메뉴 건너뛰기




Volumn 107, Issue 6, 2010, Pages 689-699

Two close, too close: Sarcoplasmic reticulum-mitochondrial crosstalk and cardiomyocyte fate

Author keywords

apoptosis; calcium; endoplasmic reticulum; mitochondrial fusion; mitochondrial permeability transition

Indexed keywords

CALCIUM ION; MITOFUSIN 1; PROTEIN BCL 2;

EID: 77957284223     PISSN: 00097330     EISSN: 15244571     Source Type: Journal    
DOI: 10.1161/CIRCRESAHA.110.225714     Document Type: Review
Times cited : (66)

References (136)
  • 1
    • 68649092333 scopus 로고    scopus 로고
    • The Role of Ca(2 +) Signaling in the Coordination of Mitochondrial ATP Production with Cardiac Work
    • Balaban RS. The role of Ca(2 +) signaling in the coordination of mitochondrial ATP production with cardiac work. Biochim Biophys Acta. 2009;1787:1334-1341.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 1334-1341
    • Balaban, R.S.1
  • 2
    • 67349222523 scopus 로고    scopus 로고
    • Controlling metabolism and cell death: At the heart of mitochondrial calcium signalling
    • Murgia M, Giorgi C, Pinton P, Rizzuto R. Controlling metabolism and cell death: at the heart of mitochondrial calcium signalling. J Mol Cell Cardiol. 2009;46:781-788.
    • (2009) J Mol Cell Cardiol , vol.46 , pp. 781-788
    • Murgia, M.1    Giorgi, C.2    Pinton, P.3    Rizzuto, R.4
  • 4
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 1997; 91:479-489.
    • (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
  • 5
    • 0030900980 scopus 로고    scopus 로고
    • Intracellular adenosine triphosphate (ATP) concentration: A switch in the decision between apoptosis and necrosis
    • Leist M, Single B, Castoldi AF, KÅhnle S, Nicotera P. Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis. J Exp Med. 1997;185:1481-1486.
    • (1997) J Exp Med , vol.185 , pp. 1481-1486
    • Leist, M.1    Single, B.2    Castoldi, A.F.3    Kåhnle, S.4    Nicotera, P.5
  • 6
    • 0030915587 scopus 로고    scopus 로고
    • Intracellular ATP levels determine cell death fate by apoptosis or necrosis
    • Eguchi Y, Shimizu S, Tsujimoto Y. Intracellular ATP levels determine cell death fate by apoptosis or necrosis. Cancer Res. 1997;57: 1835-1840. (Pubitemid 27209706)
    • (1997) Cancer Research , vol.57 , Issue.10 , pp. 1835-1840
    • Eguchi, Y.1    Shimizu, S.2    Tsujimoto, Y.3
  • 7
    • 27344438327 scopus 로고    scopus 로고
    • Cells die with increased cytosolic ATP during apoptosis: A bioluminescence study with intracellular luciferase
    • Zamaraeva MV, Sabirov RZ, Maeno E, Ando-Akatsuka Y, Bessonova SV, Okada Y. Cells die with increased cytosolic ATP during apoptosis: a bioluminescence study with intracellular luciferase. Cell Death Differ. 2005;12:1390-1397.
    • (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
  • 8
    • 33746620461 scopus 로고    scopus 로고
    • (De) constructing mitochondria: What for?
    • Dimmer KS, Scorrano L. (De)constructing mitochondria: what for? Physiology (Bethesda). 2006;21:233-241.
    • (2006) Physiology (Bethesda) , vol.21 , pp. 233-241
    • Dimmer, K.S.1    Scorrano, L.2
  • 9
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner MO. The biochemistry of apoptosis. Nature. 2000;407: 770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 10
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • Danial NN, Korsmeyer SJ. Cell death: critical control points. Cell. 2004;116:205-219.
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 13
    • 0028047262 scopus 로고
    • Dynamics of mitochondria in living cells: Shape changes, dislocations, fusion, and fission of mitochondria
    • Bereiter-Hahn J, Voth M. Dynamics of mitochondria in living cells: shape changes, dislocations, fusion, and fission of mitochondria. Microsc Res Tech. 1994;27:198-219.
    • (1994) Microsc Res Tech , vol.27 , pp. 198-219
    • Bereiter-Hahn, J.1    Voth, M.2
  • 14
    • 0034235229 scopus 로고    scopus 로고
    • The internal structure of mitochondria
    • Frey TG, Mannella CA. The internal structure of mitochondria. Trends Biochem Sci. 2000;25:319-324.
    • (2000) Trends Biochem Sci , vol.25 , pp. 319-324
    • Frey, T.G.1    Mannella, C.A.2
  • 15
    • 0035166814 scopus 로고    scopus 로고
    • Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells
    • Smirnova E, Griparic L, Shurland DL, van der Bliek AM. Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol Biol Cell. 2001;12:2245-2256.
