The Journal of General Physiology
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Published online September 24, 2007
doi:10.1085/jgp.200709783
The Journal of General Physiology, Vol. 130, No. 4, 389-398
The Rockefeller University Press, 0022-1295 $30.00
© 2007 Petrushanko et al.
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ARTICLE

 Oxygen-induced Regulation of Na/K ATPase in Cerebellar Granule Cells



Irina Yu. Petrushanko1,2, Nikolai B. Bogdanov1,3, N. Lapina1, Alexander A. Boldyrev3, Max Gassmann1, and Anna Yu. Bogdanova1

1 Institute of Veterinary Physiology, Vetsuisse Faculty and Zurich Centre of Integrative Human Physiology (ZIHP), University of Zurich, Zurich CH-8057, Switzerland
2 Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia
3 International Biotechnological Center of Lomonosov, Department of Biochemistry, Moscow State University, Moscow, 119992 Russia

Correspondence to Anna Yu. Bogdanova: annab{at}access.unizh.ch

Adjustment of the Na/K ATPase activity to changes in oxygen availability is a matter of survival for neuronal cells. We have used freshly isolated rat cerebellar granule cells to study oxygen sensitivity of the Na/K ATPase function. Along with transport and hydrolytic activity of the enzyme we have monitored alterations in free radical production, cellular reduced glutathione, and ATP levels. Both active K+ influx and ouabain-sensitive inorganic phosphate production were maximal within the physiological pO2 range of 3–5 kPa. Transport and hydrolytic activity of the Na/K ATPase was equally suppressed under hypoxic and hyperoxic conditions. The ATPase response to changes in oxygenation was isoform specific and limited to the {alpha}1-containing isozyme whereas {alpha}2/3-containing isozymes were oxygen insensitive. Rapid activation of the enzyme within a narrow window of oxygen concentrations did not correlate with alterations in the cellular ATP content or substantial shifts in redox potential but was completely abolished when NO production by the cells was blocked by L-NAME. Taken together our observations suggest that NO and its derivatives are involved in maintenance of high Na/K ATPase activity under physiological conditions.

Abbreviations used in this paper: DAF-FM DA, 4-amino-5- methylamino-2',7'-difluorofluorescein diacetate; GSH, reduced glutathione; GSSG, oxidased glutathione; H2DCF-DA, 2,7-dichlorodihydrofluorescein diacetate; MPG, mercaptopropionyl glycine; ß-NADH-Na2, ß-nicotinamide adenine dinucleotide, reduced disodium salt; L-NAME, N{omega}-nitro-L-arginine; NOS, nitric oxide syntase; PI, propidium iodide; TCA, trichloracetic acid.


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