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Volumn 584, Issue 10, 2010, Pages 2049-2056

Contribution of voltage-gated potassium channels to the regulation of apoptosis

Author keywords

Apoptosis; Kv1.3; Mitochondria; Potassium channel; Pro apoptotic Bax

Indexed keywords

POTASSIUM CHANNEL KV1.3;

EID: 77952671757     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.01.038     Document Type: Review
Times cited : (76)

References (111)
  • 1
    • 0027380629 scopus 로고
    • Structure-function studies on the pore of potassium channels
    • Pongs O. Structure-function studies on the pore of potassium channels. J. Membr. Biol. 1993, 136:1-8.
    • (1993) J. Membr. Biol. , vol.136 , pp. 1-8
    • Pongs, O.1
  • 3
    • 0025706152 scopus 로고
    • Mutations affecting TEA blockade and ion permeation in voltage-activated K+ channels
    • MacKinnon R., Yellen G. Mutations affecting TEA blockade and ion permeation in voltage-activated K+ channels. Science 1990, 250:276-279.
    • (1990) Science , vol.250 , pp. 276-279
    • MacKinnon, R.1    Yellen, G.2
  • 4
    • 0026058182 scopus 로고
    • Alteration of ionic selectivity of a K+ channel by mutation of the H5 region
    • Yool A.J., Schwarz T.L. Alteration of ionic selectivity of a K+ channel by mutation of the H5 region. Nature 1991, 349:700-704.
    • (1991) Nature , vol.349 , pp. 700-704
    • Yool, A.J.1    Schwarz, T.L.2
  • 5
    • 8144228615 scopus 로고    scopus 로고
    • Voltage-gated potassium channels in cell proliferation
    • Pardo L.A. Voltage-gated potassium channels in cell proliferation. Physiology (Bethesda) 2004, 19:285-292.
    • (2004) Physiology (Bethesda) , vol.19 , pp. 285-292
    • Pardo, L.A.1
  • 8
    • 11844307184 scopus 로고    scopus 로고
    • Roles of K+ channels in regulating tumour cell proliferation and apoptosis
    • Wang Z. Roles of K+ channels in regulating tumour cell proliferation and apoptosis. Pflugers Arch. Eur. J. Physiol. 2004, 448:274-286.
    • (2004) Pflugers Arch. Eur. J. Physiol. , vol.448 , pp. 274-286
    • Wang, Z.1
  • 11
    • 0035064074 scopus 로고    scopus 로고
    • Calcium signalling mechanisms in T lymphocytes
    • Lewis R.S. Calcium signalling mechanisms in T lymphocytes. Ann. Rev. Immunol. 2001, 19:497-521.
    • (2001) Ann. Rev. Immunol. , vol.19 , pp. 497-521
    • Lewis, R.S.1
  • 12
    • 70349162817 scopus 로고    scopus 로고
    • The functional network of ion channels in lymphocytes
    • Cahalan M.D., Chandy K.G. The functional network of ion channels in lymphocytes. Immunol. Rev. 2009, 231:59-97.
    • (2009) Immunol. Rev. , vol.231 , pp. 59-97
    • Cahalan, M.D.1    Chandy, K.G.2
  • 14
    • 34249879293 scopus 로고    scopus 로고
    • Cell shrinkage and monovalent cation fluxes: role in apoptosis
    • Bortner C.D., Cidlowski J.A. Cell shrinkage and monovalent cation fluxes: role in apoptosis. Arch. Biochem. Biophys. 2007, 462:176-188.
    • (2007) Arch. Biochem. Biophys. , vol.462 , pp. 176-188
    • Bortner, C.D.1    Cidlowski, J.A.2
  • 15
    • 40349110969 scopus 로고    scopus 로고
    • Potassium channels in the regulation of pulmonary artery smooth muscle cell proliferation and apoptosis: pharmacotherapeutic implications
    • Burg E.D., Remillard C.V., Yuan J.X. Potassium channels in the regulation of pulmonary artery smooth muscle cell proliferation and apoptosis: pharmacotherapeutic implications. Br. J. Pharmacol. 2008, 153:S99-S111.
    • (2008) Br. J. Pharmacol. , vol.153
    • Burg, E.D.1    Remillard, C.V.2    Yuan, J.X.3
  • 16
    • 0042829363 scopus 로고    scopus 로고
    • Regulation and critical role of potassium homeostasis in apoptosis
    • Yu S.P. Regulation and critical role of potassium homeostasis in apoptosis. Prog. Neurobiol. 2003, 70:363-386.