    • (2001) Mol Biol Cell , vol.12 , pp. 2245-2256
    • Smirnova, E.1    Griparic, L.2    Shurland, D.L.3    Van Der Bliek, A.M.4
  • 16
    • 0033231549 scopus 로고    scopus 로고
    • C. elegans dynamin-related protein DRP-1 controls severing of the mitochondrial outer membrane
    • Labrousse AM, Zappaterra MD, Rube DA, van der Bliek AM. C. elegans dynamin-related protein DRP-1 controls severing of the mitochondrial outer membrane. Mol Cell. 1999;4:815-826.
    • (1999) Mol Cell , vol.4 , pp. 815-826
    • Labrousse, A.M.1    Zappaterra, M.D.2    Rube, D.A.3    Van Der Bliek, A.M.4
  • 17
    • 0141592470 scopus 로고    scopus 로고
    • HFis1, a novel component of the mammalian mitochondrial fission machinery
    • James DI, Parone PA, Mattenberger Y, Martinou JC. hFis1, a novel component of the mammalian mitochondrial fission machinery. J Biol Chem. 2003;278:36373-36379.
    • (2003) J Biol Chem , vol.278 , pp. 36373-36379
    • James, D.I.1    Parone, P.A.2    Mattenberger, Y.3    Martinou, J.C.4
  • 19
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p
    • Mozdy AD, McCaffery JM, Shaw JM. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J Cell Biol. 2000;151:367-380.
    • (2000) J Cell Biol , vol.151 , pp. 367-380
    • Mozdy, A.D.1    McCaffery, J.M.2    Shaw, J.M.3
  • 20
    • 0043092647 scopus 로고    scopus 로고
    • The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1
    • Yoon Y, Krueger EW, Oswald BJ, McNiven MA. The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1. Mol Cell Biol. 2003;23:5409-5420.
    • (2003) Mol Cell Biol , vol.23 , pp. 5409-5420
    • Yoon, Y.1    Krueger, E.W.2    Oswald, B.J.3    McNiven, M.A.4
  • 22
    • 34848840991 scopus 로고    scopus 로고
    • Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death
    • Cribbs JT, Strack S. Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death. EMBO Rep. 2007;8:939-944.
    • (2007) EMBO Rep , vol.8 , pp. 939-944
    • Cribbs, J.T.1    Strack, S.2
  • 23
    • 34547611925 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology
    • Chang CR, Blackstone C. Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology. J Biol Chem. 2007;282:21583-21587.
    • (2007) J Biol Chem , vol.282 , pp. 21583-21587
    • Chang, C.R.1    Blackstone, C.2
  • 24
    • 34249689057 scopus 로고    scopus 로고
    • Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission
    • Taguchi N, Ishihara N, Jofuku A, Oka T, Mihara K. Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission. J Biol Chem. 2007;282:11521-11529.
    • (2007) J Biol Chem , vol.282 , pp. 11521-11529
    • Taguchi, N.1    Ishihara, N.2    Jofuku, A.3    Oka, T.4    Mihara, K.5
  • 26
    • 1542380494 scopus 로고    scopus 로고
    • Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission
    • Harder Z, Zunino R, McBride H. Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission. Curr Biol. 2004;14: 340-345.
    • (2004) Curr Biol , vol.14 , pp. 340-345
    • Harder, Z.1    Zunino, R.2    McBride, H.3
  • 27
    • 34248182897 scopus 로고    scopus 로고
    • Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death
    • Wasiak S, Zunino R, McBride HM. Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death. J Cell Biol. 2007;177:439-450.
    • (2007) J Cell Biol , vol.177 , pp. 439-450
    • Wasiak, S.1    Zunino, R.2    McBride, H.M.3
  • 28
    • 4644242944 scopus 로고    scopus 로고
    • Endophilin B1 is required for the maintenance of mitochondrial morphology
    • Karbowski M, Jeong SY, Youle RJ. Endophilin B1 is required for the maintenance of mitochondrial morphology. J Cell Biol. 2004;166: 1027-1039.
    • (2004) J Cell Biol , vol.166 , pp. 1027-1039
    • Karbowski, M.1    Jeong, S.Y.2    Youle, R.J.3
  • 30
    • 0037089084 scopus 로고    scopus 로고
    • Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo
    • Rojo M, Legros F, Chateau D, Lombes A. Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo. J Cell Sci. 2002;115:1663-1674.
    • (2002) J Cell Sci , vol.115 , pp. 1663-1674
    • Rojo, M.1    Legros, F.2    Chateau, D.3    Lombes, A.4
  • 31
    • 13444287961 scopus 로고    scopus 로고
    • Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity
    • Ishihara N, Eura Y, Mihara K. Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity. J Cell Sci. 2004; 117:6535-6546.
    • (2004) J Cell Sci , vol.117 , pp. 6535-6546
    • Ishihara, N.1    Eura, Y.2    Mihara, K.3
  • 34
    • 0142058391 scopus 로고    scopus 로고
    • Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion
    • Eura Y, Ishihara N, Yokota S, Mihara K. Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion. J Biochem. 2003;134:333-344.
    • (2003) J Biochem , vol.134 , pp. 333-344
    • Eura, Y.1    Ishihara, N.2    Yokota, S.3    Mihara, K.4
  • 38
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • De Brito OM, Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature. 2008;456:605-610.
