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Volumn 588, Issue 16, 2010, Pages 3011-3030

Kinetic analysis of the effects of H+ or Ni2+ on Kv1.5 current shows that both ions enhance slow inactivation and induce resting inactivation

Author keywords

[No Author keywords available]

Indexed keywords

NICKEL; POTASSIUM CHANNEL KV1.5; PROTON; HYDROGEN;

EID: 77955724594     PISSN: 00223751     EISSN: 14697793     Source Type: Journal    
DOI: 10.1113/jphysiol.2010.191544     Document Type: Article
Times cited : (11)

References (42)
  • 1
    • 0032537513 scopus 로고    scopus 로고
    • Pore accessibility during C-type inactivation in Shaker K+ channels
    • Basso C, Labarca P, Stefani E, Alvarez O, Latorre R. Pore accessibility during C-type inactivation in Shaker K+ channels. FEBS Lett 1998, 429:375-380.
    • (1998) FEBS Lett , vol.429 , pp. 375-380
    • Basso, C.1    Labarca, P.2    Stefani, E.3    Alvarez, O.4    Latorre, R.5
  • 2
    • 0028793256 scopus 로고
    • Modulation of K+ current by frequency and external [K+]: a tale of two inactivation mechanisms
    • Baukrowitz T, Yellen G. Modulation of K+ current by frequency and external [K+]: a tale of two inactivation mechanisms. Neuron 1995, 15:951-960.
    • (1995) Neuron , vol.15 , pp. 951-960
    • Baukrowitz, T.1    Yellen, G.2
  • 3
    • 58149159238 scopus 로고    scopus 로고
    • External Ba2+ block of human Kv1.5 at neutral and acidic pH: evidence for Ho+-induced constriction of the outer pore mouth at rest
    • Cheng YM, Fedida D, Kehl SJ. External Ba2+ block of human Kv1.5 at neutral and acidic pH: evidence for Ho+-induced constriction of the outer pore mouth at rest. Biophys J 2008, 95:4456-4468.
    • (2008) Biophys J , vol.95 , pp. 4456-4468
    • Cheng, Y.M.1    Fedida, D.2    Kehl, S.J.3
  • 4
    • 56849104625 scopus 로고    scopus 로고
    • Closed-state inactivation induced in Kv1 channels by extracellular acidification
    • Claydon TW, Kehl SJ, Fedida D. Closed-state inactivation induced in Kv1 channels by extracellular acidification. Channels (Austin) 2008, 2:139-142.
    • (2008) Channels (Austin) , vol.2 , pp. 139-142
    • Claydon, T.W.1    Kehl, S.J.2    Fedida, D.3
  • 6
    • 0000410893 scopus 로고    scopus 로고
    • A Q-matrix cookbook: How to write only one program to calculate the single-channel and macroscopic predictions for any kinetic mechanism
    • Sakmann B, Neher E. 2nd edn, ed, Springer, New York
    • Colquhoun D, Hawkes AG. A Q-matrix cookbook: How to write only one program to calculate the single-channel and macroscopic predictions for any kinetic mechanism. Single-Channel Recording 2009, 589-633. Sakmann B, Neher E. 2nd edn, ed, Springer, New York
    • (2009) Single-Channel Recording , pp. 589-633
    • Colquhoun, D.1    Hawkes, A.G.2
  • 7
    • 33947324979 scopus 로고    scopus 로고
    • SCAM analysis reveals a discrete region of the pore turret that modulates slow inactivation in Kv1.5
    • Eduljee C, Claydon TW, Viswanathan V, Fedida D, Kehl SJ. SCAM analysis reveals a discrete region of the pore turret that modulates slow inactivation in Kv1.5. Am J Physiol Cell Physiol 2007, 292:C1041-C1052.
