The balance between copper-zinc superoxide dismutase and catalase affects the sensitivity of mouse epidermal cells to oxidative stress

Biochemistry ◽  
1991 ◽  
Vol 30 (38) ◽  
pp. 9305-9313 ◽  
Author(s):  
Paul Amstad ◽  
A. Peskin ◽  
Girish Shah ◽  
Marc Edouard Mirault ◽  
Remy Moret ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Epidermal Cells ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Copper Zinc

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.

Molecular mechanism on two fluoroquinolones inducing oxidative stress: evidence from copper/zinc superoxide dismutase

RSC Advances ◽  
2016 ◽  
Vol 6 (94) ◽  
pp. 91141-91149 ◽  
Author(s):  
Xingren Pan ◽  
Pengfei Qin ◽  
Rutao Liu ◽  
Jianfeng Li ◽  
Fucui Zhang
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Molecular Mechanism ◽  
Copper Zinc Superoxide Dismutase ◽  
Cellular Analysis ◽  
Zinc Superoxide Dismutase ◽  
Increased Risk ◽  
Copper Zinc

The combination of molecular and cellular analysis suggested that the structural and functional alterations of Cu/Zn-SOD were closely associated with increased risk of oxidative stress initiated by both CPFX and ENFX.

scholarly journals The Megavirus Chilensis Cu,Zn-Superoxide Dismutase: the First Viral Structure of a Typical Cellular Copper Chaperone-Independent Hyperstable Dimeric Enzyme

2014 ◽  
Vol 89 (1) ◽  
pp. 824-832 ◽  
Author(s):  
Audrey Lartigue ◽  
Bénédicte Burlat ◽  
Bruno Coutard ◽  
Florence Chaspoul ◽  
Jean-Michel Claverie ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Crystallographic Structure ◽  
Copper Chaperone ◽  
Content Type ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Activity Measurements ◽  
Copper Zinc ◽  
Giant Viruses

ABSTRACTGiant viruses able to replicate inAcanthamoeba castellaniipenetrate their host through phagocytosis. After capsid opening, a fusion between the internal membranes of the virion and the phagocytic vacuole triggers the transfer in the cytoplasm of the viral DNA together with the DNA repair enzymes and the transcription machinery present in the particles. In addition, the proteome analysis of purified mimivirus virions revealed the presence of many enzymes meant to resist oxidative stress and conserved in theMimiviridae. Megavirus chilensis encodes a predicted copper, zinc superoxide dismutase (Cu,Zn-SOD), an enzyme known to detoxify reactive oxygen species released in the course of host defense reactions. While it was thought that the metal ions are required for the formation of the active-site lid and dimer stabilization, megavirus chilensis SOD forms a very stable metal-free dimer. We used electron paramagnetic resonance (EPR) analysis and activity measurements to show that the supplementation of the bacterial culture with copper and zinc during the recombinant expression of Mg277 is sufficient to restore a fully active holoenzyme. These results demonstrate that the viral enzyme's activation is independent of a chaperone both for disulfide bridge formation and for copper incorporation and suggest that its assembly may not be as regulated as that of its cellular counterparts. A SOD protein is encoded by a variety of DNA viruses but is absent from mimivirus. As in poxviruses, the enzyme might be dispensable when the virus infectsAcanthamoebacells but may allow megavirus chilensis to infect a broad range of eukaryotic hosts.IMPORTANCEMimiviridaeare giant viruses encoding more than 1,000 proteins. The virion particles are loaded with proteins used by the virus to resist the vacuole's oxidative stress. The megavirus chilensis virion contains a predicted copper, zinc superoxide dismutase (Cu,Zn-SOD). The corresponding gene is present in some megavirus chilensis relatives but is absent from mimivirus. This first crystallographic structure of a viral Cu,Zn-SOD highlights the features that it has in common with and its differences from cellular SODs. It corresponds to a very stable dimer of the apo form of the enzyme. We demonstrate that upon supplementation of the growth medium with Cu and Zn, the recombinant protein is fully active, suggesting that the virus's SOD activation is independent of a copper chaperone for SOD generally used by eukaryotic SODs.

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