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Volumn 10, Issue 2, 2014, Pages 85-102

Brain Na+, K+-ATPase activity in aging and disease

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM);

EID: 84903552010     PISSN: 15509702     EISSN: 15552810     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (160)

References (175)
  • 1
    • 0001409028 scopus 로고
    • The influence of some cations on an adenosine triphosphatase from peripheral nerves
    • Skou J. The influence of some cations on an adenosine triphosphatase from peripheral nerves. Biochim. Biophys. Acta. 1957; 23: 394-401.
    • (1957) Biochim. Biophys. Acta , vol.23 , pp. 394-401
    • Skou, J.1
  • 5
    • 0014057051 scopus 로고
    • Ultrastructural and enzymic studies of cholinergic and non-cholinergic synaptic membranes isolated from brain cortex
    • Rodríguez de Lores Arnaiz G, Alberici M, De Robertis E. Ultrastructural and enzymic studies of cholinergic and non-cholinergic synaptic membranes isolated from brain cortex. J. Neurochem. 1967; 14: 215-225.
    • (1967) J. Neurochem , vol.14 , pp. 215-225
    • Rodríguez de Lores Arnaiz, G.1    Alberici, M.2    De Robertis, E.3
  • 7
    • 77951883450 scopus 로고    scopus 로고
    • The Physiological Significance of the Cardiotonic Steroid/Ouabain-Binding site of the Na, K-ATPase
    • Lingrel JB. The Physiological Significance of the Cardiotonic Steroid/Ouabain-Binding site of the Na, K-ATPase. Ann. Rev. Physiol. 2010; 72: 395-412.
    • (2010) Ann. Rev. Physiol , vol.72 , pp. 395-412
    • Lingrel, J.B.1
  • 8
    • 63849168850 scopus 로고    scopus 로고
    • Endogenous cardiotonic steroids: Physiology, pharmacology, and novel therapeutic targets
    • Bagrov AY, Shapiro JI, Fedorova OV. Endogenous cardiotonic steroids: physiology, pharmacology, and novel therapeutic targets. Pharmacol. Rev. 2009; 61: 9-38.
    • (2009) Pharmacol. Rev , vol.61 , pp. 9-38
    • Bagrov, A.Y.1    Shapiro, J.I.2    Fedorova, O.V.3
  • 12
    • 0026332219 scopus 로고
    • Phosphorylation of the catalytic subunit of Na+, K+-ATPase inhibits the activity of the enzyme
    • Bertorello AM, Aperia A, Walaas SI, Nairn AC, et al. Phosphorylation of the catalytic subunit of Na+, K+-ATPase inhibits the activity of the enzyme. Proc. Natl. Acad. Sci. USA. 1991; 88: 11359-11362.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11359-11362
    • Bertorello, A.M.1    Aperia, A.2    Walaas, S.I.3    Nairn, A.C.4
  • 13
    • 0026507984 scopus 로고
    • Inhibition of protein kinase C restores Na+, K+-ATPase activity in sciatic nerve of diabetic mice
    • Hermenegildo C, Felipo V, Miñana MD, Grisolía S. Inhibition of protein kinase C restores Na+, K+-ATPase activity in sciatic nerve of diabetic mice. J. Neurochem. 1992; 58: 1246-1249.
    • (1992) J. Neurochem , vol.58 , pp. 1246-1249
    • Hermenegildo, C.1    Felipo, V.2    Miñana, M.D.3    Grisolía, S.4
  • 14
    • 0027526475 scopus 로고
    • Sustained recovery of Na(+)-K(+)-ATPase activity in the sciatic nerve of diabetic mice by administration of H7 or calphostin C, inhibitors of PKC
    • Hermenegildo C, Felipo V, Miñana MD, Romero FJ, et al. Sustained recovery of Na(+)-K(+)-ATPase activity in the sciatic nerve of diabetic mice by administration of H7 or calphostin C, inhibitors of PKC. Diabetes. 1993; 42: 257-262.
    • (1993) Diabetes , vol.42 , pp. 257-262
    • Hermenegildo, C.1    Felipo, V.2    Miñana, M.D.3    Romero, F.J.4
  • 15
    • 0030887172 scopus 로고    scopus 로고
    • Calcineurin regulation of synaptic function: From ion channels to transmitter release and gene transcription
    • Yakel JL. Calcineurin regulation of synaptic function: from ion channels to transmitter release and gene transcription. Trends Pharmacol. Sci. 1997; 18: 124-134.
    • (1997) Trends Pharmacol. Sci , vol.18 , pp. 124-134
    • Yakel, J.L.1
  • 16
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin: Form and function
    • Rusnak F, Mertz P. Calcineurin: form and function. Physiol. Rev. 2000; 80: 1483-1521.
    • (2000) Physiol. Rev , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 17
    • 0028811105 scopus 로고
    • Protein phosphatase-1 in the kidney: Evidence for a role in the regulation of medullary Na(+)-K(+)-ATPase
    • Li D, Aperia A, Celsi G, da Cruz e Silva EF, et al. Protein phosphatase-1 in the kidney: evidence for a role in the regulation of medullary Na(+)-K(+)-ATPase. Am. J. Physiol. 1995; 269: F673-F680.
    • (1995) Am. J. Physiol , vol.269
    • Li, D.1    Aperia, A.2    Celsi, G.3    da Cruz e Silva, E.F.4
  • 18
    • 0028580746 scopus 로고
    • A putative fourth Na+, K(+)-ATPase alphasubunit gene is expressed in testis
    • Shamraj OI, Lingrel JB. A putative fourth Na+, K(+)-ATPase alphasubunit gene is expressed in testis. Proc. Natl. Acad. Sci. USA. 1994; 91: 12952-12956.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12952-12956
    • Shamraj, O.I.1    Lingrel, J.B.2
  • 19
    • 0025911177 scopus 로고
    • Epitope mapping by amino-acid-sequence-specific antibodies reveals that both ends of the alpha subunit of Na+/K(+)-ATPase are located on the cytoplasmic side of the membrane
    • Antolovic R, Bruller H J, Bunk S, Linder D, Schoner W. Epitope mapping by amino-acid-sequence-specific antibodies reveals that both ends of the alpha subunit of Na+/K(+)-ATPase are located on the cytoplasmic side of the membrane. Eur. J. Biochem. 1991; 199: 195-202.
    • (1991) Eur. J. Biochem , vol.199 , pp. 195-202
    • Antolovic, R.1    Bruller, H.J.2    Bunk, S.3    Linder, D.4    Schoner, W.5
  • 20
    • 0024564828 scopus 로고
    • Isozymes of Na+, K+-ATPase
    • Sweadner KJ. Isozymes of Na+, K+-ATPase. Biochim. Biophys. Acta. 1989; 988: 185-220.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 185-220
    • Sweadner, K.J.1
  • 22
    • 0025954861 scopus 로고
    • Immunofluorescent localization of three Na, K-ATPase isozymes in the rat central nervous system: Both neurons and glia express more than one Na, K-ATPase
    • McGrail KM, Phillips JM, Sweadner KJ. Immunofluorescent localization of three Na, K-ATPase isozymes in the rat central nervous system: both neurons and glia express more than one Na, K-ATPase. J. Neurosci. 1991; 11: 381-391.
    • (1991) J. Neurosci , vol.11 , pp. 381-391
    • McGrail, K.M.1    Phillips, J.M.2    Sweadner, K.J.3
  • 23
    • 0036266311 scopus 로고    scopus 로고
    • Similar perisynaptic glial localization for the Na+, K+-ATPase alpha 2 subunit and the glutamate transporters GLAST and GLT-1 in the rat somatosensory cortex
    • Cholet N, Pellerin L, Magistretti PJ, Hamel E. Similar perisynaptic glial localization for the Na+, K+-ATPase alpha 2 subunit and the glutamate transporters GLAST and GLT-1 in the rat somatosensory cortex. Cerebr. Cortex. 2002; 12: 515-525.
    • (2002) Cerebr. Cortex , vol.12 , pp. 515-525
    • Cholet, N.1    Pellerin, L.2    Magistretti, P.J.3    Hamel, E.4
  • 24
    • 0037687290 scopus 로고    scopus 로고
    • The Na, KATPase alpha 2 isoform is expressed in neurons, and its absence disrupts neuronal activity in newborn mice
    • Moseley AE, Lieske SP, Wetzel RK, James, PF, He S, et al. The Na, KATPase alpha 2 isoform is expressed in neurons, and its absence disrupts neuronal activity in newborn mice. J. Biol. Chem. 2003; 278: 5317-5324.
    • (2003) J. Biol. Chem , vol.278 , pp. 5317-5324
    • Moseley, A.E.1    Lieske, S.P.2    Wetzel, R.K.3    James, P.F.4    He, S.5
  • 26
    • 0027021364 scopus 로고
    • In search of synaptosomal Na+, K+-ATPase regulators
    • Rodríguez de Lores Arnaiz G. In search of synaptosomal Na+, K+-ATPase regulators. Molec. Neurobiol. 1992; 6: 359-375.
    • (1992) Molec. Neurobiol , vol.6 , pp. 359-375
    • Rodríguez de Lores Arnaiz, G.1
  • 28
    • 0034484750 scopus 로고    scopus 로고
    • The Na/K-ATPase regulation by neurotransmitters in ontogeny
    • Kometiani Z, Jariashvili T. The Na/K-ATPase regulation by neurotransmitters in ontogeny. Arch. Physiol. Biochem. 2000; 108: 360-370.
    • (2000) Arch. Physiol. Biochem , vol.108 , pp. 360-370
    • Kometiani, Z.1    Jariashvili, T.2
  • 29
    • 0038578531 scopus 로고    scopus 로고
    • Isoform-specific regulation of Na+, K+-ATPase endocytosis and recruitment to the plasma membrane
    • Teixeira VL, Katz AI, Pedemonte CH, Bertorello AM. Isoform-specific regulation of Na+, K+-ATPase endocytosis and recruitment to the plasma membrane. Ann. N. Y. Acad. Sci. 2003; 986: 587-594.
    • (2003) Ann. N.Y. Acad. Sci , vol.986 , pp. 587-594
    • Teixeira, V.L.1    Katz, A.I.2    Pedemonte, C.H.3    Bertorello, A.M.4
  • 30
    • 0028359422 scopus 로고
    • The influence of beta subunit structure on the stability of Na+/K+-ATPase complexes and interaction with K+
    • Eakle KA, Kabalin MA, Wang SG, Farley RA. The influence of beta subunit structure on the stability of Na+/K+-ATPase complexes and interaction with K+. J. Biol. Chem. 1994; 269: 6550-6557.
    • (1994) J. Biol. Chem , vol.269 , pp. 6550-6557
    • Eakle, K.A.1    Kabalin, M.A.2    Wang, S.G.3    Farley, R.A.4
  • 31
    • 0029137474 scopus 로고
    • Functional significance of the beta-subunit for heterodimeric P-type ATPases
    • Chow DC, Forte JG. Functional significance of the beta-subunit for heterodimeric P-type ATPases. J. Exp. Biol. 1995; 198: 1-17.