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 41
    • 0033535345 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria during apoptosis of NGF-deprived sympathetic neurons is a reversible event
    • Martinou I, Desagher S, Eskes R, Antonsson B, Andre E, Fakan S, Martinou JC. The release of cytochrome c from mitochondria during apoptosis of NGF-deprived sympathetic neurons is a reversible event. J Cell Biol. 1999;144:883-889.
    • (1999) J Cell Biol , vol.144 , pp. 883-889
    • Martinou, I.1    Desagher, S.2    Eskes, R.3    Antonsson, B.4    Andre, E.5    Fakan, S.6    Martinou, J.C.7
  • 42
    • 6344274848 scopus 로고    scopus 로고
    • Roles of the mammalian mitochondrial fission and fusion mediators Fis1 Drp1 and Opa1 in apoptosis
    • Lee YJ, Jeong SY, Karbowski M, Smith CL, Youle RJ. Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis. Mol Biol Cell. 2004;15:5001-5011.
    • (2004) Mol Biol Cell , vol.15 , pp. 5001-5011
    • Lee, Y.J.1    Jeong, S.Y.2    Karbowski, M.3    Smith, C.L.4    Youle, R.J.5
  • 43
    • 13944278072 scopus 로고    scopus 로고
    • DRP-1-mediated mito-chondrial fragmentation during EGL-1-induced cell death in C. elegans
    • Jagasia R, Grote P, Westermann B, Conradt B. DRP-1-mediated mito-chondrial fragmentation during EGL-1-induced cell death in C. elegans. Nature. 2005;433:754-760.
    • (2005) Nature , vol.433 , pp. 754-760
    • Jagasia, R.1    Grote, P.2    Westermann, B.3    Conradt, B.4
  • 44
    • 1242307475 scopus 로고    scopus 로고
    • Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis
    • Karbowski M, Arnoult D, Chen H, Chan DC, Smith CL, Youle RJ. Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis. J Cell Biol. 2004;164:493-499.
    • (2004) J Cell Biol , vol.164 , pp. 493-499
    • Karbowski, M.1    Arnoult, D.2    Chen, H.3    Chan, D.C.4    Smith, C.L.5    Youle, R.J.6
  • 45
    • 27444446030 scopus 로고    scopus 로고
    • Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation
    • Arnoult D, Grodet A, Lee YJ, Estaquier J, Blackstone C. Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation. J Biol Chem. 2005;280:35742-35750.
    • (2005) J Biol Chem , vol.280 , pp. 35742-35750
    • Arnoult, D.1    Grodet, A.2    Lee, Y.J.3    Estaquier, J.4    Blackstone, C.5
  • 46
    • 28444487509 scopus 로고    scopus 로고
    • Bax/Bak-dependent release of DDP/TIMM8a promotes Drp1-mediated mitochondrial fission and mitoptosis during programmed cell death
    • Arnoult D, Rismanchi N, Grodet A, Roberts RG, Seeburg DP, Estaquier J, Sheng M, Blackstone C. Bax/Bak-dependent release of DDP/TIMM8a promotes Drp1-mediated mitochondrial fission and mitoptosis during programmed cell death. Curr Biol. 2005;15:2112-2118.
    • (2005) Curr Biol , vol.15 , pp. 2112-2118
    • Arnoult, D.1    Rismanchi, N.2    Grodet, A.3    Roberts, R.G.4    Seeburg, D.P.5    Estaquier, J.6    Sheng, M.7    Blackstone, C.8
  • 47
    • 18444400187 scopus 로고    scopus 로고
    • Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis
    • Germain M, Mathai JP, McBride HM, Shore GC. Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis. EMBO J. 2005;24:1546-1556.
    • (2005) EMBO J , vol.24 , pp. 1546-1556
    • Germain, M.1    Mathai, J.P.2    McBride, H.M.3    Shore, G.C.4
  • 48
    • 0037417334 scopus 로고    scopus 로고
    • Caspase cleavage product of BAP31 induces mitochondrial fission through endo-plasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
    • Breckenridge DG, Stojanovic M, Marcellus RC, Shore GC. Caspase cleavage product of BAP31 induces mitochondrial fission through endo-plasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol. J Cell Biol. 2003;160:1115-1127.
    • (2003) J Cell Biol , vol.160 , pp. 1115-1127
    • Breckenridge, D.G.1    Stojanovic, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 49
    • 33750526651 scopus 로고    scopus 로고
    • The mitochondrial fission protein hFis1 requires the endo-plasmic reticulum gateway to induce apoptosis
    • Alirol E, James D, Huber D, Marchetto A, Vergani L, Martinou JC, Scorrano L. The mitochondrial fission protein hFis1 requires the endo-plasmic reticulum gateway to induce apoptosis. Mol Biol Cell. 2006;17: 4593-4605.
    • (2006) Mol Biol Cell , vol.17 , pp. 4593-4605
    • Alirol, E.1    James, D.2    Huber, D.3    Marchetto, A.4    Vergani, L.5    Martinou, J.C.6    Scorrano, L.7
  • 50
    • 4944222095 scopus 로고    scopus 로고
    • Drp-1-dependent division of the mitochondrial network blocks intraorganellar Ca2 + waves and protects against Ca2 +-mediated apoptosis
    • Szabadkai G, Simoni AM, Chami M, Wieckowski MR, Youle RJ, Rizzuto R. Drp-1-dependent division of the mitochondrial network blocks intraorganellar Ca2 + waves and protects against Ca2 +-mediated apoptosis. Mol Cell. 2004;16:59-68.
