Abstract
Mammalian cells are surrounded by a fluid medium that contains a high concentration of sodium and a low concentration of potassium. In contrast, the cell cytoplasm is high in potassium and low in sodium. To maintain this chemical gradient, the cell must transport excess sodium out of, and potassium into, the cell. The mechanism underlying this phenomenon was first proposed by (1941), who realized that there must be active sodium excretion to control intracellular sodium levels in skeletal muscle. (1953) showed that the sodium and potassium fluxes across red blood cell membranes are dependent on adenosine triphosphate (ATP), and that these fluxes can be inhibited by cardiac glycosides. The idea of an “active” ion transport mechanism (ion pump) was thus formulated. Subsequent studies by (1957) have indicated that there is a Mg2+-dependent adenosine triphosphatase (Mg2+-ATPase) in the microsomal fraction of crab nerve that is markedly activated by the concurrent presence of sodium and potassium ions. Twenty-six years have lapsed since this original observation, and it is now accepted that the enzyme system described by (1957) is responsible for the active transport of sodium and potassium across the cell membrane. The enzyme system was named Na+, K+-activated, Mg2+-dependent adenosine triphosphatase (Na+/K+-ATPase) (EC 3.6.1.3).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Ahmed K. and Judah J. D. (1964) Preparation of lipoproteins containing cation-dependent ATPase. Biochim. Biophys. Acta 93, 603–613.
Ahmed K. and Judah J. D. (1965) Identification of active phosphoprotein in a cation-activated adenosine triphosphatase. Biochim. Biophys. Acta 104, 112–120.
Ahmed K., Judah J. D., and Scholefield P. G. (1966) Interaction of sodium and potassium with a cation-dependent adenosine triphosphatase system from rat brain. Biochim. Biophys. Acta 120, 351–360.
Akagawa K. and Tsukuda Y. (1979) Presence and characteristics of catecholamine-sensitive Na-K ATPase in rat striatum. J. Neurochem. 32, 269–271.
Akera T. and Brody T. M. (1968) Inhibition of brain sodium-and potassium-stimulated adenosine triphosphatase activity by chlorpromazine free radical. Mol Pharmacol. 4, 600–612.
Akera T. and Brody T. M. (1969) The interaction between chlorpromazine free radical and microsomal sodium-and potassium-activated adenosine triphosphatase from rat brain. Mol. Pharmacol. 5, 605–614.
Akera T. and Brody T. M. (1970) Inhibitory sites on sodium-and potassium-activated adenosine triphosphatase for chlorpromazine free radical and ouabain. Mol. Pharmacol. 6, 557–566.
Akera T. and Brody T. M. (1971) Membrane adenosine triphosphatase. The effect of potassium on the formation and dissociation of the ouabain-enzyme complex. J. Pharmacol. Exp. Ther. 176, 545–557.
Akera T., Rech R. H., Marquis W.J., Tobin T., and Brody T. M. (1973) The lack of relationship between brain Na+, K+-activated adenosine triphosphatase and the development of tolerance to ethanol in rats. J. Pharmacol Exp. Ther. 185, 594–601.
Albers R. W (1967) Biochemical aspects of active transport. Ann Rev. Biochem 36, 727–756.
Albers R W., Koval G. J., and Siegel G. J. (1968) Studies on the interaction of ouabain and other cardioactive steroids with sodium-potassium-activated adenosine triphosphatase. Mol. Pharmacol. 4, 324–326.
Albers R. W., Rodriguez de Lores G., and De Robertis E. (1965) Sodium-potassium-activated ATPase and potassium-activated p-nitro-phenylphosphatase: A comparison of their subcellular localizations in rat brain Proc. Natl. Acad Sci USA 53, 557–564.
Alexander D. R. and Rodnight R. (1970) Separation at neutral pH of a 32P-labelled membrane protein associated with the sodium-plus-magnesium ion-activated adenosine triphosphatase from ox brain. Biochemistry J. 119, 44–45P
Ames G. F. L. (1974) Resolution of bacterial protein by polyacrylamide gel electrophoresis on slabs membrane, soluble and periplasmic fractions. J. Biol Chem. 249, 634–644.
Asano Y., Tashima Y., and Matsui H. (1970) (Na plus minus K plus)-ATPase from the frog bladder and its relationship to sodium transport. Biochim Biophys. Acta 219, 169–178.
Askari A. and Huang W. (1980) Na+, K+-ATPase: Half-of-the subunits cross-linking reactivity suggests an oligomeric structure containing a mimmum of four catalytic subunits. Biochem. Biophys. Res. Commun. 93, 448–453.
Askari A. and Huang W. (1981) Na+, K+-ATPase in (Ca2+ + ouabain)-dependent phosphorylation by Pi. FEBS Lett. 126, 215–218.
Atkinson A. and Lowe A. G. (1972) The pH dependence of the effects of Na+, pK+ and ouabain on the ATPase activity of NaI-treated brain microsomes with Mg2+, Mn2+, Ca2+ and Zn2+ as divalent metal activators. Biochim. Biophys Acta 266, 103–115.
Atkinson A., Hunt S., and Lowe A. G. (1968) Manganese activation of a (Na + K)-dependent ATPase in pig brain microsomes. Biochim. Biophys. Acta 167, 469.
Avruch J. and Fairbanks G. (1972) Demonstration of a phosphopeptide intermediate, Na+-and K+-stimulated adenosine triphosphatase reaction of the erythrocyte membrane. Proc. Natl. Acad. Sci. USA 69, 1216–1220.
Banerjee S. P. and Sen A. K (1969) On the mechanism of inhibition of (Na + K)-ATPase by N-ethylmaleimide and ethacrynic acid. Fed. Proc. 28, 589.
Banerjee S. P. and Sen A. K. (1970) Inhibition of sodium-and potassium-dependent adenosine triphosphatase by ethacrynic acid: Two modes of action. Mol Pharmacol. 6, 680–690.
Banerjee S. P. and Sharma V. K. (1978) 3H-ouabain binding to peripheral organs of cats. Effects of ethanol. Br. J. Pharmacol. 62, 475–479.