    • (1995) J. Exp. Biol , vol.198 , pp. 1-17
    • Chow, D.C.1    Forte, J.G.2
  • 32
    • 0027097820 scopus 로고
    • The beta subunit modulates potassium activation of the Na-K pump
    • Jaisser F, Horisberger JD, Rossier BC. The beta subunit modulates potassium activation of the Na-K pump. Ann. N. Y. Acad. Sci. 1992; 671: 113-119.
    • (1992) Ann. N.Y. Acad. Sci , vol.671 , pp. 113-119
    • Jaisser, F.1    Horisberger, J.D.2    Rossier, B.C.3
  • 33
    • 0027236527 scopus 로고
    • An essential role for the extracellular domain of the Na, K-ATPase beta-subunit in cation occlusion
    • Lutsenko S, Kaplan JH. An essential role for the extracellular domain of the Na, K-ATPase beta-subunit in cation occlusion. Biochemistry. 1993; 32: 6737-6743.
    • (1993) Biochemistry , vol.32 , pp. 6737-6743
    • Lutsenko, S.1    Kaplan, J.H.2
  • 34
    • 0039438642 scopus 로고    scopus 로고
    • The gamma subunit is a specific component of the Na, K-ATPase and modulates its transport function
    • Beguin P, Wang X, Firsov D, Puoti A, Claeys D, et al. The gamma subunit is a specific component of the Na, K-ATPase and modulates its transport function. EMBO J. 1997; 16: 4250-4260.
    • (1997) EMBO J , vol.16 , pp. 4250-4260
    • Beguin, P.1    Wang, X.2    Firsov, D.3    Puoti, A.4    Claeys, D.5
  • 36
    • 0038578770 scopus 로고    scopus 로고
    • FXYD proteins: New tissue-and isoform-specific regulators of Na, K-ATPase
    • Geering K, Beguin P, Garty H, Karlish S, Fuzesi M, et al. FXYD proteins: new tissue-and isoform-specific regulators of Na, K-ATPase. Ann. N. Y. Acad. Sci. 2003; 986: 388-394.
    • (2003) Ann. N.Y. Acad. Sci , vol.986 , pp. 388-394
    • Geering, K.1    Beguin, P.2    Garty, H.3    Karlish, S.4    Fuzesi, M.5
  • 37
    • 0034662757 scopus 로고    scopus 로고
    • The FXYD gene family of small ion transport regulators or channels: CDNA sequence, protein signature sequence, and expression
    • Sweadner KJ, Rael E. The FXYD gene family of small ion transport regulators or channels: cDNA sequence, protein signature sequence, and expression. Genomics. 2000; 68: 41-56.
    • (2000) Genomics , vol.68 , pp. 41-56
    • Sweadner, K.J.1    Rael, E.2
  • 38
    • 0038481242 scopus 로고    scopus 로고
    • Functional modulation of the sodium pump: The regulatory proteins "Fixit"
    • Cornelius F, Mahmmoud Y. Functional modulation of the sodium pump: the regulatory proteins "Fixit". News Physiol. Sci. 2003; 18: 119-124.
    • (2003) News Physiol. Sci , vol.18 , pp. 119-124
    • Cornelius, F.1    Mahmmoud, Y.2
  • 39
    • 77958522856 scopus 로고    scopus 로고
    • Association with {beta}-COP regulates the trafficking of the newly synthesized Na, K-ATPase
    • Morton MJ, Farr GA, Hull M, Capendeguy O, Horisberger JD, et al. Association with {beta}-COP regulates the trafficking of the newly synthesized Na, K-ATPase. J. Biol. Chem. 2010; 285: 33737-33746.
    • (2010) J. Biol. Chem , vol.285 , pp. 33737-33746
    • Morton, M.J.1    Farr, G.A.2    Hull, M.3    Capendeguy, O.4    Horisberger, J.D.5
  • 40
    • 0034623045 scopus 로고    scopus 로고
    • Involvement of Src and epidermal growth factor receptor in the signal-transducing function of Na+/K+-ATPase
    • Haas M, Askari A, Xie Z. Involvement of Src and epidermal growth factor receptor in the signal-transducing function of Na+/K+-ATPase. J. Biol. Chem. 2000; 275: 27832-27837.
    • (2000) J. Biol. Chem , vol.275 , pp. 27832-27837
    • Haas, M.1    Askari, A.2    Xie, Z.3
  • 41
    • 0038578665 scopus 로고    scopus 로고
    • Molecular mechanisms of Na/K-ATPase-mediated signal transduction
    • Xie Z. Molecular mechanisms of Na/K-ATPase-mediated signal transduction. Ann. N. Y. Acad. Sci. 2003; 986: 497-503.
    • (2003) Ann. N.Y. Acad. Sci , vol.986 , pp. 497-503
    • Xie, Z.1
  • 42
    • 0036098774 scopus 로고    scopus 로고
    • Na(+)/K(+)-ATPase as a signal transducer
    • Xie Z, Askari A. Na(+)/K(+)-ATPase as a signal transducer. Eur. J. Biochem. 2002; 269: 2434-2439.
    • (2002) Eur. J. Biochem , vol.269 , pp. 2434-2439
    • Xie, Z.1    Askari, A.2
  • 43
    • 2342487353 scopus 로고    scopus 로고
    • Na+-K+-ATPase-mediated signal transduction: From protein interaction to cellular function
    • Xie Z, Cai T. Na+-K+-ATPase-mediated signal transduction: from protein interaction to cellular function. Mol. Interv. 2003; 3: 157-168.
    • (2003) Mol. Interv , vol.3 , pp. 157-168
    • Xie, Z.1    Cai, T.2
  • 44
    • 2342424240 scopus 로고    scopus 로고
    • Ouabain assembles signaling cascades through the caveolar Na+/K+-ATPase
    • Wang H, Haas M, Liang M, Cai T, Tian J, et al. Ouabain assembles signaling cascades through the caveolar Na+/K+-ATPase. J. Biol. Chem. 2004; 279: 17250-17259.
    • (2004) J. Biol. Chem , vol.279 , pp. 17250-17259
    • Wang, H.1    Haas, M.2    Liang, M.3    Cai, T.4    Tian, J.5
  • 45
    • 0038368147 scopus 로고    scopus 로고
    • No evidence for a role in signal-transduction of Na+/K+-ATPase interaction with putative endogenous ouabain
    • Hansen, O. 2003. No evidence for a role in signal-transduction of Na+/K+-ATPase interaction with putative endogenous ouabain. Eur. J. Biochem. 270: 1916-1919.
    • (2003) Eur. J. Biochem , vol.270 , pp. 1916-1919
    • Hansen, O.1
  • 46
    • 3042805201 scopus 로고    scopus 로고
    • Ouabain induces endocytosis of plasmalemmal Na/K-ATPase in LLC-PK 1 cells by a clathrin-dependent mechanism
    • Liu J, Kesiry R, Periyasamy SM, Malhotra D, Xie Z, et al. Ouabain induces endocytosis of plasmalemmal Na/K-ATPase in LLC-PK 1 cells by a clathrin-dependent mechanism. Kidney Int. 2004; 66: 227-241.
    • (2004) Kidney Int , vol.66 , pp. 227-241
    • Liu, J.1    Kesiry, R.2    Periyasamy, S.M.3    Malhotra, D.4    Xie, Z.5
  • 47
    • 84877689321 scopus 로고    scopus 로고
    • Identification of a mutant α1 Na/K-ATPase that pumps but is defective in signal transduction
    • Lai F, Madan N, Ye Q, Duan Q, Li Z, et al. Identification of a mutant α1 Na/K-ATPase that pumps but is defective in signal transduction. J. Biol. Chem. 2013; 288: 13295-13304.
    • (2013) J. Biol. Chem , vol.288 , pp. 13295-13304
    • Lai, F.1    Madan, N.2    Ye, Q.3    Duan, Q.4    Li, Z.5
  • 48
    • 62149104775 scopus 로고    scopus 로고
    • The Na/K-ATPase/Src complex and cardiotonic steroidactivated protein kinase cascades
    • Li Z, Xie Z. The Na/K-ATPase/Src complex and cardiotonic steroidactivated protein kinase cascades. Pflugers Arch. 2009; 457: 635-644.
    • (2009) Pflugers Arch , vol.457 , pp. 635-644
    • Li, Z.1    Xie, Z.2
  • 50
    • 0036818893 scopus 로고    scopus 로고
    • Identification of the cofilin-binding sites in the large cytoplasmic domain of Na, K-ATPase
    • Kim M, Jung J, Park CS, Lee K. Identification of the cofilin-binding sites in the large cytoplasmic domain of Na, K-ATPase. Biochimie. 2002; 84: 1021-1029.
    • (2002) Biochimie , vol.84 , pp. 1021-1029
    • Kim, M.1    Jung, J.2    Park, C.S.3    Lee, K.4
  • 51
    • 35848934128 scopus 로고    scopus 로고
    • Arrestins and spinophilin competitively regulate Na+, K+-ATPase trafficking through association with a large cytoplasmic loop of the Na+, K+-ATPase
    • Kimura T, Allen PB, Nairn AC, Caplan MJ. Arrestins and spinophilin competitively regulate Na+, K+-ATPase trafficking through association with a large cytoplasmic loop of the Na+, K+-ATPase. Mol. Biol. Cell. 2007; 18: 4508-4518.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4508-4518
    • Kimura, T.1    Allen, P.B.2    Nairn, A.C.3    Caplan, M.J.4
  • 52
    • 0034612370 scopus 로고    scopus 로고
    • Phosphoinositide-3 kinase binds to a proline-rich motif in the Na+, K+-ATPase alpha subunit and regulates its trafficking
    • Yudowski GA, Efendiev R, Pedemonte CH, Katz AI, Berggren PO, et al. Phosphoinositide-3 kinase binds to a proline-rich motif in the Na+, K+-ATPase alpha subunit and regulates its trafficking. Proc. Natl. Acad. Sci. USA. 2000; 97: 6556-6561.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6556-6561
    • Yudowski, G.A.1    Efendiev, R.2    Pedemonte, C.H.3    Katz, A.I.4    Berggren, P.O.5
  • 53
    • 52249104702 scopus 로고    scopus 로고
    • Regulation of caveolin-1 membrane trafficking by the Na/K-ATPase
    • Cai T, Wang H, Chen Y, Liu L, Gunning WT, et al. Regulation of caveolin-1 membrane trafficking by the Na/K-ATPase. J. Cell. Biol. 2008; 182: 1153-1169.
    • (2008) J. Cell. Biol , vol.182 , pp. 1153-1169
    • Cai, T.1    Wang, H.2    Chen, Y.3    Liu, L.4    Gunning, W.T.5
  • 55
    • 77953686002 scopus 로고    scopus 로고
    • Functional and molecular interactions between aquaporins and Na, KATPase
    • Illarionova NB, Gunnarson E, Li Y, Brismar H, Bondar A, et al. Functional and molecular interactions between aquaporins and Na, KATPase. Neuroscience. 2010; 168: 915-925.