    • (2003) Prog. Neurobiol. , vol.70 , pp. 363-386
    • Yu, S.P.1
  • 18
    • 0034788224 scopus 로고    scopus 로고
    • Apoptosis, cell volume regulation and volume regulatory chloride channels
    • Okada Y., Maeno E. Apoptosis, cell volume regulation and volume regulatory chloride channels. Comp. Biochem. Physiol. A 2001, 130:377-383.
    • (2001) Comp. Biochem. Physiol. A , vol.130 , pp. 377-383
    • Okada, Y.1    Maeno, E.2
  • 19
  • 20
    • 0032489679 scopus 로고    scopus 로고
    • The tyrosine kinase p56lck mediates activation of swelling-induced chloride channels in lymphocytes
    • Lepple-Wienhues A.L., Szabò I., Laun T., Kaba N.K., Gulbins E., Fang F. The tyrosine kinase p56lck mediates activation of swelling-induced chloride channels in lymphocytes. J. Cell Biol. 1998, 141:281-286.
    • (1998) J. Cell Biol. , vol.141 , pp. 281-286
    • Lepple-Wienhues, A.L.1    Szabò, I.2    Laun, T.3    Kaba, N.K.4    Gulbins, E.5    Fang, F.6
  • 21
    • 0034662989 scopus 로고    scopus 로고
    • Normotonic cell shrinkage because of disordered volume regulation is an early prerequisite to apoptosis
    • Maeno E., Ishizaki Y., Kanaseki T., Hazama A., Okada Y. Normotonic cell shrinkage because of disordered volume regulation is an early prerequisite to apoptosis. Proc. Natl. Acad. Sci. USA 2000, 97:9487-9492.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9487-9492
    • Maeno, E.1    Ishizaki, Y.2    Kanaseki, T.3    Hazama, A.4    Okada, Y.5
  • 23
    • 0033776392 scopus 로고    scopus 로고
    • Effects of tetraethylammonium analogs on apoptosis and membrane currents in cultured cortical neurons
    • Wang X., Xiao A.Y., Ichinose T., Yu S.P. Effects of tetraethylammonium analogs on apoptosis and membrane currents in cultured cortical neurons. J. Pharmacol. Exp. Ther. 2000, 295:524-530.
    • (2000) J. Pharmacol. Exp. Ther. , vol.295 , pp. 524-530
    • Wang, X.1    Xiao, A.Y.2    Ichinose, T.3    Yu, S.P.4
  • 24
    • 0038304416 scopus 로고    scopus 로고
    • Potassium channel blockers attenuate hypoxia- and ischemia-induced neuronal death in vitro and in vivo
    • Wei L., Yu S.P., Gottron F., Snider B.J., Zipfel G.J., Choi D.W. Potassium channel blockers attenuate hypoxia- and ischemia-induced neuronal death in vitro and in vivo. Stroke 2003, 34:1281-1286.
    • (2003) Stroke , vol.34 , pp. 1281-1286
    • Wei, L.1    Yu, S.P.2    Gottron, F.3    Snider, B.J.4    Zipfel, G.J.5    Choi, D.W.6
  • 25
    • 0032578531 scopus 로고    scopus 로고
    • Apoptotic proteins Reaper and Grim induce stable inactivation in voltage-gated potassium channels
    • Avdonin V., Kasuya J., Ciorba M.A., Kaplan B., Hoshi T., Iverson L. Apoptotic proteins Reaper and Grim induce stable inactivation in voltage-gated potassium channels. Proc. Natl. Acad. Sci. USA 1998, 95:11703-11708.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11703-11708
    • Avdonin, V.1    Kasuya, J.2    Ciorba, M.A.3    Kaplan, B.4    Hoshi, T.5    Iverson, L.6
  • 26
    • 0030936280 scopus 로고    scopus 로고
    • 4-Aminopyridine causes apoptosis and blocks an outward rectifier K+ channel in malignant astrocytoma cell lines
    • Chin L.S., Park C.C., Zitnay K.M., Sinha M., DiPatri A.J., Perillan P., Simard J.M. 4-Aminopyridine causes apoptosis and blocks an outward rectifier K+ channel in malignant astrocytoma cell lines. J. Neurosci. Res. 1997, 48:122-127.