    • (2004) Mol Cell , vol.16 , pp. 59-68
    • Szabadkai, G.1    Simoni, A.M.2    Chami, M.3    Wieckowski, M.R.4    Youle, R.J.5    Rizzuto, R.6
  • 51
    • 38849094092 scopus 로고    scopus 로고
    • Stressed out: The skeletal muscle ryanodine receptor as a target of stress
    • Bellinger AM, Mongillo M, Marks AR. Stressed out: the skeletal muscle ryanodine receptor as a target of stress. J Clin Invest. 2008;118: 445-453.
    • (2008) J Clin Invest , vol.118 , pp. 445-453
    • Bellinger, A.M.1    Mongillo, M.2    Marks, A.R.3
  • 52
    • 33845665302 scopus 로고    scopus 로고
    • Regulation of Ca2 + and Na+ in normal and failing cardiac myocytes
    • Bers DM, Despa S, Bossuyt J. Regulation of Ca2 + and Na+ in normal and failing cardiac myocytes. Ann N Y Acad Sci. 2006;1080:165-177.
    • (2006) Ann N y Acad Sci , vol.1080 , pp. 165-177
    • Bers, D.M.1    Despa, S.2    Bossuyt, J.3
  • 53
    • 33751065132 scopus 로고    scopus 로고
    • Reversal of calcium cycling defects in advanced heart failure toward molecular therapy
    • Hoshijima M, Knoll R, Pashmforoush M, Chien KR. Reversal of calcium cycling defects in advanced heart failure toward molecular therapy. J Am Coll Cardiol. 2006;48:A15-23.
    • (2006) J Am Coll Cardiol , vol.48
    • Hoshijima, M.1    Knoll, R.2    Pashmforoush, M.3    Chien, K.R.4
  • 58
    • 76349084460 scopus 로고    scopus 로고
    • Phospholamban ablation rescues sarcoplasmic reticulum Ca(2 +) handling but exacerbates cardiac dysfunction in CaMKIIdelta(C) transgenic mice
    • Zhang T, Guo T, Mishra S, Dalton ND, Kranias EG, Peterson KL, Bers DM, Brown JH. Phospholamban ablation rescues sarcoplasmic reticulum Ca(2 +) handling but exacerbates cardiac dysfunction in CaMKIIdelta(C) transgenic mice. Circ Res. 2010;106:354-362.
    • (2010) Circ Res , vol.106 , pp. 354-362
    • Zhang, T.1    Guo, T.2    Mishra, S.3    Dalton, N.D.4    Kranias, E.G.5    Peterson, K.L.6    Bers, D.M.7    Brown, J.H.8
  • 59
    • 0012300264 scopus 로고    scopus 로고
    • Re-evaluating sarcoplasmic reticulum function in heart failure
    • Delling U, Sussman MA, Molkentin JD. Re-evaluating sarcoplasmic reticulum function in heart failure. Nat Med. 2000;6:942-943.
    • (2000) Nat Med , vol.6 , pp. 942-943
    • Delling, U.1    Sussman, M.A.2    Molkentin, J.D.3
  • 60
    • 0037307565 scopus 로고    scopus 로고
    • Ablation of PLB exacerbates ischemic injury to a lesser extent in female than male mice: Protective role of NO
    • Cross HR, Kranias EG, Murphy E, Steenbergen C. Ablation of PLB exacerbates ischemic injury to a lesser extent in female than male mice: protective role of NO. Am J Physiol Heart Circ Physiol. 2003;284: H683-H690.
    • (2003) Am J Physiol Heart Circ Physiol , vol.284
    • Cross, H.R.1    Kranias, E.G.2    Murphy, E.3    Steenbergen, C.4
  • 62
    • 9444225488 scopus 로고    scopus 로고
    • Adenoviral SERCA1 overexpression triggers an apoptotic response in cultured neonatal but not in adult rat cardiomyocytes
    • Wu G, Long X, Marin-Garcia J. Adenoviral SERCA1 overexpression triggers an apoptotic response in cultured neonatal but not in adult rat cardiomyocytes. Mol Cell Biochem. 2004;267:123-132.
    • (2004) Mol Cell Biochem , vol.267 , pp. 123-132
    • Wu, G.1    Long, X.2    Marin-Garcia, J.3
  • 64
    • 33644686649 scopus 로고    scopus 로고
    • Ca2 + dysregulation induces mitochondrial depolarization and apoptosis: Role of Na +/Ca2+ exchanger and AKT
    • Miyamoto S, Howes AL, Adams JW, Dorn GW II, Brown JH. Ca2 + dysregulation induces mitochondrial depolarization and apoptosis: role of Na +/Ca2+ exchanger and AKT. J Biol Chem. 2005;280: 38505-38512.