Banerjee S. P., Wong S. M. E., and Sen A. K. (1970) Differentiation between two conformations of (Na + K)-ATPase by N-ethylmaleimide. Fed. Proc. 29, 723.
Barnett R. E. (1970) Effect of monovalent cations on the ouabain inhibition of the sodium and potassium ion activated adenosine triphosphatase. Biochemistry 9, 4644–4648.
Beauge L. A. and Glynn I. M. (1978) Commercial ATP containing traces of vanadate alters the response of (Na+ + K′) ATPase to external potassium. Nature 272, 551–552.
Bond G. H. and Hudgins P. M. (1979) Kinetics of inhibition of Na+, K+-ATPase by Mg2+, K+ and vanadate. Biochemistry 18, 325–331.
Bonting S. L. (1970) Sodium-Potassium Activated Adenosine Triphosphatase and Cation Transport, in Membrane Ion Transport, Vol. I. (Bittar E. E., ed.), Wiley Interscience, New York.
Bonting S. L., Simon K. A., and Hawkins N. M. (1961) Studies on sodium-potassium-activated adenosine triphosphatase. I. Quantitative distribution in several tissues of the cat. Arch. Biochem. Biophys. 95, 416–423.
Breer H. and Jeserich G. (1979) Ganglioside interaction with synaptosomal membranes, in Glyco-Conjugates, Proceedings of the 5th International Symposium (Schauer R., Booer P., Buddecke E., Kramer M. F., Vliegenthart J. C. G., and Wiegandt H. eds.), pp. 575–575, Georg Thieme, Stuttgart.
Britten J. S. and Blank M. (1968) Thallium activation of the (Na+ + K+)-activated ATPase of rabbit kidney. Biochim. Biophys. Acta 159, 160–166.
Brodsky W. A. and Shamoo A. E. (1973) Binding of ATP to and release from microsomal Na+, K+-ATPase. Biochim. Biophys. Acta 291, 208–228.
Brodsky W. and Sohn R. J, (1974) Acid-stable and heat-stable phosphoenzyme complex of (Na+ + K+)-ATPase in the eel electric organ, and the related concept of active Na transport. Ann. NY Acad. Sci 242, 106–119.
Cantley L. C., Jr. and Josephson L. (1976) A slow interconversion between active and inactive states of (Na-K)-ATPase. Biochemistry 15, 5280–5287.
Cantley L. C., Cantley L. G., and Josephson L. (1978a) A characterization of vanadate interactions with the (Na-K)-ATPase mechanistic and regulatory implications. J. Biol. Chem. 253, 7361–7368.
Cantley L. C., Ferguson J. H., and Kustin K. (1978b) Norepinephrine complexes and reduces vanadium (V) to reverse vanadate inhibition of the (Na-K)-ATPase. J. Am. Chem. Soc. 100, 5210–5212.
Cantley L. C., Jr., Josephson L., Warner R., Yanacisawa M., Lechene C., and Guidotti G. (1977) Vanadate is a potent (Na-K)-ATPase inhibitor found in ATP derived from muscle. J. Biol. Chem. 252, 7421–7423.
Caputto R., Maccloni A. H. R., and Caputto B. I. (1977) Activation of deoxycholate-solubilized adenosine triphosphatase by ganglioside and aslaloganglioside preparations. Biochem. Biophys. Res. Commun. 74, 1046–1052.
Chan S. L. and Quastel J. H (1970) Effects of neurotropic drugs on sodium influx into rat brain cortex in vitro. Biochem Pharmacol 19, 1071–1085.
Charney A. N., Silva P., and Epstein F. H. (1975) An in vitro inhibitor of Na-K-ATPase present in an adenosine triphosphate preparation. J. Appl. Physiol. 39, 156–158.
Charnock J. S., Rosenthal A. S., and Post R. L. (1963) Studies of the mechanism of cation transport. II. A phosphorylated intermediate in the cation-stimulated enzymic hydrolysis of adenosine triphosphate. Aust. J. Exp. Biol. Med. Sci. 41, 675–686.
Cheng E Y. and Cutkomp L. K (1975) The ATPase system in American cockroach muscle and nerve cord. Insect. Biochem. 5, 421–427.
Chow Y. R. and Akera T. (1978) Membrane (Na+, K+)-ATPase of canine brain, heart and kidney Tissue-dependent differences in kinetic properties and the influence of purification procedures. Biochim. Biophys. Acta 508, 313–327
Collins R. C. and Albers R. W. (1972) The phosphoryl acceptor protein of Na-K-ATPase from various tissues J Neurochem. 19, 1209–1213.
Collins J. H., Forbush B., III, Lane L. K., Ling E., Schwartz A., and Zot A. (1982) Purification and characterization of an (Na+ + K+)-ATPase proteolipid labelled with a photoaffinity derivative of ouabain. Biochim Biophys. Acta 686, 7–12.
Cortas N. and Walser M. (1971) Sodium-potassium dependent ATPase in toad bladder: Novel response to ouabain. Fed. Proc. 30, 331.
Cummins J. and Hyden H. (1962) Adenosine triphosphate levels and adenosine triphosphatases in neurons, glia and neuronal membranes of the vestibular nucleus. Biochim. Biophys Acta 60, 271–283.
Cutkomp L. K., Yap H. H., Vea E. U., and Koch R. B. (1971) Inhibition of oligomycin-sensitive (mitochondrial) Mg2+-ATPase by DDT and selected analogs in fish and insect tissue. Life Sci. 10, 1201–1209.
Dahl J. L. and Hokin L. E. (1974) The sodium-potassium adenosine-triphosphatase. Ann. Rev Biochem. 43, 327–356.
Daly J. (1977) Cyclic Nucleotides in the Nervous System. Plenum, New York
Dean R. B. (1941) Theories of electrolyte equilibrium in muscle. Biol. Symp. 3, 331–348.