    • (2010) Neuroscience , vol.168 , pp. 915-925
    • Illarionova, N.B.1    Gunnarson, E.2    Li, Y.3    Brismar, H.4    Bondar, A.5
  • 56
    • 14844315982 scopus 로고    scopus 로고
    • Novel role for Na, K-ATPase in phosphatidylinositol 3-kinase signaling and suppression of cell motility
    • Barwe SP, Anilkumar G, Moon SY, Zheng Y, Whitelegge JP, et al. Novel role for Na, K-ATPase in phosphatidylinositol 3-kinase signaling and suppression of cell motility. Mol. Biol. Cell. 2005; 16: 1082-1094.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1082-1094
    • Barwe, S.P.1    Anilkumar, G.2    Moon, S.Y.3    Zheng, Y.4    Whitelegge, J.P.5
  • 58
    • 39349094888 scopus 로고    scopus 로고
    • Regulation of apical NHE3 trafficking by ouabain-induced activation of the basolateral Na+-K+-ATPase receptor comple
    • Cai H, Wu L, Qu W, Malhotra D, Xie Z. et al. Regulation of apical NHE3 trafficking by ouabain-induced activation of the basolateral Na+-K+-ATPase receptor comple. Am. J. Physiol. Cell. Physiol. 2008; 294: C555-563.
    • (2008) Am. J. Physiol. Cell. Physiol , vol.294
    • Cai, H.1    Wu, L.2    Qu, W.3    Malhotra, D.4    Xie, Z.5
  • 60
    • 84887119851 scopus 로고    scopus 로고
    • Neuron-specific specificity protein 4 bigenomically regulates the transcription of all mitochondria-and nucleus-encoded cytochrome c oxidase subunit genes in neurons
    • Johar K, Priya A, Dhar S, Liu Q, Wong-Riley MT. Neuron-specific specificity protein 4 bigenomically regulates the transcription of all mitochondria-and nucleus-encoded cytochrome c oxidase subunit genes in neurons. J. Neurochem. 2013; 127: 496-508.
    • (2013) J. Neurochem , vol.127 , pp. 496-508
    • Johar, K.1    Priya, A.2    Dhar, S.3    Liu, Q.4    Wong-Riley, M.T.5
  • 61
    • 84894107295 scopus 로고    scopus 로고
    • Regulation of Na(+)/K(+)-ATPase by neuronspecific transcription factor Sp4: Implication in the tight coupling of energy production, neuronal activity and energy consumption in neurons
    • Johar K, Priya A, Wong-Riley MT. Regulation of Na(+)/K(+)-ATPase by neuronspecific transcription factor Sp4: implication in the tight coupling of energy production, neuronal activity and energy consumption in neurons. Eur. J. Neurosci. 2014; 39: 566-578.
    • (2014) Eur. J. Neurosci , vol.39 , pp. 566-578
    • Johar, K.1    Priya, A.2    Wong-Riley, M.T.3
  • 62
    • 0018087946 scopus 로고
    • Development of (Na+-K+)-ATPase in rat cerebrum: Correlation with Na+-dependent phosphorylation and K+-paranitrophenylphosphatase
    • Bertoni JM, Siegel GJ. Development of (Na+-K+)-ATPase in rat cerebrum: correlation with Na+-dependent phosphorylation and K+-paranitrophenylphosphatase. J. Neurochem. 1978; 31: 1501-1511.
    • (1978) J. Neurochem , vol.31 , pp. 1501-1511
    • Bertoni, J.M.1    Siegel, G.J.2
  • 63
    • 0022858711 scopus 로고
    • Developmental and thyroid hormone regulation of two molecular forms of Na+, K+-ATPase in brain
    • Schmitt CA, MacDonough AA. Developmental and thyroid hormone regulation of two molecular forms of Na+, K+-ATPase in brain. J. Biol. Chem. 1986; 261: 10439-10444.
    • (1986) J. Biol. Chem , vol.261 , pp. 10439-10444
    • Schmitt, C.A.1    McDonough, A.A.2
  • 64
    • 0014529529 scopus 로고
    • Effect of hypothyroidism on ionic metabolism and Na-K activated ATP phosphohydrolase activity in the developing rat brain
    • Valcana T, Timiras PS. Effect of hypothyroidism on ionic metabolism and Na-K activated ATP phosphohydrolase activity in the developing rat brain. J. Neurochem. 1969; 16: 935-943.
    • (1969) J. Neurochem , vol.16 , pp. 935-943
    • Valcana, T.1    Timiras, P.S.2
  • 65
    • 0024271001 scopus 로고
    • Thyroid hormone regulates and isoforms of Na+, K+-ATPase during development in neonatal rat brain J
    • Schmitt CA, MacDonough AA. Thyroid hormone regulates and isoforms of Na+, K+-ATPase during development in neonatal rat brain J. Biol. Chem. 1988; 263: 17643-17649.
    • (1988) Biol. Chem , vol.263 , pp. 17643-17649
    • Schmitt, C.A.1    McDonough, A.A.2
  • 66
    • 0028694915 scopus 로고
    • Age-related alterations by chronic intermittent hypoxia on cerebral synaptosomal ATPase activities
    • Benzi G, Gorini A, Arnaboldi R, Ghigini B, Villa RF. Age-related alterations by chronic intermittent hypoxia on cerebral synaptosomal ATPase activities. J. Neural Transm Suppl. 1994; 44: 159-171.
    • (1994) J. Neural Transm Suppl , vol.44 , pp. 159-171
    • Benzi, G.1    Gorini, A.2    Arnaboldi, R.3    Ghigini, B.4    Villa, R.F.5
  • 67
    • 0029874316 scopus 로고    scopus 로고
    • In situ analysis of Na, K-ATPase alpha1-and alpha3-isoform mRNAs in aging rat hippocampus
    • Chauhan NB, Siegel GJ. In situ analysis of Na, K-ATPase alpha1-and alpha3-isoform mRNAs in aging rat hippocampus. J. Neurochem. 1996; 66: 1742-1751.
    • (1996) J. Neurochem , vol.66 , pp. 1742-1751
    • Chauhan, N.B.1    Siegel, G.J.2
  • 68
    • 0031024452 scopus 로고    scopus 로고
    • Differential expression of Na, K-ATPase alphaisoform mRNAs in aging rat cerebellum
    • Chauhan N, Siegel G. Differential expression of Na, K-ATPase alphaisoform mRNAs in aging rat cerebellum. J. Neurosci. Res. 1997a; 47: 287-299.
    • (1997) J. Neurosci. Res , vol.47 , pp. 287-299
    • Chauhan, N.1    Siegel, G.2
  • 69
    • 0030986952 scopus 로고    scopus 로고
    • Na, K-ATPase: Increases in alpha1-messenger RNA and decreases in alpha3-messenger RNA levels in aging rat cerebral cortex
    • Chauhan NB, Siegel GJ. Na, K-ATPase: increases in alpha1-messenger RNA and decreases in alpha3-messenger RNA levels in aging rat cerebral cortex. Neuroscience. 1997b; 78: 7-11.
    • (1997) Neuroscience , vol.78 , pp. 7-11
    • Chauhan, N.B.1    Siegel, G.J.2
  • 70
    • 0034727491 scopus 로고    scopus 로고
    • Quantification of the alpha(3) subunit of the Na(+)/K(+)-ATPase in developing rat cerebellum
    • Biser PS, Thayne KA, Kong JQ, Fleming WW, Taylor DA. Quantification of the alpha(3) subunit of the Na(+)/K(+)-ATPase in developing rat cerebellum. Brain Res. Dev. Brain Res. 2000; 123: 165-172.
    • (2000) Brain Res. Dev. Brain Res , vol.123 , pp. 165-172
    • Biser, P.S.1    Thayne, K.A.2    Kong, J.Q.3    Fleming, W.W.4    Taylor, D.A.5
  • 71
    • 0036057085 scopus 로고    scopus 로고
    • Comparison of the activities of the Na(+), K(+)-ATPase in brains of rats at different ages
    • Kocak H, Oner P, Oztaş B. Comparison of the activities of the Na(+), K(+)-ATPase in brains of rats at different ages. Gerontology. 2002; 48: 279-281.
    • (2002) Gerontology , vol.48 , pp. 279-281
    • Kocak, H.1    Oner, P.2    Oztaş, B.3
  • 72
    • 0022527137 scopus 로고
    • Brain water and aging
    • Cohadon F, Desbordes P. Brain water and aging. Gerontology. 1986; 32 Suppl. 1: 46-49.
    • (1986) Gerontology , vol.32 , Issue.SUPPL. 1 , pp. 46-49
    • Cohadon, F.1    Desbordes, P.2
  • 73
    • 0025139686 scopus 로고
    • Synaptic aging as revealed by changes in membrane potential and decreased activity of Na(+), K(+)-ATPase
    • Tanaka Y, Ando S. Synaptic aging as revealed by changes in membrane potential and decreased activity of Na(+), K(+)-ATPase. Brain Res. 1990; 506: 46-52.
    • (1990) Brain Res , vol.506 , pp. 46-52
    • Tanaka, Y.1    Ando, S.2
  • 74
    • 0025358360 scopus 로고
    • Synaptic membrane aging in the central nervous system
    • Ando S, Tanaka Y. Synaptic membrane aging in the central nervous system. Gerontology. 1990; 36 Suppl 1: 10-14.
    • (1990) Gerontology , vol.36 , Issue.SUPPL. 1 , pp. 10-14
    • Ando, S.1    Tanaka, Y.2
  • 75
    • 0026659120 scopus 로고
    • Age-related changes in [3H] ouabain binding to synaptic plasma membranes isolated from mouse brains
    • Tanaka Y, Ando S. Age-related changes in [3H] ouabain binding to synaptic plasma membranes isolated from mouse brains. J. Biochem. 1992; 112: 117-121.
    • (1992) J. Biochem , vol.112 , pp. 117-121
    • Tanaka, Y.1    Ando, S.2
  • 78
    • 0021798743 scopus 로고
    • Aging: Effects on sodium-and potassium-activated adenosine triphosphatase activity and ouabain binding sites in rat brain
    • Kennedy RH, Akera T, Katano Y. Aging: effects on sodium-and potassium-activated adenosine triphosphatase activity and ouabain binding sites in rat brain. J. Gerontol. 1985; 40: 401-408.
    • (1985) J. Gerontol , vol.40 , pp. 401-408
    • Kennedy, R.H.1    Akera, T.2    Katano, Y.3
  • 79
    • 15444366140 scopus 로고    scopus 로고
    • Na-K-ATPase activity decreases with aging in female rat brain synaptosomes Am
    • Fraser CL, Arieff AI. Na-K-ATPase activity decreases with aging in female rat brain synaptosomes Am. J. Physiol. Renal Physiol. 2001; 281: F674-F678.
    • (2001) J. Physiol. Renal Physiol , vol.281
    • Fraser, C.L.1    Arieff, A.I.2
  • 80
    • 0038241846 scopus 로고    scopus 로고
    • Agerelated oxidative inactivation of Na+, K+-ATPase in rat brain crude synaptosomes
    • Chakraborty H, Sen P, Sur A, Chatterjee U, Chakrabarti S. Agerelated oxidative inactivation of Na+, K+-ATPase in rat brain crude synaptosomes. Exp. Gerontol. 2003; 38: 705-710.
