scholarly journals Basal Glutathionylation of Na,K-ATPaseα-Subunit Depends on Redox Status of Cells during the Enzyme Biosynthesis

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Vladimir A. Mitkevich ◽  
Irina Yu. Petrushanko ◽  
Yuri M. Poluektov ◽  
Ksenia M. Burnysheva ◽  
Valentina A. Lakunina ◽  
...  

Many viruses induce oxidative stress and cause S-glutathionylation of Cys residues of the host and viral proteins. Changes in cell functioning during viral infection may be associated with glutathionylation of a number of key proteins including Na,K-ATPase which creates a gradient of sodium and potassium ions. It was found that Na,K-ATPaseα-subunit has a basal glutathionylation which is not abrogated by reducing agent. We have shown that acute hypoxia leads to increase of total glutathionylation level of Na,K-ATPaseα-subunit; however, basal glutathionylation ofα-subunit increases under prolonged hypoxia only. The role of basal glutathionylation in Na,K-ATPase function remains unclear. Understanding significance of basal glutathionylation is complicated by the fact that there are no X-ray structures of Na,K-ATPase with the identified glutathione molecules. We have analyzed all X-ray structures of the Na,K-ATPaseα-subunit from pig kidney and found that there are a number of isolated cavities with unresolved electron density close to the relevant cysteine residues. Analysis of the structures showed that this unresolved density in the structure can be occupied by glutathione associated with cysteine residues. Here, we discuss the role of basal glutathionylation of Na,K-ATPaseα-subunit and provide evidence supporting the view that this modification is cotranslational.

1995 ◽  
Vol 92 (10) ◽  
pp. 4616-4620 ◽  
Author(s):  
S. Takahashi ◽  
B. F. Driscoll ◽  
M. J. Law ◽  
L. Sokoloff

Author(s):  
Timothy Duignan ◽  
Gregory K. Schenter ◽  
Mirza Galib ◽  
Marcel D. Baer ◽  
Jan Wilhelm ◽  
...  

<div><div><div><p>The ability to reproduce the structure of water around the sodium and potassium ions as determined by experiment is a key test of the quality of interaction potentials due to the central importance of these ions in a wide range of important phenomena. Here, we simulate the Na+ and K+ ions in bulk water using the recently developed strongly constrained and appropriately normed (SCAN) functional and compare with experimental X-ray diffraction (XRD) and X-ray adsorption fine structure (EXAFS) measurements to demonstrate that it accurately reproduces important structural details of the hydration structure of the sodium and potassium cations. We demonstrate that it performs substantially better than the generalized gradient approximation (GGA) based dispersion corrected revised Perdew, Burke, and Ernzerhof functional (revPBE-D3) and is even better than the random phase approximation level for potassium. Both of these functionals have been demonstrated to accurately reproduce the structure of bulk water. This improved performance compared with revPBE-D3 is attributed to smaller fluctuations of the mean error of ion-water cluster binding energies utilizing a novel benchmark for testing functionals.</p></div></div></div>


1968 ◽  
Vol 51 (4) ◽  
pp. 552-578 ◽  
Author(s):  
Sadayuki F. Takagi ◽  
Gordon A. Wyse ◽  
Harunobu Kitamura ◽  
Katsuhiro Ito

In order to clarify whether or not the electronegative olfactory mucosal potentials (EOG) are generator potentials, the effects of changed ionic enviroment were studied. The EOG decreased in amplitude and in some cases nearly or completely disappeared, when Na+ in the bathing Ringer solution was replaced by sucrose, Li+, choline+, tetraethylammonium+ (TEA), or hydrazine. In the K+-free Ringer solution, the negative EOG's initially increased and then decreased in amplitude. In Ringer's solution with increased K+, the negative EOG's increased in amplitude. When K+ was increased in exchange for Na+ in Ringer's solution, the negative EOG's decreased, disappeared, and then reversed their polarity (Fig. 6). Next, when the K+ was replaced by equimolar sucrose, Li+, choline+, TEA+, hydrazine, or Na+, the reversed potentials recovered completely only in Na+-Ringer's solution, but never in the other solutions. Thus, the essential role of Na+ and K+ in the negative EOG's was demonstrated. Ba++ was found to depress selectively the electropositive EOG, but it hardly decreased and never increased the negative EOG. Hence, it is concluded that Ba++ interferes only with Cl- influx, and that the negative EOG's are elicited by an increase in permeability of the olfactory receptive membrane to Na+ and K+, but not to Cl-. From the ionic mechanism it is inferred that the negative EOG's are in most cases composites of generator and positive potentials.


Author(s):  
Timothy Duignan ◽  
Gregory K. Schenter ◽  
John Fulton ◽  
Thomas huthwelker ◽  
mahalingam balasubramanian ◽  
...  

<div><div><div><p>The ability to reproduce the experimental structure of water around the sodium and potassium ions is a key test of the quality of interaction potentials due to the central importance of these ions in a wide range of important phenomena. Here, we simulate the Na+ and K+ ions in bulk water using three density functional theory functionals: 1) The generalized gradient approximation (GGA) based dispersion corrected revised Perdew, Burke, and Ernzerhof functional (revPBE-D3) 2) The recently developed strongly constrained and appropriately normed (SCAN) functional 3) The random phase approximation (RPA) functional for potassium. We compare with experimental X-ray diffraction (XRD) and X-ray absorption fine structure (EXAFS) measurements to demonstrate that SCAN accurately reproduces key structural details of the hydra- tion structure around the sodium and potassium cations, whereas revPBE-D3 fails to do so. However, we show that SCAN provides a worse description of pure water in comparison with revPBE-D3. RPA also shows an improvement for K+, but slow convergence prevents rigorous comparison. Finally, we analyse cluster energetics to show SCAN and RPA have smaller fluctuations of the mean error of ion-water cluster binding energies compared with revPBE-D3.</p></div></div></div>


2019 ◽  
Author(s):  
Timothy Duignan ◽  
Gregory K. Schenter ◽  
John Fulton ◽  
Thomas huthwelker ◽  
mahalingam balasubramanian ◽  
...  

<div><div><div><p>The ability to reproduce the experimental structure of water around the sodium and potassium ions is a key test of the quality of interaction potentials due to the central importance of these ions in a wide range of important phenomena. Here, we simulate the Na+ and K+ ions in bulk water using three density functional theory functionals: 1) The generalized gradient approximation (GGA) based dispersion corrected revised Perdew, Burke, and Ernzerhof functional (revPBE-D3) 2) The recently developed strongly constrained and appropriately normed (SCAN) functional 3) The random phase approximation (RPA) functional for potassium. We compare with experimental X-ray diffraction (XRD) and X-ray absorption fine structure (EXAFS) measurements to demonstrate that SCAN accurately reproduces key structural details of the hydra- tion structure around the sodium and potassium cations, whereas revPBE-D3 fails to do so. However, we show that SCAN provides a worse description of pure water in comparison with revPBE-D3. RPA also shows an improvement for K+, but slow convergence prevents rigorous comparison. Finally, we analyse cluster energetics to show SCAN and RPA have smaller fluctuations of the mean error of ion-water cluster binding energies compared with revPBE-D3.</p></div></div></div>


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