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Volumn 82, Issue , 2015, Pages 36-47

Regulation of the cardiac Na+ channel NaV1.5 by post-translational modifications

Author keywords

Arrhythmias; Cardiac NaV1.5 channels; Native proteomics; Post translational modifications

Indexed keywords

ADENOSINE MONOPHOSPHATE ACTIVATED PROTEIN KINASE; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CYCLIC AMP DEPENDENT PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE; PROTEIN KINASE C; PROTEIN KINASE FYN; SERUM AND GLUCOCORTICOID REGULATED KINASE 1; SODIUM CHANNEL NAV1.5; UNCLASSIFIED DRUG;

EID: 84936932605     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2015.02.013     Document Type: Review
Times cited : (85)

References (136)
  • 1
    • 18844479760 scopus 로고    scopus 로고
    • Basic mechanisms of cardiac impulse propagation and associated arrhythmias
    • Kleber A.G., Rudy Y. Basic mechanisms of cardiac impulse propagation and associated arrhythmias. Physiol Rev 2004, 84:431-488.
    • (2004) Physiol Rev , vol.84 , pp. 431-488
    • Kleber, A.G.1    Rudy, Y.2
  • 2
    • 73049097840 scopus 로고    scopus 로고
    • Cardiac sodium channel Na(v)1.5 and interacting proteins: physiology and pathophysiology
    • Abriel H. Cardiac sodium channel Na(v)1.5 and interacting proteins: physiology and pathophysiology. J Mol Cell Cardiol 2010, 48:2-11.
    • (2010) J Mol Cell Cardiol , vol.48 , pp. 2-11
    • Abriel, H.1
  • 3
    • 84867400864 scopus 로고    scopus 로고
    • Role of "non-cardiac" voltage-gated sodium channels in cardiac cells
    • Rougier J.S., Abriel H. Role of "non-cardiac" voltage-gated sodium channels in cardiac cells. J Mol Cell Cardiol 2012, 53:589-590.
    • (2012) J Mol Cell Cardiol , vol.53 , pp. 589-590
    • Rougier, J.S.1    Abriel, H.2
  • 4
    • 84926104165 scopus 로고    scopus 로고
    • Cardiac sodium channel mutations: why so many phenotypes?
    • Liu M., Yang K.C., Dudley S.C. Cardiac sodium channel mutations: why so many phenotypes?. Nat Rev Cardiol 2014, 11:607-615.
    • (2014) Nat Rev Cardiol , vol.11 , pp. 607-615
    • Liu, M.1    Yang, K.C.2    Dudley, S.C.3
  • 5
    • 79954578382 scopus 로고    scopus 로고
    • Phenotypical manifestations of mutations in the genes encoding subunits of the cardiac sodium channel
    • Wilde A.A., Brugada R. Phenotypical manifestations of mutations in the genes encoding subunits of the cardiac sodium channel. Circ Res 2011, 108:884-897.
    • (2011) Circ Res , vol.108 , pp. 884-897
    • Wilde, A.A.1    Brugada, R.2
  • 6
    • 61849156873 scopus 로고    scopus 로고
    • SCN5A channelopathies-an update on mutations and mechanisms
    • Zimmer T., Surber R. SCN5A channelopathies-an update on mutations and mechanisms. Prog Biophys Mol Biol 2008, 98:120-136.
    • (2008) Prog Biophys Mol Biol , vol.98 , pp. 120-136
    • Zimmer, T.1    Surber, R.2
  • 7
    • 84873522590 scopus 로고    scopus 로고
    • Cardiac channelopathies: genetic and molecular mechanisms
    • Abriel H., Zaklyazminskaya E.V. Cardiac channelopathies: genetic and molecular mechanisms. Gene 2013, 517:1-11.
    • (2013) Gene , vol.517 , pp. 1-11
    • Abriel, H.1    Zaklyazminskaya, E.V.2
  • 8
    • 84885751310 scopus 로고    scopus 로고
    • Noncanonical roles of voltage-gated sodium channels
    • Black J.A., Waxman S.G. Noncanonical roles of voltage-gated sodium channels. Neuron 2013, 80:280-291.
    • (2013) Neuron , vol.80 , pp. 280-291
    • Black, J.A.1    Waxman, S.G.2
  • 10
    • 0242330187 scopus 로고    scopus 로고
    • A ubiquitous splice variant and a common polymorphism affect heterologous expression of recombinant human SCN5A heart sodium channels
    • Makielski J.C., Ye B., Valdivia C.R., Pagel M.D., Pu J., Tester D.J., et al. A ubiquitous splice variant and a common polymorphism affect heterologous expression of recombinant human SCN5A heart sodium channels. Circ Res 2003, 93:821-828.
    • (2003) Circ Res , vol.93 , pp. 821-828
    • Makielski, J.C.1    Ye, B.2    Valdivia, C.R.3    Pagel, M.D.4    Pu, J.5    Tester, D.J.6
  • 11
    • 84857211318 scopus 로고    scopus 로고
    • Na channel beta subunits: overachievers of the ion channel family
    • Brackenbury W.J., Isom L.L. Na channel beta subunits: overachievers of the ion channel family. Front Pharmacol 2011, 2:53.
    • (2011) Front Pharmacol , vol.2 , pp. 53
    • Brackenbury, W.J.1    Isom, L.L.2
  • 12
    • 84875073626 scopus 로고    scopus 로고
    • V1.5 distribution in myocytes via interacting proteins: the multiple pool model
    • V1.5 distribution in myocytes via interacting proteins: the multiple pool model. Biochim Biophys Acta 2013, 1833:886-894.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 886-894
    • Shy, D.1    Gillet, L.2    Abriel, H.3
  • 13
    • 84881639229 scopus 로고    scopus 로고
    • Post-translational modifications of the cardiac Na channel: contribution of CaMKII-dependent phosphorylation to acquired arrhythmias
    • Herren A.W., Bers D.M., Grandi E. Post-translational modifications of the cardiac Na channel: contribution of CaMKII-dependent phosphorylation to acquired arrhythmias. Am J Physiol Heart Circ Physiol 2013, 305:H431-H445.
    • (2013) Am J Physiol Heart Circ Physiol , vol.305 , pp. H431-H445
    • Herren, A.W.1    Bers, D.M.2    Grandi, E.3
  • 14
    • 7244225020 scopus 로고    scopus 로고
    • The sialic acid component of the beta1 subunit modulates voltage-gated sodium channel function
    • Johnson D., Montpetit M.L., Stocker P.J., Bennett E.S. The sialic acid component of the beta1 subunit modulates voltage-gated sodium channel function. J Biol Chem 2004, 279:44303-44310.
    • (2004) J Biol Chem , vol.279 , pp. 44303-44310
    • Johnson, D.1    Montpetit, M.L.2    Stocker, P.J.3    Bennett, E.S.4
  • 15
    • 79961227410 scopus 로고    scopus 로고
    • The cardiac sodium channel is post-translationally modified by arginine methylation
    • Beltran-Alvarez P., Pagans S., Brugada R. The cardiac sodium channel is post-translationally modified by arginine methylation. J Proteome Res 2011, 10:3712-3719.
    • (2011) J Proteome Res , vol.10 , pp. 3712-3719
    • Beltran-Alvarez, P.1    Pagans, S.2    Brugada, R.3
  • 16
    • 84907549543 scopus 로고    scopus 로고
    • Identification of N-terminal protein acetylation and arginine methylation of the voltage-gated sodium channel in end-stage heart failure human heart
    • Beltran-Alvarez P., Tarradas A., Chiva C., Perez-Serra A., Batlle M., Perez-Villa F., et al. Identification of N-terminal protein acetylation and arginine methylation of the voltage-gated sodium channel in end-stage heart failure human heart. J Mol Cell Cardiol 2014, 76C:126-129.
    • (2014) J Mol Cell Cardiol , vol.76C , pp. 126-129
    • Beltran-Alvarez, P.1    Tarradas, A.2    Chiva, C.3    Perez-Serra, A.4    Batlle, M.5    Perez-Villa, F.6
  • 17
    • 77950664798 scopus 로고    scopus 로고
    • Multisite phosphorylation of voltage-gated sodium channel alpha subunits from rat brain
    • Berendt F.J., Park K.S., Trimmer J.S. Multisite phosphorylation of voltage-gated sodium channel alpha subunits from rat brain. J Proteome Res 2010, 9:1976-1984.