    • (2003) Exp. Gerontol , vol.38 , pp. 705-710
    • Chakraborty, H.1    Sen, P.2    Sur, A.3    Chatterjee, U.4    Chakrabarti, S.5
  • 81
    • 0031305777 scopus 로고    scopus 로고
    • Na, K-ATPase mRNA levels and plaque load in Alzheimer's disease
    • Chauhan NB, Lee JM, Siegel GJ. Na, K-ATPase mRNA levels and plaque load in Alzheimer's disease. J. Mol. Neurosci. 1997; 9: 151-166.
    • (1997) J. Mol. Neurosci , vol.9 , pp. 151-166
    • Chauhan, N.B.1    Lee, J.M.2    Siegel, G.J.3
  • 82
    • 0036140362 scopus 로고    scopus 로고
    • ATPases enzyme activities during ageing in different types of somatic and synaptic plasma membranes from rat frontal cerebral cortex
    • Gorini A, Canosi U, Devecchi E, Geroldi D, Villa RF. ATPases enzyme activities during ageing in different types of somatic and synaptic plasma membranes from rat frontal cerebral cortex. Prog. Neuropsychopharmacol. Biol. Psychiatry. 2002; 26: 81-90.
    • (2002) Prog. Neuropsychopharmacol. Biol. Psychiatry , vol.26 , pp. 81-90
    • Gorini, A.1    Canosi, U.2    Devecchi, E.3    Geroldi, D.4    Villa, R.F.5
  • 83
    • 33847233962 scopus 로고    scopus 로고
    • The Na+, K+-ATPase activity is increased in the hippocampus after multiple status epilepticus induced by pilocarpine in developing rats
    • Reime Kinjo E, Arida RM, Mara de Oliveira D, da Silva Fernandes MJ. The Na+, K+-ATPase activity is increased in the hippocampus after multiple status epilepticus induced by pilocarpine in developing rats. Brain Res. 2007; 1138: 203-207.
    • (2007) Brain Res , vol.1138 , pp. 203-207
    • Reime Kinjo, E.1    Arida, R.M.2    Mara de Oliveira, D.3    da Silva Fernandes, M.J.4
  • 84
    • 41949135167 scopus 로고    scopus 로고
    • Cognitive neuroscience of aging
    • Grady CL. Cognitive neuroscience of aging. Ann. N. Y. Acad. Sci. 2008; 1124: 127-144.
    • (2008) Ann. N.Y. Acad. Sci , vol.1124 , pp. 127-144
    • Grady, C.L.1
  • 85
    • 84863055620 scopus 로고    scopus 로고
    • Effect of L-deprenyl treatment on electrical activity, Na+, K+-ATPase, and protein kinase C activities in hippocampal subfields (CA1 and CA3) of aged rat brain
    • Singh R, Mishra M, Singh S, Sharma D. Effect of L-deprenyl treatment on electrical activity, Na+, K+-ATPase, and protein kinase C activities in hippocampal subfields (CA1 and CA3) of aged rat brain. Indian J. Exp. Biol. 2012; 50: 101-109.
    • (2012) Indian J. Exp. Biol , vol.50 , pp. 101-109
    • Singh, R.1    Mishra, M.2    Singh, S.3    Sharma, D.4
  • 86
    • 0036744937 scopus 로고    scopus 로고
    • ATPases of Synaptic Plasma Membranes from Hippocampus after Ischemia and Recovery during Ageing
    • Villa RF, Gorini A, Hoyer S. ATPases of Synaptic Plasma Membranes from Hippocampus after Ischemia and Recovery during Ageing. Neurochem. Res. 2002; 27: 861-870.
    • (2002) Neurochem. Res , vol.27 , pp. 861-870
    • Villa, R.F.1    Gorini, A.2    Hoyer, S.3
  • 87
    • 0027944476 scopus 로고
    • Dietary sodium and central vs peripheral ouabain-like activity in Dahl salt-sensitive vs. salt-resistant rats
    • Leenen FH, Harmsen E, Yu H. Dietary sodium and central vs. peripheral ouabain-like activity in Dahl salt-sensitive vs. salt-resistant rats. Am. J. Physiol. 1994; 267: H1916-H1920.
    • (1994) Am. J. Physiol , vol.267
    • Leenen, F.H.1    Harmsen, E.2    Yu, H.3
  • 88
    • 0037135104 scopus 로고    scopus 로고
    • Changes in brain Na, K-ATPase isoform expression and enzymatic activity after aortic constriction
    • Chow MK, Shao Q, Ren B, Leenen FH, Van Huysse JW. Changes in brain Na, K-ATPase isoform expression and enzymatic activity after aortic constriction. Brain Res. 2002; 944: 124-134.
    • (2002) Brain Res , vol.944 , pp. 124-134
    • Chow, M.K.1    Shao, Q.2    Ren, B.3    Leenen, F.H.4    Van Huysse, J.W.5
  • 89
    • 0028891691 scopus 로고
    • Normal sensitivity of Na+, K+-ATPase isolated from brain and kidney of spontaneouly hypertensive rats to sodium, ouabain or mercury
    • Anner BM, Imesch E, Moosmayer M. Normal sensitivity of Na+, K+-ATPase isolated from brain and kidney of spontaneouly hypertensive rats to sodium, ouabain or mercury. Biochim. Biophys. Acta. 1995; 1270: 95-99.
    • (1995) Biochim. Biophys. Acta , vol.1270 , pp. 95-99
    • Anner, B.M.1    Imesch, E.2    Moosmayer, M.3
  • 90
    • 0025719485 scopus 로고
    • Inhibition of sodium-potassium-ATPase: A potentially ubiquitous mechanism contributing to central nervous system neuropathology
    • Lees GJ. Inhibition of sodium-potassium-ATPase: a potentially ubiquitous mechanism contributing to central nervous system neuropathology. Brain Res. Brain Res. Rev. 1991; 16: 283-300.
    • (1991) Brain Res. Brain Res. Rev , vol.16 , pp. 283-300
    • Lees, G.J.1
  • 91
    • 0035029425 scopus 로고    scopus 로고
    • Cerebral edema
    • Kempski O. Cerebral edema. Semin. Nephrol. 2001; 21: 303-307.
    • (2001) Semin. Nephrol , vol.21 , pp. 303-307
    • Kempski, O.1
  • 93
    • 0028144566 scopus 로고
    • Diffusion-weighted magnetic resonance imaging of acute focal cerebral ischemia: Comparison of signal intensity with changes in brain water and Na(+), K(+)-ATPase activity
    • Mintorovitch J, Yang GY, Shimizu H, Kucharczyk J, Chan PH, et al. Diffusion-weighted magnetic resonance imaging of acute focal cerebral ischemia: comparison of signal intensity with changes in brain water and Na(+), K(+)-ATPase activity. J. Cerebr. Blood Flow Metab. 1994; 14: 332-336.
    • (1994) J. Cerebr. Blood Flow Metab , vol.14 , pp. 332-336
    • Mintorovitch, J.1    Yang, G.Y.2    Shimizu, H.3    Kucharczyk, J.4    Chan, P.H.5
  • 94
    • 0031558668 scopus 로고    scopus 로고
    • Changes in ouabain affinity of Na+, K+-ATPase during focal cerebral ischaemia in the mouse
    • Jamme I, Petit E, Gerbi A., Maixent JM, MacKenzie ET, et al. Changes in ouabain affinity of Na+, K+-ATPase during focal cerebral ischaemia in the mouse. Brain Res. 1997; 774: 123-130.
    • (1997) Brain Res , vol.774 , pp. 123-130
    • Jamme, I.1    Petit, E.2    Gerbi, A.3    Maixent, J.M.4    McKenzie, E.T.5
  • 95
    • 0033585833 scopus 로고    scopus 로고
    • Focal cerebral ischaemia induces a decrease in activity and a shift in ouabain affinity of Na+, K+-ATPase isoforms without modifications in mRNA and protein expression
    • Jamme I, Barbey O, Trouve P, Charlemagne D, Maixent JM, et al. Focal cerebral ischaemia induces a decrease in activity and a shift in ouabain affinity of Na+, K+-ATPase isoforms without modifications in mRNA and protein expression. Brain Res. 1999; 819: 132-142.
    • (1999) Brain Res , vol.819 , pp. 132-142
    • Jamme, I.1    Barbey, O.2    Trouve, P.3    Charlemagne, D.4    Maixent, J.M.5
  • 96
    • 0033893843 scopus 로고    scopus 로고
    • Preconditioning prevents the inhibition of Na+, K+-ATPase activity after brain ischemia
    • de Souza Wyse AT, Streck EL, Worm P, Wajner A, Ritter F, et al. Preconditioning prevents the inhibition of Na+, K+-ATPase activity after brain ischemia. Neurochem. Res. 2000; 25: 971-975.
    • (2000) Neurochem. Res , vol.25 , pp. 971-975
    • de Souza Wyse, A.T.1    Streck, E.L.2    Worm, P.3    Wajner, A.4    Ritter, F.5
  • 97
    • 44449123229 scopus 로고    scopus 로고
    • Protein kinase M zeta regulation of Na/K-ATPase: A persistent neuroprotective mechanism of ischemic preconditioning in hippocampal slice cultures
    • Tian D, Dmitrieva RI, Doris PA, Crary JF, Sondhi R, et al. Protein kinase M zeta regulation of Na/K-ATPase: a persistent neuroprotective mechanism of ischemic preconditioning in hippocampal slice cultures. Brain Res. 2008; 1213: 127-139.
    • (2008) Brain Res , vol.1213 , pp. 127-139
    • Tian, D.1    Dmitrieva, R.I.2    Doris, P.A.3    Crary, J.F.4    Sondhi, R.5
  • 98
    • 0022254432 scopus 로고
    • Characterization of the stimulation of neuronal Na(+), K(+)-ATPase activty by low concentrations of ouabain
    • Lichtstein D, Samuelov S, Bourrit A. Characterization of the stimulation of neuronal Na(+), K(+)-ATPase activty by low concentrations of ouabain. Neurochem. Int. 1985; 7: 709-715.
    • (1985) Neurochem. Int , vol.7 , pp. 709-715
    • Lichtstein, D.1    Samuelov, S.2    Bourrit, A.3
  • 99
    • 77949917575 scopus 로고    scopus 로고
    • Low-dose cardiotonic steroids increase sodium-potassium ATPase activity that protects hippocampal slice cultures from experimental ischemia
    • Oselkin M, Tian D, Bergold PJ. Low-dose cardiotonic steroids increase sodium-potassium ATPase activity that protects hippocampal slice cultures from experimental ischemia. Neurosci. Lett. 2010; 473: 67-71.
    • (2010) Neurosci. Lett , vol.473 , pp. 67-71
    • Oselkin, M.1    Tian, D.2    Bergold, P.J.3
  • 100
    • 79960167058 scopus 로고    scopus 로고
    • Hypoxic preconditioning induces neuroprotection against transient global ischemia in adult rats via preservation the activity of Na+, K+-ATPase
    • Zhan L, Peng W, Sun W, Xu E. Hypoxic preconditioning induces neuroprotection against transient global ischemia in adult rats via preservation the activity of Na+, K+-ATPase. Neurochem. Int. 2011; 59: 65-72.