    • (1997) J. Neurosci. Res. , vol.48 , pp. 122-127
    • Chin, L.S.1    Park, C.C.2    Zitnay, K.M.3    Sinha, M.4    DiPatri, A.J.5    Perillan, P.6    Simard, J.M.7
  • 27
    • 0030928648 scopus 로고    scopus 로고
    • The potassium channel opener cromakalim prevents glutamate-induced cell death in hippocampal neurons
    • Lauritzen I., De Weille J.R., Lazdunski M. The potassium channel opener cromakalim prevents glutamate-induced cell death in hippocampal neurons. J. Neurochem. 1997, 69:1570-1579.
    • (1997) J. Neurochem. , vol.69 , pp. 1570-1579
    • Lauritzen, I.1    De Weille, J.R.2    Lazdunski, M.3
  • 28
    • 0029810967 scopus 로고    scopus 로고
    • Tyrosine-phosphorylation-dependent suppression of a voltage-gated K+ channel in T lymphocytes upon Fas stimulation
    • Szabò I., Gulbins E., Apfel H., Zhang X., Barth P., Busch A.E., Schlottmann K., Pongs O., Lang F. Tyrosine-phosphorylation-dependent suppression of a voltage-gated K+ channel in T lymphocytes upon Fas stimulation. J. Biol. Chem. 1996, 271:20465-20469.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20465-20469
    • Szabò, I.1    Gulbins, E.2    Apfel, H.3    Zhang, X.4    Barth, P.5    Busch, A.E.6    Schlottmann, K.7    Pongs, O.8    Lang, F.9
  • 29
    • 0031451872 scopus 로고    scopus 로고
    • A primary role for K+ and Na+ efflux in the activation of apoptosis
    • Bortner C.D., Hughes F.M., Cidlowski J.A. A primary role for K+ and Na+ efflux in the activation of apoptosis. J. Biol. Chem. 1997, 272:32436-32442.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32436-32442
    • Bortner, C.D.1    Hughes, F.M.2    Cidlowski, J.A.3
  • 30
    • 0041355326 scopus 로고    scopus 로고
    • Stimulation of Kv1.3 potassium channels by death receptors during apoptosis in Jurkat T lymphocytes
    • Storey N.M., Gomez-Angelats M., Bortner C.D., Armstrong D.L., Cidlowski J.A. Stimulation of Kv1.3 potassium channels by death receptors during apoptosis in Jurkat T lymphocytes. J. Biol. Chem. 2003, 278:33319-33326.
    • (2003) J. Biol. Chem. , vol.278 , pp. 33319-33326
    • Storey, N.M.1    Gomez-Angelats, M.2    Bortner, C.D.3    Armstrong, D.L.4    Cidlowski, J.A.5
  • 32
  • 34
    • 48249146171 scopus 로고    scopus 로고
    • Kv1.1 is associated with neuronal apoptosis and modulated by protein kinase C in the rat cerebellar granule cell
    • Hu C.L., Zeng X.M., Zhou M.H., Shi Y.T., Cao H., Mei Y.A. Kv1.1 is associated with neuronal apoptosis and modulated by protein kinase C in the rat cerebellar granule cell. J. Neurochem. 2008, 106:1125-1137.
    • (2008) J. Neurochem. , vol.106 , pp. 1125-1137
    • Hu, C.L.1    Zeng, X.M.2    Zhou, M.H.3    Shi, Y.T.4    Cao, H.5    Mei, Y.A.6
  • 35
    • 79959375470 scopus 로고    scopus 로고
    • Kv1.1 and Kv1.3 contribute to the degeneration of retinal ganglion cells after optic nerve transection in vivo
    • Koeberle P.D., Wang Y., Schlichter L.C. Kv1.1 and Kv1.3 contribute to the degeneration of retinal ganglion cells after optic nerve transection in vivo. Cell Death Diff. 2009, 1-11.
    • (2009) Cell Death Diff. , pp. 1-11
    • Koeberle, P.D.1    Wang, Y.2    Schlichter, L.C.3
  • 36
    • 70449470623 scopus 로고    scopus 로고
    • Contribution of Kv channel subunits to glutamate-induced apoptosis in cultured rat hippocampal neurons
    • Shen Q.J., Zhao Y.M., Cao D.X., Wang X.L. Contribution of Kv channel subunits to glutamate-induced apoptosis in cultured rat hippocampal neurons. J. Neurosci. Res. 2009, 87:3153-3160.