Desaiah D. and Ho I. K. (1977) Kinetics of catecholamine sensitive Na+-K+-ATPase activity in mouse brain synaptosomes. Biochem. Pharmacol. 26, 2029–2035.
Desaiah D. and Koch R. B. (1975) Inhibition of fish brain ATPases by aldrin-transdiol, aldrin, dieldrin and photodieldrin. Biochem Biophys. Res. Commun. 64, 13–19.
Duggan D. E. and Noll R. M. (1965) Effects of ethacrynic acid and cardiac glycosides upon a membrane adenosine triphosphatase of renal cortex. Arch. Biochem Biophys 109, 388–396.
Dunham E. T. and Glynn I. M. (1961) Adenosine triphosphatase activity and the active movements of alkali metal ions. J. Physiol. (Lond.) 156, 274–293.
Eayrs J. T. (1955) The cerebral cortex of normal and hypothyroid rats. Acta Anat. (Basel) 25, 160–163.
Epstein F. H. and Whittam R (1966) The mode of inhibition by calcium of cell-membrane adenosine triphosphatase activity. Biochem. J. 99, 232–238.
Fagan J. B and Racker E. (1977) Reversible inhibition of (Na+-K+)-ATPase by Mg2+, adenosine triphosphate and K. Biochemistry 16, 152–158.
Fahn S. and Cote L. J, (1968) Regional distribution of sodium-potassium activated adenosine triphosphatase in the brain of the Rhesus monkey. J. Neurochem. 15, 433–436.
Fahn S. Hurley M. R., Koval G. J., and Albers R. W. (1966a) Sodium-potassium-activated adenosine triphosphatase of Electrophorus electric organ. J Biol. Chem. 241, 1890–1895.
Fahn S., Koval G. J, and Albers R. W. (1966b) Sodium-potassium-activated adenosine triphosphatase of Electrophorus electric organ. J Biol. Chem. 241, 1882–1889.
Festoff B W. and Appel S. H. (1968) Effect of diphenylhydantoin on synaptosome Na+, K+-ATPase. J Clin. Invest. 47, 2752–2758.
Fiske C. H. and Subbarow Y. (1925) The calorimetric determination of phosphorus. J. Biol. Chem. 66, 375–400.
Fishman P. H., Moss J., and Vaughan M. (1976) Uptake and metabolism of gangliosides in transformed mouse fibroblasts. Relationship of ganglioside structure to choleragen response. J Biol. Chem. 251, 4490–4494
Folmar L. C (1978) In vitro inhibition of rat brain ATPase, PNPPase and ATP-32Pi exchange by chlorinated-diphenyl ethanes and cyclodiene insecticides. Bull Environ Contam Tox 19, 481–487
Forbush B., III, Kaplan J H, and Hoffman J. F. (1978) Characterization of a new photoaffinity derivative of ouabain: Labelling of the large polypeptide and of a proteolipid component of the Na,K-ATPase. Biochemisty 17, 3667–3676.
Formby B. (1975) Age-dependent changes in (Na,K)-ATPase in brains of mice susceptible to seizures. Experientia 31, 315–316.
Froehlich J. P., Albers R. W., Koval G. J., Goebel R., and Berman M. (1976) Evidence for a new intermediate state in the mechanism of (Na+ + K+)-adenosine triphosphatase. J. Biol. Chem. 251, 2186–2188.
Fukushima Y. and Tonomura Y. (1973) Two kinds of high energy phosphorylated intermediate, with and without bound ADP in the reaction of Na+-K+-dependent ATPase. J. Biochem. (Tokyo) 74, 135–142.
Geel S. E., Valcana T., and Timiras P. S. (1967) Effect of neonatal hypothyroidism and of thyroxine on l-(14C)-lucine incorporation in protein in vivo and the relationship to ionic levels in the developing brain of the rat. Brain Res. 4, 143–150.
Gilbert J. G, Wyllie M. G., and Davison D. V. (1975) Nerve terminal ATPase as possible trigger for neurotransmitter release. Nature 255, 237–238.
Giotta G. J. (1975) Native (Na+ + K+)-dependent adenosine triphosphatase has two trypsin-sensitive sites. J Biol Chem 250, 5159–5164.
Glick N. B. (1972) Inhibition of Transport Reactions. A. Inhibitors of ATPase. NaK-ATPase and Related Enzymic Activities, in Metabolic Inhibitors (Quastel J. H., Kates M., and Hochester R. M., eds.), Academic, New York, London.
Glynn I. M. (1957) The action of cardiac glycosides on sodium and potassium movements in human red cells. J. Physiol. (Lond.) 136, 148–173.
Glynn I. M. (1963) Transport of adenosine triphosphatase in electric organ. The relation between ion transport and oxidative phosphorylation. J Physiol. (Lond.) 169, 452–465.
Godfraind T., Koch M.-C., and Verbeke N. (1974) The action of EGTA on the catecholamines stimulation of rat brain Na-K-ATPase. Biochem. Pharmacol 23, 3505–3511.
Grasso A. (1967) A sodium-and potassium-stimulated adenosine triphosphatase in the cockroach nerve cord. Life Sci. 6, 1911–1918.
Green I. and Mommaerts W. F. H. M. (1953) Adenosine triphosphatase systems of muscle. I. An electrotitrimetic method of measurement. J. Biol. Chem. 202, 541–549.
Gurd F. R. N and Murray G. R., Jr (1954) Preparation and properties of serum and plasma proteins. XXXIX. The interaction of human serum albumin with plumbous ions. J. Am. Chem Soc 76, 187–190.
Hackenberg H. and Krieglstein J. (1972) Comparative study on the inhibition of Na+, K+-ATPase by chlorpromazine, promazine, imipramine and their monodesmethyl metabolites. Naunyn-Schmiedebergs Arch. Pharmacol. 247, 63–73.
Hansen O. (1976) Non-uniform populations of g-strophanthin binding sites of (Na+ + K+)-activated: ATPase apparent conversion to uniformity by K+. Biochim. Biophys. Acta 433, 383–392.