    • (2010) J Proteome Res , vol.9 , pp. 1976-1984
    • Berendt, F.J.1    Park, K.S.2    Trimmer, J.S.3
  • 19
    • 33747592823 scopus 로고    scopus 로고
    • Graded regulation of the Kv2.1 potassium channel by variable phosphorylation
    • Park K.S., Mohapatra D.P., Misonou H., Trimmer J.S. Graded regulation of the Kv2.1 potassium channel by variable phosphorylation. Science 2006, 313:976-979.
    • (2006) Science , vol.313 , pp. 976-979
    • Park, K.S.1    Mohapatra, D.P.2    Misonou, H.3    Trimmer, J.S.4
  • 20
    • 40349089867 scopus 로고    scopus 로고
    • Potassium channel phosphorylation in excitable cells: providing dynamic functional variability to a diverse family of ion channels
    • Park K.S., Yang J.W., Seikel E., Trimmer J.S. Potassium channel phosphorylation in excitable cells: providing dynamic functional variability to a diverse family of ion channels. Physiology (Bethesda) 2008, 23:49-57.
    • (2008) Physiology (Bethesda) , vol.23 , pp. 49-57
    • Park, K.S.1    Yang, J.W.2    Seikel, E.3    Trimmer, J.S.4
  • 21
    • 52049111074 scopus 로고    scopus 로고
    • Profiling the phospho-status of the BKCa channel alpha subunit in rat brain reveals unexpected patterns and complexity
    • Yan J., Olsen J.V., Park K.S., Li W., Bildl W., Schulte U., et al. Profiling the phospho-status of the BKCa channel alpha subunit in rat brain reveals unexpected patterns and complexity. Mol Cell Proteomics 2008, 7:2188-2198.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 2188-2198
    • Yan, J.1    Olsen, J.V.2    Park, K.S.3    Li, W.4    Bildl, W.5    Schulte, U.6
  • 22
    • 38049132028 scopus 로고    scopus 로고
    • Trafficking-dependent phosphorylation of Kv1.2 regulates voltage-gated potassium channel cell surface expression
    • Yang J.W., Vacher H., Park K.S., Clark E., Trimmer J.S. Trafficking-dependent phosphorylation of Kv1.2 regulates voltage-gated potassium channel cell surface expression. Proc Natl Acad Sci U S A 2007, 104:20055-20060.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 20055-20060
    • Yang, J.W.1    Vacher, H.2    Park, K.S.3    Clark, E.4    Trimmer, J.S.5
  • 23
    • 0034923505 scopus 로고    scopus 로고
    • Analysis of proteins and proteomes by mass spectrometry
    • Mann M., Hendrickson R.C., Pandey A. Analysis of proteins and proteomes by mass spectrometry. Annu Rev Biochem 2001, 70:437-473.
    • (2001) Annu Rev Biochem , vol.70 , pp. 437-473
    • Mann, M.1    Hendrickson, R.C.2    Pandey, A.3
  • 25
    • 84855932755 scopus 로고    scopus 로고
    • Advances in quantitative phosphoproteomics
    • Nilsson C.L. Advances in quantitative phosphoproteomics. Anal Chem 2012, 84:735-746.
    • (2012) Anal Chem , vol.84 , pp. 735-746
    • Nilsson, C.L.1
  • 26
    • 84856209928 scopus 로고    scopus 로고
    • Increasing phosphoproteomic coverage through sequential digestion by complementary proteases
    • Gilmore J.M., Kettenbach A.N., Gerber S.A. Increasing phosphoproteomic coverage through sequential digestion by complementary proteases. Anal Bioanal Chem 2012, 402:711-720.
    • (2012) Anal Bioanal Chem , vol.402 , pp. 711-720
    • Gilmore, J.M.1    Kettenbach, A.N.2    Gerber, S.A.3
  • 28
    • 84862214081 scopus 로고    scopus 로고
    • Modulation of voltage-gated ion channels by sialylation
    • Ednie A.R., Bennett E.S. Modulation of voltage-gated ion channels by sialylation. Compr Physiol 2012, 2:1269-1301.
    • (2012) Compr Physiol , vol.2 , pp. 1269-1301
    • Ednie, A.R.1    Bennett, E.S.2
  • 29
    • 0027171497 scopus 로고
    • Partial characterization of the rH1 sodium channel protein from rat heart using subtype-specific antibodies
    • Cohen S.A., Levitt L.K. Partial characterization of the rH1 sodium channel protein from rat heart using subtype-specific antibodies. Circ Res 1993, 73:735-742.
    • (1993) Circ Res , vol.73 , pp. 735-742
    • Cohen, S.A.1    Levitt, L.K.2
  • 30
    • 84899757715 scopus 로고    scopus 로고
    • Tuning the electrical properties of the heart by differential trafficking of KATP ion channel complexes
    • Arakel E.C., Brandenburg S., Uchida K., Zhang H., Lin Y.W., Kohl T., et al. Tuning the electrical properties of the heart by differential trafficking of KATP ion channel complexes. J Cell Sci 2014, 127:2106-2119.
    • (2014) J Cell Sci , vol.127 , pp. 2106-2119
    • Arakel, E.C.1    Brandenburg, S.2    Uchida, K.3    Zhang, H.4    Lin, Y.W.5    Kohl, T.6
  • 31
    • 34047125225 scopus 로고    scopus 로고
    • In silico determination of intracellular glycosylation and phosphorylation sites in human selectins: implications for biological function
    • Ahmad I., Hoessli D.C., Gupta R., Walker-Nasir E., Rafik S.M., Choudhary M.I., et al. In silico determination of intracellular glycosylation and phosphorylation sites in human selectins: implications for biological function. J Cell Biochem 2007, 100:1558-1572.
    • (2007) J Cell Biochem , vol.100 , pp. 1558-1572
    • Ahmad, I.1    Hoessli, D.C.2    Gupta, R.3    Walker-Nasir, E.4    Rafik, S.M.5    Choudhary, M.I.6
  • 32
    • 78651105000 scopus 로고    scopus 로고
    • Mass spectrometry based glycoproteomics-from a proteomics perspective
    • (R110 003251)
    • Pan S., Chen R., Aebersold R., Brentnall T.A. Mass spectrometry based glycoproteomics-from a proteomics perspective. Mol Cell Proteomics 2011, 10. (R110 003251).
    • (2011) Mol Cell Proteomics , vol.10
    • Pan, S.1    Chen, R.2    Aebersold, R.3    Brentnall, T.A.4
  • 33
    • 0036487068 scopus 로고    scopus 로고
    • Isoform-specific effects of sialic acid on voltage-dependent Na+ channel gating: functional sialic acids are localized to the S5-S6 loop of domain I
    • Bennett E.S. Isoform-specific effects of sialic acid on voltage-dependent Na+ channel gating: functional sialic acids are localized to the S5-S6 loop of domain I. J Physiol 2002, 538:675-690.
    • (2002) J Physiol , vol.538 , pp. 675-690
    • Bennett, E.S.1
  • 34
    • 33644598193 scopus 로고    scopus 로고
    • Differential sialylation modulates voltage-gated Na+ channel gating throughout the developing myocardium
    • Stocker P.J., Bennett E.S. Differential sialylation modulates voltage-gated Na+ channel gating throughout the developing myocardium. J Gen Physiol 2006, 127:253-265.
    • (2006) J Gen Physiol , vol.127 , pp. 253-265
    • Stocker, P.J.1    Bennett, E.S.2
  • 36
    • 84875359727 scopus 로고    scopus 로고
    • Expression of the sialyltransferase, ST3Gal4, impacts cardiac voltage-gated sodium channel activity, refractory period and ventricular conduction
    • Ednie A.R., Horton K.K., Wu J., Bennett E.S. Expression of the sialyltransferase, ST3Gal4, impacts cardiac voltage-gated sodium channel activity, refractory period and ventricular conduction. J Mol Cell Cardiol 2013, 59:117-127.