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Eduljee, C.1    Claydon, T.W.2    Viswanathan, V.3    Fedida, D.4    Kehl, S.J.5
  • 8
    • 0033106231 scopus 로고    scopus 로고
    • Modulation of slow inactivation in human cardiac Kv1.5 channels by extra- and intracellular permeant cations
    • Fedida D, Maruoka ND, Lin S. Modulation of slow inactivation in human cardiac Kv1.5 channels by extra- and intracellular permeant cations. J Physiol 1999, 515:315-329.
    • (1999) J Physiol , vol.515 , pp. 315-329
    • Fedida, D.1    Maruoka, N.D.2    Lin, S.3
  • 9
    • 0027288356 scopus 로고
    • Identity of a novel delayed rectifier current from human heart with a cloned K+ channel current
    • Fedida D, Wible B, Wang Z, Fermini B, Faust F, Nattel S, Brown AM. Identity of a novel delayed rectifier current from human heart with a cloned K+ channel current. Circ Res 1993, 73:210-216.
    • (1993) Circ Res , vol.73 , pp. 210-216
    • Fedida, D.1    Wible, B.2    Wang, Z.3    Fermini, B.4    Faust, F.5    Nattel, S.6    Brown, A.M.7
  • 10
    • 23344436260 scopus 로고    scopus 로고
    • Synergistic inhibition of the maximum conductance of Kv1.5 channels by extracellular K+ reduction and acidification
    • Fedida D, Zhang S, Kwan DC, Eduljee C, Kehl SJ. Synergistic inhibition of the maximum conductance of Kv1.5 channels by extracellular K+ reduction and acidification. Cell Biochem Biophys 2005, 43:231-242.
    • (2005) Cell Biochem Biophys , vol.43 , pp. 231-242
    • Fedida, D.1    Zhang, S.2    Kwan, D.C.3    Eduljee, C.4    Kehl, S.J.5
  • 12
    • 0031594195 scopus 로고    scopus 로고
    • A permanent ion binding site located between two gates of the Shaker K+ channel
    • Harris RE, Larsson HP, Isacoff EY. A permanent ion binding site located between two gates of the Shaker K+ channel. Biophys J 1998, 74:1808-1820.
    • (1998) Biophys J , vol.74 , pp. 1808-1820
    • Harris, R.E.1    Larsson, H.P.2    Isacoff, E.Y.3
  • 13
    • 73249138872 scopus 로고    scopus 로고
    • Specificities of atrial electrophysiology: Clues to a better understanding of cardiac function and the mechanisms of arrhythmias
    • Hatem SN, Coulombe A, Balse E. Specificities of atrial electrophysiology: Clues to a better understanding of cardiac function and the mechanisms of arrhythmias. J Mol Cell Cardiol 2010, 48:90-95.
    • (2010) J Mol Cell Cardiol , vol.48 , pp. 90-95
    • Hatem, S.N.1    Coulombe, A.2    Balse, E.3
  • 14
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi T, Zagotta WN, Aldrich RW. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science 1990, 250:533-538.
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 15
    • 0035846854 scopus 로고    scopus 로고
    • Regulation of a mammalian Shaker-related potassium channel, hKv1.5, by extracellular potassium and pH
    • Jäger H, Grissmer S. Regulation of a mammalian Shaker-related potassium channel, hKv1.5, by extracellular potassium and pH. FEBS Lett 2001, 488:45-50.
    • (2001) FEBS Lett , vol.488 , pp. 45-50
    • Jäger, H.1    Grissmer, S.2
  • 16
    • 0343198556 scopus 로고    scopus 로고
    • Regulation of mammalian Shaker-related K+ channels: evidence for non-conducting closed and non-conducting inactivated states
    • Jäger H, Rauer H, Nguyen AN, Aiyar J, Chandy KG, Grissmer S. Regulation of mammalian Shaker-related K+ channels: evidence for non-conducting closed and non-conducting inactivated states. J Physiol 1998, 506:291-301.