    • (2011) Neurochem. Int , vol.59 , pp. 65-72
    • Zhan, L.1    Peng, W.2    Sun, W.3    Xu, E.4
  • 101
    • 80051588227 scopus 로고    scopus 로고
    • The involvement of Na+, K+-ATPase activity and free radical generation in the susceptibility to pentylenetetrazol-induced seizures after experimental traumatic brain injury
    • Silva LF, Hoffmann MS, Rambo LM, Ribeiro LR, Lima FD, et al. The involvement of Na+, K+-ATPase activity and free radical generation in the susceptibility to pentylenetetrazol-induced seizures after experimental traumatic brain injury. J. Neurol. Sci. 2011; 308: 35-40.
    • (2011) J. Neurol. Sci , vol.308 , pp. 35-40
    • Silva, L.F.1    Hoffmann, M.S.2    Rambo, L.M.3    Ribeiro, L.R.4    Lima, F.D.5
  • 102
    • 84856494477 scopus 로고    scopus 로고
    • Exercise pre-conditioning reduces brain inflammation and protects against toxicity induced by traumatic brain injury: Behavioral and neurochemical approach
    • Mota BC, Pereira L, Souza MA, Silva LF, Magni DV, et al. Exercise pre-conditioning reduces brain inflammation and protects against toxicity induced by traumatic brain injury: behavioral and neurochemical approach. Neurotox. Res. 2012; 21: 175-184.
    • (2012) Neurotox. Res , vol.21 , pp. 175-184
    • Mota, B.C.1    Pereira, L.2    Souza, M.A.3    Silva, L.F.4    Magni, D.V.5
  • 103
    • 0036154412 scopus 로고    scopus 로고
    • Endogenous digitalis-like ligands of the sodium pump: Possible involvement in mood control and ethanol addiction
    • Bagrov AY, Bagrov YY, Fedorova OV, Kashkin VA, Patkina NA, et al. Endogenous digitalis-like ligands of the sodium pump: possible involvement in mood control and ethanol addiction. Eur. Neuropsychopharmacol. 2002; 12: 1-12.
    • (2002) Eur. Neuropsychopharmacol , vol.12 , pp. 1-12
    • Bagrov, A.Y.1    Bagrov, Y.Y.2    Fedorova, O.V.3    Kashkin, V.A.4    Patkina, N.A.5
  • 104
    • 0034474422 scopus 로고    scopus 로고
    • The mood cycle hypothesis: Possible involvement of steroid hormones in mood regulation by means of Na+, K+-ATPase inhibition
    • Traub N, Lichtstein D. The mood cycle hypothesis: possible involvement of steroid hormones in mood regulation by means of Na+, K+-ATPase inhibition. J. Basic Clin. Physiol. Pharmacol. 2000; 11: 375-394.
    • (2000) J. Basic Clin. Physiol. Pharmacol , vol.11 , pp. 375-394
    • Traub, N.1    Lichtstein, D.2
  • 105
    • 0035068941 scopus 로고    scopus 로고
    • Genetic risk, number of previous depressive episodes, and stressful life events in predicting onset of major depression
    • Kendler KS, Thornton LM, Gardner CO. Genetic risk, number of previous depressive episodes, and stressful life events in predicting onset of major depression. Am. J. Psychiatry. 2001; 158: 582-586.
    • (2001) Am. J. Psychiatry , vol.158 , pp. 582-586
    • Kendler, K.S.1    Thornton, L.M.2    Gardner, C.O.3
  • 106
    • 0019257982 scopus 로고
    • Erythrocyte membrane cation carrier in manic-depressive psychosis
    • Naylor GJ, Smith AH, Dick EG, Dick DA, McHarg AM, et al. Erythrocyte membrane cation carrier in manic-depressive psychosis. Psycol. Med. 1980; 10: 521-525.
    • (1980) Psycol. Med , vol.10 , pp. 521-525
    • Naylor, G.J.1    Smith, A.H.2    Dick, E.G.3    Dick, D.A.4    McHarg, A.M.5
  • 107
    • 0024950179 scopus 로고
    • Deficient erythrocyte NaKATPase activity in different affective states in bipolar affective disorder and normalization by lithium therapy
    • Hokin-Neaverson M, Jefferson JW. Deficient erythrocyte NaKATPase activity in different affective states in bipolar affective disorder and normalization by lithium therapy. Neuropsychobiology. 1989; 22: 18-25.
    • (1989) Neuropsychobiology , vol.22 , pp. 18-25
    • Hokin-Neaverson, M.1    Jefferson, J.W.2
  • 108
    • 0026024457 scopus 로고
    • Altered in vitro adaptive responses of lymphocyte Na(+), K(+)-ATPase in patients with manic depressive psychosis
    • Wood AJ, Smith CE, Clarke EE, Cowen PJ, et al. Altered in vitro adaptive responses of lymphocyte Na(+), K(+)-ATPase in patients with manic depressive psychosis. J. Affect. Disord. 1991; 21: 199-206.
    • (1991) J. Affect. Disord , vol.21 , pp. 199-206
    • Wood, A.J.1    Smith, C.E.2    Clarke, E.E.3    Cowen, P.J.4
  • 109
    • 38649119109 scopus 로고    scopus 로고
    • Gene expression profiling of major depression and suicide in the prefrontal cortex of postmortem brains
    • Tochigi M, Iwamoto K, Bundo M, Sasaki T, Kato N, et al. Gene expression profiling of major depression and suicide in the prefrontal cortex of postmortem brains. Neurosci. Res. 2008; 60: 184-191.
    • (2008) Neurosci. Res , vol.60 , pp. 184-191
    • Tochigi, M.1    Iwamoto, K.2    Bundo, M.3    Sasaki, T.4    Kato, N.5
  • 110
    • 0041378075 scopus 로고    scopus 로고
    • Reduction of hippocampal Na+, K+-ATPase activity in rats subjected to an experimental model of depression
    • Gamaro GD, Streck EL, Matte C, Prediger ME, Wyse AT. Reduction of hippocampal Na+, K+-ATPase activity in rats subjected to an experimental model of depression. Neurochem. Res. 2003; 28: 1339-1344.
    • (2003) Neurochem. Res , vol.28 , pp. 1339-1344
    • Gamaro, G.D.1    Streck, E.L.2    Matte, C.3    Prediger, M.E.4    Wyse, A.T.5
  • 111
    • 23744476842 scopus 로고    scopus 로고
    • Na+, K+-ATPase activity is reduced in hippocampus of rats submitted to an experimental model of depression: Effect of chronic lithium treatment and possible involvement in learning deficits
    • a. de Vasconcellos AP, Zugno AI, Dos Santos AH, Nietto FB, Crema LM, et al. Na+, K+-ATPase activity is reduced in hippocampus of rats submitted to an experimental model of depression: effect of chronic lithium treatment and possible involvement in learning deficits. Neurobiol. Learn. Mem. 2005; 84: 102-110.
    • (2005) Neurobiol. Learn. Mem , vol.84 , pp. 102-110
    • de Vasconcellos, A.A.P.1    Zugno, A.I.2    Dos Santos, A.H.3    Nietto, F.B.4    Crema, L.M.5
  • 112
    • 80054864694 scopus 로고    scopus 로고
    • The transcription factor SP4 is reduced in postmortem cerebellum of bipolar disorder subjects: Control by depolarization and lithium
    • Pinacho R, Villalmanzo N, Lalonde J, Haro JM, Meana JJ, et al. The transcription factor SP4 is reduced in postmortem cerebellum of bipolar disorder subjects: control by depolarization and lithium. Bipolar Disord. 2011; 13: 474-485.
    • (2011) Bipolar Disord , vol.13 , pp. 474-485
    • Pinacho, R.1    Villalmanzo, N.2    Lalonde, J.3    Haro, J.M.4    Meana, J.J.5
  • 113
    • 79959959879 scopus 로고    scopus 로고
    • Decreased neuronal Na+, K+-ATPase activity in Atp1a3 heterozygous mice increases susceptibility to depression-like endophenotypes by chronic variable stress
    • Kirshenbaum GS, Saltzman K, Rose B, Petersen J, Vilsen B, et al. Decreased neuronal Na+, K+-ATPase activity in Atp1a3 heterozygous mice increases susceptibility to depression-like endophenotypes by chronic variable stress. Genes Brain Behav. 2011; 10: 542-550.
    • (2011) Genes Brain Behav , vol.10 , pp. 542-550
    • Kirshenbaum, G.S.1    Saltzman, K.2    Rose, B.3    Petersen, J.4    Vilsen, B.5
  • 114
    • 84872317535 scopus 로고    scopus 로고
    • Inhibition of calcineurin in the prefrontal cortex induced depressive-like behavior through mTOR signaling pathway
    • Yu JJ, Zhang Y, Wang Y, Wen ZY, Liu XH, et al. Inhibition of calcineurin in the prefrontal cortex induced depressive-like behavior through mTOR signaling pathway. Psychopharmacology (Berl). 2013; 225: 361-372.
    • (2013) Psychopharmacology (Berl) , vol.225 , pp. 361-372
    • Yu, J.J.1    Zhang, Y.2    Wang, Y.3    Wen, Z.Y.4    Liu, X.H.5
  • 115
    • 0242269060 scopus 로고    scopus 로고
    • Intracerebroventricular administration of ouabain as a model of mania in rats
    • El-Mallakh RS, El-Masri MA, Huff MO, Li XP, Decker S, et al. Intracerebroventricular administration of ouabain as a model of mania in rats. Bipolar Disord. 2003; 5: 362-365.
    • (2003) Bipolar Disord , vol.5 , pp. 362-365
    • El-Mallakh, R.S.1    El-Masri, M.A.2    Huff, M.O.3    Li, X.P.4    Decker, S.5
  • 116
    • 51349128054 scopus 로고    scopus 로고
    • Dose-dependent effect of intracerebroventricular injection of ouabain on the phosphorylation of the MEK1/2-ERK1/2-p90RSK pathway in the rat brain related to locomotor activity
    • Kim SH, Yu HS, Park HG, Jeon WJ, Song JY, et al. Dose-dependent effect of intracerebroventricular injection of ouabain on the phosphorylation of the MEK1/2-ERK1/2-p90RSK pathway in the rat brain related to locomotor activity. Prog. Neuropsychopharmacol. Biol. Psychiatry. 2008; 32: 1637-1642.
    • (2008) Prog. Neuropsychopharmacol. Biol. Psychiatry , vol.32 , pp. 1637-1642
    • Kim, S.H.1    Yu, H.S.2    Park, H.G.3    Jeon, W.J.4    Song, J.Y.5
  • 117
    • 78049440126 scopus 로고    scopus 로고
    • Activation of Akt signaling in rat brain by intracerebroventricular injection of ouabain: A rat model for mania
    • Yu HS, Kim SH, Park HG, Kim YS, Ahn YM. Activation of Akt signaling in rat brain by intracerebroventricular injection of ouabain: a rat model for mania. Prog. Neuropsychopharmacol. Biol. Psychiatry. 2010; 34: 888-894.
