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Volumn 1848, Issue 10, 2015, Pages 2532-2546

Ion channels in the regulation of apoptosis

Author keywords

Apoptosis; Calcium; Chloride; Ion channel; Potassium; Sodium

Indexed keywords

CALCIUM; CALCIUM CHANNEL; CARRIER PROTEIN; CHLORIDE; CHLORIDE CHANNEL; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; ION CHANNEL; MITOCHONDRIAL CALCIUM UNIPORTER; POTASSIUM; POTASSIUM CHANNEL; RYANODINE RECEPTOR; STORE OPERATED CALCIUM CHANNEL; TRANSIENT RECEPTOR POTENTIAL CHANNEL; UNCLASSIFIED DRUG; VOLTAGE DEPENDENT ANION CHANNEL; VOLTAGE GATED CALCIUM CHANNEL; SODIUM;

EID: 84941142074     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2014.10.030     Document Type: Review
Times cited : (156)

References (275)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • J.F. Kerr, A.H. Wyllie, and A.R. Currie Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics Br. J. Cancer 26 1972 239 257
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 2
    • 84877582384 scopus 로고    scopus 로고
    • Shaping organisms with apoptosis
    • M. Suzanne, and H. Steller Shaping organisms with apoptosis Cell Death Differ. 20 2013 669 675
    • (2013) Cell Death Differ. , vol.20 , pp. 669-675
    • Suzanne, M.1    Steller, H.2
  • 3
    • 0034641936 scopus 로고    scopus 로고
    • Apoptosis in the nervous system
    • J. Yuan, and B.A. Yankner Apoptosis in the nervous system Nature 407 2000 802 809
    • (2000) Nature , vol.407 , pp. 802-809
    • Yuan, J.1    Yankner, B.A.2
  • 4
    • 79951828231 scopus 로고    scopus 로고
    • Interdigital cell death function and regulation: New insights on an old programmed cell death model
    • R. Hernandez-Martinez, and L. Covarrubias Interdigital cell death function and regulation: new insights on an old programmed cell death model Dev. Growth Differ. 53 2011 245 258
    • (2011) Dev. Growth Differ. , vol.53 , pp. 245-258
    • Hernandez-Martinez, R.1    Covarrubias, L.2
  • 6
    • 0344198588 scopus 로고    scopus 로고
    • Shutdown of an acute T cell immune response to viral infection is mediated by the proapoptotic Bcl-2 homology 3-only protein Bim
    • M. Pellegrini, G. Belz, P. Bouillet, and A. Strasser Shutdown of an acute T cell immune response to viral infection is mediated by the proapoptotic Bcl-2 homology 3-only protein Bim Proc. Natl. Acad. Sci. U. S. A. 100 2003 14175 14180
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 14175-14180
    • Pellegrini, M.1    Belz, G.2    Bouillet, P.3    Strasser, A.4
  • 7
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • C.B. Thompson Apoptosis in the pathogenesis and treatment of disease Science 267 1995 1456 1462
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 8
    • 67649595826 scopus 로고    scopus 로고
    • Apoptosis and cancer: The genesis of a research field
    • T.G. Cotter Apoptosis and cancer: the genesis of a research field Nat. Rev. Cancer 9 2009 501 507
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 501-507
    • Cotter, T.G.1
  • 9
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • D. Hanahan, and R.A. Weinberg Hallmarks of cancer: the next generation Cell 144 2011 646 674
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 10
    • 84885355413 scopus 로고    scopus 로고
    • Targeting apoptosis by the remodelling of calcium-transporting proteins in cancerogenesis
    • C. Dubois, F. Vanden Abeele, and N. Prevarskaya Targeting apoptosis by the remodelling of calcium-transporting proteins in cancerogenesis FEBS J. 280 2013 5500 5510
    • (2013) FEBS J. , vol.280 , pp. 5500-5510
    • Dubois, C.1    Vanden Abeele, F.2    Prevarskaya, N.3
  • 11
    • 84923226555 scopus 로고    scopus 로고
    • Targeting apoptosis for anticancer therapy
    • S. Fulda Targeting apoptosis for anticancer therapy Semin. Cancer Biol. 2014
    • (2014) Semin. Cancer Biol.
    • Fulda, S.1
  • 13
    • 0036399360 scopus 로고    scopus 로고
    • Molecular interplay between ion channels and the regulation of apoptosis
    • M.A. Razik, and J.A. Cidlowski Molecular interplay between ion channels and the regulation of apoptosis Biol. Res. 35 2002 203 207
    • (2002) Biol. Res. , vol.35 , pp. 203-207
    • Razik, M.A.1    Cidlowski, J.A.2
  • 17
    • 34250308322 scopus 로고    scopus 로고
    • Apoptosis: A review of programmed cell death
    • S. Elmore Apoptosis: a review of programmed cell death Toxicol. Pathol. 35 2007 495 516
    • (2007) Toxicol. Pathol. , vol.35 , pp. 495-516
    • Elmore, S.1
  • 19
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • M.O. Hengartner The biochemistry of apoptosis Nature 407 2000 770 776
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 21
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: Outer membrane permeabilization and beyond
    • S.W. Tait, and D.R. Green Mitochondria and cell death: outer membrane permeabilization and beyond Nat. Rev. Mol. Cell Biol. 11 2010 621 632
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 22
    • 33746912767 scopus 로고    scopus 로고
    • The permeability transition pore complex in cancer cell death
    • C. Brenner, and S. Grimm The permeability transition pore complex in cancer cell death Oncogene 25 2006 4744 4756
    • (2006) Oncogene , vol.25 , pp. 4744-4756
    • Brenner, C.1    Grimm, S.2
  • 23
    • 84900395214 scopus 로고    scopus 로고
    • Mitochondrial channels: Ion fluxes and more
    • I. Szabo, and M. Zoratti Mitochondrial channels: ion fluxes and more Physiol. Rev. 94 2014 519 608
    • (2014) Physiol. Rev. , vol.94 , pp. 519-608
    • Szabo, I.1    Zoratti, M.2
  • 24
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • G. Kroemer, L. Galluzzi, and C. Brenner Mitochondrial membrane permeabilization in cell death Physiol. Rev. 87 2007 99 163
    • (2007) Physiol. Rev. , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 25
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • P. Li, D. Nijhawan, I. Budihardjo, S.M. Srinivasula, M. Ahmad, E.S. Alnemri, and X. Wang Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade Cell 91 1997 479 489
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 26
    • 0034710649 scopus 로고    scopus 로고
    • Structural and biochemical basis of apoptotic activation by Smac/DIABLO
    • J. Chai, C. Du, J.W. Wu, S. Kyin, X. Wang, and Y. Shi Structural and biochemical basis of apoptotic activation by Smac/DIABLO Nature 406 2000 855 862
    • (2000) Nature , vol.406 , pp. 855-862
    • Chai, J.1    Du, C.2    Wu, J.W.3    Kyin, S.4    Wang, X.5    Shi, Y.6
  • 30
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • L.Y. Li, X. Luo, and X. Wang Endonuclease G is an apoptotic DNase when released from mitochondria Nature 412 2001 95 99
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 31
    • 0037204952 scopus 로고    scopus 로고
    • The Fas signaling pathway: More than a paradigm
    • H. Wajant The Fas signaling pathway: more than a paradigm Science 296 2002 1635 1636
    • (2002) Science , vol.296 , pp. 1635-1636
    • Wajant, H.1
  • 32
    • 0035399893 scopus 로고    scopus 로고
    • Biochemistry and function of the DISC
    • H. Walczak, and M.R. Sprick Biochemistry and function of the DISC Trends Biochem. Sci. 26 2001 452 453
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 452-453
    • Walczak, H.1    Sprick, M.R.2
  • 33
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • H. Li, H. Zhu, C.J. Xu, and J. Yuan Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis Cell 94 1998 491 501
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 34
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • X. Luo, I. Budihardjo, H. Zou, C. Slaughter, and X. Wang Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors Cell 94 1998 481 490
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 35
    • 79251468749 scopus 로고    scopus 로고
    • Dependence receptors: From basic research to drug development
    • P. Mehlen, and D.E. Bredesen Dependence receptors: from basic research to drug development Sci. Signal. 4 2011 mr2
    • (2011) Sci. Signal. , vol.4 , pp. mr2
    • Mehlen, P.1    Bredesen, D.E.2
  • 38
    • 54949110895 scopus 로고    scopus 로고
    • Calcium and apoptosis: ER-mitochondria Ca2 + transfer in the control of apoptosis
    • P. Pinton, C. Giorgi, R. Siviero, E. Zecchini, and R. Rizzuto Calcium and apoptosis: ER-mitochondria Ca2 + transfer in the control of apoptosis Oncogene 27 2008 6407 6418
    • (2008) Oncogene , vol.27 , pp. 6407-6418
    • Pinton, P.1    Giorgi, C.2    Siviero, R.3    Zecchini, E.4    Rizzuto, R.5
  • 40
    • 33750523442 scopus 로고    scopus 로고
    • Mitochondrial calcium signalling and cell death: Approaches for assessing the role of mitochondrial Ca2 + uptake in apoptosis
    • G. Hajnoczky, G. Csordas, S. Das, C. Garcia-Perez, M. Saotome, S. Sinha Roy, and M. Yi Mitochondrial calcium signalling and cell death: approaches for assessing the role of mitochondrial Ca2 + uptake in apoptosis Cell Calcium 40 2006 553 560
    • (2006) Cell Calcium , vol.40 , pp. 553-560
    • Hajnoczky, G.1    Csordas, G.2    Das, S.3    Garcia-Perez, C.4    Saotome, M.5    Sinha Roy, S.6    Yi, M.7
  • 41
    • 0035903235 scopus 로고    scopus 로고
    • Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion
    • M. Chen, H. He, S. Zhan, S. Krajewski, J.C. Reed, and R.A. Gottlieb Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion J. Biol. Chem. 276 2001 30724 30728
    • (2001) J. Biol. Chem. , vol.276 , pp. 30724-30728
    • Chen, M.1    He, H.2    Zhan, S.3    Krajewski, S.4    Reed, J.C.5    Gottlieb, R.A.6
  • 44
    • 0037072937 scopus 로고    scopus 로고
    • An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12
    • N. Morishima, K. Nakanishi, H. Takenouchi, T. Shibata, and Y. Yasuhiko An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12 J. Biol. Chem. 277 2002 34287 34294
    • (2002) J. Biol. Chem. , vol.277 , pp. 34287-34294
    • Morishima, N.1    Nakanishi, K.2    Takenouchi, H.3    Shibata, T.4    Yasuhiko, Y.5
  • 45
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • T. Nakagawa, H. Zhu, N. Morishima, E. Li, J. Xu, B.A. Yankner, and J. Yuan Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta Nature 403 2000 98 103
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 46
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • T. Nakagawa, and J. Yuan Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis J. Cell Biol. 150 2000 887 894
    • (2000) J. Cell Biol. , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 50
    • 84863206432 scopus 로고    scopus 로고
    • The permeability transition pore as a Ca(2 +) release channel: New answers to an old question
    • P. Bernardi, and S. von Stockum The permeability transition pore as a Ca(2 +) release channel: new answers to an old question Cell Calcium 52 2012 22 27
    • (2012) Cell Calcium , vol.52 , pp. 22-27
    • Bernardi, P.1    Von Stockum, S.2
  • 52
    • 34248584090 scopus 로고    scopus 로고
    • Inositol trisphosphate receptor Ca2 + release channels
    • J.K. Foskett, C. White, K.H. Cheung, and D.O. Mak Inositol trisphosphate receptor Ca2 + release channels Physiol. Rev. 87 2007 593 658
    • (2007) Physiol. Rev. , vol.87 , pp. 593-658
    • Foskett, J.K.1    White, C.2    Cheung, K.H.3    Mak, D.O.4
  • 53
    • 34247480926 scopus 로고    scopus 로고
    • IP3 receptors in cell survival and apoptosis: Ca2 + release and beyond
    • S.K. Joseph, and G. Hajnoczky IP3 receptors in cell survival and apoptosis: Ca2 + release and beyond Apoptosis 12 2007 951 968
    • (2007) Apoptosis , vol.12 , pp. 951-968
    • Joseph, S.K.1    Hajnoczky, G.2
  • 55
    • 0030973158 scopus 로고    scopus 로고
    • T cells deficient in inositol 1,4,5-trisphosphate receptor are resistant to apoptosis
    • T. Jayaraman, and A.R. Marks T cells deficient in inositol 1,4,5-trisphosphate receptor are resistant to apoptosis Mol. Cell. Biol. 17 1997 3005 3012
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3005-3012
    • Jayaraman, T.1    Marks, A.R.2
  • 58
    • 0025273937 scopus 로고
    • Phospholipid synthesis in a membrane fraction associated with mitochondria
    • J.E. Vance Phospholipid synthesis in a membrane fraction associated with mitochondria J. Biol. Chem. 265 1990 7248 7256
    • (1990) J. Biol. Chem. , vol.265 , pp. 7248-7256
    • Vance, J.E.1
  • 60
    • 0027340729 scopus 로고
    • Microdomains with high Ca2 + close to IP3-sensitive channels that are sensed by neighboring mitochondria
    • R. Rizzuto, M. Brini, M. Murgia, and T. Pozzan Microdomains with high Ca2 + close to IP3-sensitive channels that are sensed by neighboring mitochondria Science 262 1993 744 747
    • (1993) Science , vol.262 , pp. 744-747
    • Rizzuto, R.1    Brini, M.2    Murgia, M.3    Pozzan, T.4
  • 62
    • 84876587328 scopus 로고    scopus 로고
    • Fragmented inositol 1,4,5-trisphosphate receptors retain tetrameric architecture and form functional Ca2 + release channels
    • K.J. Alzayady, R. Chandrasekhar, and D.I. Yule Fragmented inositol 1,4,5-trisphosphate receptors retain tetrameric architecture and form functional Ca2 + release channels J. Biol. Chem. 288 2013 11122 11134
    • (2013) J. Biol. Chem. , vol.288 , pp. 11122-11134
    • Alzayady, K.J.1    Chandrasekhar, R.2    Yule, D.I.3
  • 63
    • 0033607673 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptor type 1 is a substrate for caspase-3 and is cleaved during apoptosis in a caspase-3-dependent manner
    • J. Hirota, T. Furuichi, and K. Mikoshiba Inositol 1,4,5-trisphosphate receptor type 1 is a substrate for caspase-3 and is cleaved during apoptosis in a caspase-3-dependent manner J. Biol. Chem. 274 1999 34433 34437
    • (1999) J. Biol. Chem. , vol.274 , pp. 34433-34437
    • Hirota, J.1    Furuichi, T.2    Mikoshiba, K.3
  • 64
    • 80053925001 scopus 로고    scopus 로고
    • Calpain-cleaved type 1 inositol 1,4,5-trisphosphate receptor (InsP(3)R1) has InsP(3)-independent gating and disrupts intracellular Ca(2 +) homeostasis
    • C.M. Kopil, H. Vais, K.H. Cheung, A.P. Siebert, D.O. Mak, J.K. Foskett, and R.W. Neumar Calpain-cleaved type 1 inositol 1,4,5-trisphosphate receptor (InsP(3)R1) has InsP(3)-independent gating and disrupts intracellular Ca(2 +) homeostasis J. Biol. Chem. 286 2011 35998 36010
    • (2011) J. Biol. Chem. , vol.286 , pp. 35998-36010
    • Kopil, C.M.1    Vais, H.2    Cheung, K.H.3    Siebert, A.P.4    Mak, D.O.5    Foskett, J.K.6    Neumar, R.W.7
  • 65
    • 30344453043 scopus 로고    scopus 로고
    • Uncoupled IP3 receptor can function as a Ca2 +-leak channel: Cell biological and pathological consequences
    • K. Szlufcik, L. Missiaen, J.B. Parys, G. Callewaert, and H. De Smedt Uncoupled IP3 receptor can function as a Ca2 +-leak channel: cell biological and pathological consequences Biol. Cell 98 2006 1 14
    • (2006) Biol. Cell , vol.98 , pp. 1-14
    • Szlufcik, K.1    Missiaen, L.2    Parys, J.B.3    Callewaert, G.4    De Smedt, H.5
  • 66
    • 0344825875 scopus 로고    scopus 로고
    • Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis
    • D. Boehning, R.L. Patterson, L. Sedaghat, N.O. Glebova, T. Kurosaki, and S.H. Snyder Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis Nat. Cell Biol. 5 2003 1051 1061
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1051-1061
    • Boehning, D.1    Patterson, R.L.2    Sedaghat, L.3    Glebova, N.O.4    Kurosaki, T.5    Snyder, S.H.6
  • 67
    • 84872528492 scopus 로고    scopus 로고
    • Altered Ca(2 +) signaling in cancer cells: Proto-oncogenes and tumor suppressors targeting IP3 receptors
    • H. Akl, and G. Bultynck Altered Ca(2 +) signaling in cancer cells: proto-oncogenes and tumor suppressors targeting IP3 receptors Biochim. Biophys. Acta 1835 2013 180 193
    • (2013) Biochim. Biophys. Acta , vol.1835 , pp. 180-193
    • Akl, H.1    Bultynck, G.2
  • 69
    • 84887589243 scopus 로고    scopus 로고
    • Identification of PTEN at the ER and MAMs and its regulation of Ca(2 +) signaling and apoptosis in a protein phosphatase-dependent manner
    • A. Bononi, M. Bonora, S. Marchi, S. Missiroli, F. Poletti, C. Giorgi, P.P. Pandolfi, and P. Pinton Identification of PTEN at the ER and MAMs and its regulation of Ca(2 +) signaling and apoptosis in a protein phosphatase-dependent manner Cell Death Differ. 20 2013 1631 1643
    • (2013) Cell Death Differ. , vol.20 , pp. 1631-1643
    • Bononi, A.1    Bonora, M.2    Marchi, S.3    Missiroli, S.4    Poletti, F.5    Giorgi, C.6    Pandolfi, P.P.7    Pinton, P.8
  • 73
    • 20044391606 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate (IP3) receptor type1 (IP3R1) modulates the acquisition of cisplatin resistance in bladder cancer cell lines
    • T. Tsunoda, H. Koga, A. Yokomizo, K. Tatsugami, M. Eto, J. Inokuchi, A. Hirata, K. Masuda, K. Okumura, and S. Naito Inositol 1,4,5-trisphosphate (IP3) receptor type1 (IP3R1) modulates the acquisition of cisplatin resistance in bladder cancer cell lines Oncogene 24 2005 1396 1402
    • (2005) Oncogene , vol.24 , pp. 1396-1402
    • Tsunoda, T.1    Koga, H.2    Yokomizo, A.3    Tatsugami, K.4    Eto, M.5    Inokuchi, J.6    Hirata, A.7    Masuda, K.8    Okumura, K.9    Naito, S.10
  • 74
    • 84867271703 scopus 로고    scopus 로고
    • Coupling of ryanodine receptor 2 and voltage-dependent anion channel 2 is essential for Ca(2)+ transfer from the sarcoplasmic reticulum to the mitochondria in the heart
    • C.K. Min, D.R. Yeom, K.E. Lee, H.K. Kwon, M. Kang, Y.S. Kim, Z.Y. Park, H. Jeon, and H. Kim do Coupling of ryanodine receptor 2 and voltage-dependent anion channel 2 is essential for Ca(2)+ transfer from the sarcoplasmic reticulum to the mitochondria in the heart Biochem. J. 447 2012 371 379
    • (2012) Biochem. J. , vol.447 , pp. 371-379
    • Min, C.K.1    Yeom, D.R.2    Lee, K.E.3    Kwon, H.K.4    Kang, M.5    Kim, Y.S.6    Park, Z.Y.7    Jeon, H.8    Kim do, H.9
  • 75
    • 0034525627 scopus 로고    scopus 로고
    • Control of apoptosis by IP(3) and ryanodine receptor driven calcium signals
    • G. Hajnoczky, G. Csordas, M. Madesh, and P. Pacher Control of apoptosis by IP(3) and ryanodine receptor driven calcium signals Cell Calcium 28 2000 349 363
    • (2000) Cell Calcium , vol.28 , pp. 349-363
    • Hajnoczky, G.1    Csordas, G.2    Madesh, M.3    Pacher, P.4
  • 76
    • 0036877961 scopus 로고    scopus 로고
    • Old players in a new role: Mitochondria-associated membranes, VDAC, and ryanodine receptors as contributors to calcium signal propagation from endoplasmic reticulum to the mitochondria