    • (2009) J. Neurosci. Res. , vol.87 , pp. 3153-3160
    • Shen, Q.J.1    Zhao, Y.M.2    Cao, D.X.3    Wang, X.L.4
  • 37
    • 0041932216 scopus 로고    scopus 로고
    • Potassium channel gene therapy can prevent neuron death resulting from necrotic and apoptotic insults
    • Lee A.L., Dumas T.C., Tarapore P.E., Webster B.R., Ho D.Y., Kaufer D., Sapolsky R.M. Potassium channel gene therapy can prevent neuron death resulting from necrotic and apoptotic insults. J. Neurochem. 2003, 86:1079-1088.
    • (2003) J. Neurochem. , vol.86 , pp. 1079-1088
    • Lee, A.L.1    Dumas, T.C.2    Tarapore, P.E.3    Webster, B.R.4    Ho, D.Y.5    Kaufer, D.6    Sapolsky, R.M.7
  • 38
    • 0007572102 scopus 로고    scopus 로고
    • K+ efflux mediated by delayed rectifier K+ channels contributes of neuronal death
    • John Wiley & Sons, New York, K. Iqbal, D.F. Swaab, B. Winblad, H.M. Wisniewski (Eds.)
    • Yu S.P., Choi D.W. K+ efflux mediated by delayed rectifier K+ channels contributes of neuronal death. Alzheimer's disease and related disorders 1999, 371-382. John Wiley & Sons, New York. K. Iqbal, D.F. Swaab, B. Winblad, H.M. Wisniewski (Eds.).
    • (1999) Alzheimer's disease and related disorders , pp. 371-382
    • Yu, S.P.1    Choi, D.W.2
  • 40
    • 0032492407 scopus 로고    scopus 로고
    • Attenuated K+ channel gene transcription in primary pulmonary hypertension
    • Yuan X.J., Wang J., Juhaszova M., Gaine S.P., Rubin L.J. Attenuated K+ channel gene transcription in primary pulmonary hypertension. Lancet 1998, 351:726-727.
    • (1998) Lancet , vol.351 , pp. 726-727
    • Yuan, X.J.1    Wang, J.2    Juhaszova, M.3    Gaine, S.P.4    Rubin, L.J.5
  • 47
    • 0034118777 scopus 로고    scopus 로고
    • Suppression of the rat microglia Kv1.3 current by Src-family tyrosine kinases and oxygen/glucose deprivation
    • Cayabyab F.S., Khanna R., Jones O.T., Schlichter L.C. Suppression of the rat microglia Kv1.3 current by Src-family tyrosine kinases and oxygen/glucose deprivation. Eur. J. Neurosci. 2000, 12:1949-1960.
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 1949-1960
    • Cayabyab, F.S.1    Khanna, R.2    Jones, O.T.3    Schlichter, L.C.4
  • 50
    • 0346727499 scopus 로고    scopus 로고
    • Activation of K+ channels: an essential pathway in programmed cell death
    • Remillard C.V., Yuan J.X. Activation of K+ channels: an essential pathway in programmed cell death. Am. J. Physiol. Lung Cell Mol. Physiol. 2004, 286:L49-L67.
    • (2004) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.286
    • Remillard, C.V.1    Yuan, J.X.2
  • 53
    • 0042530130 scopus 로고    scopus 로고
    • Activity of potassium channel blockers in breast cancer
    • Abdul M., Santo A., Hoosein N. Activity of potassium channel blockers in breast cancer. Anticancer Res. 2003, 23:3347-3351.
    • (2003) Anticancer Res. , vol.23 , pp. 3347-3351
    • Abdul, M.1    Santo, A.2    Hoosein, N.3
  • 54
    • 70349564255 scopus 로고    scopus 로고
    • Kv1.3 voltage-gated K+ channel subunit as potential diagnostic marker and therapeutic target for breast cancer
    • Jang S.H., Kang K.S., Ryu P.D., Lee S.Y. Kv1.3 voltage-gated K+ channel subunit as potential diagnostic marker and therapeutic target for breast cancer. BMB Rep. 2009, 42:535-539.
