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Portacaval shunting causes differential mitochondrial superoxide production in brain regions

dc.contributor.authorKosenko E.A.
dc.contributor.authorTikhonova L.A.
dc.contributor.authorAlilova G.A.
dc.contributor.authorMontoliu C.
dc.contributor.authorBarreto G.E.
dc.contributor.authorAliev G.
dc.contributor.authorKaminsky Y.G.
dc.date.accessioned2020-09-02T22:21:08Z
dc.date.available2020-09-02T22:21:08Z
dc.date.issued2017
dc.identifier10.1016/j.freeradbiomed.2017.09.023
dc.identifier.citation113, , 109-118
dc.identifier.issn08915849
dc.identifier.urihttps://hdl.handle.net/20.500.12728/5006
dc.descriptionThe portacaval shunting (PCS) prevents portal hypertension and recurrent bleeding of esophageal varices. On the other hand, it can induce chronic hyperammonemia and is considered to be the best model of mild hepatic encephalopathy (HE). Pathogenic mechanisms of HE and dysfunction of the brain in hyperammonemia are not fully elucidated, but it was originally suggested that the pathogenetic defect causes destruction of antioxidant defense which leads to an increase in the production of reactive oxygen species (ROS) and the occurrence of oxidative stress. In order to gain insight into the pathogenic mechanisms of HE in the brain tissue, we investigated the effects of PCS in rats on free radicals production and activity levels of antioxidant and prooxidant enzymes in mitochondria isolated from different brain areas. We found that O2 ·− production, activities of Mn-superoxide dismutase (Mn-SOD), glutathione peroxidase (GPx), glutathione reductase (GR), glutathione transferase (GT), nitric oxide synthase (NOS), and levels of carbonylated proteins differed between the four brain regions both in the amount and response to PCS. In PCS rats, Mn-SOD activity in the cerebellum was significantly decreased, and remained unchanged in the neocortex, hippocampus and striatum compared with that in sham-operated animals. Among the four brain regions in control rats, the levels of the carbonyl groups in mitochondrial proteins were maximal in the cerebellum. 4 weeks after PCS, the content of carbonylated proteins were higher only in mitochondria of this brain region. Under control conditions, O2 ·− production by submitochondrial particles in the cerebellum was significantly higher than in other brain regions, but was significantly increased in each brain region from PCS animals. Indeed, the production of O2 ·− by submitochondrial particles correlated with mitochondrial ammonia levels in the four brain regions of control and PCS-animals. These findings are the first to suggest that in vivo levels of ammonia in the brain directly affect the rate of mitochondrial O2 ·− production. © 2017 Elsevier Inc.
dc.language.isoen
dc.publisherElsevier Inc.
dc.subjectAmmonia
dc.subjectAntioxidant enzymes
dc.subjectBrain regions
dc.subjectCarbonylated proteins
dc.subjectCerebellum
dc.subjectMitochondria
dc.subjectNitric oxide synthase
dc.subjectPortacaval anastomosis
dc.subjectSuperoxide radical
dc.subjectammonia
dc.subjectcarbonyl derivative
dc.subjectfree radical
dc.subjectglutathione peroxidase
dc.subjectglutathione reductase
dc.subjectglutathione transferase
dc.subjectmanganese superoxide dismutase
dc.subjectnitric oxide synthase
dc.subjectoxygen
dc.subjectsuperoxide
dc.subjectcatalase
dc.subjectcopper zinc superoxide dismutase
dc.subjectglutathione peroxidase
dc.subjectglutathione reductase
dc.subjectglutathione transferase
dc.subjectmanganese superoxide dismutase
dc.subjectnitric oxide synthase
dc.subjectsuperoxide
dc.subjectsuperoxide dismutase
dc.subjectanimal cell
dc.subjectanimal experiment
dc.subjectanimal model
dc.subjectanimal tissue
dc.subjectArticle
dc.subjectbrain mitochondrion
dc.subjectbrain region
dc.subjectbrain tissue
dc.subjectcerebellum
dc.subjectcontrolled study
dc.subjectenzyme activity
dc.subjectenzyme analysis
dc.subjecthepatic encephalopathy
dc.subjectin vivo study
dc.subjectneuropathology
dc.subjectnonhuman
dc.subjectoxidative stress
dc.subjectportocaval shunt
dc.subjectpriority journal
dc.subjectprotein carbonylation
dc.subjectsubmitochondrial particle
dc.subjectanimal
dc.subjectbrain
dc.subjectdisease model
dc.subjectenzymology
dc.subjecthyperammonemia
dc.subjectmale
dc.subjectmetabolism
dc.subjectmitochondrion
dc.subjectoxidative stress
dc.subjectpathophysiology
dc.subjectportocaval shunt
dc.subjectrat
dc.subjectWistar rat
dc.subjectAnimals
dc.subjectBrain
dc.subjectCatalase
dc.subjectDisease Models, Animal
dc.subjectGlutathione Peroxidase
dc.subjectGlutathione Reductase
dc.subjectGlutathione Transferase
dc.subjectHepatic Encephalopathy
dc.subjectHyperammonemia
dc.subjectMale
dc.subjectMitochondria
dc.subjectNitric Oxide Synthase
dc.subjectOxidative Stress
dc.subjectPortacaval Shunt, Surgical
dc.subjectRats
dc.subjectRats, Wistar
dc.subjectSuperoxide Dismutase
dc.subjectSuperoxide Dismutase-1
dc.subjectSuperoxides
dc.titlePortacaval shunting causes differential mitochondrial superoxide production in brain regions
dc.typeArticle


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