    • G. Hajnoczky, G. Csordas, and M. Yi Old players in a new role: mitochondria-associated membranes, VDAC, and ryanodine receptors as contributors to calcium signal propagation from endoplasmic reticulum to the mitochondria Cell Calcium 32 2002 363 377
    • (2002) Cell Calcium , vol.32 , pp. 363-377
    • Hajnoczky, G.1    Csordas, G.2    Yi, M.3
  • 77
    • 0037199911 scopus 로고    scopus 로고
    • Tumor necrosis factor induces apoptosis in hepatoma cells by increasing Ca(2 +) release from the endoplasmic reticulum and suppressing Bcl-2 expression
    • B.C. Kim, H.T. Kim, M. Mamura, I.S. Ambudkar, K.S. Choi, and S.J. Kim Tumor necrosis factor induces apoptosis in hepatoma cells by increasing Ca(2 +) release from the endoplasmic reticulum and suppressing Bcl-2 expression J. Biol. Chem. 277 2002 31381 31389
    • (2002) J. Biol. Chem. , vol.277 , pp. 31381-31389
    • Kim, B.C.1    Kim, H.T.2    Mamura, M.3    Ambudkar, I.S.4    Choi, K.S.5    Kim, S.J.6
  • 79
    • 70349829186 scopus 로고    scopus 로고
    • Endoplasmic reticulum Ca(2 +) release through ryanodine and IP(3) receptors contributes to neuronal excitotoxicity
    • A. Ruiz, C. Matute, and E. Alberdi Endoplasmic reticulum Ca(2 +) release through ryanodine and IP(3) receptors contributes to neuronal excitotoxicity Cell Calcium 46 2009 273 281
    • (2009) Cell Calcium , vol.46 , pp. 273-281
    • Ruiz, A.1    Matute, C.2    Alberdi, E.3
  • 82
    • 80051936634 scopus 로고    scopus 로고
    • A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
    • D. De Stefani, A. Raffaello, E. Teardo, I. Szabo, and R. Rizzuto A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter Nature 476 2011 336 340
    • (2011) Nature , vol.476 , pp. 336-340
    • De Stefani, D.1    Raffaello, A.2    Teardo, E.3    Szabo, I.4    Rizzuto, R.5
  • 84
    • 84880471564 scopus 로고    scopus 로고
    • Mitochondrial calcium uniporter silencing potentiates caspase-independent cell death in MDA-MB-231 breast cancer cells
    • M.C. Curry, A.A. Peters, P.A. Kenny, S.J. Roberts-Thomson, and G.R. Monteith Mitochondrial calcium uniporter silencing potentiates caspase-independent cell death in MDA-MB-231 breast cancer cells Biochem. Biophys. Res. Commun. 434 2013 695 700
    • (2013) Biochem. Biophys. Res. Commun. , vol.434 , pp. 695-700
    • Curry, M.C.1    Peters, A.A.2    Kenny, P.A.3    Roberts-Thomson, S.J.4    Monteith, G.R.5
  • 86
    • 84893355839 scopus 로고    scopus 로고
    • Life without the mitochondrial calcium uniporter
    • S. Herzig, K. Maundrell, and J.C. Martinou Life without the mitochondrial calcium uniporter Nat. Cell Biol. 15 2013 1398 1400
    • (2013) Nat. Cell Biol. , vol.15 , pp. 1398-1400
    • Herzig, S.1    Maundrell, K.2    Martinou, J.C.3
  • 88
    • 84897967621 scopus 로고    scopus 로고
    • Molecular mechanisms of cell death: Central implication of ATP synthase in mitochondrial permeability transition
    • M. Bonora, M.R. Wieckowski, C. Chinopoulos, O. Kepp, G. Kroemer, L. Galluzzi, and P. Pinton Molecular mechanisms of cell death: central implication of ATP synthase in mitochondrial permeability transition Oncogene 0 2014
    • (2014) Oncogene
    • Bonora, M.1    Wieckowski, M.R.2    Chinopoulos, C.3    Kepp, O.4    Kroemer, G.5    Galluzzi, L.6    Pinton, P.7
  • 90
    • 0942297436 scopus 로고    scopus 로고
    • The voltage-dependent anion channel: Characterization, modulation, and role in mitochondrial function in cell life and death
    • V. Shoshan-Barmatz, and D. Gincel The voltage-dependent anion channel: characterization, modulation, and role in mitochondrial function in cell life and death Cell Biochem. Biophys. 39 2003 279 292
    • (2003) Cell Biochem. Biophys. , vol.39 , pp. 279-292
    • Shoshan-Barmatz, V.1    Gincel, D.2
  • 91
    • 1442327526 scopus 로고    scopus 로고
    • Essential role of the voltage-dependent anion channel (VDAC) in mitochondrial permeability transition pore opening and cytochrome c release induced by arsenic trioxide
    • Y. Zheng, Y. Shi, C. Tian, C. Jiang, H. Jin, J. Chen, A. Almasan, H. Tang, and Q. Chen Essential role of the voltage-dependent anion channel (VDAC) in mitochondrial permeability transition pore opening and cytochrome c release induced by arsenic trioxide Oncogene 23 2004 1239 1247
    • (2004) Oncogene , vol.23 , pp. 1239-1247
    • Zheng, Y.1    Shi, Y.2    Tian, C.3    Jiang, C.4    Jin, H.5    Chen, J.6    Almasan, A.7    Tang, H.8    Chen, Q.9
  • 92
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death
    • C.P. Baines, R.A. Kaiser, T. Sheiko, W.J. Craigen, and J.D. Molkentin Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death Nat. Cell Biol. 9 2007 550 555
    • (2007) Nat. Cell Biol. , vol.9 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 93
    • 52449104836 scopus 로고    scopus 로고
    • VDAC regulation: Role of cytosolic proteins and mitochondrial lipids
    • T.K. Rostovtseva, and S.M. Bezrukov VDAC regulation: role of cytosolic proteins and mitochondrial lipids J. Bioenerg. Biomembr. 40 2008 163 170
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 163-170
    • Rostovtseva, T.K.1    Bezrukov, S.M.2
  • 96
    • 34948846577 scopus 로고    scopus 로고
    • VDAC closure increases calcium ion flux
    • W. Tan, and M. Colombini VDAC closure increases calcium ion flux Biochim. Biophys. Acta 1768 2007 2510 2515
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2510-2515
    • Tan, W.1    Colombini, M.2
  • 103
    • 27144515996 scopus 로고    scopus 로고
    • STIM1 is a Ca2 + sensor that activates CRAC channels and migrates from the Ca2 + store to the plasma membrane
    • S.L. Zhang, Y. Yu, J. Roos, J.A. Kozak, T.J. Deerinck, M.H. Ellisman, K.A. Stauderman, and M.D. Cahalan STIM1 is a Ca2 + sensor that activates CRAC channels and migrates from the Ca2 + store to the plasma membrane Nature 437 2005 902 905
    • (2005) Nature , vol.437 , pp. 902-905
    • Zhang, S.L.1    Yu, Y.2    Roos, J.3    Kozak, J.A.4    Deerinck, T.J.5    Ellisman, M.H.6    Stauderman, K.A.7    Cahalan, M.D.8
  • 104
    • 15544368216 scopus 로고    scopus 로고
    • Store-operated calcium channels
    • A.B. Parekh, and J.W. Putney Jr. Store-operated calcium channels Physiol. Rev. 85 2005 757 810
    • (2005) Physiol. Rev. , vol.85 , pp. 757-810
    • Parekh, A.B.1    Putney, J.W.2
  • 105
    • 84873900703 scopus 로고    scopus 로고
    • Targeting Ca(2)(+) transport in cancer: Close reality or long perspective?
    • N. Prevarskaya, R. Skryma, and Y. Shuba Targeting Ca(2)(+) transport in cancer: close reality or long perspective? Expert Opin. Ther. Targets 17 2013 225 241
    • (2013) Expert Opin. Ther. Targets , vol.17 , pp. 225-241
    • Prevarskaya, N.1    Skryma, R.2    Shuba, Y.3
  • 110
    • 84885854516 scopus 로고    scopus 로고
    • The apoptosis of non-small cell lung cancer induced by cisplatin through modulation of STIM1
    • W. Li, M. Zhang, L. Xu, D. Lin, S. Cai, and F. Zou The apoptosis of non-small cell lung cancer induced by cisplatin through modulation of STIM1 Exp. Toxicol. Pathol. 65 2013 1073 1081
    • (2013) Exp. Toxicol. Pathol. , vol.65 , pp. 1073-1081
    • Li, W.1    Zhang, M.2    Xu, L.3    Lin, D.4    Cai, S.5    Zou, F.6
  • 111
    • 80053919268 scopus 로고    scopus 로고
    • Calcium entry via ORAI1 regulates glioblastoma cell proliferation and apoptosis
    • H. Liu, J.D. Hughes, S. Rollins, B. Chen, and E. Perkins Calcium entry via ORAI1 regulates glioblastoma cell proliferation and apoptosis Exp. Mol. Pathol. 91 2011 753 760
    • (2011) Exp. Mol. Pathol. , vol.91 , pp. 753-760
    • Liu, H.1    Hughes, J.D.2    Rollins, S.3    Chen, B.4    Perkins, E.5
  • 113
    • 84905055572 scopus 로고    scopus 로고
    • Enhanced Orai1 and STIM1 expression as well as store operated Ca2 + entry in therapy resistant ovary carcinoma cells
    • S. Schmidt, G. Liu, W. Yang, S. Honisch, S. Pantelakos, C. Stournaras, A. Honig, and F. Lang Enhanced Orai1 and STIM1 expression as well as store operated Ca2 + entry in therapy resistant ovary carcinoma cells Oncotarget 5 2014 4799 4810
    • (2014) Oncotarget , vol.5 , pp. 4799-4810
    • Schmidt, S.1    Liu, G.2    Yang, W.3    Honisch, S.4    Pantelakos, S.5    Stournaras, C.6    Honig, A.7    Lang, F.8
  • 114
    • 34347342283 scopus 로고    scopus 로고
    • Calcium inhibition and calcium potentiation of Orai1, Orai2, and Orai3 calcium release-activated calcium channels
    • W.I. DeHaven, J.T. Smyth, R.R. Boyles, and J.W. Putney Jr. Calcium inhibition and calcium potentiation of Orai1, Orai2, and Orai3 calcium release-activated calcium channels J. Biol. Chem. 282 2007 17548 17556
    • (2007) J. Biol. Chem. , vol.282 , pp. 17548-17556
    • DeHaven, W.I.1    Smyth, J.T.2    Boyles, R.R.3    Putney, J.W.4
  • 115
    • 84880743513 scopus 로고    scopus 로고
    • The neglected CRAC proteins: Orai2, Orai3, and STIM2
    • M. Hoth, and B.A. Niemeyer The neglected CRAC proteins: Orai2, Orai3, and STIM2 Curr. Top. Membr. 71 2013 237 271
    • (2013) Curr. Top. Membr. , vol.71 , pp. 237-271
    • Hoth, M.1    Niemeyer, B.A.2
  • 116
    • 34547521545 scopus 로고    scopus 로고
    • TRP channels in disease
    • B. Nilius TRP channels in disease Biochim. Biophys. Acta 1772 2007 805 812
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 805-812
    • Nilius, B.1
  • 117
    • 80052338518 scopus 로고    scopus 로고
    • TRP channels in cell survival and cell death in normal and transformed cells