    • (2009) BMB Rep. , vol.42 , pp. 535-539
    • Jang, S.H.1    Kang, K.S.2    Ryu, P.D.3    Lee, S.Y.4
  • 56
    • 34447130413 scopus 로고    scopus 로고
    • Reduced Kv 1.3 potassium channel expression in human prostate cancer
    • Abdul M., Hoosein N. Reduced Kv 1.3 potassium channel expression in human prostate cancer. J. Membr. Biol. 2006, 214:99-102.
    • (2006) J. Membr. Biol. , vol.214 , pp. 99-102
    • Abdul, M.1    Hoosein, N.2
  • 57
    • 0036725867 scopus 로고    scopus 로고
    • Voltage-gated potassium ion channels in colon cancer
    • Abdul M., Hoosein N. Voltage-gated potassium ion channels in colon cancer. Oncol. Rep. 2002, 9:961-964.
    • (2002) Oncol. Rep. , vol.9 , pp. 961-964
    • Abdul, M.1    Hoosein, N.2
  • 59
  • 60
    • 0021203354 scopus 로고
    • Voltage-gated potassium channels are required for human T lymphocyte activation
    • Chandy K.G., DeCoursey T.E., Cahalan M.D., McLaughlin C., Gupta S. Voltage-gated potassium channels are required for human T lymphocyte activation. J. Exp. Med. 1984, 160:369-385.
    • (1984) J. Exp. Med. , vol.160 , pp. 369-385
    • Chandy, K.G.1    DeCoursey, T.E.2    Cahalan, M.D.3    McLaughlin, C.4    Gupta, S.5
  • 63
    • 0029916913 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the Kv1.3 potassium channel
    • Holmes T.C., Fadool D.A., Levitan I.B. Tyrosine phosphorylation of the Kv1.3 potassium channel. J. Neurosci. 1996, 16:1581-1590.
    • (1996) J. Neurosci. , vol.16 , pp. 1581-1590
    • Holmes, T.C.1    Fadool, D.A.2    Levitan, I.B.3
  • 64
    • 0030832241 scopus 로고    scopus 로고
    • Ceramide-induced inhibition of T lymphocyte voltage-gated potassium channel is mediated by tyrosine kinases
    • Gulbins E., Szabò I., Baltzer K., Lang F. Ceramide-induced inhibition of T lymphocyte voltage-gated potassium channel is mediated by tyrosine kinases. Proc. Natl. Acad. Sci. USA 1997, 94:7661-7666.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7661-7666
    • Gulbins, E.1    Szabò, I.2    Baltzer, K.3    Lang, F.4
  • 66
    • 27844489501 scopus 로고    scopus 로고
    • Death or survival: membrane ceramide controls the fate and activation of antigen-specific T cells depending on signal strength and duration
    • Detre C., Kiss E., Varga Z., Ludanyi K., Paszty K., Enyedi A., Kovesdi D., Panyi G., Rajnavolgyi E., Matko J. Death or survival: membrane ceramide controls the fate and activation of antigen-specific T cells depending on signal strength and duration. Cell. Signal. 2006, 18:294-306.
    • (2006) Cell. Signal. , vol.18 , pp. 294-306
    • Detre, C.1    Kiss, E.2    Varga, Z.3    Ludanyi, K.4    Paszty, K.5    Enyedi, A.6    Kovesdi, D.7    Panyi, G.8    Rajnavolgyi, E.9    Matko, J.10
  • 67
    • 0027441927 scopus 로고
    • Heterologous expression of specific K+ channels in T lymphocytes: functional consequences for volume regulation
    • Deutsch C., Chen L.Q. Heterologous expression of specific K+ channels in T lymphocytes: functional consequences for volume regulation. Proc. Natl. Acad. Sci. USA 1993, 90:10036-10040.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10036-10040
    • Deutsch, C.1    Chen, L.Q.2
  • 69
    • 33746530063 scopus 로고    scopus 로고
    • Re-evaluation of the distinction between type I and type II cells: the necessary role of the mitochondria in both the extrinsic and intrinsic signaling pathways upon Fas receptor activation
    • Tafani M., Karpinich N.O., Serroni A., Russo M.A., Farber J.L. Re-evaluation of the distinction between type I and type II cells: the necessary role of the mitochondria in both the extrinsic and intrinsic signaling pathways upon Fas receptor activation. J. Cell. Physiol. 2006, 208:556-565.
