We studied the effect of various detergents (Tween-20, Triton X-100, and sodium deoxycholate) on activity and magnesium-dependent properties of Na+,K+-ATPase of the crude membrane fraction of rat cerebral cortex. All studied detergents significantly increased activity of the studied enzyme in a concentration-dependent manner. Sodium deoxycholate provided significantly higher values Na+,K+-ATPase activity (by ≈50%) than Triton X-100 and Tween-20. In the presence of Triton X-100, a changed pattern of the dependence of enzyme activity on the concentration of magnesium ions in the incubation solution was noted. Separate measurement of activities of Na+,K+-ATPase isoforms made it possible to assume that changes in magnesium-dependent properties are due to the predominant effect of Triton X-100 on ouabain-sensitive α2- and α3-isoforms.
Similar content being viewed by others
References
Kravtsova VV, Petrov AM, Vasil’ev AN, Zefirov AL, Krivoi II. Role of cholesterol in the maintenance of endplate electrogenesis in rat diaphragm. Bull. Exp. Biol. Med. 2015;158(3):298-300. https://doi.org/10.1007/s10517-015-2745-8
Ahyayauch H, Bennouna M, Alonso A, Goñi FM. Detergent effects on membranes at subsolubilizing concentrations: transmembrane lipid motion, bilayer permeabilization, and vesicle lysis/reassembly are independent phenomena. Langmuir. 2010;26(10):7307-7313. https://doi.org/10.1021/la904194a
Apell HJ, Hitzler T, Schreiber G. Modulation of the Na,KATPase by magnesium ions. Biochemistry. 2017;56(7):1005-1016. https://doi.org/10.1021/acs.biochem.6b01243
Chu Y, Parada I, Prince DA. Temporal and topographic alterations in expression of the alpha3 isoform of Na+, K+-ATPase in the rat freeze lesion model of microgyria and epileptogenesis. Neuroscience. 2009;162(2):339-348. https://doi.org/10.1016/j.neuroscience.2009.04.003
Cornelius F, Habeck M, Kanai R, Toyoshima C, Karlish SJ. General and specific lipid-protein interactions in Na,KATPase. Biochim. Biophys. Acta. 2015;1848(9):1729-1743. https://doi.org/10.1016/j.bbamem.2015.03.012
Gatto C, Arnett KL, Milanick MA. Divalent cation interactions with Na,K-ATPase cytoplasmic cation sites: implications for the para-nitrophenyl phosphatase reaction mechanism. J. Membr. Biol. 2007;216(1):49-59. https://doi.org/10.1007/s00232-007-9028-x
Habeck M, Haviv H, Katz A, Kapri-Pardes E, Ayciriex S, Shevchenko A, Ogawa H, Toyoshima C, Karlish SJD. Stimulation, inhibition, or stabilization of Na,K-ATPase caused by specific lipid interactions at distinct sites. J. Biol. Chem. 2015;290(8):4829-4842. https://doi.org/10.1074/jbc.M114.611384
Habeck M, Kapri-Pardes E, Sharon M, Karlish SJ. Specific phospholipid binding to Na,K-ATPase at two distinct sites. Proc. Natl Acad. Sci. USA. 2017;114(11):2904-2909. https://doi.org/10.1073/pnas.1620799114
Jorgensen PL, Hakansson KO, Karlish SJ. Structure and mechanism of Na,K-ATPase: functional sites and their interactions. Annu. Rev. Physiol. 2003;65:817-849. https://doi.org/10.1146/annurev.physiol.65.092101.142558
Koley D, Bard AJ. Triton X-100 concentration effects on membrane permeability of a single HeLa cell by scanning electrochemical microscopy (SECM). Proc. Natl Acad. Sci. USA. 2010;107(39):16783-16787. https://doi.org/10.1073/pnas.1011614107
Lopez LB, Quintas LE, Noël F. Influence of development on Na(+)/K(+)-ATPase expression: isoform- and tissue-dependency. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 2002;131(2):323-333. https://doi.org/10.1016/s1095-6433(01)00482-2
Lopina OD, Tverskoi AM, Klimanova EA, Sidorenko SV, Orlov SN. Ouabain-induced cell death and survival. Role of α1-Na,K-ATPase-mediated signaling and [Na+]i/[K+]i-dependent gene expression. Front. Physiol. 2020;11:1060. https://doi.org/10.3389/fphys.2020.01060
Matchkov VV, Krivoi II. Specialized functional diversity and interactions of the Na,K-ATPase. Front. Physiol. 2016;7:179. https://doi.org/10.3389/fphys.2016.00179
Retamales-Ortega R, Vio CP, Inestrosa NC. P2C-type ATPases and their regulation. Mol. Neurobiol. 2016;53(2):1343-1354. https://doi.org/10.1007/s12035-014-9076-z
Taguchi K, Kumanogoh H, Nakamura S, Maekawa S. Ouabain-induced isoform-specific localization change of the Na+, K+-ATPase alpha subunit in the synaptic plasma membrane of rat brain. Neurosci. Lett. 2007;413(1):42-45. https://doi.org/10.1016/j.neulet.2006.11.061
Author information
Authors and Affiliations
Corresponding author
Additional information
Translated from Byulleten’ Eksperimental’noi Biologii i Meditsiny, Vol. 171, No. 5, pp. 583-587, May, 2021
Rights and permissions
About this article
Cite this article
Dubrovskii, V.N., Orlova, L.A. Effect of Detergents on Activity and Magnesium-Dependent Properties of Different Isoforms of Na+,K+-ATPase in the Crude Membrane Fraction of Rat Cerebral Cortex. Bull Exp Biol Med 171, 611–614 (2021). https://doi.org/10.1007/s10517-021-05279-0
Received:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10517-021-05279-0