Kinetic Parameters of Na/K‐ATPase Modified by Free Radicals in Vitro and in Vivoa

Kurella, Ekaterina G.; Kukley, Maria; Tyulina, O. V.; Dobrota, Dušan; Matejovičová, Milena; Mézesová, V; Boldyrev, Alexander A.

doi:10.1111/j.1749-6632.1997.tb52344.x

Cited by 46 publications

(13 citation statements)

References 6 publications

(2 reference statements)

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“…These results are in accordance with previous in vitro and in vivo experimental data showing that GA and 3HGA inhibit this enzyme activity in rat brain and in primary neuronal cultures from chick embryo telencephalons [12,23,55]. As regards to the mechanism by which Na + , K + -ATPase is inhibited, it is of note that this enzyme is highly vulnerable to free radical attack [56][57][58][59][60] and oxidative stress were recently shown to be elicited in brain of young Gcdh−/− mice submitted to a Lys overload [28], so that oxidative damage may represent a possible mechanism of Na + , K + -ATPase inhibition in this KO model. We also observed that high dietary Lys intake did not intensify the decreased activity of this enzyme in the cerebral cortex nor significantly altered the activities of brain α-KGDH and CK.…”

Section: Discussionsupporting

confidence: 93%

Reduction of Na+, K+-ATPase activity and expression in cerebral cortex of glutaryl-CoA dehydrogenase deficient mice: A possible mechanism for brain injury in glutaric aciduria type I

Amaral

Seminotti

Cecatto

et al. 2012

Molecular Genetics and Metabolism

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Section: Discussionsupporting

confidence: 93%

Reduction of Na+, K+-ATPase activity and expression in cerebral cortex of glutaryl-CoA dehydrogenase deficient mice: A possible mechanism for brain injury in glutaric aciduria type I

Amaral

Seminotti

Cecatto

et al. 2012

Molecular Genetics and Metabolism

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“…This enzyme activity is present at high concentrations in the brain, consuming about 40-50% of the ATP generated in this tissue, highlighting its importance for normal brain functioning. Alterations of this enzyme activity are mainly due to free radical attack [26,27] or to changes in membrane fluidity [28]. Under our experimental conditions, it is unlikely that free radicals could provoke oxidative damage on vulnerable groups of the enzyme leading to a reduction of its activity since GSH, a well known protector of thiol groups and scavenger of reactive species, was not able to change this effect.…”

Section: Discussionmentioning

confidence: 72%

Neurochemical Evidence that Pristanic Acid Impairs Energy Production and Inhibits Synaptic Na+, K+-ATPase Activity in Brain of Young Rats

et al. 2011

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Pristanic acid (Prist) accumulates in some peroxisomal disorders characterized by neurologic dysfunction and brain abnormalities. The present work investigated the in vitro effects of Prist on important parameters of energy metabolism in brain cortex of young rats. CO(2) production from labeled acetate and the activities of the respiratory chain complexes I-IV, creatine kinase and synaptic Na(+), K(+)-ATPase were measured. Prist decreased CO(2) production and the activities of complexes I, II and II-III. Prist also reduced Na(+), K(+)-ATPase activity, but did not affect the activity of creatine kinase. Considering the importance of the citric acid cycle and the electron flow through the respiratory chain for brain energy production and of Na(+), K(+)-ATPase for the maintenance of membrane potential, the present data indicate that Prist compromises brain bioenergetics and neurotransmission. It is presumed that these pathomechanisms may be involved in the neurological damage found in patients affected by disorders in which Prist accumulates.

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“…,K ? -ATPase activity may be secondary to free radical attack (Kurella et al 1997;Lees 1993;Yousef et al 2002) or to changes in membrane fluidity (Erecinska et al 2004;Erecinska and Silver 1994;Wheeler et al 1975). In this context, we found that the antioxidants MEL, TRO, and L-NAME were able to attenuate the synaptic Na ?…”

Section: Discussionmentioning

confidence: 94%

3-Methylcrotonylglycine Disrupts Mitochondrial Energy Homeostasis and Inhibits Synaptic Na+,K+-ATPase Activity in Brain of Young Rats

et al. 2011

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Deficiency of 3-methylcrotonyl-CoA carboxylase activity is an inherited metabolic disease biochemically characterized by accumulation and high urinary excretion of 3-methylcrotonylglycine (3MCG), and also of 3-hydroisovalerate in lesser amounts. Affected patients usually have neurologic dysfunction, brain abnormalities and cardiomyopathy, whose pathogenesis is still unknown. The present study investigated the in vitro effects of 3MCG on important parameters of energy metabolism, including CO(2) production from labeled acetate, enzyme activities of the citric acid cycle, as well as of the respiratory chain complexes I-IV (oxidative phosphorylation), creatine kinase (intracellular ATP transfer), and synaptic Na(+),K(+)-ATPase (neurotransmission) in brain cortex of young rats. 3MCG significantly reduced CO(2) production, implying that this compound compromises citric acid cycle activity. Furthermore, 3MCG diminished the activities of complex II-III of the respiratory chain, mitochondrial creatine kinase and synaptic membrane Na(+),K(+)-ATPase. Furthermore, antioxidants were able to attenuate or fully prevent the inhibitory effect of 3MCG on creatine kinase and synaptic membrane Na(+),K(+)-ATPase activities. We also observed that lipid peroxidation was elicited by 3MCG, suggesting the involvement of free radicals on 3MCG-induced effects. Considering the importance of the citric acid cycle and the electron flow through the respiratory chain for brain energy production, creatine kinase for intracellular energy transfer, and Na(+),K(+)-ATPase for the maintenance of the cell membrane potential, the present data indicate that 3MCG potentially impairs mitochondrial brain energy homeostasis and neurotransmission. It is presumed that these pathomechanisms may be involved in the neurological damage found in patients affected by 3-methylcrotonyl-CoA carboxylase deficiency.

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Kinetic Parameters of Na/K‐ATPase Modified by Free Radicals in Vitro and in Vivo^a

Cited by 46 publications

References 6 publications

Reduction of Na+, K+-ATPase activity and expression in cerebral cortex of glutaryl-CoA dehydrogenase deficient mice: A possible mechanism for brain injury in glutaric aciduria type I

Reduction of Na+, K+-ATPase activity and expression in cerebral cortex of glutaryl-CoA dehydrogenase deficient mice: A possible mechanism for brain injury in glutaric aciduria type I

Neurochemical Evidence that Pristanic Acid Impairs Energy Production and Inhibits Synaptic Na+, K+-ATPase Activity in Brain of Young Rats

3-Methylcrotonylglycine Disrupts Mitochondrial Energy Homeostasis and Inhibits Synaptic Na+,K+-ATPase Activity in Brain of Young Rats

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