    • (2006) J. Cell. Physiol. , vol.208 , pp. 556-565
    • Tafani, M.1    Karpinich, N.O.2    Serroni, A.3    Russo, M.A.4    Farber, J.L.5
  • 72
    • 74049131721 scopus 로고    scopus 로고
    • Potassium channels in brain mitochondria
    • Bednarczyk P. Potassium channels in brain mitochondria. Acta Biochim. Pol. 2009, 56:385-392.
    • (2009) Acta Biochim. Pol. , vol.56 , pp. 385-392
    • Bednarczyk, P.1
  • 73
    • 77952669421 scopus 로고    scopus 로고
    • Role of Kv1.3 mitochondrial potassium channel in apoptotic signalling in lymphocytes. BBA Bioenerg. (in press).
    • Gulbins, E., Sassi, N., Grassmè, H., Zoratti, M. and Szabò, I. (2009) Role of Kv1.3 mitochondrial potassium channel in apoptotic signalling in lymphocytes. BBA Bioenerg. (in press).
    • (2009)
    • Gulbins, E.1    Sassi, N.2    Grassmè, H.3    Zoratti, M.4    Szabò, I.5
  • 75
    • 33846002728 scopus 로고    scopus 로고
    • A mitochondria-K+-channel axis is suppressed in cancer and its normalization promotes apoptosis and inhibits cancer growth
    • Bonnet S., Archer S.L., Allalunis-Turner J., Haromy A., Beaulieu C., Thompson R., et al. A mitochondria-K+-channel axis is suppressed in cancer and its normalization promotes apoptosis and inhibits cancer growth. Cancer Cell 2006, 11:37-51.
    • (2006) Cancer Cell , vol.11 , pp. 37-51
    • Bonnet, S.1    Archer, S.L.2    Allalunis-Turner, J.3    Haromy, A.4    Beaulieu, C.5    Thompson, R.6
  • 76
  • 77
    • 26844554628 scopus 로고    scopus 로고
    • Mitochondrial ion channels: gatekeepers of life and death
    • O'Rourke B., Cortassa S., Aon M.A. Mitochondrial ion channels: gatekeepers of life and death. Physiology 2005, 20:303-315.
    • (2005) Physiology , vol.20 , pp. 303-315
    • O'Rourke, B.1    Cortassa, S.2    Aon, M.A.3
  • 78
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy M.P. How mitochondria produce reactive oxygen species. Biochem. J. 2009, 417:1-13.
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 79
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M., Szabò I. The mitochondrial permeability transition. Biochim. Biophys. Acta 1995, 1241:139-176.
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabò, I.2
  • 80
    • 0029863399 scopus 로고    scopus 로고
    • Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites
    • Costantini P., Chernyak B.V., Petronilli V., Bernardi P. Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites. J. Biol. Chem. 1996, 271:6746-6751.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6746-6751
    • Costantini, P.1    Chernyak, B.V.2    Petronilli, V.3    Bernardi, P.4
  • 82
    • 60249089101 scopus 로고    scopus 로고
    • Putative partners in Bax-mediated cytochrome c release: ANT, CypD, VSAC or none of them?
    • Kumarswamy A., Chandna S. Putative partners in Bax-mediated cytochrome c release: ANT, CypD, VSAC or none of them?. Mitochondrion 2009, 9:1-8.
    • (2009) Mitochondrion , vol.9 , pp. 1-8
    • Kumarswamy, A.1    Chandna, S.2
  • 83
    • 68949141833 scopus 로고    scopus 로고
    • Opening the doors to cytochrome c: changes in mitochondrial shape and apoptosis
    • Scorrano L. Opening the doors to cytochrome c: changes in mitochondrial shape and apoptosis. Int. J. Biochem. Cell Biol. 2009, 41:1875-1883.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1875-1883
    • Scorrano, L.1
  • 84
    • 34250789163 scopus 로고    scopus 로고
    • Role of cardiolipin in cytochrome c release from mitochondria
    • Ott M., Zhivotovsky B., Orrenius S. Role of cardiolipin in cytochrome c release from mitochondria. Cell Death Differ. 2007, 14:1243-1247.
    • (2007) Cell Death Differ. , vol.14 , pp. 1243-1247
    • Ott, M.1    Zhivotovsky, B.2    Orrenius, S.3
  • 86
    • 73649092745 scopus 로고    scopus 로고
    • Increased potassium conductance of brain mitochondria induces resistance to permeability transition by enhancing matrix volume
    • Hansson M.J., Morota S., Teilum M., Mattiasson G., Uchino H., Elmèr E. Increased potassium conductance of brain mitochondria induces resistance to permeability transition by enhancing matrix volume. J. Biol. Chem. 2010, 285:741-750.
