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.

scholarly journals Exogenous Superoxide Dismutase: Action on Liver Oxidative Stress in Animals with Streptozotocin-Induced Diabetes

2011 ◽  
Vol 2011 ◽  
pp. 1-6 ◽  
Author(s):  
Fábio Cangeri Di Naso ◽  
Alexandre Simões Dias ◽  
Marilene Porawski ◽  
Norma Anair Possa Marroni
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Superoxide Radical ◽  
Inos Expression ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Significant Difference ◽  
Male Wistar Rats ◽  
Streptozotocin Induced Diabetes ◽  
Copper Zinc

Aim. To investigate the effects of exogenous antioxidant copper zinc superoxide dismutase (Cu/Zn SOD) on oxidative stress in the experimental model of diabetes mellitus (DM).Methods. Twenty eight male Wistar rats divided in four groups were used: control (CO), controls treated with SOD (CO + SOD), diabetics (DM), and diabetics treated with SOD (DM + SOD). SOD (orgotein, 13 mg/Kg body weight was administered. DM was induced by a single streptozotocin injection (i.p., 70 mg/kg), and 60 days later, we evaluated liver oxidative stress.Results. Liver lipoperoxidation was increased in the DM group and significantly decreased in the DM + SOD group. Nitrite and nitrate measures were reduced in the DM and increased in the DM + SOD group, while iNOS expression in the DM group was 32% greater than in the CO and 53% greater in the DM + SOD group than in the DM group (P<.01). P65 expression was 37% higher in the DM (P<.05), and there was no significant difference between the DM and DM + SOD groups.Conclusion. SOD treatment reduced liver oxidative stress in diabetic animals, even though it did not change NFκB. SOD also increased NO, probably by the increased dismutation of the superoxide radical. The iNOS expression increase, which became even more evident after SOD administration.

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 Periplasmic copper-zinc superoxide dismutase protects Haemophilus ducreyi from exogenous superoxide

1998 ◽  
Vol 27 (2) ◽  
pp. 391-404 ◽  
Author(s):  
Lani R. San Mateo ◽  
Marcia M. Hobbs ◽  
Thomas H. Kawula
Keyword(s):  
Superoxide Dismutase ◽  
Haemophilus Ducreyi ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Copper Zinc

scholarly journals Copper-zinc superoxide dismutase deficiency impairs sperm motility and in vivo fertility

Reproduction ◽  
2013 ◽  
Vol 146 (4) ◽  
pp. 297-304 ◽  
Author(s):  
Michael Garratt ◽  
Roslyn Bathgate ◽  
Simon P de Graaf ◽  
Robert C Brooks
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Sperm Motility ◽  
Physiological Role ◽  
Enzymatic Antioxidants ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Copper Zinc ◽  
And Function

Oxidative stress, overproduction of reactive oxygen species (ROS) in relation to defence mechanisms, is considered to be a major cause of male infertility. For protection against the deleterious effects of ROS, animals have a variety of enzymatic antioxidants that reduce these molecules to less reactive forms. The physiological role of these antioxidantsin vivohas been explored extensively through genetic inhibition of gene expression; surprisingly, many of these animals remain fertile in spite of increased oxidative stress. Copper-zinc superoxide dismutase-deficient (Sod1−/−) male mice are one such example for whichin vivofertility has been repeatedly reported as normal, although examination of fertility has consisted of simply pairing animals of the same strain and checking for litters. This is a fairly low criterion by which to assess fertility. Herein, we show thatSod1-deficient males have zero fertilisation success in sperm competition trials that pit them against wild-type males of an otherwise identical genetic background and are almost completely infertile when mated singly with females of a different genotype. We also show that various aspects of sperm motility and function are impaired inSod1-deficient mice. Testing the breeding capabilities of mice under more ecologically relevant conditions and with females of different genotypes may help reveal additional physiological causes of infertility.

Effect of Copper-Zinc Superoxide Dismutase on Endothelium-Dependent Vasodilation in Patients With Essential Hypertension

Hypertension ◽  
1995 ◽  
Vol 26 (6) ◽  
pp. 863-868 ◽  
Author(s):  
Carlos E. García ◽  
Crescence M. Kilcoyne ◽  
Carmine Cardillo ◽  
Richard O. Cannon ◽  
Arshed A. Quyyumi ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Essential Hypertension ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Copper Zinc ◽  
Effect Of Copper

Copper as a Cofactor and Regulator of Copper,Zinc Superoxide Dismutase

1992 ◽  
Vol 122 (suppl_3) ◽  
pp. 636-640 ◽  
Author(s):  
Edward D. Harris
Keyword(s):  
Superoxide Dismutase ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Copper Zinc

scholarly journals The complete amino acid sequence of copper, zinc superoxide dismutase from Saccharomyces cerevisiae

1979 ◽  
Vol 44 (4) ◽  
pp. 201-217 ◽  
Author(s):  
Jack T. Johansen ◽  
Carsten Overballe-Petersen ◽  
Brian Martin ◽  
Villy Hasemann ◽  
Ib Svendsen
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Superoxide Dismutase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Copper Zinc Superoxide Dismutase ◽  
Complete Amino Acid Sequence ◽  
Zinc Superoxide Dismutase ◽  
Copper Zinc
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