    • G. Shapovalov, V. Lehen'kyi, R. Skryma, and N. Prevarskaya TRP channels in cell survival and cell death in normal and transformed cells Cell Calcium 50 2011 295 302
    • (2011) Cell Calcium , vol.50 , pp. 295-302
    • Shapovalov, G.1    Lehen'kyi, V.2    Skryma, R.3    Prevarskaya, N.4
  • 119
    • 77951893358 scopus 로고    scopus 로고
    • Transient receptor potential melastatin 2 is required for lipopolysaccharide-induced cytokine production in human monocytes
    • J. Wehrhahn, R. Kraft, C. Harteneck, and S. Hauschildt Transient receptor potential melastatin 2 is required for lipopolysaccharide-induced cytokine production in human monocytes J. Immunol. 184 2010 2386 2393
    • (2010) J. Immunol. , vol.184 , pp. 2386-2393
    • Wehrhahn, J.1    Kraft, R.2    Harteneck, C.3    Hauschildt, S.4
  • 122
    • 55549140796 scopus 로고    scopus 로고
    • Identification of novel sense and antisense transcription at the TRPM2 locus in cancer
    • U. Orfanelli, A.K. Wenke, C. Doglioni, V. Russo, A.K. Bosserhoff, and G. Lavorgna Identification of novel sense and antisense transcription at the TRPM2 locus in cancer Cell Res. 18 2008 1128 1140
    • (2008) Cell Res. , vol.18 , pp. 1128-1140
    • Orfanelli, U.1    Wenke, A.K.2    Doglioni, C.3    Russo, V.4    Bosserhoff, A.K.5    Lavorgna, G.6
  • 123
    • 0035131504 scopus 로고    scopus 로고
    • TRP-PLIK, a bifunctional protein with kinase and ion channel activities
    • L.W. Runnels, L. Yue, and D.E. Clapham TRP-PLIK, a bifunctional protein with kinase and ion channel activities Science 291 2001 1043 1047
    • (2001) Science , vol.291 , pp. 1043-1047
    • Runnels, L.W.1    Yue, L.2    Clapham, D.E.3
  • 125
    • 84867934428 scopus 로고    scopus 로고
    • Retrovirus-mediated siRNA targeting TRPM7 gene induces apoptosis in RBL-2H3 cells
    • N.M. Ng, S.P. Jiang, and Z.Q. Lv Retrovirus-mediated siRNA targeting TRPM7 gene induces apoptosis in RBL-2H3 cells Eur. Rev. Med. Pharmacol. Sci. 16 2012 1172 1178
    • (2012) Eur. Rev. Med. Pharmacol. Sci. , vol.16 , pp. 1172-1178
    • Ng, N.M.1    Jiang, S.P.2    Lv, Z.Q.3
  • 126
    • 35748972654 scopus 로고    scopus 로고
    • Functional transient receptor potential melastatin 7 channels are critical for human mast cell survival
    • R.C. Wykes, M. Lee, S.M. Duffy, W. Yang, E.P. Seward, and P. Bradding Functional transient receptor potential melastatin 7 channels are critical for human mast cell survival J. Immunol. 179 2007 4045 4052
    • (2007) J. Immunol. , vol.179 , pp. 4045-4052
    • Wykes, R.C.1    Lee, M.2    Duffy, S.M.3    Yang, W.4    Seward, E.P.5    Bradding, P.6
  • 128
    • 57349188508 scopus 로고    scopus 로고
    • Suppression of transient receptor potential melastatin 7 channel induces cell death in gastric cancer
    • B.J. Kim, E.J. Park, J.H. Lee, J.H. Jeon, S.J. Kim, and I. So Suppression of transient receptor potential melastatin 7 channel induces cell death in gastric cancer Cancer Sci. 99 2008 2502 2509
    • (2008) Cancer Sci. , vol.99 , pp. 2502-2509
    • Kim, B.J.1    Park, E.J.2    Lee, J.H.3    Jeon, J.H.4    Kim, S.J.5    So, I.6
  • 130
    • 0037034931 scopus 로고    scopus 로고
    • Identification of a cold receptor reveals a general role for TRP channels in thermosensation
    • D.D. McKemy, W.M. Neuhausser, and D. Julius Identification of a cold receptor reveals a general role for TRP channels in thermosensation Nature 416 2002 52 58
    • (2002) Nature , vol.416 , pp. 52-58
    • McKemy, D.D.1    Neuhausser, W.M.2    Julius, D.3
  • 132
    • 0035328671 scopus 로고    scopus 로고
    • Trp-p8, a novel prostate-specific gene, is up-regulated in prostate cancer and other malignancies and shares high homology with transient receptor potential calcium channel proteins
    • L. Tsavaler, M.H. Shapero, S. Morkowski, and R. Laus Trp-p8, a novel prostate-specific gene, is up-regulated in prostate cancer and other malignancies and shares high homology with transient receptor potential calcium channel proteins Cancer Res. 61 2001 3760 3769
    • (2001) Cancer Res. , vol.61 , pp. 3760-3769
    • Tsavaler, L.1    Shapero, M.H.2    Morkowski, S.3    Laus, R.4
  • 134
  • 135
    • 8544233547 scopus 로고    scopus 로고
    • Evidence that TRPM8 is an androgen-dependent Ca2 + channel required for the survival of prostate cancer cells
    • L. Zhang, and G.J. Barritt Evidence that TRPM8 is an androgen-dependent Ca2 + channel required for the survival of prostate cancer cells Cancer Res. 64 2004 8365 8373
    • (2004) Cancer Res. , vol.64 , pp. 8365-8373
    • Zhang, L.1    Barritt, G.J.2
  • 137
    • 70849085425 scopus 로고    scopus 로고
    • Menthol induces cell death via the TRPM8 channel in the human bladder cancer cell line T24
    • Q. Li, X. Wang, Z. Yang, B. Wang, and S. Li Menthol induces cell death via the TRPM8 channel in the human bladder cancer cell line T24 Oncology 77 2009 335 341
    • (2009) Oncology , vol.77 , pp. 335-341
    • Li, Q.1    Wang, X.2    Yang, Z.3    Wang, B.4    Li, S.5
  • 138
    • 84892941747 scopus 로고    scopus 로고
    • Involvement of transient receptor potential melastatin-8 (TRPM8) in menthol-induced calcium entry, reactive oxygen species production and cell death in rheumatoid arthritis rat synovial fibroblasts
    • S. Zhu, Y. Wang, L. Pan, S. Yang, Y. Sun, X. Wang, and F. Hu Involvement of transient receptor potential melastatin-8 (TRPM8) in menthol-induced calcium entry, reactive oxygen species production and cell death in rheumatoid arthritis rat synovial fibroblasts Eur. J. Pharmacol. 725 2014 1 9
    • (2014) Eur. J. Pharmacol. , vol.725 , pp. 1-9
    • Zhu, S.1    Wang, Y.2    Pan, L.3    Yang, S.4    Sun, Y.5    Wang, X.6    Hu, F.7
  • 139
    • 84891462597 scopus 로고    scopus 로고
    • Knockdown of TRPM8 suppresses cancer malignancy and enhances epirubicin-induced apoptosis in human osteosarcoma cells
    • Y. Wang, Z. Yang, Z. Meng, H. Cao, G. Zhu, T. Liu, and X. Wang Knockdown of TRPM8 suppresses cancer malignancy and enhances epirubicin-induced apoptosis in human osteosarcoma cells Int. J. Biol. Sci. 10 2013 90 102
    • (2013) Int. J. Biol. Sci. , vol.10 , pp. 90-102
    • Wang, Y.1    Yang, Z.2    Meng, Z.3    Cao, H.4    Zhu, G.5    Liu, T.6    Wang, X.7
  • 144
    • 69449089475 scopus 로고    scopus 로고
    • Triggering of transient receptor potential vanilloid type 1 (TRPV1) by capsaicin induces Fas/CD95-mediated apoptosis of urothelial cancer cells in an ATM-dependent manner
    • C. Amantini, P. Ballarini, S. Caprodossi, M. Nabissi, M.B. Morelli, R. Lucciarini, M.A. Cardarelli, G. Mammana, and G. Santoni Triggering of transient receptor potential vanilloid type 1 (TRPV1) by capsaicin induces Fas/CD95-mediated apoptosis of urothelial cancer cells in an ATM-dependent manner Carcinogenesis 30 2009 1320 1329
    • (2009) Carcinogenesis , vol.30 , pp. 1320-1329
    • Amantini, C.1    Ballarini, P.2    Caprodossi, S.3    Nabissi, M.4    Morelli, M.B.5    Lucciarini, R.6    Cardarelli, M.A.7    Mammana, G.8    Santoni, G.9
  • 148
    • 33947304343 scopus 로고    scopus 로고
    • TRPV6 mediates capsaicin-induced apoptosis in gastric cancer cells - Mechanisms behind a possible new "hot" cancer treatment
    • J. Chow, M. Norng, J. Zhang, and J. Chai TRPV6 mediates capsaicin-induced apoptosis in gastric cancer cells - mechanisms behind a possible new "hot" cancer treatment Biochim. Biophys. Acta 1773 2007 565 576
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 565-576
    • Chow, J.1    Norng, M.2    Zhang, J.3    Chai, J.4
  • 150
    • 0033119629 scopus 로고    scopus 로고
    • A capsaicin-receptor homologue with a high threshold for noxious heat
    • M.J. Caterina, T.A. Rosen, M. Tominaga, A.J. Brake, and D. Julius A capsaicin-receptor homologue with a high threshold for noxious heat Nature 398 1999 436 441
    • (1999) Nature , vol.398 , pp. 436-441
    • Caterina, M.J.1    Rosen, T.A.2    Tominaga, M.3    Brake, A.J.4    Julius, D.5
  • 151
    • 84886092237 scopus 로고    scopus 로고
    • TRPV2 (transient receptor potential cation channel, subfamily V, member 2)
    • V. Lehen'kyi, and N. Prevarskaya TRPV2 (transient receptor potential cation channel, subfamily V, member 2) Atlas Genet. Cytogenet. Oncol. Haematol. 16 8 2012 563 567
    • (2012) Atlas Genet. Cytogenet. Oncol. Haematol. , vol.16 , Issue.8 , pp. 563-567
    • Lehen'kyi, V.1    Prevarskaya, N.2
  • 153
    • 84872128254 scopus 로고    scopus 로고
    • Triggering of the TRPV2 channel by cannabidiol sensitizes glioblastoma cells to cytotoxic chemotherapeutic agents
    • M. Nabissi, M.B. Morelli, M. Santoni, and G. Santoni Triggering of the TRPV2 channel by cannabidiol sensitizes glioblastoma cells to cytotoxic chemotherapeutic agents Carcinogenesis 34 2013 48 57
    • (2013) Carcinogenesis , vol.34 , pp. 48-57
    • Nabissi, M.1    Morelli, M.B.2    Santoni, M.3    Santoni, G.4
  • 154
    • 77955712868 scopus 로고    scopus 로고
    • TRPV2 activation induces apoptotic cell death in human T24 bladder cancer cells: A potential therapeutic target for bladder cancer
    • (509 e501-507)
    • T. Yamada, T. Ueda, Y. Shibata, Y. Ikegami, M. Saito, Y. Ishida, S. Ugawa, K. Kohri, and S. Shimada TRPV2 activation induces apoptotic cell death in human T24 bladder cancer cells: a potential therapeutic target for bladder cancer Urology 76 2010 (509 e501-507)