    • (2010) J. Biol. Chem. , vol.285 , pp. 741-750
    • Hansson, M.J.1    Morota, S.2    Teilum, M.3    Mattiasson, G.4    Uchino, H.5    Elmèr, E.6
  • 87
    • 70350023058 scopus 로고    scopus 로고
    • Adenine nucleotide translocase: a component of the phylogenetically conserved death machinery
    • Zhivotovsky B., Galluzzi L., Kepp O., Kroemer G. Adenine nucleotide translocase: a component of the phylogenetically conserved death machinery. Cell Death Diff. 2009, 16:1419-1426.
    • (2009) Cell Death Diff. , vol.16 , pp. 1419-1426
    • Zhivotovsky, B.1    Galluzzi, L.2    Kepp, O.3    Kroemer, G.4
  • 88
    • 67649794783 scopus 로고    scopus 로고
    • New insights into mitochondrial structure during cell death
    • Perkins G., Bossy-Wetzel E., Ellisman M.H. New insights into mitochondrial structure during cell death. Exp. Neurol. 2009, 218:183-192.
    • (2009) Exp. Neurol. , vol.218 , pp. 183-192
    • Perkins, G.1    Bossy-Wetzel, E.2    Ellisman, M.H.3
  • 90
    • 0034525413 scopus 로고    scopus 로고
    • VDAC regulation by the Bcl-2 family of proteins
    • Tsujimoto Y., Shimizu S. VDAC regulation by the Bcl-2 family of proteins. Cell Death Differ. 2000, 7:1174-1181.
    • (2000) Cell Death Differ. , vol.7 , pp. 1174-1181
    • Tsujimoto, Y.1    Shimizu, S.2
  • 91
    • 33846207499 scopus 로고    scopus 로고
    • NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL
    • Malia T.J., Wagner G. NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL. Biochemistry 2007, 46:514-525.
    • (2007) Biochemistry , vol.46 , pp. 514-525
    • Malia, T.J.1    Wagner, G.2
  • 93
    • 67649813198 scopus 로고    scopus 로고
    • Molecular participants in mitochondrial cell death channel formation during neuronal ischemia
    • Jonas E.A. Molecular participants in mitochondrial cell death channel formation during neuronal ischemia. Exp. Neurol. 2009, 218:203-212.
    • (2009) Exp. Neurol. , vol.218 , pp. 203-212
    • Jonas, E.A.1
  • 96
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: channels, exchangers, and permeability transition
    • Bernardi P. Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol. Rev. 1999, 79:1127-1155.
    • (1999) Physiol. Rev. , vol.79 , pp. 1127-1155
    • Bernardi, P.1
  • 97
    • 0142011184 scopus 로고    scopus 로고
    • Mitochondrial potassium transport: the K+ cycle
    • Garlid K., Paucek P. Mitochondrial potassium transport: the K+ cycle. Biochim. Biophys. Acta 2003, 1606:23-41.
    • (2003) Biochim. Biophys. Acta , vol.1606 , pp. 23-41
    • Garlid, K.1    Paucek, P.2
  • 98
    • 67349113204 scopus 로고    scopus 로고
    • Pathophysiology of mitochondrial volume homeostasis: potassium transport and permeability transition
    • Nowikowsky K., Schweyen R.J., Bernardi P. Pathophysiology of mitochondrial volume homeostasis: potassium transport and permeability transition. Biochim. Biophys. Acta Bioenerg. 2009, 1787(2009):345-350.
    • (2009) Biochim. Biophys. Acta Bioenerg. , vol.1787 , Issue.2009 , pp. 345-350
    • Nowikowsky, K.1    Schweyen, R.J.2    Bernardi, P.3
  • 99
    • 0025913049 scopus 로고
    • ATP-sensitive K+ channel in the mitochondrial inner membrane
    • Inoue I., Nagase H., Kishi K., Higuti T. ATP-sensitive K+ channel in the mitochondrial inner membrane. Nature 1991, 352:244-247.
