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Basal brain oxidative and nitrative stress levels are finely regulated by the interplay between superoxide dismutase 2 and p53

dc.contributor.authorBarone E.
dc.contributor.authorCenini G.
dc.contributor.authorDi Domenico F.
dc.contributor.authorNoel T.
dc.contributor.authorWang C.
dc.contributor.authorPerluigi M.
dc.contributor.authorSt Clair D.K.
dc.contributor.authorButterfield D.A.
dc.date.accessioned2020-09-02T22:12:58Z
dc.date.available2020-09-02T22:12:58Z
dc.date.issued2015
dc.identifier10.1002/jnr.23627
dc.identifier.citation93, 11, 1728-1739
dc.identifier.issn03604012
dc.identifier.urihttps://hdl.handle.net/20.500.12728/3680
dc.descriptionSuperoxide dismutases (SODs) are the primary reactive oxygen species (ROS)-scavenging enzymes of the cell and catalyze the dismutation of superoxide radicals O2- to H2O2 and molecular oxygen (O2). Among the three forms of SOD identified, manganese-containing SOD (MnSOD, SOD2) is a homotetramer located wholly in the mitochondrial matrix. Because of the SOD2 strategic location, it represents the first mechanism of defense against the augmentation of ROS/reactive nitrogen species levels in the mitochondria for preventing further damage. This study seeks to understand the effects that the partial lack (SOD2-/+) or the overexpression (TgSOD2) of MnSOD produces on oxidative/nitrative stress basal levels in different brain isolated cellular fractions (i.e., mitochondrial, nuclear, cytosolic) as well as in the whole-brain homogenate. Furthermore, because of the known interaction between SOD2 and p53 protein, this study seeks to clarify the impact that the double mutation has on oxidative/nitrative stress levels in the brain of mice carrying the double mutation (p53-/- × SOD2-/+ and p53-/- × TgSOD2). We show that each mutation affects mitochondrial, nuclear, and cytosolic oxidative/nitrative stress basal levels differently, but, overall, no change or reduction of oxidative/nitrative stress levels was found in the whole-brain homogenate. The analysis of well-known antioxidant systems such as thioredoxin-1 and Nrf2/HO-1/BVR-A suggests their potential role in the maintenance of the cellular redox homeostasis in the presence of changes of SOD2 and/or p53 protein levels. © 2015 Wiley Periodicals, Inc.
dc.language.isoen
dc.publisherJohn Wiley and Sons Inc.
dc.subjectBiliverdin reductase-A
dc.subjectHeme oxygenase-1
dc.subjectMnSOD
dc.subjectp53
dc.subjectOxidative stress
dc.subjectRRID:AB_10618757
dc.subjectRRID:AB_10850321
dc.subjectRRID:AB_1840351
dc.subjectRRID:AB_2049199
dc.subjectRRID:AB_2256876
dc.subjectRRID:AB_476744
dc.subjectRRID:AB_881705
dc.subjectRRID:AB_958795
dc.subjectheme oxygenase 1
dc.subjectmanganese superoxide dismutase
dc.subjectprotein p53
dc.subjectthioredoxin 1
dc.subjecttranscription factor Nrf2
dc.subjectmanganese superoxide dismutase
dc.subjectprotein p53
dc.subjectreactive nitrogen species
dc.subjectreactive oxygen metabolite
dc.subjectsuperoxide dismutase
dc.subjectanimal cell
dc.subjectanimal experiment
dc.subjectArticle
dc.subjectbrain homogenate
dc.subjectcell nucleus
dc.subjectcellular stress response
dc.subjectconcentration (parameters)
dc.subjectcontrolled study
dc.subjectcytosol
dc.subjectencephale isole
dc.subjectgene mutation
dc.subjectgene overexpression
dc.subjectmale
dc.subjectmitochondrion
dc.subjectmouse
dc.subjectnitrative stress
dc.subjectnonhuman
dc.subjectoxidation reduction reaction
dc.subjectoxidative stress
dc.subjectpriority journal
dc.subjectprotein protein interaction
dc.subjectanimal
dc.subjectbrain
dc.subjectmetabolism
dc.subjectmutant mouse strain
dc.subjectnitrosation
dc.subjectoxidative stress
dc.subjectphysiology
dc.subjectWestern blotting
dc.subjectAnimals
dc.subjectBlotting, Western
dc.subjectBrain
dc.subjectMice
dc.subjectMice, Mutant Strains
dc.subjectMitochondria
dc.subjectNitrosation
dc.subjectOxidative Stress
dc.subjectReactive Nitrogen Species
dc.subjectReactive Oxygen Species
dc.subjectSuperoxide Dismutase
dc.subjectTumor Suppressor Protein p53
dc.titleBasal brain oxidative and nitrative stress levels are finely regulated by the interplay between superoxide dismutase 2 and p53
dc.typeArticle


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