    • (2010) Urology , vol.76
    • Yamada, T.1    Ueda, T.2    Shibata, Y.3    Ikegami, Y.4    Saito, M.5    Ishida, Y.6    Ugawa, S.7    Kohri, K.8    Shimada, S.9
  • 156
    • 84858175916 scopus 로고    scopus 로고
    • The role of the TRPV6 channel in cancer
    • V. Lehen'kyi, M. Raphael, and N. Prevarskaya The role of the TRPV6 channel in cancer J. Physiol. 590 2012 1369 1376
    • (2012) J. Physiol. , vol.590 , pp. 1369-1376
    • Lehen'kyi, V.1    Raphael, M.2    Prevarskaya, N.3
  • 158
    • 36148992621 scopus 로고    scopus 로고
    • TRPV6 channel controls prostate cancer cell proliferation via Ca(2 +)/NFAT-dependent pathways
    • V. Lehen'kyi, M. Flourakis, R. Skryma, and N. Prevarskaya TRPV6 channel controls prostate cancer cell proliferation via Ca(2 +)/NFAT-dependent pathways Oncogene 26 2007 7380 7385
    • (2007) Oncogene , vol.26 , pp. 7380-7385
    • Lehen'kyi, V.1    Flourakis, M.2    Skryma, R.3    Prevarskaya, N.4
  • 159
    • 77957001219 scopus 로고    scopus 로고
    • Suppression of aberrant transient receptor potential cation channel, subfamily V, member 6 expression in hyperproliferative colonic crypts by dietary calcium
    • S. Peleg, J.H. Sellin, Y. Wang, M.R. Freeman, and S. Umar Suppression of aberrant transient receptor potential cation channel, subfamily V, member 6 expression in hyperproliferative colonic crypts by dietary calcium Am. J. Physiol. Gastrointest. Liver Physiol. 299 2010 G593 601
    • (2010) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.299 , pp. G593-601
    • Peleg, S.1    Sellin, J.H.2    Wang, Y.3    Freeman, M.R.4    Umar, S.5
  • 160
    • 84881569670 scopus 로고    scopus 로고
    • P53 increases intra-cellular calcium release by transcriptional regulation of calcium channel TRPC6 in GaQ3-treated cancer cells
    • E. Madan, R. Gogna, B. Keppler, and U. Pati p53 increases intra-cellular calcium release by transcriptional regulation of calcium channel TRPC6 in GaQ3-treated cancer cells PLoS One 8 2013 e71016
    • (2013) PLoS One , vol.8 , pp. e71016
    • Madan, E.1    Gogna, R.2    Keppler, B.3    Pati, U.4
  • 161
    • 84877017382 scopus 로고    scopus 로고
    • High glucose-induced apoptosis in cultured podocytes involves TRPC6-dependent calcium entry via the RhoA/ROCK pathway
    • H. Yang, B. Zhao, C. Liao, R. Zhang, K. Meng, J. Xu, and J. Jiao High glucose-induced apoptosis in cultured podocytes involves TRPC6-dependent calcium entry via the RhoA/ROCK pathway Biochem. Biophys. Res. Commun. 434 2013 394 400
    • (2013) Biochem. Biophys. Res. Commun. , vol.434 , pp. 394-400
    • Yang, H.1    Zhao, B.2    Liao, C.3    Zhang, R.4    Meng, K.5    Xu, J.6    Jiao, J.7
  • 163
    • 48249148378 scopus 로고    scopus 로고
    • Induced TRPC1 expression increases protein phosphatase 2A sensitizing intestinal epithelial cells to apoptosis through inhibition of NF-kappaB activation
    • B.S. Marasa, L. Xiao, J.N. Rao, T. Zou, L. Liu, J. Wang, E. Bellavance, D.J. Turner, and J.Y. Wang Induced TRPC1 expression increases protein phosphatase 2A sensitizing intestinal epithelial cells to apoptosis through inhibition of NF-kappaB activation Am. J. Physiol. Cell Physiol. 294 2008 C1277 1287
    • (2008) Am. J. Physiol. Cell Physiol. , vol.294 , pp. C1277-1287
    • Marasa, B.S.1    Xiao, L.2    Rao, J.N.3    Zou, T.4    Liu, L.5    Wang, J.6    Bellavance, E.7    Turner, D.J.8    Wang, J.Y.9
  • 164
    • 33746062079 scopus 로고    scopus 로고
    • TRPC1 protects human SH-SY5Y cells against salsolinol-induced cytotoxicity by inhibiting apoptosis
    • S. Bollimuntha, M. Ebadi, and B.B. Singh TRPC1 protects human SH-SY5Y cells against salsolinol-induced cytotoxicity by inhibiting apoptosis Brain Res. 1099 2006 141 149
    • (2006) Brain Res. , vol.1099 , pp. 141-149
    • Bollimuntha, S.1    Ebadi, M.2    Singh, B.B.3
  • 165
    • 84872676834 scopus 로고    scopus 로고
    • Stimulation of the chemosensory TRPA1 cation channel by volatile toxic substances promotes cell survival of small cell lung cancer cells
    • E.A. Schaefer, S. Stohr, M. Meister, A. Aigner, T. Gudermann, and T.R. Buech Stimulation of the chemosensory TRPA1 cation channel by volatile toxic substances promotes cell survival of small cell lung cancer cells Biochem. Pharmacol. 85 2013 426 438
    • (2013) Biochem. Pharmacol. , vol.85 , pp. 426-438
    • Schaefer, E.A.1    Stohr, S.2    Meister, M.3    Aigner, A.4    Gudermann, T.5    Buech, T.R.6
  • 167
    • 84874620146 scopus 로고    scopus 로고
    • Intracellular two-phase Ca2 + release and apoptosis controlled by TRP-ML1 channel activity in coronary arterial myocytes
    • M. Xu, X. Li, S.W. Walsh, Y. Zhang, J.M. Abais, K.M. Boini, and P.L. Li Intracellular two-phase Ca2 + release and apoptosis controlled by TRP-ML1 channel activity in coronary arterial myocytes Am. J. Physiol. Cell Physiol. 304 2013 C458 466
    • (2013) Am. J. Physiol. Cell Physiol. , vol.304 , pp. C458-466
    • Xu, M.1    Li, X.2    Walsh, S.W.3    Zhang, Y.4    Abais, J.M.5    Boini, K.M.6    Li, P.L.7
  • 168
    • 67649406472 scopus 로고    scopus 로고
    • Life and death of sensory hair cells expressing constitutively active TRPML3
    • C. Grimm, S. Jors, and S. Heller Life and death of sensory hair cells expressing constitutively active TRPML3 J. Biol. Chem. 284 2009 13823 13831
    • (2009) J. Biol. Chem. , vol.284 , pp. 13823-13831
    • Grimm, C.1    Jors, S.2    Heller, S.3
  • 169
    • 77449137885 scopus 로고    scopus 로고
    • Constitutive activity of the human TRPML2 channel induces cell degeneration
    • S. Lev, D.A. Zeevi, A. Frumkin, V. Offen-Glasner, G. Bach, and B. Minke Constitutive activity of the human TRPML2 channel induces cell degeneration J. Biol. Chem. 285 2010 2771 2782
    • (2010) J. Biol. Chem. , vol.285 , pp. 2771-2782
    • Lev, S.1    Zeevi, D.A.2    Frumkin, A.3    Offen-Glasner, V.4    Bach, G.5    Minke, B.6
  • 171
    • 22644444450 scopus 로고    scopus 로고
    • Voltage-dependent calcium channels
    • L. Lacinova Voltage-dependent calcium channels Gen. Physiol. Biophys. 24 Suppl. 1 2005 1 78
    • (2005) Gen. Physiol. Biophys. , vol.24 , pp. 1-78
    • Lacinova, L.1
  • 172
    • 0035955638 scopus 로고    scopus 로고
    • Calcium entry through L-type calcium channels causes mitochondrial disruption and chromaffin cell death
    • M.F. Cano-Abad, M. Villarroya, A.G. Garcia, N.H. Gabilan, and M.G. Lopez Calcium entry through L-type calcium channels causes mitochondrial disruption and chromaffin cell death J. Biol. Chem. 276 2001 39695 39704
    • (2001) J. Biol. Chem. , vol.276 , pp. 39695-39704
    • Cano-Abad, M.F.1    Villarroya, M.2    Garcia, A.G.3    Gabilan, N.H.4    Lopez, M.G.5
  • 175
    • 0032933208 scopus 로고    scopus 로고
    • A low voltage-activated Ca2 + current mediates cytokine-induced pancreatic beta-cell death
    • L. Wang, A. Bhattacharjee, Z. Zuo, F. Hu, R.E. Honkanen, P.O. Berggren, and M. Li A low voltage-activated Ca2 + current mediates cytokine-induced pancreatic beta-cell death Endocrinology 140 1999 1200 1204
    • (1999) Endocrinology , vol.140 , pp. 1200-1204
    • Wang, L.1    Bhattacharjee, A.2    Zuo, Z.3    Hu, F.4    Honkanen, R.E.5    Berggren, P.O.6    Li, M.7
  • 176
    • 84897073331 scopus 로고    scopus 로고
    • T-type Ca2 + channel inhibition induces p53-dependent cell growth arrest and apoptosis through activation of p38-MAPK in colon cancer cells
    • B. Dziegielewska, D.L. Brautigan, J.M. Larner, and J. Dziegielewski T-type Ca2 + channel inhibition induces p53-dependent cell growth arrest and apoptosis through activation of p38-MAPK in colon cancer cells Mol. Cancer Res. 12 2014 348 358
    • (2014) Mol. Cancer Res. , vol.12 , pp. 348-358
    • Dziegielewska, B.1    Brautigan, D.L.2    Larner, J.M.3    Dziegielewski, J.4
  • 179
    • 33644857376 scopus 로고    scopus 로고
    • Changes in cytosolic Ca2 + levels regulate Bcl-xS and Bcl-xL expression in spermatogenic cells during apoptotic death
    • D.P. Mishra, R. Pal, and C. Shaha Changes in cytosolic Ca2 + levels regulate Bcl-xS and Bcl-xL expression in spermatogenic cells during apoptotic death J. Biol. Chem. 281 2006 2133 2143
    • (2006) J. Biol. Chem. , vol.281 , pp. 2133-2143
    • Mishra, D.P.1    Pal, R.2    Shaha, C.3
  • 180
    • 84896543008 scopus 로고    scopus 로고
    • T-type calcium channels blockers as new tools in cancer therapies
    • B. Dziegielewska, L.S. Gray, and J. Dziegielewski T-type calcium channels blockers as new tools in cancer therapies Pflugers Arch. 466 2014 801 810
    • (2014) Pflugers Arch. , vol.466 , pp. 801-810
    • Dziegielewska, B.1    Gray, L.S.2    Dziegielewski, J.3
  • 181
    • 34249879293 scopus 로고    scopus 로고
    • Cell shrinkage and monovalent cation fluxes: Role in apoptosis
    • C.D. Bortner, and J.A. Cidlowski Cell shrinkage and monovalent cation fluxes: role in apoptosis Arch. Biochem. Biophys. 462 2007 176 188
    • (2007) Arch. Biochem. Biophys. , vol.462 , pp. 176-188
    • Bortner, C.D.1    Cidlowski, J.A.2
  • 182
    • 0031451872 scopus 로고    scopus 로고
    • A primary role for K + and Na + efflux in the activation of apoptosis
    • C.D. Bortner, F.M. Hughes Jr., and J.A. Cidlowski A primary role for K + and Na + efflux in the activation of apoptosis J. Biol. Chem. 272 1997 32436 32442
    • (1997) J. Biol. Chem. , vol.272 , pp. 32436-32442