Hart W. M., Jr. and Titus E. O. (1973a) Isolation of a protein component of sodium-potassium transport: Adenosine triphosphatase containing ligand-protected sulfhydryl groups. J. Biol. Chem. 248, 1365–1371.
Hart W. M., Jr. and Titus E. O. (1973b) Sulfhydryl groups of Na+, K+-ATPase: Protection by physiological ligands and exposure by phosphorylation. J. Biol Chem. 248, 4674–4681.
Hasie R. J. A. (1965) The localization of adenosine triphosphatases in morphologically characterized subcellular fractions of guinea-pig brain. Biochem. J. 96, 404–412.
Heinz E. and Hoffman J. F. (1965) Phosphate incorporation and Na, K-ATPase activity in human red blood cell ghosts. J. Cell Comp. Physiol. 65, 31–43.
Herd P. A., Horwitz B. A., and Smith R. E. (1970) Norepinephrine-sensitive Na+/K+-ATPase activity in brown adipose tissue. Experientia 26, 825–826
Hertz L., Schousboe A., Formby B., and Lennox-Buchthal M. (1974) Some age-dependent biochemical changes in mice susceptible to seizures. Epilepsia 15, 619–631.
Hexum T. D. (1974) Studies on the reaction catalyzed by transport (Na,K) adenosine triphosphatase. I. Effects of divalent metals. Biochem. Pharmacol. 23, 3441–3447.
Hexum T. D. (1977) The effect of catecholamines on transport (Na,K) adenosine triphosphatase. Biochem. Pharmacol. 26, 1221–1227.
Hoffman J. F. (1962) The active transport of sodium by ghosts of human red blood cells. J Gen. Physiol. 45, 837–859.
Hokin L. E. (1973) Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. X. Purification of the enzyme from the rectal gland of Squalus acanthias. J. Biol. Chem. 248, 2593–2605.
Hokin L. W. and Hokin M. R. (1963) Biological transport. Ann. Rev. Biochem 32, 553–578.
Hokin L. E., Dahl J. L., Deupree J. D., Dixon J. F., Hackney J. F., and Perdue J. F. (1973) Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. X. Purification of the enzyme from the rectal gland of Squalus acanthias J. Biol. Chem 248, 2593–2605.
Huang W. and Askari A. (1978) Na,K+-ATPase: On the nature of the “cross-1mked” subunit obtained in the presence of O-phenanthroline and cupric ion. Biochem. Biophys. Res. Commun. 82, 1314–1319.
Huang W and Askari A (1979) Na+,K+-ATPase: Effects of detergents on the cross-linking of subunit in the presence of Cu2+ and O-phenanthroline Biochim. Biophys. Acta 578, 547–552.
Hudgins P. M. and Bond G. H. (1977) (Mg2+ + K+)-dependent inhibition of Na,K-ATPase due to a contaminant in equine muscle ATP. Biochem Biophys. Res. Commun. 77, 1024–1029.
Israel M. A. and Kuriyama K. (1971) Effect of in vivo ethanol administration on adenosine triphosphatase activity of subcellular fractions of mouse brain and liver. Life Sci. 10, 591–599.
Iwangoff P., Enz A., and Chappeus A. (1974) Effect of adrenergic blockers on the activation of brain ATPase by noradrenaline. Experientia 30, 688.
Jarnefelt J. (1961) Inhibition of the brain microsomal ATPase by depolarizing agents. Biochim Biophys Acta 48, 111–116.
Jarnefelt J. (1964) Conversion of the Na+ and K+ independent art of the brain microsomal ATPase to a form requiring added Na+ and K+. Biochem Biophys Res Commun 17, 330–334.
Jean D. H. and Albers R. W (1976) Immunochemical studies on the large polypeptide of Electrophorous electroplax (Na+ + K+)-ATPase. Biochim. Biophys. Acta 452, 219–226.
Johnstone R. M. (1963) Sulfhydryl Agents, Arsenicals, in Metabolic In-hibitors, Vol. 2. (Hochster R. M. and Quastel J H., eds.), Academic, New York.
Jones V. D., Lockett G., and Landon E. J. (1965) A cellular action of mercurial diuretics. J Pharmacol. Exp Ther. 147, 23–31.
Jorgensen P. L. (1974) Purification of Na+,K+-ATPase: Active site determination of criteria of purity. Ann. NY Acad. Sci. 242, 36–52.
Jorgensen P. L. and Skou J. C. (1971) Purification and characterization of (Na+ + K+)-ATPase. I. The influence of detergents on the activity of (Na+ + K+)-ATPase in preparations from the outer medulla of rabbit kidneys. Biochim. Biophys. Acta 233, 366–380.
Josephson L. and Cantley L. C. (1977) Isolation of a potent (Na-K)-ATPase inhibitor from striated muscle. Biochemistry 16, 4572–4578.
Kahlenberg A., Dulak N. C., Dixon J. F., Galsworthy P. R., and Hokin L. E. (1969) Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. V. Partial purification of the Lubrol-solubilized beef brain enzyme. Arch. Biochem. Biophys. 131, 253–262.
Kahlenberg A., Galsworthy P. R., and Hokin L. E. (1968) Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. II. Characterization of the acyl phosphate intermediate as an l-glutamyl-gamma-phosphate residue. Arch. Biochem. Biophys. 126, 331–324.
Kanazawa T., Saito M., and Tonomura Y. (1967) Properties of a phosphorylated protein as a reaction intermediate of Na+-K+-sensitive ATPase. J. Biochem. (Tokyo) 61, 555–566.
Kanazawa T., Saito M., and Tonomura Y. (1970) Formation and decomposition of a phosphorylated intermediate in the reaction of Na+-K+-dependent ATPase. J. Biochem. (Tokyo) 67, 693–711.
Karlish S. J, (1980) Characterization of conformational changes in (Na,K)-ATPase labelled with fluorescein at the active site. J. Bioenerg. Biomemb. 12, 111–136.
Klara P. M., Brizzee K. R., Chen I.-Li, and Yates R. D. (1978) Ultrastructural localization of ATPase activity in the dog area postrema. Brain Res. 146, 165–171.