    • (1998) J Physiol , vol.506 , pp. 291-301
    • Jäger, H.1    Rauer, H.2    Nguyen, A.N.3    Aiyar, J.4    Chandy, K.G.5    Grissmer, S.6
  • 17
    • 0037095942 scopus 로고    scopus 로고
    • Molecular determinants of the inhibition of human Kv1.5 potassium currents by external protons and Zn2+
    • Kehl SJ, Eduljee C, Kwan DC, Zhang S, Fedida D. Molecular determinants of the inhibition of human Kv1.5 potassium currents by external protons and Zn2+. J Physiol 2002, 541:9-24.
    • (2002) J Physiol , vol.541 , pp. 9-24
    • Kehl, S.J.1    Eduljee, C.2    Kwan, D.C.3    Zhang, S.4    Fedida, D.5
  • 18
    • 0031897384 scopus 로고    scopus 로고
    • Modulation of C-type inactivation by K+ at the potassium channel selectivity filter
    • Kiss L, Korn SJ. Modulation of C-type inactivation by K+ at the potassium channel selectivity filter. Biophys J 1998, 74:1840-1849.
    • (1998) Biophys J , vol.74 , pp. 1840-1849
    • Kiss, L.1    Korn, S.J.2
  • 19
    • 0034902362 scopus 로고    scopus 로고
    • U-type inactivation of Kv3.1 and Shaker potassium channels
    • Klemic KG, Kirsch GE, Jones SW. U-type inactivation of Kv3.1 and Shaker potassium channels. Biophys J 2001, 81:814-826.
    • (2001) Biophys J , vol.81 , pp. 814-826
    • Klemic, K.G.1    Kirsch, G.E.2    Jones, S.W.3
  • 20
    • 33745216690 scopus 로고    scopus 로고
    • A structural interpretation of voltage-gated potassium channel inactivation
    • Kurata HT, Fedida D. A structural interpretation of voltage-gated potassium channel inactivation. Prog Biophys Mol Biol 2006, 92:185-208.
    • (2006) Prog Biophys Mol Biol , vol.92 , pp. 185-208
    • Kurata, H.T.1    Fedida, D.2
  • 21
    • 1942487651 scopus 로고    scopus 로고
    • The external K+ concentration and mutations in the outer pore mouth affect the inhibition of Kv1.5 current by Ni2+
    • Kwan DC, Eduljee C, Lee L, Zhang S, Fedida D, Kehl SJ. The external K+ concentration and mutations in the outer pore mouth affect the inhibition of Kv1.5 current by Ni2+. Biophys J 2004, 86:2238-2250.
    • (2004) Biophys J , vol.86 , pp. 2238-2250
    • Kwan, D.C.1    Eduljee, C.2    Lee, L.3    Zhang, S.4    Fedida, D.5    Kehl, S.J.6
  • 22
    • 33645778112 scopus 로고    scopus 로고
    • Single channel analysis reveals different modes of Kv1.5 gating behavior regulated by changes of external pH
    • Kwan DC, Fedida D, Kehl SJ. Single channel analysis reveals different modes of Kv1.5 gating behavior regulated by changes of external pH. Biophys J 2006, 90:1212-1222.
    • (2006) Biophys J , vol.90 , pp. 1212-1222
    • Kwan, D.C.1    Fedida, D.2    Kehl, S.J.3
  • 23
    • 23844441476 scopus 로고    scopus 로고
    • Characterization of a proton-activated, outwardly rectifying anion channel
    • Lambert S, Oberwinkler J. Characterization of a proton-activated, outwardly rectifying anion channel. J Physiol 2005, 567:191-213.
    • (2005) J Physiol , vol.567 , pp. 191-213
    • Lambert, S.1    Oberwinkler, J.2
  • 24
    • 0029774160 scopus 로고    scopus 로고
    • A voltage-dependent role for K+ in recovery from C-type inactivation
    • Levy DI, Deutsch C. A voltage-dependent role for K+ in recovery from C-type inactivation. Biophys J 1996, 71:3157-3166.