    • Bortner, C.D.1    Hughes, F.M.2    Cidlowski, J.A.3
  • 183
    • 0035834691 scopus 로고    scopus 로고
    • Physiological concentrations of K + inhibit cytochrome c-dependent formation of the apoptosome
    • K. Cain, C. Langlais, X.M. Sun, D.G. Brown, and G.M. Cohen Physiological concentrations of K + inhibit cytochrome c-dependent formation of the apoptosome J. Biol. Chem. 276 2001 41985 41990
    • (2001) J. Biol. Chem. , vol.276 , pp. 41985-41990
    • Cain, K.1    Langlais, C.2    Sun, X.M.3    Brown, D.G.4    Cohen, G.M.5
  • 184
    • 15644374609 scopus 로고    scopus 로고
    • Intracellular K + suppresses the activation of apoptosis in lymphocytes
    • F.M. Hughes Jr., C.D. Bortner, G.D. Purdy, and J.A. Cidlowski Intracellular K + suppresses the activation of apoptosis in lymphocytes J. Biol. Chem. 272 1997 30567 30576
    • (1997) J. Biol. Chem. , vol.272 , pp. 30567-30576
    • Hughes, F.M.1    Bortner, C.D.2    Purdy, G.D.3    Cidlowski, J.A.4
  • 186
    • 0033624616 scopus 로고    scopus 로고
    • ROMK1 (Kir1.1) causes apoptosis and chronic silencing of hippocampal neurons
    • H. Nadeau, S. McKinney, D.J. Anderson, and H.A. Lester ROMK1 (Kir1.1) causes apoptosis and chronic silencing of hippocampal neurons J. Neurophysiol. 84 2000 1062 1075
    • (2000) J. Neurophysiol. , vol.84 , pp. 1062-1075
    • Nadeau, H.1    McKinney, S.2    Anderson, D.J.3    Lester, H.A.4
  • 188
    • 0035397708 scopus 로고    scopus 로고
    • Elevated extracellular [K +] inhibits death-receptor- and chemical-mediated apoptosis prior to caspase activation and cytochrome c release
    • G.J. Thompson, C. Langlais, K. Cain, E.C. Conley, and G.M. Cohen Elevated extracellular [K +] inhibits death-receptor- and chemical-mediated apoptosis prior to caspase activation and cytochrome c release Biochem. J. 357 2001 137 145
    • (2001) Biochem. J. , vol.357 , pp. 137-145
    • Thompson, G.J.1    Langlais, C.2    Cain, K.3    Conley, E.C.4    Cohen, G.M.5
  • 189
    • 0033635776 scopus 로고    scopus 로고
    • Potassium channels: Molecular defects, diseases, and therapeutic opportunities
    • C.C. Shieh, M. Coghlan, J.P. Sullivan, and M. Gopalakrishnan Potassium channels: molecular defects, diseases, and therapeutic opportunities Pharmacol. Rev. 52 2000 557 594
    • (2000) Pharmacol. Rev. , vol.52 , pp. 557-594
    • Shieh, C.C.1    Coghlan, M.2    Sullivan, J.P.3    Gopalakrishnan, M.4
  • 190
    • 11844307184 scopus 로고    scopus 로고
    • Roles of K + channels in regulating tumour cell proliferation and apoptosis
    • Z. Wang Roles of K + channels in regulating tumour cell proliferation and apoptosis Pflugers Arch. 448 2004 274 286
    • (2004) Pflugers Arch. , vol.448 , pp. 274-286
    • Wang, Z.1
  • 192
    • 84890992887 scopus 로고    scopus 로고
    • The roles of K(+) channels in cancer
    • L.A. Pardo, and W. Stuhmer The roles of K(+) channels in cancer Nat. Rev. Cancer 14 2014 39 48
    • (2014) Nat. Rev. Cancer , vol.14 , pp. 39-48
    • Pardo, L.A.1    Stuhmer, W.2
  • 193
    • 0042829363 scopus 로고    scopus 로고
    • Regulation and critical role of potassium homeostasis in apoptosis
    • S.P. Yu Regulation and critical role of potassium homeostasis in apoptosis Prog. Neurobiol. 70 2003 363 386
    • (2003) Prog. Neurobiol. , vol.70 , pp. 363-386
    • Yu, S.P.1
  • 194
    • 77952671757 scopus 로고    scopus 로고
    • Contribution of voltage-gated potassium channels to the regulation of apoptosis
    • I. Szabo, M. Zoratti, and E. Gulbins Contribution of voltage-gated potassium channels to the regulation of apoptosis FEBS Lett. 584 2010 2049 2056
    • (2010) FEBS Lett. , vol.584 , pp. 2049-2056
    • Szabo, I.1    Zoratti, M.2    Gulbins, E.3
  • 196
    • 84869210513 scopus 로고    scopus 로고
    • Differential role of IK and BK potassium channels as mediators of intrinsic and extrinsic apoptotic cell death
    • M.B. McFerrin, K.L. Turner, V.A. Cuddapah, and H. Sontheimer Differential role of IK and BK potassium channels as mediators of intrinsic and extrinsic apoptotic cell death Am. J. Physiol. Cell Physiol. 303 2012 C1070 1078
    • (2012) Am. J. Physiol. Cell Physiol. , vol.303 , pp. C1070-1078
    • McFerrin, M.B.1    Turner, K.L.2    Cuddapah, V.A.3    Sontheimer, H.4
  • 197
    • 84882807404 scopus 로고    scopus 로고
    • Convergent Ca2 + and Zn2 + signaling regulates apoptotic Kv2.1 K + currents
    • M.C. McCord, and E. Aizenman Convergent Ca2 + and Zn2 + signaling regulates apoptotic Kv2.1 K + currents Proc. Natl. Acad. Sci. U. S. A. 110 2013 13988 13993
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 13988-13993
    • McCord, M.C.1    Aizenman, E.2
  • 200
    • 0034617098 scopus 로고    scopus 로고
    • Activation of potassium and chloride channels by tumor necrosis factor alpha. Role in liver cell death
    • H.H. Nietsch, M.W. Roe, J.F. Fiekers, A.L. Moore, and S.D. Lidofsky Activation of potassium and chloride channels by tumor necrosis factor alpha. Role in liver cell death J. Biol. Chem. 275 2000 20556 20561
    • (2000) J. Biol. Chem. , vol.275 , pp. 20556-20561
    • Nietsch, H.H.1    Roe, M.W.2    Fiekers, J.F.3    Moore, A.L.4    Lidofsky, S.D.5
  • 201
  • 202
    • 16544372024 scopus 로고    scopus 로고
    • The 2P-domain K + channels: Role in apoptosis and tumorigenesis
    • A.J. Patel, and M. Lazdunski The 2P-domain K + channels: role in apoptosis and tumorigenesis Pflugers Arch. 448 2004 261 273
    • (2004) Pflugers Arch. , vol.448 , pp. 261-273
    • Patel, A.J.1    Lazdunski, M.2
  • 203
    • 84892653559 scopus 로고    scopus 로고
    • Enhancement of TWIK-related acid-sensitive potassium channel 3 (TASK3) two-pore domain potassium channel activity by tumor necrosis factor alpha
    • M.F. El Hachmane, K.A. Rees, E.L. Veale, V.V. Sumbayev, and A. Mathie Enhancement of TWIK-related acid-sensitive potassium channel 3 (TASK3) two-pore domain potassium channel activity by tumor necrosis factor alpha J. Biol. Chem. 289 2014 1388 1401
    • (2014) J. Biol. Chem. , vol.289 , pp. 1388-1401
    • El Hachmane, M.F.1    Rees, K.A.2    Veale, E.L.3    Sumbayev, V.V.4    Mathie, A.5
  • 205
    • 0036086809 scopus 로고    scopus 로고
    • Apoptosis recruits two-pore domain potassium channels used for homeostatic volume regulation
    • J.R. Trimarchi, L. Liu, P.J. Smith, and D.L. Keefe Apoptosis recruits two-pore domain potassium channels used for homeostatic volume regulation Am. J. Physiol. Cell Physiol. 282 2002 C588 594
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282 , pp. C588-594
    • Trimarchi, J.R.1    Liu, L.2    Smith, P.J.3    Keefe, D.L.4
  • 207
    • 0034811051 scopus 로고    scopus 로고
    • Bcl-2 decreases voltage-gated K + channel activity and enhances survival in vascular smooth muscle cells
    • D. Ekhterae, O. Platoshyn, S. Krick, Y. Yu, S.S. McDaniel, and J.X. Yuan Bcl-2 decreases voltage-gated K + channel activity and enhances survival in vascular smooth muscle cells Am. J. Physiol. Cell Physiol. 281 2001 C157 165
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281 , pp. C157-165
    • Ekhterae, D.1    Platoshyn, O.2    Krick, S.3    Yu, Y.4    McDaniel, S.S.5    Yuan, J.X.6
  • 209
    • 84856695390 scopus 로고    scopus 로고
    • Physiology of potassium channels in the inner membrane of mitochondria
    • I. Szabo, L. Leanza, E. Gulbins, and M. Zoratti Physiology of potassium channels in the inner membrane of mitochondria Pflugers Arch. 463 2012 231 246
    • (2012) Pflugers Arch. , vol.463 , pp. 231-246
    • Szabo, I.1    Leanza, L.2    Gulbins, E.3    Zoratti, M.4
  • 211
    • 84870410761 scopus 로고    scopus 로고
    • Induction of apoptosis in macrophages via Kv1.3 and Kv1.5 potassium channels
    • L. Leanza, M. Zoratti, E. Gulbins, and I. Szabo Induction of apoptosis in macrophages via Kv1.3 and Kv1.5 potassium channels Curr. Med. Chem. 19 2012 5394 5404
    • (2012) Curr. Med. Chem. , vol.19 , pp. 5394-5404
    • Leanza, L.1    Zoratti, M.2    Gulbins, E.3    Szabo, I.4
  • 212
    • 84863473765 scopus 로고    scopus 로고
    • Inhibitors of mitochondrial Kv1.3 channels induce Bax/Bak-independent death of cancer cells
    • L. Leanza, B. Henry, N. Sassi, M. Zoratti, K.G. Chandy, E. Gulbins, and I. Szabo Inhibitors of mitochondrial Kv1.3 channels induce Bax/Bak-independent death of cancer cells EMBO Mol. Med. 4 2012 577 593
    • (2012) EMBO Mol. Med. , vol.4 , pp. 577-593
    • Leanza, L.1    Henry, B.2    Sassi, N.3    Zoratti, M.4    Chandy, K.G.5    Gulbins, E.6    Szabo, I.7
  • 213
    • 84881479922 scopus 로고    scopus 로고
    • Clofazimine, Psora-4 and PAP-1, inhibitors of the potassium channel Kv1.3, as a new and selective therapeutic strategy in chronic lymphocytic leukemia
    • L. Leanza, L. Trentin, K.A. Becker, F. Frezzato, M. Zoratti, G. Semenzato, E. Gulbins, and I. Szabo Clofazimine, Psora-4 and PAP-1, inhibitors of the potassium channel Kv1.3, as a new and selective therapeutic strategy in chronic lymphocytic leukemia Leukemia 27 2013 1782 1785
    • (2013) Leukemia , vol.27 , pp. 1782-1785
    • Leanza, L.1    Trentin, L.2    Becker, K.A.3    Frezzato, F.4    Zoratti, M.5    Semenzato, G.6    Gulbins, E.7    Szabo, I.8
  • 214
  • 217
    • 84892959692 scopus 로고    scopus 로고
    • Correlation between potassium channel expression and sensitivity to drug-induced cell death in tumor cell lines