    • (2013) J Mol Cell Cardiol , vol.59 , pp. 117-127
    • Ednie, A.R.1    Horton, K.K.2    Wu, J.3    Bennett, E.S.4
  • 37
    • 79952419012 scopus 로고    scopus 로고
    • Mass spectrometry-based phosphoproteomics reveals multisite phosphorylation on mammalian brain voltage-gated sodium and potassium channels
    • Baek J.H., Cerda O., Trimmer J.S. Mass spectrometry-based phosphoproteomics reveals multisite phosphorylation on mammalian brain voltage-gated sodium and potassium channels. Semin Cell Dev Biol 2011, 22:153-159.
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 153-159
    • Baek, J.H.1    Cerda, O.2    Trimmer, J.S.3
  • 38
    • 79953206567 scopus 로고    scopus 로고
    • Regulation of sodium channel activity by phosphorylation
    • Scheuer T. Regulation of sodium channel activity by phosphorylation. Semin Cell Dev Biol 2011, 22:160-165.
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 160-165
    • Scheuer, T.1
  • 39
    • 84880055131 scopus 로고    scopus 로고
    • The fibroblast growth factor 14·voltage-gated sodium channel complex is a new target of glycogen synthase kinase 3 (GSK3)
    • Shavkunov A.S., Wildburger N.C., Nenov M.N., James T.F., Buzhdygan T.P., Panova-Elektronova N.I., et al. The fibroblast growth factor 14·voltage-gated sodium channel complex is a new target of glycogen synthase kinase 3 (GSK3). J Biol Chem 2013, 288:19370-19385.
    • (2013) J Biol Chem , vol.288 , pp. 19370-19385
    • Shavkunov, A.S.1    Wildburger, N.C.2    Nenov, M.N.3    James, T.F.4    Buzhdygan, T.P.5    Panova-Elektronova, N.I.6
  • 40
    • 78650907529 scopus 로고    scopus 로고
    • Mining recent brain proteomic databases for ion channel phosphosite nuggets
    • Cerda O., Baek J.H., Trimmer J.S. Mining recent brain proteomic databases for ion channel phosphosite nuggets. J Gen Physiol 2011, 137:3-16.
    • (2011) J Gen Physiol , vol.137 , pp. 3-16
    • Cerda, O.1    Baek, J.H.2    Trimmer, J.S.3
  • 41
    • 77954565509 scopus 로고    scopus 로고
    • Brain phosphoproteome obtained by a FASP-based method reveals plasma membrane protein topology
    • Wisniewski J.R., Nagaraj N., Zougman A., Gnad F., Mann M. Brain phosphoproteome obtained by a FASP-based method reveals plasma membrane protein topology. J Proteome Res 2010, 9:3280-3289.
    • (2010) J Proteome Res , vol.9 , pp. 3280-3289
    • Wisniewski, J.R.1    Nagaraj, N.2    Zougman, A.3    Gnad, F.4    Mann, M.5
  • 42
    • 0026505405 scopus 로고
    • Enhancement of rabbit cardiac sodium channels by beta-adrenergic stimulation
    • Matsuda J.J., Lee H., Shibata E.F. Enhancement of rabbit cardiac sodium channels by beta-adrenergic stimulation. Circ Res 1992, 70:199-207.
    • (1992) Circ Res , vol.70 , pp. 199-207
    • Matsuda, J.J.1    Lee, H.2    Shibata, E.F.3
  • 43
    • 0024309970 scopus 로고
    • Beta-adrenergic inhibition of cardiac sodium channels by dual G-protein pathways
    • Schubert B., VanDongen A.M., Kirsch G.E., Brown A.M. Beta-adrenergic inhibition of cardiac sodium channels by dual G-protein pathways. Science 1989, 245:516-519.
    • (1989) Science , vol.245 , pp. 516-519
    • Schubert, B.1    VanDongen, A.M.2    Kirsch, G.E.3    Brown, A.M.4
  • 44
    • 84903598796 scopus 로고    scopus 로고
    • A mutation causing Brugada syndrome identifies a mechanism for altered autonomic and oxidant regulation of cardiac sodium currents
    • Aiba T., Farinelli F., Kostecki G., Hesketh G.G., Edwards D., Biswas S., et al. A mutation causing Brugada syndrome identifies a mechanism for altered autonomic and oxidant regulation of cardiac sodium currents. Circ Cardiovasc Genet 2014, 7:249-256.
    • (2014) Circ Cardiovasc Genet , vol.7 , pp. 249-256
    • Aiba, T.1    Farinelli, F.2    Kostecki, G.3    Hesketh, G.G.4    Edwards, D.5    Biswas, S.6
  • 45
    • 5444225595 scopus 로고    scopus 로고
    • Can PKA activators rescue Na+ channel function in epicardial border zone cells that survive in the infarcted canine heart?
    • Baba S., Dun W., Boyden P.A. Can PKA activators rescue Na+ channel function in epicardial border zone cells that survive in the infarcted canine heart?. Cardiovasc Res 2004, 64:260-267.
    • (2004) Cardiovasc Res , vol.64 , pp. 260-267
    • Baba, S.1    Dun, W.2    Boyden, P.A.3
  • 46
    • 0031015604 scopus 로고    scopus 로고
    • Modulation of the human cardiac sodium channel alpha-subunit by cAMP-dependent protein kinase and the responsible sequence domain
    • Frohnwieser B., Chen L.Q., Schreibmayer W., Kallen R.G. Modulation of the human cardiac sodium channel alpha-subunit by cAMP-dependent protein kinase and the responsible sequence domain. J Physiol 1997, 498(Pt 2):309-318.
    • (1997) J Physiol , vol.498 , pp. 309-318
    • Frohnwieser, B.1    Chen, L.Q.2    Schreibmayer, W.3    Kallen, R.G.4
  • 47
    • 33749452422 scopus 로고    scopus 로고
    • Quantitation of protein kinase A-mediated trafficking of cardiac sodium channels in living cells
    • Hallaq H., Yang Z., Viswanathan P.C., Fukuda K., Shen W., Wang D.W., et al. Quantitation of protein kinase A-mediated trafficking of cardiac sodium channels in living cells. Cardiovasc Res 2006, 72:250-261.
    • (2006) Cardiovasc Res , vol.72 , pp. 250-261
    • Hallaq, H.1    Yang, Z.2    Viswanathan, P.C.3    Fukuda, K.4    Shen, W.5    Wang, D.W.6
  • 48
    • 0028670820 scopus 로고
    • Beta-adrenergic modulation of currents produced by rat cardiac Na+ channels expressed in Xenopus laevis oocytes
    • Schreibmayer W., Frohnwieser B., Dascal N., Platzer D., Spreitzer B., Zechner R., et al. Beta-adrenergic modulation of currents produced by rat cardiac Na+ channels expressed in Xenopus laevis oocytes. Receptors Channels 1994, 2:339-350.
    • (1994) Receptors Channels , vol.2 , pp. 339-350
    • Schreibmayer, W.1    Frohnwieser, B.2    Dascal, N.3    Platzer, D.4    Spreitzer, B.5    Zechner, R.6
  • 49
    • 0037144621 scopus 로고    scopus 로고
    • Phosphorylation and putative ER retention signals are required for protein kinase A-mediated potentiation of cardiac sodium current
    • Zhou J., Shin H.G., Yi J., Shen W., Williams C.P., Murray K.T. Phosphorylation and putative ER retention signals are required for protein kinase A-mediated potentiation of cardiac sodium current. Circ Res 2002, 91:540-546.
    • (2002) Circ Res , vol.91 , pp. 540-546
    • Zhou, J.1    Shin, H.G.2    Yi, J.3    Shen, W.4    Williams, C.P.5    Murray, K.T.6
  • 50
    • 0034617141 scopus 로고    scopus 로고
    • Activation of protein kinase A modulates trafficking of the human cardiac sodium channel in Xenopus oocytes
    • Zhou J., Yi J., Hu N., George A.L., Murray K.T. Activation of protein kinase A modulates trafficking of the human cardiac sodium channel in Xenopus oocytes. Circ Res 2000, 87:33-38.