    • (2010) Prog. Neuropsychopharmacol. Biol. Psychiatry , vol.34 , pp. 888-894
    • Yu, H.S.1    Kim, S.H.2    Park, H.G.3    Kim, Y.S.4    Ahn, Y.M.5
  • 118
    • 80053176271 scopus 로고    scopus 로고
    • Intracerebroventricular administration of ouabain, a Na/K-ATPase inhibitor, activates tyrosine hydroxylase through extracellular signal-regulated kinase in rat striatum
    • Yu HS, Kim SH, Park HG, Kim YS, Ahn YM. Intracerebroventricular administration of ouabain, a Na/K-ATPase inhibitor, activates tyrosine hydroxylase through extracellular signal-regulated kinase in rat striatum. Neurochem. Int. 2011; 59: 779-786.
    • (2011) Neurochem. Int , vol.59 , pp. 779-786
    • Yu, H.S.1    Kim, S.H.2    Park, H.G.3    Kim, Y.S.4    Ahn, Y.M.5
  • 119
    • 33646026385 scopus 로고    scopus 로고
    • Alpha3 Na+/K+-ATPase is a neuronal receptor for agrin
    • Hilgenberg LG, Su H, Gu H, O'Dowd DK, Smith MA. Alpha3 Na+/K+-ATPase is a neuronal receptor for agrin. Cell. 2006; 125: 359-369.
    • (2006) Cell , vol.125 , pp. 359-369
    • Hilgenberg, L.G.1    Su, H.2    Gu, H.3    O'Dowd, D.K.4    Smith, M.A.5
  • 120
    • 81055130232 scopus 로고    scopus 로고
    • Mania-like behavior induced by genetic dysfunction of the neuronspecific Na+, K+-ATPase α3 sodium pump
    • Kirshenbaum GS, Clapcote SJ, Duffy S, Burgess CR, Petersen J, et al. Mania-like behavior induced by genetic dysfunction of the neuronspecific Na+, K+-ATPase α3 sodium pump. Proc. Natl. Acad. Sci. USA. 2011b; 108: 18144-18149.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 18144-18149
    • Kirshenbaum, G.S.1    Clapcote, S.J.2    Duffy, S.3    Burgess, C.R.4    Petersen, J.5
  • 121
    • 84862025297 scopus 로고    scopus 로고
    • Genetic suppression of agrin reduces mania-like behavior in Na+, K+-ATPase alpha3 mutant mice
    • Kirshenbaum GS, Clapcote SJ, Petersen J, Vilsen B, Ralph MR, et al. Genetic suppression of agrin reduces mania-like behavior in Na+, K+-ATPase alpha3 mutant mice. Genes Brain Behav. 2012; 11: 436-443.
    • (2012) Genes Brain Behav , vol.11 , pp. 436-443
    • Kirshenbaum, G.S.1    Clapcote, S.J.2    Petersen, J.3    Vilsen, B.4    Ralph, M.R.5
  • 122
    • 80055017364 scopus 로고    scopus 로고
    • Association between Na+, K+-ATPase activity and the vulnerability/resilience to mood disorders induced by early life experience
    • Silveira PP, Portella AK, Benetti Cda S, Zugno AI, Scherer EB, et al. Association between Na+, K+-ATPase activity and the vulnerability/resilience to mood disorders induced by early life experience. Neurochem. Res. 2011; 36: 2075-2082.
    • (2011) Neurochem. Res , vol.36 , pp. 2075-2082
    • Silveira, P.P.1    Portella, A.K.2    Benetti Cda, S.3    Zugno, A.I.4    Scherer, E.B.5
  • 123
    • 84984588807 scopus 로고    scopus 로고
    • Effect of repeated restraint stress and clomipramine on Na+/K+-ATPase activity and behavior in rats
    • Balk RdeS, Silva MH, Bridi JC, Carvalho NR, Portella RdeL, et al. Effect of repeated restraint stress and clomipramine on Na+/K+-ATPase activity and behavior in rats. Int. J. Dev. Neurosci. 2011; 29: 909-916.
    • (2011) Int. J. Dev. Neurosci , vol.29 , pp. 909-916
    • Balk Rde, S.1    Silva, M.H.2    Bridi, J.C.3    Carvalho, N.R.4    Portella Rde, L.5
  • 124
    • 0026570918 scopus 로고
    • Neonatal status convulsivus, spongiform encephalopathy, and low activity of Na+, K+-ATPase in the brain
    • Renkawek K, Renier WO, de Pont JJ, Vogels OJ, Gabreels FJ. Neonatal status convulsivus, spongiform encephalopathy, and low activity of Na+, K+-ATPase in the brain. Epilepsia. 1992; 33: 58-64.
    • (1992) Epilepsia , vol.33 , pp. 58-64
    • Renkawek, K.1    Renier, W.O.2    de Pont, J.J.3    Vogels, O.J.4    Gabreels, F.J.5
  • 125
    • 0014473320 scopus 로고
    • Astroglial swelling and phosphohydrolases in cerebral cortex of metrazol convulsant rats
    • De Robertis E, Alberici M, Rodríguez de Lores Arnaiz G. Astroglial swelling and phosphohydrolases in cerebral cortex of metrazol convulsant rats. Brain Res. 1969; 12: 461-466.
    • (1969) Brain Res , vol.12 , pp. 461-466
    • De Robertis, E.1    Alberici, M.2    Rodríguez de Lores Arnaiz, G.3
  • 126
    • 0025886563 scopus 로고
    • Phosphorylation of brain (Na+, K+)-ATPase alpha catalytic subunits in normal and epileptic cerebral cortex: I. The audiogenic mice and the cat with a freeze lesion
    • Guillaume D, Grisar T, Delgado-Escueta AV, Bureau-Heeren M, Laschet J. Phosphorylation of brain (Na+, K+)-ATPase alpha catalytic subunits in normal and epileptic cerebral cortex: I. The audiogenic mice and the cat with a freeze lesion. J. Neurosci. Res. 1991; 29: 207-217.
    • (1991) J. Neurosci. Res , vol.29 , pp. 207-217
    • Guillaume, D.1    Grisar, T.2    Delgado-Escueta, A.V.3    Bureau-Heeren, M.4    Laschet, J.5
  • 127
    • 0034019524 scopus 로고    scopus 로고
    • Sodium pump activity, not glial spatial buffering, clears potassium after epileptiform activity induced in the dentate gyrus
    • Xiong ZQ, Stringer JL. Sodium pump activity, not glial spatial buffering, clears potassium after epileptiform activity induced in the dentate gyrus. J. Neurophysiol. 2000; 83: 1443-1451.
    • (2000) J. Neurophysiol , vol.83 , pp. 1443-1451
    • Xiong, Z.Q.1    Stringer, J.L.2
  • 128
    • 0036899553 scopus 로고    scopus 로고
    • Mechanisms of Neuronal Hyperexcitability Caused by Partial Inhibition of Na+-K+-ATPases in the Rat CA1 Hippocampal Region
    • Vaillend C, Mason SE, Cuttle MF, Alger BE. Mechanisms of Neuronal Hyperexcitability Caused by Partial Inhibition of Na+-K+-ATPases in the Rat CA1 Hippocampal Region. J. Neurophysiol. 2002; 88: 2963-2978.
    • (2002) J. Neurophysiol , vol.88 , pp. 2963-2978
    • Vaillend, C.1    Mason, S.E.2    Cuttle, M.F.3    Alger, B.E.4
  • 129
    • 57649217301 scopus 로고    scopus 로고
    • Diverse functional consequences of mutations in the Na+/K+-ATPase alpha2-subunit causing familial hemiplegic migraine type 2
    • Tavraz NN, Friedrich T, Dürr KL, Koenderink JB, Bamberg E, et al. Diverse functional consequences of mutations in the Na+/K+-ATPase alpha2-subunit causing familial hemiplegic migraine type 2. J. Biol. Chem. 2008; 283: 31097-31106.
    • (2008) J. Biol. Chem , vol.283 , pp. 31097-31106
    • Tavraz, N.N.1    Friedrich, T.2    Dürr, K.L.3    Koenderink, J.B.4    Bamberg, E.5
  • 130
    • 2442713897 scopus 로고    scopus 로고
    • Variability of familial hemiplegic migraine with novel A1A2 Na+, K+-ATPase variants
    • Jurkat-Rott K, Freilinger T, Dreier JP, Herzog J, Göbel H, et al. Variability of familial hemiplegic migraine with novel A1A2 Na+, K+-ATPase variants. Neurology. 2004; 62: 1857-1861.
    • (2004) Neurology , vol.62 , pp. 1857-1861
    • Jurkat-Rott, K.1    Freilinger, T.2    Dreier, J.P.3    Herzog, J.4    Göbel, H.5
  • 131
    • 69549108667 scopus 로고    scopus 로고
    • Mutation I810N in the alpha3 isoform of Na+, K+-ATPase causes impairements in the sodium pump and hyperexcitability in the CNS
    • Clapcote SJ, Duffy S, Xie G, Kirshenbaum G, Bechard AR, et al. Mutation I810N in the alpha3 isoform of Na+, K+-ATPase causes impairements in the sodium pump and hyperexcitability in the CNS. Proc. Natl. Acad. Sci. USA. 2009; 106: 14085-14090.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 14085-14090
    • Clapcote, S.J.1    Duffy, S.2    Xie, G.3    Kirshenbaum, G.4    Bechard, A.R.5
  • 132
    • 0037465375 scopus 로고    scopus 로고
    • Evidence for a separate type of migraine with aura: Sporadic hemiplegic migraine
    • Thomsen LL, Ostergaard E, Olesen J, Russell MB. Evidence for a separate type of migraine with aura: sporadic hemiplegic migraine. Neurology. 2003; 60: 595-601.
    • (2003) Neurology , vol.60 , pp. 595-601
    • Thomsen, L.L.1    Ostergaard, E.2    Olesen, J.3    Russell, M.B.4
  • 133
    • 50249149461 scopus 로고    scopus 로고
    • A novel de novo nonsense mutation in ATP1A2 associated with sporadic hemiplegic migraine and epileptic seizures
    • Gallanti A, Tonelli A, Cardin V, Bussone G, Bresolin N, et al. A novel de novo nonsense mutation in ATP1A2 associated with sporadic hemiplegic migraine and epileptic seizures. J. Neurol. Sci. 2008; 273: 123-126.
    • (2008) J. Neurol. Sci , vol.273 , pp. 123-126
    • Gallanti, A.1    Tonelli, A.2    Cardin, V.3    Bussone, G.4    Bresolin, N.5
  • 134
    • 84856109223 scopus 로고    scopus 로고
    • Migraine-and dystoniarelated disease-mutations of Na+/K+-ATPases: Relevance of behavioral studies in mice to disease symptoms and neurological manifestations in humans
    • Bøttger P, Doǧanli C, Lykke-Hartmann K. Migraine-and dystoniarelated disease-mutations of Na+/K+-ATPases: relevance of behavioral studies in mice to disease symptoms and neurological manifestations in humans. Neurosci. Biobehav. Rev. 2012; 36: 855-871.
