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Volumn 1661, Issue 1, 2004, Pages 40-46

Polarized distribution of Na+, K+-ATPase α-subunit isoforms in electrocyte membranes

Author keywords

Electrophorus electricus (L.); Immunohistochemistry; Na+, K+ ATPase; Ouabain binding; Subunit isoform

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ELECTROLYTE; OUABAIN;

EID: 1042274830     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2003.11.020     Document Type: Article
Times cited : (5)

References (42)
  • 1
    • 0001409028 scopus 로고
    • The influence of some cations on an adenosine triphosphatase from peripheral nerves
    • Skou J.C. The influence of some cations on an adenosine triphosphatase from peripheral nerves. Biochim. Biophys. Acta. 23:1957;394-401.
    • (1957) Biochim. Biophys. Acta , vol.23 , pp. 394-401
    • Skou, J.C.1
  • 3
    • 0002591052 scopus 로고
    • The Na,K-Transporting adenosine triphosphatase
    • A. Martonosi. New York: Plenum
    • Glynn I.M. The Na,K-Transporting adenosine triphosphatase. Martonosi A. The Enzymes of Biological Membranes. 2nd ed. 1985;35-114 Plenum, New York.
    • (1985) The Enzymes of Biological Membranes 2nd Ed. , pp. 35-114
    • Glynn, I.M.1
  • 4
    • 0027281005 scopus 로고
    • Molecular cloning and immunological characterization of the γ polypeptide, a small protein associated with the Na,K-ATPase
    • Mercer R.W., Biemesderfer D., Bliss D.P. Jr., Collins J.H., Forbush B. III Molecular cloning and immunological characterization of the γ polypeptide, a small protein associated with the Na,K-ATPase. J. Cell Biol. 121:1993;579-586.
    • (1993) J. Cell Biol. , vol.121 , pp. 579-586
    • Mercer, R.W.1    Biemesderfer, D.2    Bliss Jr., D.P.3    Collins, J.H.4    Forbush III, B.5
  • 5
    • 0035133295 scopus 로고    scopus 로고
    • Sodium-potassium-adenosinetriphosphatase-dependent sodium transport in the kidney: Hormonal control
    • Féraille E., Doucet A. Sodium-potassium-adenosinetriphosphatase- dependent sodium transport in the kidney: hormonal control. Physiol. Rev. 81:2001;345-418.
    • (2001) Physiol. Rev. , vol.81 , pp. 345-418
    • Féraille, E.1    Doucet, A.2
  • 6
    • 0029137474 scopus 로고
    • Functional significance of the beta-subunit for heterodimeric P-type ATPases
    • Chow D.C., Forte J.G. Functional significance of the beta-subunit for heterodimeric P-type ATPases. J. Exp. Biol. 198:1995;1-17.
    • (1995) J. Exp. Biol. , vol.198 , pp. 1-17
    • Chow, D.C.1    Forte, J.G.2
  • 7
    • 0022253869 scopus 로고
    • Two isozymes of the Na,K-ATPase have distinct antigenic determinants
    • Sweadner K.J., Gilkeson R.C. Two isozymes of the Na,K-ATPase have distinct antigenic determinants. J. Biol. Chem. 260:1985;9016-9022.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9016-9022
    • Sweadner, K.J.1    Gilkeson, R.C.2
  • 8
    • 0026794402 scopus 로고
    • Nucleotide, protein Primary sequence and functional expression of a novel ouabain-resistant Na,K-ATPase. the beta subunit modulates potassium activation of the Na,K-pump
    • Jaisser F., Canessa C.M., Horisberger J.D., Rossier B.C. Nucleotide, protein Primary sequence and functional expression of a novel ouabain-resistant Na,K-ATPase. The beta subunit modulates potassium activation of the Na,K-pump. J. Biol. Chem. 267:1992;16895-16903.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16895-16903
    • Jaisser, F.1    Canessa, C.M.2    Horisberger, J.D.3    Rossier, B.C.4
  • 10
    • 0029147014 scopus 로고
    • Na,K-ATPase inhibitors from bovine hypothalamus and human plasma are different from ouabain: Nanogram scale CD structural analysis
    • Zhao N., Lo L.C., Berova N., Nakanishi K., Tymiak A.A., Ludens J.H., Haupert G.T. Jr. Na,K-ATPase inhibitors from bovine hypothalamus and human plasma are different from ouabain: nanogram scale CD structural analysis. Biochemistry. 34:1995;9893-9896.
    • (1995) Biochemistry , vol.34 , pp. 9893-9896