    • L. Leanza, P. O'Reilly, A. Doyle, E. Venturini, M. Zoratti, E. Szegezdi, and I. Szabo Correlation between potassium channel expression and sensitivity to drug-induced cell death in tumor cell lines Curr. Pharm. Des. 20 2014 189 200
    • (2014) Curr. Pharm. Des. , vol.20 , pp. 189-200
    • Leanza, L.1    O'Reilly, P.2    Doyle, A.3    Venturini, E.4    Zoratti, M.5    Szegezdi, E.6    Szabo, I.7
  • 218
    • 0343938842 scopus 로고    scopus 로고
    • Changes in elemental content during apoptotic cell death studied by electron probe X-ray microanalysis
    • E. Fernandez-Segura, F.J. Canizares, M.A. Cubero, A. Warley, and A. Campos Changes in elemental content during apoptotic cell death studied by electron probe X-ray microanalysis Exp. Cell Res. 253 1999 454 462
    • (1999) Exp. Cell Res. , vol.253 , pp. 454-462
    • Fernandez-Segura, E.1    Canizares, F.J.2    Cubero, M.A.3    Warley, A.4    Campos, A.5
  • 219
    • 0032946457 scopus 로고    scopus 로고
    • Changes in elemental concentrations are associated with early stages of apoptosis in human monocyte-macrophages exposed to oxidized low-density lipoprotein: An X-ray microanalytical study
    • J.N. Skepper, I. Karydis, M.R. Garnett, L. Hegyi, S.J. Hardwick, A. Warley, M.J. Mitchinson, and N.R. Cary Changes in elemental concentrations are associated with early stages of apoptosis in human monocyte-macrophages exposed to oxidized low-density lipoprotein: an X-ray microanalytical study J. Pathol. 188 1999 100 106
    • (1999) J. Pathol. , vol.188 , pp. 100-106
    • Skepper, J.N.1    Karydis, I.2    Garnett, M.R.3    Hegyi, L.4    Hardwick, S.J.5    Warley, A.6    Mitchinson, M.J.7    Cary, N.R.8
  • 220
    • 33644849471 scopus 로고    scopus 로고
    • Changes in intracellular electrolyte concentrations during apoptosis induced by UV irradiation of human myeloblastic cells
    • F. Arrebola, E. Fernandez-Segura, A. Campos, P.V. Crespo, J.N. Skepper, and A. Warley Changes in intracellular electrolyte concentrations during apoptosis induced by UV irradiation of human myeloblastic cells Am. J. Physiol. Cell Physiol. 290 2006 C638 649
    • (2006) Am. J. Physiol. Cell Physiol. , vol.290 , pp. C638-649
    • Arrebola, F.1    Fernandez-Segura, E.2    Campos, A.3    Crespo, P.V.4    Skepper, J.N.5    Warley, A.6
  • 222
    • 0141643095 scopus 로고    scopus 로고
    • Uncoupling cell shrinkage from apoptosis reveals that Na + influx is required for volume loss during programmed cell death
    • C.D. Bortner, and J.A. Cidlowski Uncoupling cell shrinkage from apoptosis reveals that Na + influx is required for volume loss during programmed cell death J. Biol. Chem. 278 2003 39176 39184
    • (2003) J. Biol. Chem. , vol.278 , pp. 39176-39184
    • Bortner, C.D.1    Cidlowski, J.A.2
  • 223
    • 0035830843 scopus 로고    scopus 로고
    • Plasma membrane depolarization without repolarization is an early molecular event in anti-Fas-induced apoptosis
    • C.D. Bortner, M. Gomez-Angelats, and J.A. Cidlowski Plasma membrane depolarization without repolarization is an early molecular event in anti-Fas-induced apoptosis J. Biol. Chem. 276 2001 4304 4314
    • (2001) J. Biol. Chem. , vol.276 , pp. 4304-4314
    • Bortner, C.D.1    Gomez-Angelats, M.2    Cidlowski, J.A.3
  • 224
    • 9644262891 scopus 로고    scopus 로고
    • Depolarisation of the plasma membrane in the arsenic trioxide (As2O3)- and anti-CD95-induced apoptosis in myeloid cells
    • F. Nolte, O. Friedrich, M. Rojewski, R.H. Fink, H. Schrezenmeier, and S. Korper Depolarisation of the plasma membrane in the arsenic trioxide (As2O3)- and anti-CD95-induced apoptosis in myeloid cells FEBS Lett. 578 2004 85 89
    • (2004) FEBS Lett. , vol.578 , pp. 85-89
    • Nolte, F.1    Friedrich, O.2    Rojewski, M.3    Fink, R.H.4    Schrezenmeier, H.5    Korper, S.6
  • 225
    • 2542493860 scopus 로고    scopus 로고
    • Involvement of sodium in early phosphatidylserine exposure and phospholipid scrambling induced by P2X7 purinoceptor activation in thymocytes
    • M.P. Courageot, S. Lepine, M. Hours, F. Giraud, and J.C. Sulpice Involvement of sodium in early phosphatidylserine exposure and phospholipid scrambling induced by P2X7 purinoceptor activation in thymocytes J. Biol. Chem. 279 2004 21815 21823
    • (2004) J. Biol. Chem. , vol.279 , pp. 21815-21823
    • Courageot, M.P.1    Lepine, S.2    Hours, M.3    Giraud, F.4    Sulpice, J.C.5
  • 226
    • 0032477641 scopus 로고    scopus 로고
    • Activation of the atrial KACh channel by the betagamma subunits of G proteins or intracellular Na + ions depends on the presence of phosphatidylinositol phosphates
    • J.L. Sui, J. Petit-Jacques, and D.E. Logothetis Activation of the atrial KACh channel by the betagamma subunits of G proteins or intracellular Na + ions depends on the presence of phosphatidylinositol phosphates Proc. Natl. Acad. Sci. U. S. A. 95 1998 1307 1312
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1307-1312
    • Sui, J.L.1    Petit-Jacques, J.2    Logothetis, D.E.3
  • 229
    • 0036307827 scopus 로고    scopus 로고
    • Epithelial sodium channel/degenerin family of ion channels: A variety of functions for a shared structure
    • S. Kellenberger, and L. Schild Epithelial sodium channel/degenerin family of ion channels: a variety of functions for a shared structure Physiol. Rev. 82 2002 735 767
    • (2002) Physiol. Rev. , vol.82 , pp. 735-767
    • Kellenberger, S.1    Schild, L.2
  • 231
    • 0037264170 scopus 로고    scopus 로고
    • Overview of the voltage-gated sodium channel family
    • F.H. Yu, and W.A. Catterall Overview of the voltage-gated sodium channel family Genome Biol. 4 2003 207
    • (2003) Genome Biol. , vol.4 , pp. 207
    • Yu, F.H.1    Catterall, W.A.2
  • 232
    • 2342596450 scopus 로고    scopus 로고
    • Activation of voltage-sensitive sodium channels during oxygen deprivation leads to apoptotic neuronal death
    • K.J. Banasiak, O. Burenkova, and G.G. Haddad Activation of voltage-sensitive sodium channels during oxygen deprivation leads to apoptotic neuronal death Neuroscience 126 2004 31 44
    • (2004) Neuroscience , vol.126 , pp. 31-44
    • Banasiak, K.J.1    Burenkova, O.2    Haddad, G.G.3
  • 233
    • 0242401920 scopus 로고    scopus 로고
    • Role and regulation of p53 in depolarization-induced neuronal death
    • J. Jordan, M.F. Galindo, C. Gonzalez-Garcia, and V. Cena Role and regulation of p53 in depolarization-induced neuronal death Neuroscience 122 2003 707 715
    • (2003) Neuroscience , vol.122 , pp. 707-715
    • Jordan, J.1    Galindo, M.F.2    Gonzalez-Garcia, C.3    Cena, V.4
  • 234
    • 0035036830 scopus 로고    scopus 로고
    • Incorporation of sodium channel blocking and free radical scavenging activities into a single drug, AM-36, results in profound inhibition of neuronal apoptosis
    • J.K. Callaway, P.M. Beart, B. Jarrott, and S.F. Giardina Incorporation of sodium channel blocking and free radical scavenging activities into a single drug, AM-36, results in profound inhibition of neuronal apoptosis Br. J. Pharmacol. 132 2001 1691 1698
    • (2001) Br. J. Pharmacol. , vol.132 , pp. 1691-1698
    • Callaway, J.K.1    Beart, P.M.2    Jarrott, B.3    Giardina, S.F.4
  • 237
    • 84862900926 scopus 로고    scopus 로고
    • Inhibition of acid-sensing ion channels by amiloride protects rat articular chondrocytes from acid-induced apoptosis via a mitochondrial-mediated pathway
    • C. Rong, F.H. Chen, S. Jiang, W. Hu, F.R. Wu, T.Y. Chen, and F.L. Yuan Inhibition of acid-sensing ion channels by amiloride protects rat articular chondrocytes from acid-induced apoptosis via a mitochondrial-mediated pathway Cell Biol. Int. 36 2012 635 641
    • (2012) Cell Biol. Int. , vol.36 , pp. 635-641
    • Rong, C.1    Chen, F.H.2    Jiang, S.3    Hu, W.4    Wu, F.R.5    Chen, T.Y.6    Yuan, F.L.7
  • 241
    • 33846269623 scopus 로고    scopus 로고
    • The neonatal splice variant of Nav1.5 potentiates in vitro invasive behaviour of MDA-MB-231 human breast cancer cells
    • W.J. Brackenbury, A.M. Chioni, J.K. Diss, and M.B. Djamgoz The neonatal splice variant of Nav1.5 potentiates in vitro invasive behaviour of MDA-MB-231 human breast cancer cells Breast Cancer Res. Treat. 101 2007 149 160
    • (2007) Breast Cancer Res. Treat. , vol.101 , pp. 149-160
    • Brackenbury, W.J.1    Chioni, A.M.2    Diss, J.K.3    Djamgoz, M.B.4
  • 243
    • 0034662989 scopus 로고    scopus 로고
    • Normotonic cell shrinkage because of disordered volume regulation is an early prerequisite to apoptosis
    • E. Maeno, Y. Ishizaki, T. Kanaseki, A. Hazama, and Y. Okada Normotonic cell shrinkage because of disordered volume regulation is an early prerequisite to apoptosis Proc. Natl. Acad. Sci. U. S. A. 97 2000 9487 9492
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9487-9492
    • Maeno, E.1    Ishizaki, Y.2    Kanaseki, T.3    Hazama, A.4    Okada, Y.5
  • 244
    • 10444257481 scopus 로고    scopus 로고
    • Effects of chloride and potassium channel blockers on apoptotic cell shrinkage and apoptosis in cortical neurons
    • L. Wei, A.Y. Xiao, C. Jin, A. Yang, Z.Y. Lu, and S.P. Yu Effects of chloride and potassium channel blockers on apoptotic cell shrinkage and apoptosis in cortical neurons Pflugers Arch. 448 2004 325 334
    • (2004) Pflugers Arch. , vol.448 , pp. 325-334