    • (2012) Neurosci. Biobehav. Rev , vol.36 , pp. 855-871
    • Bøttger, P.1    Doǧanli, C.2    Lykke-Hartmann, K.3
  • 135
    • 0037613733 scopus 로고    scopus 로고
    • Dopamine oxidation products inhibit Na+, K+-ATPase activity in crude synaptosomal-mitochondrial fraction from rat brain
    • Khan FH, Sen T, Chakrabarti S. Dopamine oxidation products inhibit Na+, K+-ATPase activity in crude synaptosomal-mitochondrial fraction from rat brain. Free Radic. Res. 2003; 37: 597-601.
    • (2003) Free Radic. Res , vol.37 , pp. 597-601
    • Khan, F.H.1    Sen, T.2    Chakrabarti, S.3
  • 136
    • 33846011388 scopus 로고    scopus 로고
    • New roles for an old enzyme: Na, K-ATPase emerges as an interesting drug target
    • Aperia A. new roles for an old enzyme: Na, K-ATPase emerges as an interesting drug target. J. Intern. Med. 2007; 261: 44-52.
    • (2007) J. Intern. Med , vol.261 , pp. 44-52
    • Aperia, A.1
  • 137
    • 84878491934 scopus 로고    scopus 로고
    • Intracerebroventricular administration of ouabain, a Na/K-ATPase inhibitor, activates mTOR signal pathways and protein translation in the rat frontal cortex
    • Kim SH, Yu HS, Park HG, Ha K, Kim YS, et al. Intracerebroventricular administration of ouabain, a Na/K-ATPase inhibitor, activates mTOR signal pathways and protein translation in the rat frontal cortex. Prog. Neuropsychopharmacol. Biol. Psychiatry. 2013; 45C: 73-82.
    • (2013) Prog. Neuropsychopharmacol. Biol. Psychiatry , vol.45 C , pp. 73-82
    • Kim, S.H.1    Yu, H.S.2    Park, H.G.3    Ha, K.4    Kim, Y.S.5
  • 138
    • 84880395280 scopus 로고    scopus 로고
    • Treadmill exercise protects against pentylenetetrazol-induced seizures and oxidative stress after traumatic brain injury
    • Silva LF, Hoffmann MS, Gerbatin Rda R, Fiorin Fda S, Dobrachinski F, et al. Treadmill exercise protects against pentylenetetrazol-induced seizures and oxidative stress after traumatic brain injury. J. Neurotrauma. 2013; 30: 1278-1287.
    • (2013) J. Neurotrauma , vol.30 , pp. 1278-1287
    • Silva, L.F.1    Hoffmann, M.S.2    Gerbatin Rda, R.3    Fiorin Fda, S.4    Dobrachinski, F.5
  • 139
    • 67349143998 scopus 로고    scopus 로고
    • Classification and basic pathology of Alzheimer disease
    • Duyckaerts C, Delatour B, Potier MC. Classification and basic pathology of Alzheimer disease. Acta Neuropathol. 2009; 118: 5-36.
    • (2009) Acta Neuropathol , vol.118 , pp. 5-36
    • Duyckaerts, C.1    Delatour, B.2    Potier, M.C.3
  • 140
    • 84882530203 scopus 로고    scopus 로고
    • Neurobiology of Alzheimer's Disease
    • In: Brady ST, Siegel GJ, Albers RW, Price D (Eds.), Basic Neurochemistry: Principles of Molecular, Cellular and Medical Neurobiology, 8th edn
    • Wong PC, Savonenko A, Li T, Price DL. Neurobiology of Alzheimer's Disease. In: Brady ST, Siegel GJ, Albers RW, Price D (Eds.), Basic Neurochemistry: Principles of Molecular, Cellular and Medical Neurobiology, 8th edn. Massachusetts, USA: Elsevier Academic Press. 2012; 815-828.
    • (2012) Massachusetts, USA: Elsevier Academic Press , pp. 815-828
    • Wong, P.C.1    Savonenko, A.2    Li, T.3    Price, D.L.4
  • 141
    • 0025699745 scopus 로고
    • Changes in Na+, K+-ATPase, Ca2+-ATPase and some soluble enzymes related to energy metabolism in brains of patients with Alzheimer's disease
    • Liguri G, Taddei N, Nassi P, Latorraca S, Neidiani C, et al. Changes in Na+, K+-ATPase, Ca2+-ATPase and some soluble enzymes related to energy metabolism in brains of patients with Alzheimer's disease. Neurosci. Lett. 1990; 112: 338-342.
    • (1990) Neurosci. Lett , vol.112 , pp. 338-342
    • Liguri, G.1    Taddei, N.2    Nassi, P.3    Latorraca, S.4    Neidiani, C.5
  • 142
    • 0028981159 scopus 로고
    • Amyloid betapeptide impairs ion-motive ATPase activities: Evidence for a role in loss of neuronal Ca2+ homeostasis and cell death
    • Marck RJ, Hensley K, Butterfield DA, Mattson MP. Amyloid betapeptide impairs ion-motive ATPase activities: evidence for a role in loss of neuronal Ca2+ homeostasis and cell death. J. Neurosci. 1995; 15: 6239-6249.
    • (1995) J. Neurosci , vol.15 , pp. 6239-6249
    • Marck, R.J.1    Hensley, K.2    Butterfield, D.A.3    Mattson, M.P.4
  • 143
    • 0031020993 scopus 로고    scopus 로고
    • Amyloid beta-peptide impairs glucose transport in hippocampaland cortical neurons: Involvement of membrane lipid peroxidation
    • Marck RJ, Pang Z, Geddes JW, Uchida K, Mattson MP. Amyloid beta-peptide impairs glucose transport in hippocampaland cortical neurons: Involvement of membrane lipid peroxidation. J. Neurosci. 1997b; 17: 1046-1054.
    • (1997) J. Neurosci , vol.17 , pp. 1046-1054
    • Marck, R.J.1    Pang, Z.2    Geddes, J.W.3    Uchida, K.4    Mattson, M.P.5
  • 144
    • 0030902464 scopus 로고    scopus 로고
    • Basic FGF attenuates beta-peptide-induced oxidative stress, mitochondrial dysfunction, and impairment of Na+/K+-ATPase activity hippocampal neurons
    • Marck RJ, Keller JN, Kruman I, Mattson MP. Basic FGF attenuates beta-peptide-induced oxidative stress, mitochondrial dysfunction, and impairment of Na+/K+-ATPase activity hippocampal neurons. Brain Res. 1997; 756: 205-214.
    • (1997) Brain Res , vol.756 , pp. 205-214
    • Marck, R.J.1    Keller, J.N.2    Kruman, I.3    Mattson, M.P.4
  • 145
    • 0032527386 scopus 로고    scopus 로고
    • Amyloid betapeptides inhibit Na+, K+-ATPase: Tissue slices versus primary cultures
    • Bores GM, Smith CP, Wirtz-Brugger F, Giovanni A. Amyloid betapeptides inhibit Na+, K+-ATPase: tissue slices versus primary cultures. Brain Res. Bull. 1998; 46: 423-427.
    • (1998) Brain Res. Bull , vol.46 , pp. 423-427
    • Bores, G.M.1    Smith, C.P.2    Wirtz-Brugger, F.3    Giovanni, A.4
  • 148
    • 84869090391 scopus 로고    scopus 로고
    • Calcium phosphatase calcineurin influences tau metabolism
    • Karch CM, Jeng AT, Goate AM. Calcium phosphatase calcineurin influences tau metabolism. Neurobiol. Aging. 2013; 34: 374-386.
    • (2013) Neurobiol. Aging , vol.34 , pp. 374-386
    • Karch, C.M.1    Jeng, A.T.2    Goate, A.M.3
  • 149
    • 77249158836 scopus 로고    scopus 로고
    • Amyloid beta induces the morphological neurodegenerative triad of spine loss, dendritic simplification, and neuritic dystrophies through calcineurin activation
    • Wu HY, Hudry E, Hashimoto T, Kuchibhotla K, Rozkaine A, et al. Amyloid beta induces the morphological neurodegenerative triad of spine loss, dendritic simplification, and neuritic dystrophies through calcineurin activation. J. Neurosci. 2010; 30: 2636-2649.
    • (2010) J. Neurosci , vol.30 , pp. 2636-2649
    • Wu, H.Y.1    Hudry, E.2    Hashimoto, T.3    Kuchibhotla, K.4    Rozkaine, A.5
  • 150
    • 84857642949 scopus 로고    scopus 로고
    • The toxic A β oligomer and Alzheimer's disease: An emperor in need of clothes
    • Benilova I, Karran E, De Strooper B. The toxic A β oligomer and Alzheimer's disease: an emperor in need of clothes. Nat. Neurosci. 2012; 15: 349-357.
    • (2012) Nat. Neurosci , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 151
    • 84884200967 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer Aβ oligomer bound to cellular prion protein
    • Um JW, Kaufman AC, Kostylev M, Heiss JK, Stagi M, et al. Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer Aβ oligomer bound to cellular prion protein. Neuron. 2013; 79: 887-902.
    • (2013) Neuron , vol.79 , pp. 887-902
    • Um, J.W.1    Kaufman, A.C.2    Kostylev, M.3    Heiss, J.K.4    Stagi, M.5
  • 152
    • 79955484857 scopus 로고    scopus 로고
    • Abeta(1-42) inhibition of LTP is mediated by a signaling pathway involving caspase-3, Akt1 and GSK-3beta
    • Jo J, Whicomb DJ, Olsen KM, Kerrigan TL, Lo SC, et al. Abeta(1-42) inhibition of LTP is mediated by a signaling pathway involving caspase-3, Akt1 and GSK-3beta. Nat. Neurosci. 2011; 14: 545-547.
    • (2011) Nat. Neurosci , vol.14 , pp. 545-547
    • Jo, J.1    Whicomb, D.J.2    Olsen, K.M.3    Kerrigan, T.L.4    Lo, S.C.5
  • 153
    • 84903513733 scopus 로고    scopus 로고
    • β-Amyloid impairs the regulation of N-methyl-D-aspartate receptors by glycogen synthase kinase 3
    • [Epub ahead]
    • Deng Y, Xiong Z, Chen P, Wei J, Chen S, et al. β-Amyloid impairs the regulation of N-methyl-D-aspartate receptors by glycogen synthase kinase 3. Neurobiol. Aging. 2013 [Epub ahead].
    • (2013) Neurobiol. Aging
    • Deng, Y.1    Xiong, Z.2    Chen, P.3    Wei, J.4    Chen, S.5
  • 154
    • 84890660655 scopus 로고    scopus 로고
    • Dysregulation of synaptic and extrasynaptic N-methyl-D-aspartate receptors induced by amyloid-β
    • oct 17 [Epub ahead of print]
    • Wang ZC, Zhao J, Li S. Dysregulation of synaptic and extrasynaptic N-methyl-D-aspartate receptors induced by amyloid-β. Neurosci. Bull. 2013; oct 17 [Epub ahead of print].