    • (2005) J Biol Chem , vol.280 , pp. 38505-38512
    • Miyamoto, S.1    Howes, A.L.2    Adams, J.W.3    Dorn, G.W.I.I.4    Brown, J.H.5
  • 66
    • 67349101773 scopus 로고    scopus 로고
    • Mitochondrial free calcium regulation during sarcoplasmic reticulum calcium release in rat cardiac myocytes
    • Andrienko TN, Picht E, Bers DM. Mitochondrial free calcium regulation during sarcoplasmic reticulum calcium release in rat cardiac myocytes. J Mol Cell Cardiol. 2009;46:1027-1036.
    • (2009) J Mol Cell Cardiol , vol.46 , pp. 1027-1036
    • Andrienko, T.N.1    Picht, E.2    Bers, D.M.3
  • 67
    • 59849110194 scopus 로고    scopus 로고
    • Autophagy in ischemic heart disease
    • Gustafsson AB, Gottlieb RA. Autophagy in ischemic heart disease. Circ Res. 2009;104:150-158.
    • (2009) Circ Res , vol.104 , pp. 150-158
    • Gustafsson, A.B.1    Gottlieb, R.A.2
  • 68
    • 58149396003 scopus 로고    scopus 로고
    • Autophagy in load-induced heart disease
    • Rothermel BA, Hill JA. Autophagy in load-induced heart disease. Circ Res. 2008;103:1363-1369.
    • (2008) Circ Res , vol.103 , pp. 1363-1369
    • Rothermel, B.A.1    Hill, J.A.2
  • 69
    • 59449098471 scopus 로고    scopus 로고
    • Apoptotic and non-apoptotic programmed cardiomyocyte death in ventricular remodelling
    • Dorn GW II. Apoptotic and non-apoptotic programmed cardiomyocyte death in ventricular remodelling. Cardiovasc Res. 2009;81:465-473.
    • (2009) Cardiovasc Res , vol.81 , pp. 465-473
    • Dorn, G.W.I.I.1
  • 70
    • 14644413468 scopus 로고    scopus 로고
    • Death begets failure in the heart
    • Foo RS, Mani K, Kitsis RN. Death begets failure in the heart. J Clin Invest. 2005;115:565-571.
    • (2005) J Clin Invest , vol.115 , pp. 565-571
    • Foo, R.S.1    Mani, K.2    Kitsis, R.N.3
  • 71
    • 0018332597 scopus 로고
    • The Ca 2+-induced membrane transition in mitochondria. II. Nature of the Ca 2+ trigger site
    • Haworth RA, Hunter DR. The Ca 2+-induced membrane transition in mitochondria. II. Nature of the Ca 2+ trigger site. Arch Biochem Biophys. 1979;195:460-467.
    • (1979) Arch Biochem Biophys , vol.195 , pp. 460-467
    • Haworth, R.A.1    Hunter, D.R.2
  • 73
    • 0025195033 scopus 로고
    • A heart mitochondrial Ca2(+)-dependent pore of possible relevance to re-perfusion-induced injury. Evidence that ADP facilitates pore interconversion between the closed and open states
    • Crompton M, Costi A. A heart mitochondrial Ca2(+)-dependent pore of possible relevance to re-perfusion-induced injury. Evidence that ADP facilitates pore interconversion between the closed and open states. Biochem J. 1990;266:33-39.
    • (1990) Biochem J , vol.266 , pp. 33-39
    • Crompton, M.1    Costi, A.2
  • 75
    • 68649090703 scopus 로고    scopus 로고
    • The role of the mitochondrial permeability transition pore in heart disease
    • Halestrap AP, Pasdois P. The role of the mitochondrial permeability transition pore in heart disease. Biochim Biophys Acta. 2009;1787: 1402-1415.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 1402-1415
    • Halestrap, A.P.1    Pasdois, P.2
  • 76
    • 70349105567 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore opening as a promising therapeutic target in cardiac diseases
    • Javadov S, Karmazyn M, Escobales N. Mitochondrial permeability transition pore opening as a promising therapeutic target in cardiac diseases. J Pharm Exp Ther. 2009;330:670-678.
    • (2009) J Pharm Exp Ther , vol.330 , pp. 670-678
    • Javadov, S.1    Karmazyn, M.2    Escobales, N.3
  • 77
    • 0027236162 scopus 로고
    • The mitochondrial permeability transition pore may comprise VDAC molecules. II. the electrophysiological properties of VDAC are compatible with those of the mitochondrial megachannel
    • Szabo I, De Pinto V, Zoratti M. The mitochondrial permeability transition pore may comprise VDAC molecules. II. The electrophysiological properties of VDAC are compatible with those of the mitochondrial megachannel. FEBS Lett. 1993;330:206-210.
    • (1993) FEBS Lett , vol.330 , pp. 206-210
    • Szabo, I.1    De Pinto, V.2    Zoratti, M.3
  • 78
    • 0030569305 scopus 로고    scopus 로고
    • Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore
    • Beutner G, Ruck A, Riede B, Welte W, Brdiczka D. Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore. FEBS Lett. 1996;396: 189-195.
    • (1996) FEBS Lett , vol.396 , pp. 189-195
    • Beutner, G.1    Ruck, A.2    Riede, B.3    Welte, W.4    Brdiczka, D.5
  • 83
    • 67349164323 scopus 로고    scopus 로고
    • Adenine nucleotide translocase-1 induces cardiomyocyte death through upregulation of the pro-apoptotic protein Bax
    • Baines CP, Molkentin JD. Adenine nucleotide translocase-1 induces cardiomyocyte death through upregulation of the pro-apoptotic protein Bax. J Mol Cell Cardiol. 2009;46:969-977.