    • Zhao, N.1    Lo, L.C.2    Berova, N.3    Nakanishi, K.4    Tymiak, A.A.5    Ludens, J.H.6    Haupert, G.T.Jr.7
  • 11
    • 0029781307 scopus 로고    scopus 로고
    • Na-K-ATPase isoform (alpha 3, alpha 2, alpha 1) abundance in rat kidney estimated by competitive RT-PCR and ouabain binding
    • Lucking K., Nielsen J.M., Pedersen P.A., Jørgensen P.L. Na-K-ATPase isoform (alpha 3, alpha 2, alpha 1) abundance in rat kidney estimated by competitive RT-PCR and ouabain binding. Am. J. Physiol. 271:1996;F253-F260.
    • (1996) Am. J. Physiol. , vol.271
    • Lucking, K.1    Nielsen, J.M.2    Pedersen, P.A.3    Jørgensen, P.L.4
  • 17
    • 0025165830 scopus 로고
    • Stability of Na,K-ATPase alpha-subunit isoforms in evolution
    • Takeyasu K., Lemas V., Fambrough D.M. Stability of Na,K-ATPase alpha-subunit isoforms in evolution. Am. J. Physiol. 259:1990;C619-C630.
    • (1990) Am. J. Physiol. , vol.259
    • Takeyasu, K.1    Lemas, V.2    Fambrough, D.M.3
  • 19
    • 0030762991 scopus 로고    scopus 로고
    • Ion pumps in epithelial cells: Sorting, stabilization, and polarity
    • Caplan M.J. Ion pumps in epithelial cells: sorting, stabilization, and polarity. Am. J. Physiol. 272:1997;G1304-G1313.
    • (1997) Am. J. Physiol. , vol.272
    • Caplan, M.J.1
  • 20
    • 84919876011 scopus 로고
    • Membrane potentials in the electroplates of the electric eel
    • Keynes R.D., Martins Ferreira H. Membrane potentials in the electroplates of the electric eel. J. Physiol. 119:1953;315-351.
    • (1953) J. Physiol. , vol.119 , pp. 315-351
    • Keynes, R.D.1    Martins Ferreira, H.2
  • 21
    • 0031966449 scopus 로고    scopus 로고
    • Electrophorus electricus as a model system for the study of membrane excitability
    • Gotter A.L., Kaetzel M.A., Dedman J.R. Electrophorus electricus as a model system for the study of membrane excitability. Comp. Biochem. Physiol., A. 119:1998;225-241.
    • (1998) Comp. Biochem. Physiol., a , vol.119 , pp. 225-241
    • Gotter, A.L.1    Kaetzel, M.A.2    Dedman, J.R.3
  • 22
    • 0017662913 scopus 로고
    • Biochemical and cytochemical localization of ATPases on the membranes of the electrocyte of Electrophorus electricus (L.)
    • Somló C., Souza W., Machado R.D., Hassón-Voloch A. Biochemical and cytochemical localization of ATPases on the membranes of the electrocyte of Electrophorus electricus (L.). Cell Tissue Res. 185:1977;115-128.
    • (1977) Cell Tissue Res. , vol.185 , pp. 115-128
    • Somló, C.1    Souza, W.2    MacHado, R.D.3    Hassón-Voloch, A.4
  • 23
    • 0004354146 scopus 로고
    • Localization histochimique de l'acetylcholinesterase dans le tissue electrique de l'Electrophorus electricus (L.)
    • Couceiro A., de Almeida D.F., Freire J.R.C. Localization histochimique de l'acetylcholinesterase dans le tissue electrique de l'Electrophorus electricus (L.). An. Acad. Bras. Cienc. 25:1953;205-214.
    • (1953) An. Acad. Bras. Cienc. , vol.25 , pp. 205-214
    • Couceiro, A.1    De Almeida, D.F.2    Freire, J.R.C.3
  • 24
    • 0018132373 scopus 로고
    • Quantitative studies on localization of the cholinergic receptor protein in normal and denervated electroplaque from Electrophorus electricus (L.)
    • Bourgeois J.P., Popot J.L., Ryter A., Changeux J.P. Quantitative studies on localization of the cholinergic receptor protein in normal and denervated electroplaque from Electrophorus electricus (L.). J. Cell Biol. 79:1978;200-216.
    • (1978) J. Cell Biol. , vol.79 , pp. 200-216
    • Bourgeois, J.P.1    Popot, J.L.2    Ryter, A.3    Changeux, J.P.4
  • 25
    • 0344950793 scopus 로고
    • The flux of cations in the single isolated electroplax of Electrophorus electricus (L.)
    • C. Chagas, & A. Paes de Carvalho. New York: Elsevier
    • Schoffeniels E. The flux of cations in the single isolated electroplax of Electrophorus electricus (L.). Chagas C., Paes de Carvalho A. Bioelectrogenesis. 1961;147-165 Elsevier, New York.
    • (1961) Bioelectrogenesis , pp. 147-165
    • Schoffeniels, E.1
  • 28