Klotz I. M., Urquhart J. M., and Fiess H. A. (1952) Interactions of metal ions with the sulfhydryl group of serum albumin. J. Am. Chem Soc. 74, 5537–5538.
Knox W. H., Perrier R. G., and Sen A. K. (1972) Effect of chronic admmistration of ethanol on Na+,K+-ATPase activity in areas of the cat brain. J. Neurochem. 19, 2881–2884.
Koch R. B. (1969) Fractionation of olfactory tissue homogenates. Isolation of a concentrated plasma membrane fraction. J. Neurochem. 16, 145–157.
Koch R. B., Cutkomp L. K., and Do F. M. (1969) Chlorinated hydrocarbon insecticide inhibition of cockroach and honey bee ATPases. Life Sci. 8, 289–297.
Kurokawa M., Sakamoto T., and Kato M. (1965) Distribution of sodiumplus-potassium-stimulated adenosine-triphosphatase activity in isolated nerve ending particles. Biochem. J. 97, 833–844.
Kyte J. (1971) Phosphorylation of a purified (Na+ + K+) adenosine triphosphatase. Biochem Biophys. Res. Commun. 43, 1259–1265.
Kyte J. (1972) Properties of the two polypeptides of sodium and potassium-dependent adenosine triphosphatase. J. Biol. Chem. 247, 7642–7649.
Kyte J. (1975) Structural studies of sodium and potassium ion-activated adenosine triphosphatase. The relationship between molecular structure and the mechanism of active transport. J. Biol. Chem. 250, 7443–7449.
Kyte J. (1976a) Immunoferritm determination of the distribution of the (Na+,K+)-ATPase over the plasma membranes of renal convoluted tubules. I. Distal segment. J. Cell. Biol. 68, 287–303.
Kyte J (1976b) Immunoferritm determination of the distribution of the (Na+,K+)-ATPase over the plasma membranes of renal convoluted tubules. I. Distal segment. J. Cell. Biol. 68, 304–381.
Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685.
Leon A., Facci L, Toffano G., Sonnino S., and Tettamanti G. (1981) Activation of (Na+,K+)-ATPase by nanomolar concentrations of GM1 ganghoside. J. Neurochem. 37, 350–357.
Liang S. and Winter C. G. (1977) Digitonin-induced changes in subunit arrangement in relation to some in vitro activities of the Na+,K+-ATPase. J. Biol. Chem. 252, 8278–8284.
Lindenmayer G. E., Laughter A. H., and Schwartz A. (1968) Incorporation of inorganic phosphate-32 into a Na+,K+-ATPase preparation. A stimulation by ouabain. Arch. Biochem. Biophys. 127, 187–192.
Lindenmayer G. E. and Schwartz A. (1970) Conformational changes induced in Na+,K+-ATPase by ouabain through a K+-sensitive reduction Kinetic and spectroscopic studies. Arch. Biochem. Blophys. 140, 371–378.
Madsen N. B. (1963) A Comprehensive Treatial, in Metabolic Inhibitors, Vol. 2 (Hochster R. M. and Quastel J. H., eds.), Academic, New York.
Matsumura F. and Patil K. C. (1969) Adenosine triphosphatase sensitive to DDT in synapses of rat brain. Science 166, 121–122.
Medzihardsky F., Kline M. H, and Hokin L. E. (1967) Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. I. Solubilization, stabilization and estimation of apparent molecular weight. Arch. Biochem. Biophys. 121, 311–316.
Millonig G. (1961) Advantages of a phosphate buffer for OsO4 solution in fixation. J. Appl. Physiol. 32, 1637.
Moczydlowski E. G. (1981a) Characterization of 2′,3′-O-(2,4,6-trinitro-cyclohexadienylidene) adenosine 5′-triphosphate as a fluorescent probe of the ATP site of sodium and potassium transport adenosine triphosphatase. Determination of nucleotide binding stoichiometry and ion induced changes in affinity for ATP. J. Biol. Chem. 256, 2346–2356.
Moczydlowski E. G. (1981b) Inhibition of sodium and potassium adenosine triphosphatase by 2′,3′-O-(2,4,6-trinitro-cyclohexadienylidene) adenine nucleotides. Implication for the structure and mechanism of the Na.K pump. J. Biol. Chem 256, 2357–2366.
Nagano K., Kanazawa T., Mizuno N., Tashima Y., Nakao T., and Nakao M. (1965) Some acyl phosphate-like properties of P32-labelled sodium-potassium-activated adenosine triphosphatase. Biochem Biophys. Res. Commun. 19, 759–764.
Ottolenghi P. and Ellory J. C. (1983) Radiation inactivation of (Na,K)-ATPase, an enzyme showmg multiple radiation-sensitrve domains. J. Biol. Chem. 258, 14895–14907.
Partington C. R. and Daly J. W. (1979) Effect of gangliosides on adenylate cyclase activity in rat cerebral cortical membranes. Mol. Pharmacol. 15, 484–491.
Peters R. A., Shorthouse M., and Walshe J. M. (1966) Studies on the toxicity of copper. II. The behaviour of microsomal membrane ATPase of the pigeon’s brain tissue to copper and some other metallic substance. Proc. Roy Soc Ser. B. 166, 285–294
Petrali E. H. and Sulakhe P. V. (1980) Isolation of plasma membrane fraction highly enriched in ouabain-sensitive Na+-K+-ATPase from rat brain white matter. Int. J. Biochem. 12, 407–420.
Phillis J. W. and Wu P. H. (1981) Catecholamines and the sodium pump in excitable cells. Prog. Neurobiol 17, 141–184.
Portuis H. J. and Repke K. (1964) Versuch emer analyse der beziehunge zwischen chemischer struktur und digitalis-ahnlicher wirksamkeit an der zezeptorebene Arzneim. Forsch. 14, 1073–1077.