    • (2009) J Mol Cell Cardiol , vol.46 , pp. 969-977
    • Baines, C.P.1    Molkentin, J.D.2
  • 84
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial- dependent cell death
    • Baines CP, Kaiser RA, Sheiko T, Craigen WJ, Molkentin JD. Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death. Nat Cell Biol. 2007;9:550-555.
    • (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
  • 86
    • 0025193488 scopus 로고
    • Inhibition of Ca2(+)-induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-trans isomerase and preventing it interacting with the adenine nucleotide translocase
    • Halestrap AP, Davidson AM. Inhibition of Ca2(+)-induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-trans isomerase and preventing it interacting with the adenine nucleotide translocase. Biochem J. 1990;268:153-160.
    • (1990) Biochem J , vol.268 , pp. 153-160
    • Halestrap, A.P.1    Davidson, A.M.2
  • 92
    • 77953389460 scopus 로고    scopus 로고
    • Targeting cyclophilin D and the mitochondrial permeability transition enhances/3-cell survival and prevents diabetes in Pdx1 deficiency
    • Fujimoto K, Chen Y, Polonsky KS, Dorn GW II. Targeting cyclophilin D and the mitochondrial permeability transition enhances/3-cell survival and prevents diabetes in Pdx1 deficiency. Proc Natl Acad Sci USA. 2010;107:10214-10219.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 10214-10219
    • Fujimoto, K.1    Chen, Y.2    Polonsky, K.S.3    Dorn, G.W.I.I.4
  • 93
    • 77952683069 scopus 로고    scopus 로고
    • Dual autonomous mitochondrial cell death pathways are activated by Nix/BNip3L and induce cardiomyopathy
    • Chen Y, Lewis W, Diwan A, Cheng EH, Matkovich SJ, Dorn GW II. Dual autonomous mitochondrial cell death pathways are activated by Nix/BNip3L and induce cardiomyopathy. Proc Natl Acad Sci USA. 2010;107:9035-9042.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 9035-9042
    • Chen, Y.1    Lewis, W.2    Diwan, A.3    Cheng, E.H.4    Matkovich, S.J.5    Dorn, G.W.I.I.6
  • 94
    • 21244446551 scopus 로고    scopus 로고
    • Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D
    • Basso E, Fante L, Fowlkes J, Petronilli V, Forte MA, Bernardi P. Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D. J Biol Chem. 2005;280:18558-18561.
    • (2005) J Biol Chem , vol.280 , pp. 18558-18561
    • Basso, E.1    Fante, L.2    Fowlkes, J.3    Petronilli, V.4    Forte, M.A.5    Bernardi, P.6
  • 95
    • 55549126837 scopus 로고    scopus 로고
    • Phosphate is essential for inhibition of the mitochondrial permeability transition pore by cyclosporin A and by cyclophilin D ablation
    • Basso E, Petronilli V, Forte MA, Bernardi P. Phosphate is essential for inhibition of the mitochondrial permeability transition pore by cyclosporin A and by cyclophilin D ablation. J Biol Chem. 2008;283: 26307-26311.
    • (2008) J Biol Chem , vol.283 , pp. 26307-26311
    • Basso, E.1    Petronilli, V.2    Forte, M.A.3    Bernardi, P.4
  • 97
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle RJ, Strasser A. The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol. 2008;9:47-59.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 98
    • 0034523818 scopus 로고    scopus 로고
    • Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c
    • Korsmeyer SJ, Wei MC, Saito M, Weiler S, Oh KJ, Schlesinger PH. Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell Death Differ. 2000;7:1166-1173.
    • (2000) Cell Death Differ , vol.7 , pp. 1166-1173
    • Korsmeyer, S.J.1    Wei, M.C.2    Saito, M.3    Weiler, S.4    Oh, K.J.5    Schlesinger, P.H.6
  • 99
    • 48049100572 scopus 로고    scopus 로고
    • Dynamics and structure of the Bax-Bak complex responsible for releasing mitochondrial proteins during apoptosis
    • Zhou L, Chang DC. Dynamics and structure of the Bax-Bak complex responsible for releasing mitochondrial proteins during apoptosis. J Cell Sci. 2008;121:2186-2196.
    • (2008) J Cell Sci , vol.121 , pp. 2186-2196
    • Zhou, L.1    Chang, D.C.2
  • 100
    • 57149135309 scopus 로고    scopus 로고
    • Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax
    • Lovell JF, Billen LP, Bindner S, Shamas-Din A, Fradin C, Leber B, Andrews DW. Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax. Cell. 2008; 135:1074-1084.
    • (2008) Cell , vol.135 , pp. 1074-1084
    • Lovell, J.F.1    Billen, L.P.2    Bindner, S.3    Shamas-Din, A.4    Fradin, C.5    Leber, B.6    Andrews, D.W.7
  • 101
    • 68149142474 scopus 로고    scopus 로고
    • Cardiac reanimation: Targeting cardiomyocyte death by BNIP3 and NIX/BNIP3L
    • Dorn GW II, Kirshenbaum LA. Cardiac reanimation: targeting cardiomyocyte death by BNIP3 and NIX/BNIP3L. Oncogene. 2008; 27(Suppl 1):S158-S167.