    • (2013) Neurosci. Bull
    • Wang, Z.C.1    Zhao, J.2    Li, S.3
  • 156
    • 36949018704 scopus 로고    scopus 로고
    • The expression of NMDA receptor subunits in cerebral cortex and hippocampus is differentially increased by administration of endobain E, a Na+, K+-ATPase inhibitor
    • Bersier MG, Peña C, Rodríguez de Lores Arnaiz G. The expression of NMDA receptor subunits in cerebral cortex and hippocampus is differentially increased by administration of endobain E, a Na+, K+-ATPase inhibitor. Neurochem. Res. 2008; 33: 66-72.
    • (2008) Neurochem. Res , vol.33 , pp. 66-72
    • Bersier, M.G.1    Peña, C.2    Rodríguez de Lores Arnaiz, G.3
  • 157
    • 68349144128 scopus 로고    scopus 로고
    • Intracerebroventricular administration of ouabain to rats changes the expression of NMDA receptor subunits in cerebral cortex and hippocampus
    • Bersier MG, Rodríguez de Lores Arnaiz G. Intracerebroventricular administration of ouabain to rats changes the expression of NMDA receptor subunits in cerebral cortex and hippocampus. Neurochem. Res. 2009; 34: 1650-1657.
    • (2009) Neurochem. Res , vol.34 , pp. 1650-1657
    • Bersier, M.G.1    Rodríguez de Lores Arnaiz, G.2
  • 158
    • 84855755558 scopus 로고    scopus 로고
    • NMDA receptor-mediated PIP5K activation to produce PI(4, 5)P2 is essential for AMPA receptor endocytosis during LTD
    • Unoki T, Matsuda S, Kakegawa W, Van NT, Kohda K, et al. NMDA receptor-mediated PIP5K activation to produce PI(4, 5)P2 is essential for AMPA receptor endocytosis during LTD. Neuron. 2012; 73: 135-148.
    • (2012) Neuron , vol.73 , pp. 135-148
    • Unoki, T.1    Matsuda, S.2    Kakegawa, W.3    Van, N.T.4    Kohda, K.5
  • 159
    • 0345304422 scopus 로고    scopus 로고
    • Effects of steroid hormones on (Na+, K+)-ATPase activity inhibition-induced amnesia on the step-through passive avoidance task in gonadectomized mice
    • Sato T, Tanaka K, Ohnishi Y, Teramoto T, Irifune M, et al. Effects of steroid hormones on (Na+, K+)-ATPase activity inhibition-induced amnesia on the step-through passive avoidance task in gonadectomized mice. Pharmacol. Res. 2004; 49: 151-159.
    • (2004) Pharmacol. Res , vol.49 , pp. 151-159
    • Sato, T.1    Tanaka, K.2    Ohnishi, Y.3    Teramoto, T.4    Irifune, M.5
  • 160
    • 0027931391 scopus 로고
    • The linked roles of nitric oxide, aldose reductase and (Na+-K+)-ATPase in the slowing of nerve conduction in the streptozotocin diabetic rat
    • Stevens MJ, Dananberg J, Feldman EL, Lattimer SA, Kamijo M, et al. The linked roles of nitric oxide, aldose reductase and (Na+-K+)-ATPase in the slowing of nerve conduction in the streptozotocin diabetic rat. J. Clin. Invest. 1994; 94: 853-859.
    • (1994) J. Clin. Invest , vol.94 , pp. 853-859
    • Stevens, M.J.1    Dananberg, J.2    Feldman, E.L.3    Lattimer, S.A.4    Kamijo, M.5
  • 161
    • 0016723851 scopus 로고
    • Effect of insulin upon membrane-bound (Na+/K+-ATPase)-ATPase extracted from skeletal muscle
    • Garvryck WA, Moore RD, Thompson RC. Effect of insulin upon membrane-bound (Na+/K+-ATPase)-ATPase extracted from skeletal muscle. J. Physiol. 1975; 252: 43-58.
    • (1975) J. Physiol , vol.252 , pp. 43-58
    • Garvryck, W.A.1    Moore, R.D.2    Thompson, R.C.3
  • 162
    • 0023263496 scopus 로고
    • Insulin modifies Na+, K+-ATPase activity of synaptosomal membranes and whole homogenates prepared from rat cerebral cortex
    • Bojorge G, Rodríguez de Lores Arnaiz G. Insulin modifies Na+, K+-ATPase activity of synaptosomal membranes and whole homogenates prepared from rat cerebral cortex. Neurochem. Int. 1987; 11: 11-16.
    • (1987) Neurochem. Int , vol.11 , pp. 11-16
    • Bojorge, G.1    Rodríguez de Lores Arnaiz, G.2
  • 163
    • 0025333184 scopus 로고
    • Insulin activation of brain Na(+) + K(+) ATPase is medi ated by alpha 2-isoform of enzyme
    • Brodsky JL. Insulin activation of brain Na(+) + K(+) ATPase is medi ated by alpha 2-isoform of enzyme. American J. Physiol. 1990; 258 Issue 5 Pt. 1, C812-C817.
    • (1990) American J. Physiol , vol.258 , Issue.5 PART 1
    • Brodsky, J.L.1
  • 164
    • 0035691617 scopus 로고    scopus 로고
    • The mechanism of alloxan and streptozotocin action in B cells of the rat pancreas
    • Szkudelski T. The mechanism of alloxan and streptozotocin action in B cells of the rat pancreas. Physiol. Res. 2001; 50: 537-546.
    • (2001) Physiol. Res , vol.50 , pp. 537-546
    • Szkudelski, T.1
  • 165
    • 0029090095 scopus 로고
    • Alterations in the properties and isoform ratios of brain Na+/K+-ATPase in streptozotocin diabetic rats
    • Vér A, Csermely P, Bányász T, Kovács T, Somogyi J. Alterations in the properties and isoform ratios of brain Na+/K+-ATPase in streptozotocin diabetic rats. Biochim. Biophys. Acta. 1995; 1237: 143-150.
    • (1995) Biochim. Biophys. Acta , vol.1237 , pp. 143-150
    • Vér, A.1    Csermely, P.2    Bányász, T.3    Kovács, T.4    Somogyi, J.5
  • 166
    • 0034999874 scopus 로고    scopus 로고
    • Reduced Na-K pump but increased Na-K-2Cl cotransporter in aorta of streptozotocin-induced diabetic rat
    • Michea L, Irribarra V, Goecke IA, Marusic ET. Reduced Na-K pump but increased Na-K-2Cl cotransporter in aorta of streptozotocin-induced diabetic rat. Am. J. Physiol. Heart Circ. Physiol. 2001; 280: H851-H858.
    • (2001) Am. J. Physiol. Heart Circ. Physiol , vol.280
    • Michea, L.1    Irribarra, V.2    Goecke, I.A.3    Marusic, E.T.4
  • 167
    • 67349149365 scopus 로고    scopus 로고
    • Effects of adult-onset streptpzotocin-induced diabetes on the rat brain antioxidant status and the activities of acetylcholinesterase, Na(+), K(+)-and Mg(2+)-ATPase: Modulation by cysteine
    • Zarros A, Liapi C, Galanopoulou P, Marinou K, Mellios Z, et al. Effects of adult-onset streptpzotocin-induced diabetes on the rat brain antioxidant status and the activities of acetylcholinesterase, Na(+), K(+)-and Mg(2+)-ATPase: modulation by cysteine. Metab. Brain Dis. 2009; 24: 337-348.
    • (2009) Metab. Brain Dis , vol.24 , pp. 337-348
    • Zarros, A.1    Liapi, C.2    Galanopoulou, P.3    Marinou, K.4    Mellios, Z.5
  • 169
    • 42149145554 scopus 로고    scopus 로고
    • The sodium pump could constitute a new target to combat gliobastomas
    • Lefranc F, Mijatovic T, Kiss R. The sodium pump could constitute a new target to combat gliobastomas. Bull. Cancer. 2008; 95: 271-281.
    • (2008) Bull. Cancer , vol.95 , pp. 271-281
    • Lefranc, F.1    Mijatovic, T.2    Kiss, R.3
  • 170
    • 40149110392 scopus 로고    scopus 로고
    • The sodium pump alpha1 subunit as a potential target to combat apoptosis-resistant gliobastomas
    • Lefranc F, Kiss R. The sodium pump alpha1 subunit as a potential target to combat apoptosis-resistant gliobastomas. Neoplasia. 2008; 10: 198-206.
    • (2008) Neoplasia , vol.10 , pp. 198-206
    • Lefranc, F.1    Kiss, R.2
  • 171
    • 77649218255 scopus 로고    scopus 로고
    • FXYD3 expression in gliomas and its clinicopathological significance
    • Wang MW, Gu P, Zhang ZL, Zhu ZL, Geng Y, et al. FXYD3 expression in gliomas and its clinicopathological significance. Oncol. Res. 2009; 18: 133-139.
    • (2009) Oncol. Res , vol.18 , pp. 133-139
    • Wang, M.W.1    Gu, P.2    Zhang, Z.L.3    Zhu, Z.L.4    Geng, Y.5
  • 172
    • 0011394545 scopus 로고
    • Properties of the isolated nerve endings
    • In: Bronner F, Kleinzeller A (Eds.) Nueva York, USA: Academic Press
    • Rodríguez de Lores Arnaiz G, De Robertis E. Properties of the isolated nerve endings. In: Bronner F, Kleinzeller A (Eds.) Current Topics in Membranes and Transport, Vol. III. Nueva York, USA: Academic Press. 1972; p237-272.
    • (1972) Current Topics in Membranes and Transport , vol.3 , pp. 237-272
    • Rodríguez de Lores Arnaiz, G.1    De Robertis, E.2
  • 173
    • 84862777147 scopus 로고    scopus 로고
    • Short-term memory of network performance via activity-dependent potentiation of Na+/K+ pump function
    • Zhang NY, Sillar KT. Short-term memory of network performance via activity-dependent potentiation of Na+/K+ pump function. Curr. Biol. 2013; 22: 526-531.
    • (2013) Curr. Biol , vol.22 , pp. 526-531
    • Zhang, N.Y.1    Sillar, K.T.2
  • 174
    • 80054823126 scopus 로고    scopus 로고
    • Ifenprodil restores GDNF-evoked Ca(2+) signaling and Na(+)/K(+)-ATPase expression in inflammation-pretreated astrocytes
    • Lundborg C, Westerlund A, Björklund U, Biber B, Hansson E. Ifenprodil restores GDNF-evoked Ca(2+) signaling and Na(+)/K(+)-ATPase expression in inflammation-pretreated astrocytes. J. Neurochem. 2011; 119: 6 86-696.
    • (2011) J. Neurochem , vol.119 , pp. 686-696
    • Lundborg, C.1    Westerlund, A.2    Björklund, U.3    Biber, B.4    Hansson, E.5
  • 175
    • 35048900274 scopus 로고    scopus 로고
    • Sp3 and Sp4 transcription factor levels are increased in brains of patients with Alzheimer disease
    • Boutillier S, Lannes B, Buée L, Delacourte A, Rouaux C, et al. Sp3 and Sp4 transcription factor levels are increased in brains of patients with Alzheimer disease. Neurodegener. Dis. 2007; 4: 413-423.
    • (2007) Neurodegener. Dis , vol.4 , pp. 413-423
    • Boutillier, S.1    Lannes, B.2    Buée, L.3    Delacourte, A.4    Rouaux, C.5


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