Post R. L., Kume S., Tobin T., Orcutt B., and Sen A. K. (1969) Flexibility of an active center in sodium-plus-potassium adenosine triphosphatase. J. Gen. Physlol. 54, 306–326
Post R. L., Sen A. K., and Rosenthal A. S. (1965) A phosphorylated intermediate tn adenosine triphosphate-dependent sodium and potassium transport across kidney membranes. J Biol. Chem. 240, 1437–1445.
Powis D. A., Wattus G. D., and Glynn I. (1981) The stimulatory effect of calcium on sodium-potassium ATPase of nervous tissue. FEBS Lett 126, 285–288.
Quastel J. H. (1970) Transport process at the brain cell membrane. Neurosci. Res. 3, 1–41.
Racker E. (1976) Structure and function of ATP-driven ion pumps. Trends Biochem Sci. 1, 244–247.
Rawson M. D. and Pincus J. H. (1968) The effect of diphenylhydantoin on sodium, potassium, magnesium-activated adenosine triphosphatase in microsomal fraction of rat and guinea pig brain and on whole homogenates of human brain. Biochem. Pharmacol. 17, 573–579.
Reichert W. H. (1975) Cerebral magnesium and sodium-potassium ATPase following audiogenic seizure in mice. Exp. Neurol. 49, 596–600.
Rendi R. and Uhr M. L (1964) Sodium, potassium-requiring adenosine triphosphatase activity. I. Purification and properties. Biochim. Biophys. Acta 89, 520–531.
Riehl R. (1980) Ultracytochemical localization of Na+, K+-activated ATPase in the oocytes of Heterandria formosa Agassiz, 1853 (Pisces, Poecilliadae). Reprod Nutr. Develop. 20, 191–196.
Robinson J. D., Lowinger J., and Bettinger B. (1968) Chlorpromazine: differential effects on membrane-bound enzymes from rat brain. Biochem Pharmacol. 17, 1113–1116.
Rodriguez de Lores Arnaiz G. and Mistrorigo de Pacheco M. (1978) Regulation of (Na+,K+) adenosine triphosphatase of nerve ending membranes. Action of norepinephrine and a soluble factor. Neurochem. Res. 3, 733–744.
Rosenblatt D. E., Lauter C. J., and Trams E. G. (1976) Deficiency of a Ca2+-ATPase in brains of seizure-prone mice. J. Neurochem. 27, 1299–1304.
Ruoho A and Kyte J. (1974) Photoaffinity labelling of the ouabain-binding site on (Na+ + K+) adenosine triphosphatase. Proc Natl Acad. Sci. USA 71, 2352–2356.
Schaefer A., Komlos M., and Seregi A. (1975) Lipid peroxidation as the cause of the ascorbic acid-induced decrease of adenosine triphosphatase activities of rat brain microsomes and its inhibition by biogenic amines and psychotropic drugs. Biochem Pharmacol. 24, 1781–1786.
Schaefer A., Seregi A., and Komlos M. (1974) Ascorbic acid-like effect of the soluble fraction of rat brain on adenosine triphosphatase and its relation to catecholamines and chelating agents. Biochem. Pharmacol. 23, 2257–2271.
Schaefer A., Unyi G., and Pfeifer A. K. (1972) The effects of a soluble factor and of catecholamines on the activity of adenosine triphosphatase in subcellular fractions of rat brain. Biochem. Pharmacol. 21, 2289–2294.
Schatzmann H. J. (1953) Herzglykoside als hemmstoffe fur der aktiven kalium-und natriumtransport durch dei Erythrocytenmembran. Helv Physiol. Pharmac. Acta 11, 346–354.
Schirachi D. Y., Allard A. A., and Trevor A. J. (1970) Partial purification and ouabain sensitivity of Lubrol-extracted sodium-potassium transport adenosine triphosphatases from brain and cardiac tissue. Biochem. Pharmacol. 19, 2893–2906.
Schurmans-Stekhovens F. and Bonting S. L. (1981) Transport adenosine triphosphatase: Properties and functions. Physiol. Rev. 61, 1–76.
Schwartz A., Bachelard H S., and McIlwain H (1962) The sodium, potassium-stimulated adenosine triphosphatase activity and other properties of cerebral microsomal fractions and subfractions. Biochem J. 84, 626–637.
Schwartz A., Lindenmayer G. F, and Allen J. C. (1975) The sodium-potassium adenosine triphosphatase. Pharmacological, physiological and biochemical aspects. Pharmacol. Rev. 27, 3–134.
Schwartz A., Matsui H., and Laughter A. H. (1968) Tritrated digoxin binding to Na+,K+-activated adenosine triphosphatase: Possible allosteric site. Science 159, 323–325.
Seiler F. R., Sedlacek N. N., Luben G., and Wiegandt H. (1976) Alteration of the lymphocyte surface by vibrio cholerae neuraminidase, gangliosides and lysolecithins. Behring Inst. Mitt. 59, 22–29.
Sen A. K., Tobin T., and Post R. L. (1969) A cycle for ouabain inhibition of sodium-and potassium-dependent adenosine triphosphate. J Biol. Chem. 244, 6596–6604
Shamoo A E. and Brodsky W. A. (1972) Functions of the E-ATP and E-P complex in the membrane ATPase reaction. Biochim Biophys. Acta 255, 220–230.
Siegel G. J. and Albers R. W. (1967) Sodium-potassium-activated adenosine triphosphatase of Electrophorus electric organ. IV. Modification of response to sodium and potassium by arsenite plus 2,3-dimercaptopropanol. J. Biol. Chem. 242, 4972–4979.
Siegel G. J. and Fogt S. M. (1977) Inhibition by lead ion of Electrophorus electroplax (Na+ + K+)-adenosine triophosphatase and K+-p-nitrophenylphosphatase J. Biol. Chem 252, 5201–5205.
Seigel G. J. and Albers R. W. (1967) Sodium-potassium-activated adenosine triphosphatase. VI. Characterization of the phosphoprotein formed from orthophosphate in the presence of ouabain. J Biol Chem. 244, 3264–3269.
Skou J. C. (1957) The influence of some cations on an adenosine triphosphatase from peripheral nerves. Biochim Biophys. Acta 23, 394–401.