    • (2008) Oncogene , vol.27 , Issue.SUPPL. 1
    • Dorn, G.W.I.I.1    Kirshenbaum, L.A.2
  • 108
    • 38349184844 scopus 로고    scopus 로고
    • Nix-mediated apoptosis links myocardial fibrosis, cardiac remodeling, and hypertrophy decompensation
    • Diwan A, Wansapura J, Syed FM, Matkovich SJ, Lorenz JN, Dorn GW II. Nix-mediated apoptosis links myocardial fibrosis, cardiac remodeling, and hypertrophy decompensation. Circulation. 2008;117: 396-404.
    • (2008) Circulation , vol.117 , pp. 396-404
    • Diwan, A.1    Wansapura, J.2    Syed, F.M.3    Matkovich, S.J.4    Lorenz, J.N.5    Dorn, G.W.I.I.6
  • 111
    • 0037088658 scopus 로고    scopus 로고
    • Bax and Bak promote apoptosis by modulating endoplasmic reticular and mitochondrial Ca 2+ stores
    • Nutt LK, Pataer A, Pahler J, Fang B, Roth J, McConkey DJ, Swisher SG. Bax and Bak promote apoptosis by modulating endoplasmic reticular and mitochondrial Ca 2+ stores. J Biol Chem. 2002;277:9219-9225.
    • (2002) J Biol Chem , vol.277 , pp. 9219-9225
    • Nutt, L.K.1    Pataer, A.2    Pahler, J.3    Fang, B.4    Roth, J.5    McConkey, D.J.6    Swisher, S.G.7
  • 113
    • 0038643573 scopus 로고    scopus 로고
    • The deltaC isoform of CaMKII is activated in cardiac hypertrophy and induces dilated cardiomyopathy and heart failure
    • Zhang T, Maier LS, Dalton ND, Miyamoto S, Ross J Jr, Bers DM, Brown JH. The deltaC isoform of CaMKII is activated in cardiac hypertrophy and induces dilated cardiomyopathy and heart failure. Circ Res. 2003;92:912-919.
    • (2003) Circ Res , vol.92 , pp. 912-919
    • Zhang, T.1    Maier, L.S.2    Dalton, N.D.3    Miyamoto, S.4    Ross Jr., J.5    Bers, D.M.6    Brown, J.H.7
  • 114
    • 33644847375 scopus 로고    scopus 로고
    • Microdomains of intracellular Ca 2 +: Molecular determinants and functional consequences
    • Rizzuto R, Pozzan T. Microdomains of intracellular Ca 2 +: molecular determinants and functional consequences. Physiol Rev. 2006;86: 369-408.
    • (2006) Physiol Rev , vol.86 , pp. 369-408
    • Rizzuto, R.1    Pozzan, T.2
  • 115
    • 22144479425 scopus 로고    scopus 로고
    • Inhibition of the mitochondrial calcium uniporter by the oxo-bridged dinuclear ruthenium amine complex (Ru360) prevents from irreversible injury in postischemic rat heart
    • De Jesus Garcia-Rivas G, Guerrero-Hernandez A, Guerrero-Serna G, Rodriguez-Zavala JS, Zazueta C. Inhibition of the mitochondrial calcium uniporter by the oxo-bridged dinuclear ruthenium amine complex (Ru360) prevents from irreversible injury in postischemic rat heart. FEBS J. 2005;272:3477-3488.
    • (2005) FEBS J , vol.272 , pp. 3477-3488
    • De Jesus Garcia-Rivas, G.1    Guerrero-Hernandez, A.2    Guerrero-Serna, G.3    Rodriguez-Zavala, J.S.4    Zazueta, C.5
  • 116
  • 117
    • 67349228215 scopus 로고    scopus 로고
    • Local control of mitochondrial membrane potential, permeability transition pore and reactive oxygen species by calcium and calmodulin in rat ventricular myocytes
    • Odagiri K, Katoh H, Kawashima H, Tanaka T, Ohtani H, Saotome M, Urushida T, Satoh H, Hayashi H. Local control of mitochondrial membrane potential, permeability transition pore and reactive oxygen species by calcium and calmodulin in rat ventricular myocytes. J Mol Cell Cardiol. 2009;46:989-997.
    • (2009) J Mol Cell Cardiol , vol.46 , pp. 989-997
    • Odagiri, K.1    Katoh, H.2    Kawashima, H.3    Tanaka, T.4    Ohtani, H.5    Saotome, M.6    Urushida, T.7    Satoh, H.8    Hayashi, H.9
  • 118
    • 33746816978 scopus 로고    scopus 로고
    • Altered energy transfer from mitochondria to sarcoplasmic reticulum after cytoarchitectural perturbations in mice hearts
    • Wilding JR, Joubert F, de Araujo C, Fortin D, Novotova M, Veksler V, Ventura-Clapier R. Altered energy transfer from mitochondria to sarcoplasmic reticulum after cytoarchitectural perturbations in mice hearts. J Physiol. 2006;575:191-200.