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske C.H., Subbarow Y. The colorimetric determination of phosphorus. J. Biol. Chem. 66:1925;375-400.
    • (1925) J. Biol. Chem. , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 29
    • 0000881529 scopus 로고
    • Reversible inhibition of electric organs cholinesterase by curare and curare-like agents
    • Hassón A., Liepin L.L. Reversible inhibition of electric organs cholinesterase by curare and curare-like agents. Biochim. Biophys. Acta. 75:1963;397-401.
    • (1963) Biochim. Biophys. Acta , vol.75 , pp. 397-401
    • Hassón, A.1    Liepin, L.L.2
  • 30
    • 0034268893 scopus 로고    scopus 로고
    • Choline acetyltransferase detection in normal and denervated electrocyte from Electrophorus electricus (L.) using a confocal scanning optical microscopy analysis
    • Nunes-Tavares N., Cunha-E-Silva N.L., Hassón-Voloch A. Choline acetyltransferase detection in normal and denervated electrocyte from Electrophorus electricus (L.) using a confocal scanning optical microscopy analysis. An. Acad. Bras. Cienc. 72:2000;331-340.
    • (2000) An. Acad. Bras. Cienc. , vol.72 , pp. 331-340
    • Nunes-Tavares, N.1    Cunha-E-Silva, N.L.2    Hassón-Voloch, A.3
  • 31
    • 0014957333 scopus 로고
    • Localization of acetylcholinesterase by immunofluorescence in eel electroplax
    • Benda P., Tsuji S., Daussant J., Changeux J.P. Localization of acetylcholinesterase by immunofluorescence in eel electroplax. Nature. 225:1970;1149-1150.
    • (1970) Nature , vol.225 , pp. 1149-1150
    • Benda, P.1    Tsuji, S.2    Daussant, J.3    Changeux, J.P.4
  • 35
    • 0031758268 scopus 로고    scopus 로고
    • Isozymes of the Na-K-ATPase: Heterogeneity in structure, diversity in function
    • Blanco G., Mercer R.W. Isozymes of the Na-K-ATPase: heterogeneity in structure, diversity in function. Am. J. Physiol. 275:1998;F633-F650.
    • (1998) Am. J. Physiol. , vol.275
    • Blanco, G.1    Mercer, R.W.2
  • 36
    • 0028024616 scopus 로고
    • Endogenous ouabain: Physiological activity and pathophysiological implications
    • Blaustein M.P. Endogenous ouabain: physiological activity and pathophysiological implications. Clin. Investig. 72:1994;706-707.
    • (1994) Clin. Investig. , vol.72 , pp. 706-707
    • Blaustein, M.P.1
  • 37
    • 0036098774 scopus 로고    scopus 로고
    • +-ATPase as a signal transducer
    • +-ATPase as a signal transducer. Eur. J. Biochem. 284:2002;2432-2439.
    • (2002) Eur. J. Biochem. , vol.284 , pp. 2432-2439
    • Xie, Z.1    Askari, A.2
  • 38
    • 0027491624 scopus 로고
    • Kinetics analysis of ouabain binding to native and mutated forms of Na,K-ATPase and identification of a new region involved in cardiac glycoside interactions
    • Schultheis P.J., Wallick E.T., Lingrel J.B. Kinetics analysis of ouabain binding to native and mutated forms of Na,K-ATPase and identification of a new region involved in cardiac glycoside interactions. J. Biol. Chem. 268/30:1993;22686-22694.
    • (1993) J. Biol. Chem. , vol.268 , Issue.30 , pp. 22686-22694
    • Schultheis, P.J.1    Wallick, E.T.2    Lingrel, J.B.3
  • 41
    • 0031052476 scopus 로고    scopus 로고
    • + pump low and high ouabain affinity α subunit isoforms are differently distributed in cells
    • + pump low and high ouabain affinity α subunit isoforms are differently distributed in cells. Proc. Natl. Acad. Sci. 94:1997;1800-1805.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 1800-1805
    • Juhaszova, M.1    Blaustein, M.P.2
  • 42
    • 0038526240 scopus 로고    scopus 로고
    • Structural Basis for alpha 1 versus alpha 2 isoform - Distinct behavior of the Na, K-ATPase
    • Segall L., Javaid Z.Z., Carl S.L., Lane L.K., Blostein R. Structural Basis for alpha 1 versus alpha 2 isoform - distinct behavior of the Na, K-ATPase. J. Biol. Chem. 278:2003;9027-9034.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9027-9034
    • Segall, L.1    Javaid, Z.Z.2    Carl, S.L.3    Lane, L.K.4    Blostein, R.5


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