide ◽  
Oxidant Damage ◽  
Heat Shock Protein Expression ◽  
Copper Zinc

Skeletal muscle reloading following disuse is characterized by profound oxidative damage. This study tested the hypothesis that intermittent hyperthermia during reloading attenuates oxidative damage and augments skeletal muscle regrowth following immobilization. Forty animals were randomly divided into four groups: control (Con), immobilized (Im), reloaded (RC), and reloaded and heated (RH). All groups but Con were immobilized for 7 days. Animals in the RC and RH groups were then reloaded for 7 days with (RH) or without (RC) hyperthermia (41–41.5°C for 30 min on alternating days) during reloading. Heating resulted in ∼25% elevation in heat shock protein expression ( P < 0.05) and an ∼30% greater soleus regrowth ( P < 0.05) in RH compared with RC. Furthermore, oxidant damage was lower in the RH group compared with RC because nitrotyrosine and 4-hydroxy-2-nonenol were returned to near baseline when heating was combined with reloading. Reduced oxidant damage was independent of antioxidant enzymes (manganese superoxide dismutase, copper-zinc superoxide dismutase, catalase, glutathione peroxidase, glutathione reductase). In summary, these data suggest that intermittent hyperthermia during reloading attenuates oxidative stress and improves the rate of skeletal muscle regrowth during reloading after immobilization.

scholarly journals Copper/Zinc-Superoxide Dismutase Is Required for Oxytetracycline Resistance of Saccharomyces cerevisiae

2000 ◽  
Vol 182 (1) ◽  
pp. 76-80 ◽  
Author(s):  
Simon V. Avery ◽  
Srividya Malkapuram ◽  
Carolina Mateus ◽  
Kimberly S. Babb
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Lipid Peroxidation ◽  
Superoxide Dismutase ◽  
Oxidative Damage ◽  
Protein Oxidation ◽  
Wild Type ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Copper Zinc

ABSTRACT Saccharomyces cerevisiae, along with other eukaryotes, is resistant to tetracyclines. We found that deletion ofSOD1 (encoding Cu/Zn superoxide dismutase) renderedS. cerevisiae hypersensitive to oxytetracycline (OTC): asod1Δ mutant exhibited a >95% reduction in colony-forming ability at an OTC concentration of 20 μg ml−1, whereas concentrations of up to 1,000 μg ml−1 had no effect on the growth of the wild type. OTC resistance was restored in the sod1Δ mutant by complementation with wild-type SOD1. The effect of OTC appeared to be cytotoxic and was not evident in a ctt1Δ (cytosolic catalase) mutant or in the presence of tetracycline.SOD1 transcription was not induced by OTC, suggesting that constitutive SOD1 expression is sufficient for wild-type OTC resistance. OTC uptake levels in wild-type and sod1Δ strains were similar. However, lipid peroxidation and protein oxidation were both enhanced during exposure of the sod1Δ mutant, but not the wild type, to OTC. We propose that Sod1p protects S. cerevisiae against a mode of OTC action that is dependent on oxidative damage.

Increased 3-nitrotyrosine and oxidative damage in mice with a human copper/zinc superoxide dismutase mutation

1997 ◽  
Vol 42 (3) ◽  
pp. 326-334 ◽  
Author(s):  
Robert J. Ferrante ◽  
Leslie A. Shinobu ◽  
J�rg B. Schulz ◽  
Russell T. Matthews ◽  
Craig E. Thomas ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Oxidative Damage ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Copper Zinc

Age-related cochlear hair cell loss is enhanced in mice lacking copper/zinc superoxide dismutase

1999 ◽  
Vol 20 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Sandra L McFadden ◽  
Dalian Ding ◽  
Andrew G Reaume ◽  
Dorothy G Flood ◽  
Richard J Salvi
Keyword(s):  
Superoxide Dismutase ◽  
Hair Cell ◽  
Cell Loss ◽  
Hair Cell Loss ◽  
Copper Zinc Superoxide Dismutase ◽  
Cochlear Hair Cell ◽  
Zinc Superoxide Dismutase ◽  
Age Related ◽  
Copper Zinc
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