    • (1996) Biophys J , vol.71 , pp. 3157-3166
    • Levy, D.I.1    Deutsch, C.2
  • 25
    • 0029990996 scopus 로고    scopus 로고
    • Dynamic rearrangement of the outer mouth of a K+ channel during gating
    • Liu Y, Jurman ME, Yellen G. Dynamic rearrangement of the outer mouth of a K+ channel during gating. Neuron 1996, 16:859-867.
    • (1996) Neuron , vol.16 , pp. 859-867
    • Liu, Y.1    Jurman, M.E.2    Yellen, G.3
  • 26
    • 0031718344 scopus 로고    scopus 로고
    • Protein rearrangements underlying slow inactivation of the Shaker K+ channel
    • Loots E, Isacoff EY. Protein rearrangements underlying slow inactivation of the Shaker K+ channel. J Gen Physiol 1998, 112:377-389.
    • (1998) J Gen Physiol , vol.112 , pp. 377-389
    • Loots, E.1    Isacoff, E.Y.2
  • 27
    • 0033756431 scopus 로고    scopus 로고
    • Molecular coupling of S4 to a K+ channel's slow inactivation gate
    • Loots E, Isacoff EY. Molecular coupling of S4 to a K+ channel's slow inactivation gate. J Gen Physiol 2000, 116:623-636.
    • (2000) J Gen Physiol , vol.116 , pp. 623-636
    • Loots, E.1    Isacoff, E.Y.2
  • 28
    • 0027828292 scopus 로고
    • Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels
    • López-Barneo J, Hoshi T, Heinemann SH, Aldrich RW. Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels. Receptors Channels 1993, 1:61-71.
    • (1993) Receptors Channels , vol.1 , pp. 61-71
    • López-Barneo, J.1    Hoshi, T.2    Heinemann, S.H.3    Aldrich, R.W.4
  • 29
    • 0030670857 scopus 로고    scopus 로고
    • Temperature and pressure dependence of Shaker K+ channel N- and C-type inactivation
    • Meyer R, Heinemann SH. Temperature and pressure dependence of Shaker K+ channel N- and C-type inactivation. Eur Biophys J 1997, 26:433-445.
    • (1997) Eur Biophys J , vol.26 , pp. 433-445
    • Meyer, R.1    Heinemann, S.H.2
  • 30
    • 0032895084 scopus 로고    scopus 로고
    • Functional consequences of a decreased potassium affinity in a potassium channel pore. Ion interactions and C-type inactivation
    • Ogielska EM, Aldrich RW. Functional consequences of a decreased potassium affinity in a potassium channel pore. Ion interactions and C-type inactivation. J Gen Physiol 1999, 113:347-358.
    • (1999) J Gen Physiol , vol.113 , pp. 347-358
    • Ogielska, E.M.1    Aldrich, R.W.2
  • 31
    • 0030656233 scopus 로고    scopus 로고
    • Correlation between charge movement and ionic current during slow inactivation in Shaker K+ channels
    • Olcese R, Latorre R, Toro L, Bezanilla F, Stefani E. Correlation between charge movement and ionic current during slow inactivation in Shaker K+ channels. J Gen Physiol 1997, 110:579-589.
    • (1997) J Gen Physiol , vol.110 , pp. 579-589
    • Olcese, R.1    Latorre, R.2    Toro, L.3    Bezanilla, F.4    Stefani, E.5
  • 33
    • 0035449645 scopus 로고    scopus 로고
    • External nickel blocks human Kv1.5 channels stably expressed in CHO cells
    • Perchenet L, Clément-Chomienne O. External nickel blocks human Kv1.5 channels stably expressed in CHO cells. J Membr Biol 2001, 183:51-60.
    • (2001) J Membr Biol , vol.183 , pp. 51-60
    • Perchenet, L.1    Clément-Chomienne, O.2
  • 34
    • 0033771705 scopus 로고    scopus 로고
    • Characterization of mibefradil block of the human heart delayed rectifier hKv1.5
    • Perchenet L, Clément-Chomienne O. Characterization of mibefradil block of the human heart delayed rectifier hKv1.5. J Pharmacol Exp Ther 2000, 295:771-778.
