Na/K‐ATPase and Oxidative Stress<sup>a</sup>

Boldyrev, Alexander A.; Bulygina, E. R.

doi:10.1111/j.1749-6632.1997.tb52345.x

Cited by 36 publications

(21 citation statements)

References 9 publications

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“…(Haddock et al, 1995a,b;Bilgin et al, 1999;Cheng et al, 1984;Boldyrev and Bulygina, 1997;Bogdanova et al, 2003b) (I. Petrushanko and A. Bogdanova, unpublished). The only study in which no effect of CDNB treatment on active K + transport in human red cells was reported is the work of Muzyamba and Gibson (Muzyamba and Gibson, 2003).…”

Section: Discussionmentioning

confidence: 99%

Hypoxic responses of Na+/K+ ATPase in trout hepatocytes

Bogdanova

Grenacher

Nikinmaa

et al. 2005

Journal of Experimental Biology

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SUMMARY Reduction in oxygenation induces inhibition of Na+/K+ATPase in a number of cells and tissues, including hepatocytes. When not reversed, decrease in Na+/K+ pump activity leads to a gradual Na+ accumulation, cell swelling and death. However, when accompanied by suppression of dissipative cation pathways, it has also been shown to be a beneficial adaptive strategy used by some hypoxia-tolerant species to reduce ATP consumption during prolonged periods of anoxia. This study aims to investigate acute hypoxic responses of the Na+/K+ ATPase in primary cultures of trout hepatocytes. Gradual decrease in oxygenation was followed by an instantaneous transient dose-dependent downregulation of the Na+/K+ ATPase transport activity, but was without an effect on hydrolytic function of the enzyme. Hypoxia-induced inhibition of active K+ influx was reversed spontaneously when hypoxic incubation time exceeded 20 min. The stimulating effect of prolonged hypoxic exposure on the Na+/K+ pump is most probably secondary to hypoxia-induced activation of the Na+/H+ exchanger with the following Na+accumulation leading to Na+/K+ ATPase activation. Hypoxia-induced inhibition of the Na+/K+ pump was not caused by ATP depletion or global oxidative stress. However, local controlled production of reactive oxygen species seems to play an important role in hypoxia-induced regulation of the Na+/K+ ATPase. Treatment of cells with mercaptopropionyl glycine (MPG), a scavenger of \batchmode \documentclass[fleqn,10pt,legalpaper]{article} \usepackage{amssymb} \usepackage{amsfonts} \usepackage{amsmath} \pagestyle{empty} \begin{document} \(\mathrm{O}\mathrm{H}^{.-}\) \end{document}, abolished hypoxia-induced inhibition of the Na+/K+ ATPase. Earlier on we have shown that activation of Na+/H+ exchanger under hypoxic conditions can be opposed by MPG treatment as well. Taken together our results suggest that regulation of both oxygen-sensitive transporters may be accomplished by local changes in free radical production.

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Section: Discussionmentioning

confidence: 99%

Hypoxic responses of Na+/K+ ATPase in trout hepatocytes

Bogdanova

Grenacher

Nikinmaa

et al. 2005

Journal of Experimental Biology

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“…Incubation of the neurons with ouabain results in ROS accumulation 3,20 and MAP kinase phosphorylation as well.…”

Section: 28mentioning

confidence: 98%

“…Na þ /K þ -ATPase or Na-pump (3.6.1.37) is an integral enzyme of outer cell membranes catalyzing the active transport of sodium ions out and potassium ions into the cells against their electrochemical gradients. 1 Additionally to its pumping function, Na þ /K þ -ATPase has been recently shown to act as a signal transducer in myocytes 2 and neurons 3 affecting the intracellular levels of reactive oxygen species (ROS) and activity of different protein kinases. 4,5 Short term incubation of living neuronal cells with ouabain resulting in an inhibition of Na þ /K þ -ATPase induces an elevation of ROS levels 6 accompanied by an activation of MAPK cascade at longer incubation time.…”

Section: Introductionmentioning

confidence: 99%

Different neuronal Na⁺/K⁺‐ATPase isoforms are involved in diverse signaling pathways