    • (2000) Circ Res , vol.87 , pp. 33-38
    • Zhou, J.1    Yi, J.2    Hu, N.3    George, A.L.4    Murray, K.T.5
  • 51
    • 0025991624 scopus 로고
    • The catalytic subunit of cyclic AMP-dependent protein kinase directly inhibits sodium channel activities in guinea-pig ventricular myocytes
    • Sunami A., Fan Z., Nakamura F., Naka M., Tanaka T., Sawanobori T., et al. The catalytic subunit of cyclic AMP-dependent protein kinase directly inhibits sodium channel activities in guinea-pig ventricular myocytes. Pflugers Arch 1991, 419:415-417.
    • (1991) Pflugers Arch , vol.419 , pp. 415-417
    • Sunami, A.1    Fan, Z.2    Nakamura, F.3    Naka, M.4    Tanaka, T.5    Sawanobori, T.6
  • 52
    • 0027410465 scopus 로고
    • Mechanism of cAMP-dependent modulation of cardiac sodium channel current kinetics
    • Ono K., Fozzard H.A., Hanck D.A. Mechanism of cAMP-dependent modulation of cardiac sodium channel current kinetics. Circ Res 1993, 72:807-815.
    • (1993) Circ Res , vol.72 , pp. 807-815
    • Ono, K.1    Fozzard, H.A.2    Hanck, D.A.3
  • 53
    • 0026535161 scopus 로고
    • Beta-adrenergic modulation of fast inward sodium current in canine myocardium. Syncytial preparations versus isolated myocytes
    • Gintant G.A., Liu D.W. Beta-adrenergic modulation of fast inward sodium current in canine myocardium. Syncytial preparations versus isolated myocytes. Circ Res 1992, 70:844-850.
    • (1992) Circ Res , vol.70 , pp. 844-850
    • Gintant, G.A.1    Liu, D.W.2
  • 54
    • 0025956067 scopus 로고
    • Influence of beta-adrenergic stimulation on the fast sodium current in the intact rat papillary muscle
    • Kirstein M., Eickhorn R., Langenfeld H., Kochsiek K., Antoni H. Influence of beta-adrenergic stimulation on the fast sodium current in the intact rat papillary muscle. Basic Res Cardiol 1991, 86:441-448.
    • (1991) Basic Res Cardiol , vol.86 , pp. 441-448
    • Kirstein, M.1    Eickhorn, R.2    Langenfeld, H.3    Kochsiek, K.4    Antoni, H.5
  • 55
    • 0024402913 scopus 로고
    • Isoproterenol, DBcAMP, and forskolin inhibit cardiac sodium current
    • Ono K., Kiyosue T., Arita M. Isoproterenol, DBcAMP, and forskolin inhibit cardiac sodium current. Am J Physiol 1989, 256:C1131-C1137.
    • (1989) Am J Physiol , vol.256 , pp. C1131-C1137
    • Ono, K.1    Kiyosue, T.2    Arita, M.3
  • 56
    • 0029802816 scopus 로고    scopus 로고
    • CAMP-dependent phosphorylation of two sites in the alpha subunit of the cardiac sodium channel
    • Murphy B.J., Rogers J., Perdichizzi A.P., Colvin A.A., Catterall W.A. cAMP-dependent phosphorylation of two sites in the alpha subunit of the cardiac sodium channel. J Biol Chem 1996, 271:28837-28843.
    • (1996) J Biol Chem , vol.271 , pp. 28837-28843
    • Murphy, B.J.1    Rogers, J.2    Perdichizzi, A.P.3    Colvin, A.A.4    Catterall, W.A.5
  • 57
    • 0344012531 scopus 로고    scopus 로고
    • Modulation of cardiac sodium channel gating by protein kinase A can be altered by disease-linked mutation
    • Tateyama M., Rivolta I., Clancy C.E., Kass R.S. Modulation of cardiac sodium channel gating by protein kinase A can be altered by disease-linked mutation. J Biol Chem 2003, 278:46718-46726.
    • (2003) J Biol Chem , vol.278 , pp. 46718-46726
    • Tateyama, M.1    Rivolta, I.2    Clancy, C.E.3    Kass, R.S.4
  • 61
    • 84903999780 scopus 로고    scopus 로고
    • Tubulin polymerization disrupts cardiac beta-adrenergic regulation of late INa
    • Dybkova N., Wagner S., Backs J., Hund T.J., Mohler P.J., Sowa T., et al. Tubulin polymerization disrupts cardiac beta-adrenergic regulation of late INa. Cardiovasc Res 2014, 103:168-177.
    • (2014) Cardiovasc Res , vol.103 , pp. 168-177
    • Dybkova, N.1    Wagner, S.2    Backs, J.3    Hund, T.J.4    Mohler, P.J.5    Sowa, T.6
  • 62
    • 84884525610 scopus 로고    scopus 로고
    • Dynamics of the late Na(+) current during cardiac action potential and its contribution to afterdepolarizations
    • Horvath B., Banyasz T., Jian Z., Hegyi B., Kistamas K., Nanasi P.P., et al. Dynamics of the late Na(+) current during cardiac action potential and its contribution to afterdepolarizations. J Mol Cell Cardiol 2013, 64:59-68.
    • (2013) J Mol Cell Cardiol , vol.64 , pp. 59-68
    • Horvath, B.1    Banyasz, T.2    Jian, Z.3    Hegyi, B.4    Kistamas, K.5    Nanasi, P.P.6
  • 63
    • 84859748901 scopus 로고    scopus 로고
    • Calmodulin kinase II and protein kinase C mediate the effect of increased intracellular calcium to augment late sodium current in rabbit ventricular myocytes
    • Ma J., Luo A., Wu L., Wan W., Zhang P., Ren Z., et al. Calmodulin kinase II and protein kinase C mediate the effect of increased intracellular calcium to augment late sodium current in rabbit ventricular myocytes. Am J Physiol Cell Physiol 2012, 302:C1141-C1151.
    • (2012) Am J Physiol Cell Physiol , vol.302 , pp. C1141-C1151
    • Ma, J.1    Luo, A.2    Wu, L.3    Wan, W.4    Zhang, P.5    Ren, Z.6
  • 65
    • 84880328248 scopus 로고    scopus 로고
    • Role of late sodium current as a potential arrhythmogenic mechanism in the progression of pressure-induced heart disease
    • Toischer K., Hartmann N., Wagner S., Fischer T.H., Herting J., Danner B.C., et al. Role of late sodium current as a potential arrhythmogenic mechanism in the progression of pressure-induced heart disease. J Mol Cell Cardiol 2013, 61:111-122.
    • (2013) J Mol Cell Cardiol , vol.61 , pp. 111-122
    • Toischer, K.1    Hartmann, N.2    Wagner, S.3    Fischer, T.H.4    Herting, J.5    Danner, B.C.6
  • 66
    • 74549157674 scopus 로고    scopus 로고
    • Oxidized calmodulin kinase II regulates conduction following myocardial infarction: a computational analysis
    • Christensen M.D., Dun W., Boyden P.A., Anderson M.E., Mohler P.J., Hund T.J. Oxidized calmodulin kinase II regulates conduction following myocardial infarction: a computational analysis. PLoS Comput Biol 2009, 5:e1000583.
    • (2009) PLoS Comput Biol , vol.5 , pp. e1000583
    • Christensen, M.D.1    Dun, W.2    Boyden, P.A.3    Anderson, M.E.4    Mohler, P.J.5    Hund, T.J.6
  • 67
    • 36849057068 scopus 로고    scopus 로고
    • Simulation of Ca-calmodulin-dependent protein kinase II on rabbit ventricular myocyte ion currents and action potentials
    • Grandi E., Puglisi J.L., Wagner S., Maier L.S., Severi S., Bers D.M. Simulation of Ca-calmodulin-dependent protein kinase II on rabbit ventricular myocyte ion currents and action potentials. Biophys J 2007, 93:3835-3847.