    • Wei, L.1    Xiao, A.Y.2    Jin, C.3    Yang, A.4    Lu, Z.Y.5    Yu, S.P.6
  • 245
    • 33646586354 scopus 로고    scopus 로고
    • Volume-sensitive chloride channels involved in apoptotic volume decrease and cell death
    • Y. Okada, T. Shimizu, E. Maeno, S. Tanabe, X. Wang, and N. Takahashi Volume-sensitive chloride channels involved in apoptotic volume decrease and cell death J. Membr. Biol. 209 2006 21 29
    • (2006) J. Membr. Biol. , vol.209 , pp. 21-29
    • Okada, Y.1    Shimizu, T.2    Maeno, E.3    Tanabe, S.4    Wang, X.5    Takahashi, N.6
  • 247
    • 0037318653 scopus 로고    scopus 로고
    • Amazing chloride channels: An overview
    • B. Nilius, and G. Droogmans Amazing chloride channels: an overview Acta Physiol. Scand. 177 2003 119 147
    • (2003) Acta Physiol. Scand. , vol.177 , pp. 119-147
    • Nilius, B.1    Droogmans, G.2
  • 249
    • 0035752583 scopus 로고    scopus 로고
    • Cellular function and control of volume-regulated anion channels
    • J. Eggermont, D. Trouet, I. Carton, and B. Nilius Cellular function and control of volume-regulated anion channels Cell Biochem. Biophys. 35 2001 263 274
    • (2001) Cell Biochem. Biophys. , vol.35 , pp. 263-274
    • Eggermont, J.1    Trouet, D.2    Carton, I.3    Nilius, B.4
  • 250
    • 2342637859 scopus 로고    scopus 로고
    • A role of reactive oxygen species in apoptotic activation of volume-sensitive Cl(-) channel
    • T. Shimizu, T. Numata, and Y. Okada A role of reactive oxygen species in apoptotic activation of volume-sensitive Cl(-) channel Proc. Natl. Acad. Sci. U. S. A. 101 2004 6770 6773
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 6770-6773
    • Shimizu, T.1    Numata, T.2    Okada, Y.3
  • 251
    • 27344438327 scopus 로고    scopus 로고
    • Cells die with increased cytosolic ATP during apoptosis: A bioluminescence study with intracellular luciferase
    • M.V. Zamaraeva, R.Z. Sabirov, E. Maeno, Y. Ando-Akatsuka, S.V. Bessonova, and Y. Okada Cells die with increased cytosolic ATP during apoptosis: a bioluminescence study with intracellular luciferase Cell Death Differ. 12 2005 1390 1397
    • (2005) Cell Death Differ. , vol.12 , pp. 1390-1397
    • Zamaraeva, M.V.1    Sabirov, R.Z.2    Maeno, E.3    Ando-Akatsuka, Y.4    Bessonova, S.V.5    Okada, Y.6
  • 252
    • 0035310427 scopus 로고    scopus 로고
    • Receptor-mediated control of regulatory volume decrease (RVD) and apoptotic volume decrease (AVD)
    • Y. Okada, E. Maeno, T. Shimizu, K. Dezaki, J. Wang, and S. Morishima Receptor-mediated control of regulatory volume decrease (RVD) and apoptotic volume decrease (AVD) J. Physiol. 532 2001 3 16
    • (2001) J. Physiol. , vol.532 , pp. 3-16
    • Okada, Y.1    Maeno, E.2    Shimizu, T.3    Dezaki, K.4    Wang, J.5    Morishima, S.6
  • 253
    • 85047681642 scopus 로고    scopus 로고
    • Induction of apoptosis by nitric oxide in macrophages is independent of apoptotic volume decrease
    • S. Hortelano, M. Zeini, A. Castrillo, A.M. Alvarez, and L. Bosca Induction of apoptosis by nitric oxide in macrophages is independent of apoptotic volume decrease Cell Death Differ. 9 2002 643 650
    • (2002) Cell Death Differ. , vol.9 , pp. 643-650
    • Hortelano, S.1    Zeini, M.2    Castrillo, A.3    Alvarez, A.M.4    Bosca, L.5
  • 254
    • 29144449807 scopus 로고    scopus 로고
    • Roles of volume-sensitive Cl- channel in cisplatin-induced apoptosis in human epidermoid cancer cells
    • T. Ise, T. Shimizu, E.L. Lee, H. Inoue, K. Kohno, and Y. Okada Roles of volume-sensitive Cl- channel in cisplatin-induced apoptosis in human epidermoid cancer cells J. Membr. Biol. 205 2005 139 145
    • (2005) J. Membr. Biol. , vol.205 , pp. 139-145
    • Ise, T.1    Shimizu, T.2    Lee, E.L.3    Inoue, H.4    Kohno, K.5    Okada, Y.6
  • 255
    • 34147208877 scopus 로고    scopus 로고
    • Impaired activity of volume-sensitive Cl- channel is involved in cisplatin resistance of cancer cells
    • E.L. Lee, T. Shimizu, T. Ise, T. Numata, K. Kohno, and Y. Okada Impaired activity of volume-sensitive Cl- channel is involved in cisplatin resistance of cancer cells J. Cell. Physiol. 211 2007 513 521
    • (2007) J. Cell. Physiol. , vol.211 , pp. 513-521
    • Lee, E.L.1    Shimizu, T.2    Ise, T.3    Numata, T.4    Kohno, K.5    Okada, Y.6
  • 256
    • 79958843174 scopus 로고    scopus 로고
    • Dysfunction of volume-sensitive chloride channels contributes to cisplatin resistance in human lung adenocarcinoma cells
    • X.J. Min, H. Li, S.C. Hou, W. He, J. Liu, B. Hu, and J. Wang Dysfunction of volume-sensitive chloride channels contributes to cisplatin resistance in human lung adenocarcinoma cells Exp. Biol. Med. (Maywood) 236 2011 483 491
    • (2011) Exp. Biol. Med. (Maywood) , vol.236 , pp. 483-491
    • Min, X.J.1    Li, H.2    Hou, S.C.3    He, W.4    Liu, J.5    Hu, B.6    Wang, J.7
  • 257
    • 0031456376 scopus 로고    scopus 로고
    • Molecular identification of a volume-regulated chloride channel
    • D. Duan, C. Winter, S. Cowley, J.R. Hume, and B. Horowitz Molecular identification of a volume-regulated chloride channel Nature 390 1997 417 421
    • (1997) Nature , vol.390 , pp. 417-421
    • Duan, D.1    Winter, C.2    Cowley, S.3    Hume, J.R.4    Horowitz, B.5
  • 258
    • 0037131278 scopus 로고    scopus 로고
    • ClC-3 is a fundamental molecular component of volume-sensitive outwardly rectifying Cl- channels and volume regulation in HeLa cells and Xenopus laevis oocytes
    • M. Hermoso, C.M. Satterwhite, Y.N. Andrade, J. Hidalgo, S.M. Wilson, B. Horowitz, and J.R. Hume ClC-3 is a fundamental molecular component of volume-sensitive outwardly rectifying Cl- channels and volume regulation in HeLa cells and Xenopus laevis oocytes J. Biol. Chem. 277 2002 40066 40074
    • (2002) J. Biol. Chem. , vol.277 , pp. 40066-40074
    • Hermoso, M.1    Satterwhite, C.M.2    Andrade, Y.N.3    Hidalgo, J.4    Wilson, S.M.5    Horowitz, B.6    Hume, J.R.7
  • 260
    • 21244443790 scopus 로고    scopus 로고
    • Alterations in the regulatory volume decrease (RVD) and swelling-activated Cl-- current associated with neuroendocrine differentiation of prostate cancer epithelial cells
    • L. Lemonnier, R. Lazarenko, Y. Shuba, S. Thebault, M. Roudbaraki, G. Lepage, N. Prevarskaya, and R. Skryma Alterations in the regulatory volume decrease (RVD) and swelling-activated Cl-- current associated with neuroendocrine differentiation of prostate cancer epithelial cells Endocr. Relat. Cancer 12 2005 335 349
    • (2005) Endocr. Relat. Cancer , vol.12 , pp. 335-349
    • Lemonnier, L.1    Lazarenko, R.2    Shuba, Y.3    Thebault, S.4    Roudbaraki, M.5    Lepage, G.6    Prevarskaya, N.7    Skryma, R.8
  • 261
    • 36348982335 scopus 로고    scopus 로고
    • Involvement of chloride channels in TGF-beta1-induced apoptosis of human bronchial epithelial cells
    • G. Cheng, Z. Shao, B. Chaudhari, and D.K. Agrawal Involvement of chloride channels in TGF-beta1-induced apoptosis of human bronchial epithelial cells Am. J. Physiol. Lung Cell. Mol. Physiol. 293 2007 L1339 1347
    • (2007) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.293 , pp. L1339-1347
    • Cheng, G.1    Shao, Z.2    Chaudhari, B.3    Agrawal, D.K.4
  • 267
    • 84878648060 scopus 로고    scopus 로고
    • TMEM16F is a component of a Ca2 + -activated Cl- channel but not a volume-sensitive outwardly rectifying Cl- channel
    • T. Shimizu, T. Iehara, K. Sato, T. Fujii, H. Sakai, and Y. Okada TMEM16F is a component of a Ca2 + -activated Cl- channel but not a volume-sensitive outwardly rectifying Cl- channel Am. J. Physiol. Cell Physiol. 304 2013 C748 759
    • (2013) Am. J. Physiol. Cell Physiol. , vol.304 , pp. C748-759
    • Shimizu, T.1    Iehara, T.2    Sato, K.3    Fujii, T.4    Sakai, H.5    Okada, Y.6
  • 268
    • 84891763415 scopus 로고    scopus 로고
    • Anoctamin 6 differs from VRAC and VSOAC but is involved in apoptosis and supports volume regulation in the presence of Ca
    • C.A. Juul, S. Grubb, K.A. Poulsen, T. Kyed, N. Hashem, I.H. Lambert, E.H. Larsen, and E.K. Hoffmann Anoctamin 6 differs from VRAC and VSOAC but is involved in apoptosis and supports volume regulation in the presence of Ca Pflugers Arch. 466 2014 1899 1910
    • (2014) Pflugers Arch. , vol.466 , pp. 1899-1910
    • Juul, C.A.1    Grubb, S.2    Poulsen, K.A.3    Kyed, T.4    Hashem, N.5    Lambert, I.H.6    Larsen, E.H.7    Hoffmann, E.K.8
  • 269
    • 78650172970 scopus 로고    scopus 로고
    • Calcium-dependent phospholipid scrambling by TMEM16F
    • J. Suzuki, M. Umeda, P.J. Sims, and S. Nagata Calcium-dependent phospholipid scrambling by TMEM16F Nature 468 2010 834 838
    • (2010) Nature , vol.468 , pp. 834-838
    • Suzuki, J.1    Umeda, M.2    Sims, P.J.3    Nagata, S.4
  • 270
    • 84887468749 scopus 로고    scopus 로고
    • Role of CFTR in oxidative stress and suicidal death of renal cells during cisplatin-induced nephrotoxicity
    • I. Rubera, C. Duranton, N. Melis, M. Cougnon, B. Mograbi, and M. Tauc Role of CFTR in oxidative stress and suicidal death of renal cells during cisplatin-induced nephrotoxicity Cell Death Dis. 4 2013 e817
    • (2013) Cell Death Dis. , vol.4 , pp. e817
    • Rubera, I.1    Duranton, C.2    Melis, N.3    Cougnon, M.4    Mograbi, B.5    Tauc, M.6
  • 271


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