    • (1991) Nature , vol.352 , pp. 244-247
    • Inoue, I.1    Nagase, H.2    Kishi, K.3    Higuti, T.4
  • 100
    • 0033551036 scopus 로고    scopus 로고
    • Ca2+-activated K+ channel of the BK-type in the inner mitochondrial membrane of a human glioma cell line
    • Siemen D., Loupatatzis C., Borecky J., Gulbins E., Lang F. Ca2+-activated K+ channel of the BK-type in the inner mitochondrial membrane of a human glioma cell line. Biochem. Biophys. Res. Commun. 1999, 257:549-554.
    • (1999) Biochem. Biophys. Res. Commun. , vol.257 , pp. 549-554
    • Siemen, D.1    Loupatatzis, C.2    Borecky, J.3    Gulbins, E.4    Lang, F.5
  • 101
    • 66949116366 scopus 로고    scopus 로고
    • Intermediate conductance Ca2+-activated potassium channel (Kca3.1) in the inner mitochondrial membrane of human colon cancer cells
    • De Marchi U., Sassi N., Fioretti B., Catacuzzeno L., Cereghetti G.M., Szabò I., Zoratti M. Intermediate conductance Ca2+-activated potassium channel (Kca3.1) in the inner mitochondrial membrane of human colon cancer cells. Cell Calcium 2009, 45:509-516.
    • (2009) Cell Calcium , vol.45 , pp. 509-516
    • De Marchi, U.1    Sassi, N.2    Fioretti, B.3    Catacuzzeno, L.4    Cereghetti, G.M.5    Szabò, I.6    Zoratti, M.7
  • 103
    • 77953777012 scopus 로고    scopus 로고
    • An investigation of the occurrence and properties of the mitochondrial intermediate-conductance Ca2+-activated K+ channel mtKCa3.1. BBA Bioenerg., doi:10.1016/j.bbabio.2009.12.015
    • Sassi, N., De Marchi, U., Fioretti, B., Biasutto, L., Gulbins, E., Francolini, F., Szabò, I. and Zoratti, M. (2009) An investigation of the occurrence and properties of the mitochondrial intermediate-conductance Ca2+-activated K+ channel mtKCa3.1. BBA Bioenerg., doi:10.1016/j.bbabio.2009.12.015.
    • (2009)
    • Sassi, N.1    De Marchi, U.2    Fioretti, B.3    Biasutto, L.4    Gulbins, E.5    Francolini, F.6    Szabò, I.7    Zoratti, M.8
  • 104
    • 0038581115 scopus 로고    scopus 로고
    • Ceramide inhibits the potassium channel Kv1.3 by the formation of membrane platform
    • Bock J., Szabò I., Gamper N., Adams C., Gulbins E. Ceramide inhibits the potassium channel Kv1.3 by the formation of membrane platform. Biochem. Biophys. Res. Commun. 2003, 305:890-897.
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 890-897
    • Bock, J.1    Szabò, I.2    Gamper, N.3    Adams, C.4    Gulbins, E.5
  • 105
    • 0028125208 scopus 로고
    • Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation
    • Smart E.J., Ying Y.S., Conrad P.A., Anderson R.G. Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation. J. Cell Biol. 1994, 127:1185-1197.
    • (1994) J. Cell Biol. , vol.127 , pp. 1185-1197
    • Smart, E.J.1    Ying, Y.S.2    Conrad, P.A.3    Anderson, R.G.4
  • 106
    • 0029560256 scopus 로고
    • Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps
    • Conrad P.A., Smart E.J., Ying Y.S., Anderson R.G., Bloom G.S. Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps. J. Cell Biol. 1995, 131:1421-1433.
    • (1995) J. Cell Biol. , vol.131 , pp. 1421-1433
    • Conrad, P.A.1    Smart, E.J.2    Ying, Y.S.3    Anderson, R.G.4    Bloom, G.S.5
  • 107
    • 4544375506 scopus 로고    scopus 로고
    • Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic
    • Pelkmans L., Brli T., Zerial M., Helenius A. Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic. Cell 2004, 118:767-780.
    • (2004) Cell , vol.118 , pp. 767-780
    • Pelkmans, L.1    Brli, T.2    Zerial, M.3    Helenius, A.4
  • 108
    • 29144458927 scopus 로고    scopus 로고
    • Secrets of caveolae- and lipid raft-mediated endocytosis revealed by mammalian viruses
    • Pelkmans L. Secrets of caveolae- and lipid raft-mediated endocytosis revealed by mammalian viruses. Biochim. Biophys. Acta 2005, 1746:295-304.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 295-304
    • Pelkmans, L.1


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