    • (2007) Biophys J , vol.93 , pp. 3835-3847
    • Grandi, E.1    Puglisi, J.L.2    Wagner, S.3    Maier, L.S.4    Severi, S.5    Bers, D.M.6
  • 69
    • 77957838101 scopus 로고    scopus 로고
    • A beta(IV)-spectrin/CaMKII signaling complex is essential for membrane excitability in mice
    • Hund T.J., Koval O.M., Li J., Wright P.J., Qian L., Snyder J.S., et al. A beta(IV)-spectrin/CaMKII signaling complex is essential for membrane excitability in mice. J Clin Invest 2010, 120:3508-3519.
    • (2010) J Clin Invest , vol.120 , pp. 3508-3519
    • Hund, T.J.1    Koval, O.M.2    Li, J.3    Wright, P.J.4    Qian, L.5    Snyder, J.S.6
  • 70
    • 84862001882 scopus 로고    scopus 로고
    • 2+/Calmodulin-dependent Protein Kinase II (CaMKII) regulates cardiac sodium channel NaV1.5 gating by multiple phosphorylation sites
    • 2+/Calmodulin-dependent Protein Kinase II (CaMKII) regulates cardiac sodium channel NaV1.5 gating by multiple phosphorylation sites. J Biol Chem 2012, 287:19856-19869.
    • (2012) J Biol Chem , vol.287 , pp. 19856-19869
    • Ashpole, N.M.1    Herren, A.W.2    Ginsburg, K.S.3    Brogan, J.D.4    Johnson, D.E.5    Cummins, T.R.6
  • 73
    • 0038643573 scopus 로고    scopus 로고
    • The deltaC isoform of CaMKII is activated in cardiac hypertrophy and induces dilated cardiomyopathy and heart failure
    • Zhang T., Maier L.S., Dalton N.D., Miyamoto S., Ross J., Bers D.M., et al. The deltaC isoform of CaMKII is activated in cardiac hypertrophy and induces dilated cardiomyopathy and heart failure. Circ Res 2003, 92:912-919.
    • (2003) Circ Res , vol.92 , pp. 912-919
    • Zhang, T.1    Maier, L.S.2    Dalton, N.D.3    Miyamoto, S.4    Ross, J.5    Bers, D.M.6
  • 75
    • 0028202763 scopus 로고
    • Modulation of cardiac Na+ channels expressed in a mammalian cell line and in ventricular myocytes by protein kinase C
    • Qu Y., Rogers J., Tanada T., Scheuer T., Catterall W.A. Modulation of cardiac Na+ channels expressed in a mammalian cell line and in ventricular myocytes by protein kinase C. Proc Natl Acad Sci U S A 1994, 91:3289-3293.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3289-3293
    • Qu, Y.1    Rogers, J.2    Tanada, T.3    Scheuer, T.4    Catterall, W.A.5
  • 76
    • 0031442019 scopus 로고    scopus 로고
    • Modulation of cardiac sodium current by alpha1-stimulation and volatile anesthetics
    • Weigt H.U., Kwok W.M., Rehmert G.C., Turner L.A., Bosnjak Z.J. Modulation of cardiac sodium current by alpha1-stimulation and volatile anesthetics. Anesthesiology 1997, 87:1507-1516.
    • (1997) Anesthesiology , vol.87 , pp. 1507-1516
    • Weigt, H.U.1    Kwok, W.M.2    Rehmert, G.C.3    Turner, L.A.4    Bosnjak, Z.J.5
  • 77
  • 78
    • 0035957681 scopus 로고    scopus 로고
    • Conventional protein kinase C isoforms and cross-activation of protein kinase A regulate cardiac Na+ current
    • Shin H.G., Murray K.T. Conventional protein kinase C isoforms and cross-activation of protein kinase A regulate cardiac Na+ current. FEBS Lett 2001, 495:154-158.
    • (2001) FEBS Lett , vol.495 , pp. 154-158
    • Shin, H.G.1    Murray, K.T.2
  • 79
    • 0026341651 scopus 로고
    • A phosphorylation site in the Na+ channel required for modulation by protein kinase C
    • West J.W., Numann R., Murphy B.J., Scheuer T., Catterall W.A. A phosphorylation site in the Na+ channel required for modulation by protein kinase C. Science 1991, 254:866-868.
    • (1991) Science , vol.254 , pp. 866-868
    • West, J.W.1    Numann, R.2    Murphy, B.J.3    Scheuer, T.4    Catterall, W.A.5
  • 80
    • 0031051126 scopus 로고    scopus 로고
    • Functional effects of protein kinase C activation on the human cardiac Na+ channel
    • Murray K.T., Hu N.N., Daw J.R., Shin H.G., Watson M.T., Mashburn A.B., et al. Functional effects of protein kinase C activation on the human cardiac Na+ channel. Circ Res 1997, 80:370-376.
    • (1997) Circ Res , vol.80 , pp. 370-376
    • Murray, K.T.1    Hu, N.N.2    Daw, J.R.3    Shin, H.G.4    Watson, M.T.5    Mashburn, A.B.6
  • 81
    • 0029854856 scopus 로고    scopus 로고
    • Phosphorylation of S1505 in the cardiac Na+ channel inactivation gate is required for modulation by protein kinase C
    • Qu Y., Rogers J.C., Tanada T.N., Catterall W.A., Scheuer T. Phosphorylation of S1505 in the cardiac Na+ channel inactivation gate is required for modulation by protein kinase C. J Gen Physiol 1996, 108:375-379.
    • (1996) J Gen Physiol , vol.108 , pp. 375-379
    • Qu, Y.1    Rogers, J.C.2    Tanada, T.N.3    Catterall, W.A.4    Scheuer, T.5
  • 82
    • 0030957101 scopus 로고    scopus 로고
    • Ionic mechanism of the effects of hydrogen peroxide in rat ventricular myocytes
    • Ward C.A., Giles W.R. Ionic mechanism of the effects of hydrogen peroxide in rat ventricular myocytes. J Physiol 1997, 500(Pt 3):631-642.
    • (1997) J Physiol , vol.500 , pp. 631-642
    • Ward, C.A.1    Giles, W.R.2
  • 83
    • 0030835745 scopus 로고    scopus 로고
    • Modulation of Na+ current inactivation by stimulation of protein kinase C in cardiac cells
    • Watson C.L., Gold M.R. Modulation of Na+ current inactivation by stimulation of protein kinase C in cardiac cells. Circ Res 1997, 81:380-386.
    • (1997) Circ Res , vol.81 , pp. 380-386
    • Watson, C.L.1    Gold, M.R.2
  • 84
    • 70349628999 scopus 로고    scopus 로고
    • GPD1L links redox state to cardiac excitability by PKC-dependent phosphorylation of the sodium channel SCN5A
    • Valdivia C.R., Ueda K., Ackerman M.J., Makielski J.C. GPD1L links redox state to cardiac excitability by PKC-dependent phosphorylation of the sodium channel SCN5A. Am J Physiol Heart Circ Physiol 2009, 297:H1446-H1452.
    • (2009) Am J Physiol Heart Circ Physiol , vol.297 , pp. H1446-H1452
    • Valdivia, C.R.1    Ueda, K.2    Ackerman, M.J.3    Makielski, J.C.4
  • 85
    • 70350125580 scopus 로고    scopus 로고
    • Cardiac Na+ current regulation by pyridine nucleotides
    • Liu M., Sanyal S., Gao G., Gurung I.S., Zhu X., Gaconnet G., et al. Cardiac Na+ current regulation by pyridine nucleotides. Circ Res 2009, 105:737-745.
    • (2009) Circ Res , vol.105 , pp. 737-745
    • Liu, M.1    Sanyal, S.2    Gao, G.3    Gurung, I.S.4    Zhu, X.5    Gaconnet, G.6
  • 86
    • 84869869380 scopus 로고    scopus 로고
    • Mitochondrial dysfunction causing cardiac sodium channel downregulation in cardiomyopathy
    • Liu M., Gu L., Sulkin M.S., Liu H., Jeong E.M., Greener I., et al. Mitochondrial dysfunction causing cardiac sodium channel downregulation in cardiomyopathy. J Mol Cell Cardiol 2013, 54:25-34.