Karpova

Bulygina

Boldyrev

2010

Cell Biochemistry & Function

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Inhibition of rat neuronal Na(+)/K(+)-ATPase alpha3 isoform at low (100 nM) ouabain concentration led to activation of MAP kinase cascade via PKC and PIP(3) kinase. In contrast to ouabain-sensitive alpha3 isoform of Na(+)/K(+)-ATPase, an ouabain-resistant alpha1 isoform (inhibition with 1 mM of ouabain) of Na(+)/K(+)-ATPase regulates MAP kinase via Src kinase dependent reactions. Using of Annexin V-FITC apoptotic test to determine the cells with early apoptotic features allows to conclude that alpha3 isoform stimulates and alpha1 suppresses apoptotic process in cerebellum neurons. These data are the first demonstration showing participation of ouabain-resistant (alpha1) and ouabain-sensitive (alpha3) Na(+)/K(+)-ATPase isoforms in diverse signaling pathways in neuronal cells.

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“…Direct evidence was recently reported by measuring the ROS level and lipid peroxidation in PS-1 KI mice (Schuessel, et al 2006). Significant impairment of Na + /K + transporting ATPase has been reported in pathologic conditions associated with the development of oxidative stress such as Parkinson’s and Alzheimer’s disease, ischemia-reperfusion injury, apoptosis, intoxication, and aging (Petrushanko, et al 2006; Boldyrev and Bulygina, 1997). Application of antioxidants and measures that efficiently reduce free radical production have been shown to restore Na + /K + ATPase activity and provide cell survival (Chen, et al 2008).…”

Section: Discussionmentioning

confidence: 99%

Quantitative Proteomic Analysis of Mitochondria in Aging PS-1 Transgenic Mice

Xiong

Lovell

et al. 2009

Cell Mol Neurobiol

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Accumulating evidence suggests mitochondrial alterations are intimately associated with the pathogenesis of Alzheimer's disease (AD). To determine if mutations of presenilin-1 (PS-1) affect levels of mitochondrial proteins at different ages we enriched mitochondrial fractions from 3, 6, 12 month old knock-in mice expressing the M146V PS-1 mutation and identified, and quantified proteins using cleavable Isotope Coded Affinity Tag (ICAT) labeling and two dimensional liquid chromatography/tandem mass spectrometry (2D-LC/MS/MS). Using this approach, 165 nonredundant proteins were identified with 80 of them present in all three age groups. Specifically, at young ages (3 and 6 months), Na + /K + ATPase and several signal transduction proteins exhibited elevated levels, but dropped dramatically at 12 months. In contrast, components of the oxidative phosporylation pathway (OXPHOS), the mitochondrial permeability transition pore (MPTP), and energy metabolism proteins remained unchanged at 3 months but significantly increased with age. We propose that alterations in calcium homeostasis induced by the PS-1 mutation have a major impact in young animals by inhibiting function of relevant proteins and inducing compensatory changes. However, in older mice combination of the PS-1 mutation and accumulated oxidative damage results in functional suppression of OXPHOS and MPTP proteins requiring a compensatory increase in expression levels. In contrast, signal transduction proteins showed decreased levels due to a break down in the compensatory mechanisms. The dysfunction of Na + /K + ATPase and signal transduction proteins may induce impaired cognition and memory before neurodegeneration occurs.

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Na/K‐ATPase and Oxidative Stress^a

Cited by 36 publications

References 9 publications

Hypoxic responses of Na+/K+ ATPase in trout hepatocytes

Hypoxic responses of Na+/K+ ATPase in trout hepatocytes

Different neuronal Na⁺/K⁺‐ATPase isoforms are involved in diverse signaling pathways

Quantitative Proteomic Analysis of Mitochondria in Aging PS-1 Transgenic Mice

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Na/K‐ATPase and Oxidative Stressa

Cited by 36 publications

References 9 publications

Hypoxic responses of Na+/K+ ATPase in trout hepatocytes

Hypoxic responses of Na+/K+ ATPase in trout hepatocytes

Different neuronal Na+/K+‐ATPase isoforms are involved in diverse signaling pathways

Quantitative Proteomic Analysis of Mitochondria in Aging PS-1 Transgenic Mice

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About

Na/K‐ATPase and Oxidative Stress^a

Different neuronal Na⁺/K⁺‐ATPase isoforms are involved in diverse signaling pathways