    • (2000) J Pharmacol Exp Ther , vol.295 , pp. 771-778
    • Perchenet, L.1    Clément-Chomienne, O.2
  • 35
    • 0032897178 scopus 로고    scopus 로고
    • H+ ion modulation of C-type inactivation of Shaker K+ channels
    • Pérez-Cornejo P. H+ ion modulation of C-type inactivation of Shaker K+ channels. Pflugers Arch 1999, 437:865-870.
    • (1999) Pflugers Arch , vol.437 , pp. 865-870
    • Pérez-Cornejo, P.1
  • 36
    • 0031808070 scopus 로고    scopus 로고
    • Evidence for multiple open and inactivated states of the hKv1.5 delayed rectifier
    • Rich TC, Snyders DJ. Evidence for multiple open and inactivated states of the hKv1.5 delayed rectifier. Biophys J 1998, 75:183-195.
    • (1998) Biophys J , vol.75 , pp. 183-195
    • Rich, T.C.1    Snyders, D.J.2
  • 37
    • 0842309099 scopus 로고    scopus 로고
    • Mechanisms of the inhibition of Shaker potassium channels by protons
    • Starkus JG, Varga Z, Schönherr R, Heinemann SH. Mechanisms of the inhibition of Shaker potassium channels by protons. Pflugers Arch 2003, 447:44-54.
    • (2003) Pflugers Arch , vol.447 , pp. 44-54
    • Starkus, J.G.1    Varga, Z.2    Schönherr, R.3    Heinemann, S.H.4
  • 38
    • 0032946237 scopus 로고    scopus 로고
    • Differential sensitivity of voltage-gated potassium channels Kv1.5 and Kv1.2 to acidic pH and molecular identification of pH sensor
    • Steidl JV, Yool AJ. Differential sensitivity of voltage-gated potassium channels Kv1.5 and Kv1.2 to acidic pH and molecular identification of pH sensor. Mol Pharmacol 1999, 55:812-820.
    • (1999) Mol Pharmacol , vol.55 , pp. 812-820
    • Steidl, J.V.1    Yool, A.J.2
  • 39
    • 0037214493 scopus 로고    scopus 로고
    • Effect of external pH on activation of the Kv1.5 potassium channel
    • Trapani JG, Korn SJ. Effect of external pH on activation of the Kv1.5 potassium channel. Biophys J 2003, 84:195-204.
    • (2003) Biophys J , vol.84 , pp. 195-204
    • Trapani, J.G.1    Korn, S.J.2
  • 40
    • 0030906796 scopus 로고    scopus 로고
    • How does the W434F mutation block current in Shaker potassium channels?
    • Yang Y, Yan Y, Sigworth FJ. How does the W434F mutation block current in Shaker potassium channels?. J Gen Physiol 1997, 109:779-789.
    • (1997) J Gen Physiol , vol.109 , pp. 779-789
    • Yang, Y.1    Yan, Y.2    Sigworth, F.J.3
  • 41
    • 0028297301 scopus 로고
    • An engineered cysteine in the external mouth of a K+ channel allows inactivation to be modulated by metal binding
    • Yellen G, Sodickson D, Chen TY, Jurman ME. An engineered cysteine in the external mouth of a K+ channel allows inactivation to be modulated by metal binding. Biophys J 1994, 66:1068-1075.
    • (1994) Biophys J , vol.66 , pp. 1068-1075
    • Yellen, G.1    Sodickson, D.2    Chen, T.Y.3    Jurman, M.E.4
  • 42
    • 0032101645 scopus 로고    scopus 로고
    • Identification of endogenous outward currents in the human embryonic kidney (HEK 293) cell line
    • Zhu G, Zhang Y, Xu H, Jiang C. Identification of endogenous outward currents in the human embryonic kidney (HEK 293) cell line. J Neurosci Methods 1998, 81:73-83.
    • (1998) J Neurosci Methods , vol.81 , pp. 73-83
    • Zhu, G.1    Zhang, Y.2    Xu, H.3    Jiang, C.4


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