    • (2013) J Mol Cell Cardiol , vol.54 , pp. 25-34
    • Liu, M.1    Gu, L.2    Sulkin, M.S.3    Liu, H.4    Jeong, E.M.5    Greener, I.6
  • 87
    • 84860376625 scopus 로고    scopus 로고
    • Suppression of phosphoinositide 3-kinase signaling and alteration of multiple ion currents in drug-induced long QT syndrome
    • (131ra50)
    • Lu Z., Wu C.Y., Jiang Y.P., Ballou L.M., Clausen C., Cohen I.S., et al. Suppression of phosphoinositide 3-kinase signaling and alteration of multiple ion currents in drug-induced long QT syndrome. Sci Transl Med 2012, 4. (131ra50).
    • (2012) Sci Transl Med , vol.4
    • Lu, Z.1    Wu, C.Y.2    Jiang, Y.P.3    Ballou, L.M.4    Clausen, C.5    Cohen, I.S.6
  • 88
    • 84891767756 scopus 로고    scopus 로고
    • Increased persistent sodium current due to decreased PI3K signaling contributes to QT prolongation in the diabetic heart
    • Lu Z., Jiang Y.P., Wu C.Y., Ballou L.M., Liu S., Carpenter E.S., et al. Increased persistent sodium current due to decreased PI3K signaling contributes to QT prolongation in the diabetic heart. Diabetes 2013, 62:4257-4265.
    • (2013) Diabetes , vol.62 , pp. 4257-4265
    • Lu, Z.1    Jiang, Y.P.2    Wu, C.Y.3    Ballou, L.M.4    Liu, S.5    Carpenter, E.S.6
  • 89
    • 0033151832 scopus 로고    scopus 로고
    • Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI 3-kinase-stimulated signaling pathway
    • Park J., Leong M.L., Buse P., Maiyar A.C., Firestone G.L., Hemmings B.A. Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI 3-kinase-stimulated signaling pathway. EMBO J 1999, 18:3024-3033.
    • (1999) EMBO J , vol.18 , pp. 3024-3033
    • Park, J.1    Leong, M.L.2    Buse, P.3    Maiyar, A.C.4    Firestone, G.L.5    Hemmings, B.A.6
  • 90
    • 0037376626 scopus 로고    scopus 로고
    • Serum and glucocorticoid inducible kinases in the regulation of the cardiac sodium channel SCN5A
    • Boehmer C., Wilhelm V., Palmada M., Wallisch S., Henke G., Brinkmeier H., et al. Serum and glucocorticoid inducible kinases in the regulation of the cardiac sodium channel SCN5A. Cardiovasc Res 2003, 57:1079-1084.
    • (2003) Cardiovasc Res , vol.57 , pp. 1079-1084
    • Boehmer, C.1    Wilhelm, V.2    Palmada, M.3    Wallisch, S.4    Henke, G.5    Brinkmeier, H.6
  • 91
    • 84868197743 scopus 로고    scopus 로고
    • Pathological role of serum- and glucocorticoid-regulated kinase 1 in adverse ventricular remodeling
    • Das S., Aiba T., Rosenberg M., Hessler K., Xiao C., Quintero P.A., et al. Pathological role of serum- and glucocorticoid-regulated kinase 1 in adverse ventricular remodeling. Circulation 2012, 126:2208-2219.
    • (2012) Circulation , vol.126 , pp. 2208-2219
    • Das, S.1    Aiba, T.2    Rosenberg, M.3    Hessler, K.4    Xiao, C.5    Quintero, P.A.6
  • 92
    • 0037016772 scopus 로고    scopus 로고
    • Serum and glucocorticoid-regulated kinase modulates Nedd4-2-mediated inhibition of the epithelial Na+ channel
    • Snyder P.M., Olson D.R., Thomas B.C. Serum and glucocorticoid-regulated kinase modulates Nedd4-2-mediated inhibition of the epithelial Na+ channel. J Biol Chem 2002, 277:5-8.
    • (2002) J Biol Chem , vol.277 , pp. 5-8
    • Snyder, P.M.1    Olson, D.R.2    Thomas, B.C.3
  • 93
    • 19044384130 scopus 로고    scopus 로고
    • Modulation of the cardiac sodium channel NaV1.5 by Fyn, a Src family tyrosine kinase
    • Ahern C.A., Zhang J.F., Wookalis M.J., Horn R. Modulation of the cardiac sodium channel NaV1.5 by Fyn, a Src family tyrosine kinase. Circ Res 2005, 96:991-998.
    • (2005) Circ Res , vol.96 , pp. 991-998
    • Ahern, C.A.1    Zhang, J.F.2    Wookalis, M.J.3    Horn, R.4
  • 95
    • 35548939087 scopus 로고    scopus 로고
    • Regulation of Na(v)1.2 channels by brain-derived neurotrophic factor, TrkB, and associated Fyn kinase
    • Ahn M., Beacham D., Westenbroek R.E., Scheuer T., Catterall W.A. Regulation of Na(v)1.2 channels by brain-derived neurotrophic factor, TrkB, and associated Fyn kinase. J Neurosci 2007, 27:11533-11542.
    • (2007) J Neurosci , vol.27 , pp. 11533-11542
    • Ahn, M.1    Beacham, D.2    Westenbroek, R.E.3    Scheuer, T.4    Catterall, W.A.5
  • 96
    • 35548936575 scopus 로고    scopus 로고
    • Sites and molecular mechanisms of modulation of Na(v)1.2 channels by Fyn tyrosine kinase
    • Beacham D., Ahn M., Catterall W.A., Scheuer T. Sites and molecular mechanisms of modulation of Na(v)1.2 channels by Fyn tyrosine kinase. J Neurosci 2007, 27:11543-11551.
    • (2007) J Neurosci , vol.27 , pp. 11543-11551
    • Beacham, D.1    Ahn, M.2    Catterall, W.A.3    Scheuer, T.4
  • 97
    • 84868493819 scopus 로고    scopus 로고
    • Toward quantitative phosphotyrosine profiling in vivo
    • Johnson H., White F.M. Toward quantitative phosphotyrosine profiling in vivo. Semin Cell Dev Biol 2012, 23:854-862.
    • (2012) Semin Cell Dev Biol , vol.23 , pp. 854-862
    • Johnson, H.1    White, F.M.2
  • 98
    • 0037461107 scopus 로고    scopus 로고
    • Constitutively active adenosine monophosphate-activated protein kinase regulates voltage-gated sodium channels in ventricular myocytes
    • Light P.E., Wallace C.H., Dyck J.R. Constitutively active adenosine monophosphate-activated protein kinase regulates voltage-gated sodium channels in ventricular myocytes. Circulation 2003, 107:1962-1965.
    • (2003) Circulation , vol.107 , pp. 1962-1965
    • Light, P.E.1    Wallace, C.H.2    Dyck, J.R.3
  • 99
    • 84884280335 scopus 로고    scopus 로고
    • Protein arginine methyl transferases-3 and -5 increase cell surface expression of cardiac sodium channel
    • Beltran-Alvarez P., Espejo A., Schmauder R., Beltran C., Mrowka R., Linke T., et al. Protein arginine methyl transferases-3 and -5 increase cell surface expression of cardiac sodium channel. FEBS Lett 2013, 587:3159-3165.
    • (2013) FEBS Lett , vol.587 , pp. 3159-3165
    • Beltran-Alvarez, P.1    Espejo, A.2    Schmauder, R.3    Beltran, C.4    Mrowka, R.5    Linke, T.6
  • 100
    • 84901724023 scopus 로고    scopus 로고
    • Reciprocal changes in phosphorylation and methylation of mammalian brain sodium channels in response to seizures
    • Baek J.H., Rubinstein M., Scheuer T., Trimmer J.S. Reciprocal changes in phosphorylation and methylation of mammalian brain sodium channels in response to seizures. J Biol Chem 2014, 289:15363-15373.
    • (2014) J Biol Chem , vol.289 , pp. 15363-15373
    • Baek, J.H.1    Rubinstein, M.2    Scheuer, T.3    Trimmer, J.S.4
  • 101
    • 84925496902 scopus 로고    scopus 로고
    • Interplay between R513 methylation and S516 phosphorylation of the cardiac voltage-gated sodium channel
    • Beltran-Alvarez P., Feixas F., Osuna S., Diaz-Hernandez R., Brugada R., Pagans S. Interplay between R513 methylation and S516 phosphorylation of the cardiac voltage-gated sodium channel. Amino Acids 2014, 47:429-434.