Skou J. C. (1960) Further mvestigations on a Mg2+ + Na+ activated adenosine triphosphatase possibly related to the active linked transport of Na+ and K+ across the nerve membrane. Biochim. Biophys Acta 42, 6–23.
Skou J. C. (1962) Preparation from mammalian brain and kidney of the enzyme system involved in active transport of Na+ and K+. Biochim. Biophys. Acta 58, 314–325.
Skou J. C. (1971) The Role of the Phosphorylated Intermediates in the Reaction of the Na+,K+-Activated Enzyme System, in Membrane Bound Enzymes (Porcellati G. and di Jeso F., eds.), Plenum, New York.
Skou J. C. (1981) Eosin, a fluorescent probe of ATP binding to the (Na+ + K+) ATPase. Biochim. Biophys. Acta 647, 232–240.
Skou J. C. and Hilberg C. (1965) The effect of sulphydryl-blocking reagents and of urea on the (Na+ + K+)-activated enzyme system. Biochim. Biophys Acta 110, 359.
Skulskii I. A., Manninen V, and Jarnefelt J, (1973) Interaction of thallous ions with the cation transport mechanism in erythrocytes. Biochim. Biophys Acta 298, 702–709
Somogyi J., Budai M., Nyiro L., Kaluza G. A., Nagel W., and Willig F (1969) Activity and structural changes in Mg2+-dependent and Na+,K+-activated adenosine triphosphatase prepared from rat brain following detergent treatment. Acta Biochem. Biophys. Acad. Sci (Hung.) 4, 219–236.
Specht S. C. and Robinson J D (1973) Stimulation of the (Na+ + K+)-dependent adenosine triphosphatase by amino acids and phosphatidylserine: Chelation of trace metal inhibitors. Arch. Biochem Biophys. 154, 314–323.
Squires R. F. (1965) On the interactions of Na+, K+, Mg2+ and ATP with the (Na+ + K+)-activated ATPase from rat brain. Biochem. Biophys. Res. Commun. 19, 27–32.
Stahl W. L., Sattin A., and McIlwain H. (1966) Separation of adenosine diphosphate-adenosine triphosphate-exchange activity from the cerebral microsomal sodium plus potassium ion-stimulated adenosine triphosphatase. Biochem. J. 99, 404–412.
Stefanovic V., Ebel A., Hermetet J. C., and Mandel P. (1974) Na+-K+-ATPase activity in brain regions of C57 and DBA mice. J. Neurochem. 22, 1139–1141.
Svoboda P. and Mosinger B. (1981a) Catecholamines and the brain microsomal Na,K-adenosine triphosphatase. I. Protection against lipoperoxidative damage. Biochem. Pharmacol. 30, 427–432
Svoboda P. and Mosinger B. (1981b) Catecholamines and the brain microsomal Na,K-adenosine triphosphatase. II. The mechanism of action. Biochem. Pharmacol 30, 433–439.
Sweadner K. J. (1977) Cross-linking and modification of Na,K-ATPase by ethyl acetimidate. Biochem. Biophys. Res. Commun. 78, 962–969.
Sweadner K. J. (1978) Purification from brain of an intrinsic membrane protein fraction enriched in (Na+ + K+)-ATPase. Biochim. Biophys. Acta 508, 486–499.
Sweadner K. J. (1979) Two molecular forms of (Na+ + K+)-stimulated ATPase in brain. Separation and difference in affinity for strophanthidin. J. Biol Chem. 254, 6060–6067.
Tanaka R. (1974) Role of lipids in activation of Na+,K+-dependent ATPase and K+-dependent phosphatase of the brain. Rev. Neurosci. 1, 181–230.
Tanford C. (1952) The effect of pH on the combination of serum albumin with metals. J. Am. Chem. Soc. 74, 211–215.
Ting-Beall H. P., Clark D. A., Snelter C. H., and Wells W. W. (1973) Studies on the interaction of chick brain microsomal (Na+ + K+)-ATPase with copper. Biochim Biophys. Acta 291, 229–236.
Tobin T., Akera T., Baskin S. I., and Brody T. M. (1973) Calcium ion and sodium-and potassium-dependent adenosine triphosphatase: Its mechanism of inhibition and identification of the E1-P intermediate. Mol. Pharmacol. 9, 336–349.
Tobin T. and Sen A. K. (1970) Stability and ligand sensitivity of 3H-ouabain binding to Na+,K+-ATPase. Biochim. Biophys. Acta 198, 120–131.
Toda G. (1968) The effects of cations on the inhibition of sodium-and potassium-activated adenosine triphosphatase by beryllium. J. Biochem. (Tokyo) 64, 457–464.
Toffano G., Benvegnu D., Bonetti A. C., Leon A., Orlando P., Ghidoni R., and Tettamanti G. (1980) Interactions of GM1 ganglioside with crude rat brain neuronal membranes. J. Neurochem. 35, 861–866.
Trauner D. A. (1980) Regional cerebral Na+,K+-ATPase activity following octanoate administration. Pediatr. Res. 14, 844–845.
Uesugi S., Kahlenberg A., Medzihrodsky F., and Hokin L. E. (1969) Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. IV. Properties of a Lubrol-solubilized beef brain microsomal enzyme. Arch. Biochem. Biophys 130, 156–163.
Uesugi S., Dulak N. C., Dixon J. F., Hexum T. I., Dahl J. L., Perdue J. F, and Hokin L. E. (1971) Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. I. Large-scale partial purification and properties of a Lubrol-solubilized bovine brain enzyme. J. Biol. Chem. 269, 531–543.
Valcana T. and Timiras P. S. (1969) Effect of hypothyroidism on ionic metabolism and Na-K-activated ATP phosphohydrolase activity in the developing rat brain. J. Neurochem. 16, 935–943.
Van der Krogt J. A. and Belfroid R. D. (1980) Characterization and localization of catecholamine-susceptible Na-K ATPase activity of rat striatum: Studies using catecholamine receptor (ant)agonists and lesion techniques. Biochem. Pharmacol. 29, 857–868.