    • (2014) Amino Acids , vol.47 , pp. 429-434
    • Beltran-Alvarez, P.1    Feixas, F.2    Osuna, S.3    Diaz-Hernandez, R.4    Brugada, R.5    Pagans, S.6
  • 102
    • 84857665522 scopus 로고    scopus 로고
    • Reactive oxygen species suppress cardiac NaV1.5 expression through Foxo1
    • Mao W., You T., Ye B., Li X., Dong H.H., Hill J.A., et al. Reactive oxygen species suppress cardiac NaV1.5 expression through Foxo1. PLoS One 2012, 7:e32738.
    • (2012) PLoS One , vol.7 , pp. e32738
    • Mao, W.1    You, T.2    Ye, B.3    Li, X.4    Dong, H.H.5    Hill, J.A.6
  • 103
    • 38349099238 scopus 로고    scopus 로고
    • NF-kappaB-dependent transcriptional regulation of the cardiac scn5a sodium channel by angiotensin II
    • Shang L.L., Sanyal S., Pfahnl A.E., Jiao Z., Allen J., Liu H., et al. NF-kappaB-dependent transcriptional regulation of the cardiac scn5a sodium channel by angiotensin II. Am J Physiol Cell Physiol 2008, 294:C372-C379.
    • (2008) Am J Physiol Cell Physiol , vol.294 , pp. C372-C379
    • Shang, L.L.1    Sanyal, S.2    Pfahnl, A.E.3    Jiao, Z.4    Allen, J.5    Liu, H.6
  • 104
    • 0032574631 scopus 로고    scopus 로고
    • Elevated levels of 8-iso-prostaglandin F2alpha in pericardial fluid of patients with heart failure: a potential role for in vivo oxidant stress in ventricular dilatation and progression to heart failure
    • Mallat Z., Philip I., Lebret M., Chatel D., Maclouf J., Tedgui A. Elevated levels of 8-iso-prostaglandin F2alpha in pericardial fluid of patients with heart failure: a potential role for in vivo oxidant stress in ventricular dilatation and progression to heart failure. Circulation 1998, 97:1536-1539.
    • (1998) Circulation , vol.97 , pp. 1536-1539
    • Mallat, Z.1    Philip, I.2    Lebret, M.3    Chatel, D.4    Maclouf, J.5    Tedgui, A.6
  • 105
    • 77958501429 scopus 로고    scopus 로고
    • Reactive oxygen species originating from mitochondria regulate the cardiac sodium channel
    • Liu M., Liu H., Dudley S.C. Reactive oxygen species originating from mitochondria regulate the cardiac sodium channel. Circ Res 2010, 107:967-974.
    • (2010) Circ Res , vol.107 , pp. 967-974
    • Liu, M.1    Liu, H.2    Dudley, S.C.3
  • 106
    • 50049096940 scopus 로고    scopus 로고
    • Oxidation of multiple methionine residues impairs rapid sodium channel inactivation
    • Kassmann M., Hansel A., Leipold E., Birkenbeil J., Lu S.Q., Hoshi T., et al. Oxidation of multiple methionine residues impairs rapid sodium channel inactivation. Pflugers Arch 2008, 456:1085-1095.
    • (2008) Pflugers Arch , vol.456 , pp. 1085-1095
    • Kassmann, M.1    Hansel, A.2    Leipold, E.3    Birkenbeil, J.4    Lu, S.Q.5    Hoshi, T.6
  • 107
    • 79952772425 scopus 로고    scopus 로고
    • Reactive oxygen species-activated Ca/calmodulin kinase IIdelta is required for late I(Na) augmentation leading to cellular Na and Ca overload
    • Wagner S., Ruff H.M., Weber S.L., Bellmann S., Sowa T., Schulte T., et al. Reactive oxygen species-activated Ca/calmodulin kinase IIdelta is required for late I(Na) augmentation leading to cellular Na and Ca overload. Circ Res 2011, 108:555-565.
    • (2011) Circ Res , vol.108 , pp. 555-565
    • Wagner, S.1    Ruff, H.M.2    Weber, S.L.3    Bellmann, S.4    Sowa, T.5    Schulte, T.6
  • 108
    • 84893817379 scopus 로고    scopus 로고
    • Proteomics methods to study methionine oxidation
    • Ghesquiere B., Gevaert K. Proteomics methods to study methionine oxidation. Mass Spectrom Rev 2014, 33:147-156.
    • (2014) Mass Spectrom Rev , vol.33 , pp. 147-156
    • Ghesquiere, B.1    Gevaert, K.2
  • 109
    • 0034666307 scopus 로고    scopus 로고
    • Induction of persistent sodium current by exogenous and endogenous nitric oxide
    • Ahern G.P., Hsu S.F., Klyachko V.A., Jackson M.B. Induction of persistent sodium current by exogenous and endogenous nitric oxide. J Biol Chem 2000, 275:28810-28815.
    • (2000) J Biol Chem , vol.275 , pp. 28810-28815
    • Ahern, G.P.1    Hsu, S.F.2    Klyachko, V.A.3    Jackson, M.B.4
  • 110
    • 0035941409 scopus 로고    scopus 로고
    • Nitric oxide modulates cardiac Na(+) channel via protein kinase A and protein kinase G
    • Ahmmed G.U., Xu Y., Hong Dong P., Zhang Z., Eiserich J., Chiamvimonvat N. Nitric oxide modulates cardiac Na(+) channel via protein kinase A and protein kinase G. Circ Res 2001, 89:1005-1013.
    • (2001) Circ Res , vol.89 , pp. 1005-1013
    • Ahmmed, G.U.1    Xu, Y.2    Hong Dong, P.3    Zhang, Z.4    Eiserich, J.5    Chiamvimonvat, N.6
  • 112
  • 113
    • 48249148221 scopus 로고    scopus 로고
    • Syntrophin mutation associated with long QT syndrome through activation of the nNOS-SCN5A macromolecular complex
    • Ueda K., Valdivia C., Medeiros-Domingo A., Tester D.J., Vatta M., Farrugia G., et al. Syntrophin mutation associated with long QT syndrome through activation of the nNOS-SCN5A macromolecular complex. Proc Natl Acad Sci U S A 2008, 105:9355-9360.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9355-9360
    • Ueda, K.1    Valdivia, C.2    Medeiros-Domingo, A.3    Tester, D.J.4    Vatta, M.5    Farrugia, G.6
  • 114
    • 33747425933 scopus 로고    scopus 로고
    • Cardiac sodium channel Nav1.5 is regulated by a multiprotein complex composed of syntrophins and dystrophin
    • Gavillet B., Rougier J.S., Domenighetti A.A., Behar R., Boixel C., Ruchat P., et al. Cardiac sodium channel Nav1.5 is regulated by a multiprotein complex composed of syntrophins and dystrophin. Circ Res 2006, 99:407-414.
    • (2006) Circ Res , vol.99 , pp. 407-414
    • Gavillet, B.1    Rougier, J.S.2    Domenighetti, A.A.3    Behar, R.4    Boixel, C.5    Ruchat, P.6
  • 115
    • 56549103545 scopus 로고    scopus 로고
    • Alpha-1-syntrophin mutation and the long-QT syndrome: a disease of sodium channel disruption
    • Wu G., Ai T., Kim J.J., Mohapatra B., Xi Y., Li Z., et al. Alpha-1-syntrophin mutation and the long-QT syndrome: a disease of sodium channel disruption. Circ Arrhythm Electrophysiol 2008, 1:193-201.
    • (2008) Circ Arrhythm Electrophysiol , vol.1 , pp. 193-201
    • Wu, G.1    Ai, T.2    Kim, J.J.3    Mohapatra, B.4    Xi, Y.5    Li, Z.6
  • 117
    • 33644665708 scopus 로고    scopus 로고
    • Oxidative mediated lipid peroxidation recapitulates proarrhythmic effects on cardiac sodium channels
    • Fukuda K., Davies S.S., Nakajima T., Ong B.H., Kupershmidt S., Fessel J., et al. Oxidative mediated lipid peroxidation recapitulates proarrhythmic effects on cardiac sodium channels. Circ Res 2005, 97:1262-1269.
    • (2005) Circ Res , vol.97 , pp. 1262-1269
    • Fukuda, K.1    Davies, S.S.2    Nakajima, T.3    Ong, B.H.4    Kupershmidt, S.5    Fessel, J.6
  • 119
    • 4043059200 scopus 로고    scopus 로고
    • Cardiac voltage-gated sodium channel Nav1.5 is regulated by Nedd4-2 mediated ubiquitination
    • van Bemmelen M.X., Rougier J.S., Gavillet B., Apotheloz F., Daidie D., Tateyama M., et al. Cardiac voltage-gated sodium channel Nav1.5 is regulated by Nedd4-2 mediated ubiquitination. Circ Res 2004, 95:284-291.
    • (2004) Circ Res , vol.95 , pp. 284-291
    • van Bemmelen, M.X.1    Rougier, J.S.2    Gavillet, B.3    Apotheloz, F.4    Daidie, D.5    Tateyama, M.6
  • 120
    • 77955232406 scopus 로고    scopus 로고
    • Ubiquitylation and SUMOylation of cardiac ion channels
    • Rougier J.S., Albesa M., Abriel H. Ubiquitylation and SUMOylation of cardiac ion channels. J Cardiovasc Pharmacol 2010, 56:22-28.
    • (2010) J Cardiovasc Pharmacol , vol.56 , pp. 22-28
    • Rougier, J.S.1    Albesa, M.2    Abriel, H.3
  • 122
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin D., Kumar S. Physiological functions of the HECT family of ubiquitin ligases. Nat Rev Mol Cell Biol 2009, 10:398-409.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 125
    • 33847639227 scopus 로고    scopus 로고
    • The KCNQ1 potassium channel is down-regulated by ubiquitylating enzymes of the Nedd4/Nedd4-like family
    • Jespersen T., Membrez M., Nicolas C.S., Pitard B., Staub O., Olesen S.P., et al. The KCNQ1 potassium channel is down-regulated by ubiquitylating enzymes of the Nedd4/Nedd4-like family. Cardiovasc Res 2007, 74:64-74.
    • (2007) Cardiovasc Res , vol.74 , pp. 64-74
    • Jespersen, T.1    Membrez, M.2    Nicolas, C.S.3    Pitard, B.4    Staub, O.5    Olesen, S.P.6
  • 126
    • 79956326435 scopus 로고    scopus 로고
    • Nedd4-2-dependent ubiquitylation and regulation of the cardiac potassium channel hERG1
    • Albesa M., Grilo L.S., Gavillet B., Abriel H. Nedd4-2-dependent ubiquitylation and regulation of the cardiac potassium channel hERG1. J Mol Cell Cardiol 2011, 51:90-98.
    • (2011) J Mol Cell Cardiol , vol.51 , pp. 90-98
    • Albesa, M.1    Grilo, L.S.2    Gavillet, B.3    Abriel, H.4
  • 127
    • 33749386740 scopus 로고    scopus 로고
    • Ubiquitin protein ligase Nedd4 binds to connexin43 by a phosphorylation-modulated process
    • Leykauf K., Salek M., Bomke J., Frech M., Lehmann W.D., Durst M., et al. Ubiquitin protein ligase Nedd4 binds to connexin43 by a phosphorylation-modulated process. J Cell Sci 2006, 119:3634-3642.
    • (2006) J Cell Sci , vol.119 , pp. 3634-3642
    • Leykauf, K.1    Salek, M.2    Bomke, J.3    Frech, M.4    Lehmann, W.D.5    Durst, M.6
  • 128
    • 70349897786 scopus 로고    scopus 로고
    • Bepridil up-regulates cardiac Na+ channels as a long-term effect by blunting proteasome signals through inhibition of calmodulin activity
    • Kang L., Zheng M.Q., Morishima M., Wang Y., Kaku T., Ono K. Bepridil up-regulates cardiac Na+ channels as a long-term effect by blunting proteasome signals through inhibition of calmodulin activity. Br J Pharmacol 2009, 157:404-414.
    • (2009) Br J Pharmacol , vol.157 , pp. 404-414
    • Kang, L.1    Zheng, M.Q.2    Morishima, M.3    Wang, Y.4    Kaku, T.5    Ono, K.6
  • 129
    • 84879495401 scopus 로고    scopus 로고
    • Proteasome inhibitor (MG132) rescues Nav1.5 protein content and the cardiac sodium current in dystrophin-deficient mdx (5cv) mice
    • Rougier J.S., Gavillet B., Abriel H. Proteasome inhibitor (MG132) rescues Nav1.5 protein content and the cardiac sodium current in dystrophin-deficient mdx (5cv) mice. Front Physiol 2013, 4:51.
    • (2013) Front Physiol , vol.4 , pp. 51
    • Rougier, J.S.1    Gavillet, B.2    Abriel, H.3
  • 130
    • 84885012783 scopus 로고    scopus 로고
    • Large-scale identification of ubiquitination sites by mass spectrometry
    • Udeshi N.D., Mertins P., Svinkina T., Carr S.A. Large-scale identification of ubiquitination sites by mass spectrometry. Nat Protoc 2013, 8:1950-1960.
    • (2013) Nat Protoc , vol.8 , pp. 1950-1960
    • Udeshi, N.D.1    Mertins, P.2    Svinkina, T.3    Carr, S.A.4
  • 131
    • 84857563430 scopus 로고    scopus 로고
    • Deubiquitylating enzyme USP2 counteracts Nedd4-2-mediated downregulation of KCNQ1 potassium channels
    • Krzystanek K., Rasmussen H.B., Grunnet M., Staub O., Olesen S.P., Abriel H., et al. Deubiquitylating enzyme USP2 counteracts Nedd4-2-mediated downregulation of KCNQ1 potassium channels. Heart Rhythm 2012, 9:440-448.
    • (2012) Heart Rhythm , vol.9 , pp. 440-448
    • Krzystanek, K.1    Rasmussen, H.B.2    Grunnet, M.3    Staub, O.4    Olesen, S.P.5    Abriel, H.6
  • 133
    • 84879658348 scopus 로고    scopus 로고
    • Dysregulation of voltage-gated sodium channels by ubiquitin ligase NEDD4-2 in neuropathic pain
    • Laedermann C.J., Cachemaille M., Kirschmann G., Pertin M., Gosselin R.D., Chang I., et al. Dysregulation of voltage-gated sodium channels by ubiquitin ligase NEDD4-2 in neuropathic pain. J Clin Invest 2013, 123:3002-3013.
    • (2013) J Clin Invest , vol.123 , pp. 3002-3013
    • Laedermann, C.J.1    Cachemaille, M.2    Kirschmann, G.3    Pertin, M.4    Gosselin, R.D.5    Chang, I.6
  • 134
    • 84876035030 scopus 로고    scopus 로고
    • Deciphering post-translational modification codes
    • Lothrop A.P., Torres M.P., Fuchs S.M. Deciphering post-translational modification codes. FEBS Lett 2013, 587:1247-1257.
    • (2013) FEBS Lett , vol.587 , pp. 1247-1257
    • Lothrop, A.P.1    Torres, M.P.2    Fuchs, S.M.3
  • 135
    • 79953173218 scopus 로고    scopus 로고
    • Ion channel regulation by protein palmitoylation
    • Shipston M.J. Ion channel regulation by protein palmitoylation. J Biol Chem 2011, 286:8709-8716.
    • (2011) J Biol Chem , vol.286 , pp. 8709-8716
    • Shipston, M.J.1
  • 136
    • 84890644637 scopus 로고    scopus 로고
    • Status of large-scale analysis of post-translational modifications by mass spectrometry
    • Olsen J.V., Mann M. Status of large-scale analysis of post-translational modifications by mass spectrometry. Mol Cell Proteomics 2013, 12:3444-3452.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 3444-3452
    • Olsen, J.V.1    Mann, M.2


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