Van Winkle W. B., Allen J. C., and Schwartz A. (1972) The nature of the transport ATPase-digitalis complex. III. Rapid binding studies and effects of ligands on the formation and stability of magnesium plus phosphate-induced glycoside-enzyme complex. Arch. Biochem. Biophys. 151, 85–92.
Vizi E. S. (1979) Pre-synaptic modulation of neurochemical transmission. Prog. Neurobiol. 12, 181–290.
Vizi E. S. (1980) Modulation of cortical release of acetylcholine by noradrenaline released from nerves arising from the rat locus coeruleus. Neuroscience 5, 2139–2144.
Whitaker J. N. (1975) The antigenicity of myelin encephalitogenic protein. Production of antibodies to encephalitogenic protein with deoxyribonucleic acid-encephalitogenic protein complexes. J. Immuno. 114, 823–828.
Whittaker V. P. (1959) The isolation and characterization of acetylcholine-containing particles from brain. Biochem. J. 72, 694–706.
Whittam R. (1962) The asymmetrical stimulation of a membrane adenosine triphosphatase in relation to active cation transport. Biochem. J. 84, 110–118.
Whittam R. and Chipperfield A. R (1973) Ouabain binding to the sodium pump in plasma membranes isolated from ox brain. Biochim. Biophys. Acta 307, 563–577
Whittam R., Wheeler K. P, and Blake A. (1964) Oligomycin and active transport reactions in cell membranes. Nature 203, 720–724.
Wilson W. E., Sivitz W. I., and Hanna L. T (1970) Inhibition of calf brain membranal sodium-and potassium-dependent adenosine triphosphatase by cardioactive sterols. A binding site model. Mol Pharmacol. 6, 449–459.
Winter C. G (1972) Differential effects of digitonin on some enzyme activities of the sodium pump. Biochim. Biophys. Acta 266, 135–143.
Wood J. G., Jean D. H., Whitaker J. N., McLaughlin B. J., and Albers W. (1977) Immunocytochemical localization of the sodium, potassium activated ATPase in knifefish brain. J. Neurocyto. 6, 571–581.
Woodbury D M. (1955) Effect of diphenylhydantoin on electrolytes and radio sodium turnover in brain and other tissues of normal hyponatremic and postictal rats. J. Pharmacol. Exp Ther 115, 74–95.
Wu P. H. and Phillis J. W. (1978) Effects of α-and β-adrenergic blocking agents on the biogenic amine stimulated (Na+,K+) ATPase of rat cerebral cortical synaptosomal membrane. Gen. Pharmacol 9, 421–424.
Wu P. H. and Phillis J. W. (1979a) Receptor-mediated noradrenaline stimulation of (Na+-K+) ATPase in rat brain cortical homogenates. Gen. Pharmacol. 10, 189–192.
Wu P. H. and Phillis J. W (1979b) Metergoline antagonism of 5-hydroxytryptamine-induced activation of rat cortical (Na+-K+) ATPase. J. Pharm. Pharmacol. 31, 782–784.
Wu P. H. and Phillis J W (1979c) Effects of vanadate on brain (Na+,K+) ATPase and p-nitrophenylphosphatase. Interactions with mono-and di-valent ions and with noradrenaline. Intl. J. Biochem. 10, 629–635.
Wu P. H. and Phillis J. W (1980) Characterization of receptor-mediated catecholamine activation of rat brain cortical Na+-K+-ATPase. Intl. J. Biochem. 12, 353–359.
Yamaguchi M. and Tonomura Y. (1979) Simultaneous bindmg of three Na+ and two K+ ions to Na+,K+-dependent ATPase and changes in its affinities for the ions induced by the formation of a phosphorylated intermediate. J. Biochem. (Tokyo) 86, 509–523.
Yamaguchi M. and Tonomura Y. (1980a) Binding of monovalent cations to Na+,K+-dependent ATPase purified from porcine kidney. I. Simultaneous binding of three sodium and two potassium or rubidium ions to the enzyme. J. Biochem. (Tokyo) 88, 1365–1375.
Yamaguchi M. and Tonomura Y. (1980b) Binding of monovalent cations to Na+,K+-dependent ATPase purified from porcine kidney. II. Acceleration of transition from a K+-bound form to a Na+-bound form by binding of ATP to a regulatory site of the enzyme. J. Biochem. (Tokyo) 88, 1377–1385.
Yamaguchi M and Tonomura Y. (1980c) Binding of monovalent cations to Na+,K+-dependent ATPase purified from porcine kidney. III. Marked changes in affinities for mono-valent cations induced by formation of an ADP-insensitive but not an ADP-sensitive phosphoenzyme. J. Biochem. (Tokyo) 88, 1387–1397.
Yap H. H., Desaiah D., Koch R. B., and Cutkomp L. K. (1972) Sensitivity of fish ATPase to polychlorinated biphenyls. Nature 233, 61–62.
Yoda A. and Hokin L. E. (1970) On the reversibility of binding of cardiotonic steroids to a partially purified (Na + K)-activated adenosine triphosphatase from beef brain Biochem. Biophys. Res. Commun. 40, 880–886.
Yoshimura K. (1973) Activation of Na-K activated ATPase in rat brain by catecholamine J Biochem. (Tokyo) 74, 389–391.
Author information
Authors and Affiliations
Editor information
Rights and permissions
Copyright information
© 1986 The Humana Press Inc.
About this protocol
Cite this protocol
Wu, P.H. (1986). Na+/K+-ATPase in Nervous Tissue. In: Boulton, A.A., Baker, G.B., Yu, P.H. (eds) Neurotransmitter Enzymes. Neuromethods, vol 5. Humana Press. https://doi.org/10.1385/0-89603-079-2:451
Download citation
DOI: https://doi.org/10.1385/0-89603-079-2:451
Publisher Name: Humana Press
Print ISBN: 978-0-89603-079-4
Online ISBN: 978-1-59259-610-2
eBook Packages: Springer Protocols