    • (2006) J Physiol , vol.575 , pp. 191-200
    • Wilding, J.R.1    Joubert, F.2    De Araujo, C.3    Fortin, D.4    Novotova, M.5    Veksler, V.6    Ventura-Clapier, R.7
  • 119
    • 0034668946 scopus 로고    scopus 로고
    • Mitochondria as all-round players of the calcium game
    • Rizzuto R, Bernardi P, Pozzan T. Mitochondria as all-round players of the calcium game. J Physiol. 2000; 529(Pt 1):37-47.
    • (2000) J Physiol , vol.529 , Issue.PART 1 , pp. 37-47
    • Rizzuto, R.1    Bernardi, P.2    Pozzan, T.3
  • 120
    • 0026659512 scopus 로고
    • Rapid changes of mitochondrial Ca2 + revealed by specifically targeted recombinant aequorin
    • Rizzuto R, Simpson AW, Brini M, Pozzan T. Rapid changes of mitochondrial Ca2 + revealed by specifically targeted recombinant aequorin. Nature. 1992;358:325-327.
    • (1992) Nature , vol.358 , pp. 325-327
    • Rizzuto, R.1    Simpson, A.W.2    Brini, M.3    Pozzan, T.4
  • 121
    • 0027340729 scopus 로고
    • Microdomains with high Ca2+ close to IP3-sensitive channels that are sensed by neighboring mitochondria
    • Rizzuto R, Brini M, Murgia M, Pozzan T. Microdomains with high Ca2+ close to IP3-sensitive channels that are sensed by neighboring mitochondria. Science. 1993;262:744-747.
    • (1993) Science , vol.262 , pp. 744-747
    • Rizzuto, R.1    Brini, M.2    Murgia, M.3    Pozzan, T.4
  • 123
    • 0029143569 scopus 로고
    • Decoding of cytosolic calcium oscillations in the mitochondria
    • Hajnoczky G, Robb-Gaspers LD, Seitz MB, Thomas AP. Decoding of cytosolic calcium oscillations in the mitochondria. Cell. 1995;82: 415-424.
    • (1995) Cell , vol.82 , pp. 415-424
    • Hajnoczky, G.1    Robb-Gaspers, L.D.2    Seitz, M.B.3    Thomas, A.P.4
  • 124
    • 0033598828 scopus 로고    scopus 로고
    • Regulation of mitochondrial ATP synthesis by calcium: Evidence for a long-term metabolic priming
    • Jouaville LS, Pinton P, Bastianutto C, Rutter GA, Rizzuto R. Regulation of mitochondrial ATP synthesis by calcium: evidence for a long-term metabolic priming. Proc Natl Acad Sci USA. 1999;96:13807-13812.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13807-13812
    • Jouaville, L.S.1    Pinton, P.2    Bastianutto, C.3    Rutter, G.A.4    Rizzuto, R.5
  • 125
    • 2342572271 scopus 로고    scopus 로고
    • Phospholipid biosynthesis in mammalian cells
    • Vance JE, Vance DE. Phospholipid biosynthesis in mammalian cells. Biochem Cell Biol. 2004;82:113-128.
    • (2004) Biochem Cell Biol , vol.82 , pp. 113-128
    • Vance, J.E.1    Vance, D.E.2
  • 126
    • 70449088871 scopus 로고    scopus 로고
    • GM1-ganglioside accumulation at the mitochondria-associated ER membranes links ER stress to Ca(2 +)-dependent mitochondrial apoptosis
    • Sano R, Annunziata I, Patterson A, Moshiach S, Gomero E, Opferman J, Forte M, d'Azzo A. GM1-ganglioside accumulation at the mitochondria-associated ER membranes links ER stress to Ca(2 +)-dependent mitochondrial apoptosis. Mol Cell. 2009;36:500-511.
    • (2009) Mol Cell , vol.36 , pp. 500-511
    • Sano, R.1    Annunziata, I.2    Patterson, A.3    Moshiach, S.4    Gomero, E.5    Opferman, J.6    Forte, M.7    D'Azzo, A.8
  • 129
    • 57749113106 scopus 로고    scopus 로고
    • Physical coupling supports the local Ca2+ transfer between sarcoplasmic reticulum subdomains and the mitochondria in heart muscle
    • Garcia-Perez C, Hajnoczky G, Csordas G. Physical coupling supports the local Ca2+ transfer between sarcoplasmic reticulum subdomains and the mitochondria in heart muscle. J Biol Chem. 2008;283: 32771-32780.
    • (2008) J Biol Chem , vol.283 , pp. 32771-32780
    • Garcia-Perez, C.1    Hajnoczky, G.2    Csordas, G.3
  • 132
  • 133
    • 34248572358 scopus 로고    scopus 로고
    • Down-regulation of mitofusin-2 expression in cardiac hypertrophy in vitro and in vivo
    • Fang L, Moore XL, Gao XM, Dart AM, Lim YL, Du XJ. Down-regulation of mitofusin-2 expression in cardiac hypertrophy in vitro and in vivo. Life Sci. 2007;80:2154-2160.
    • (2007) Life Sci , vol.80 , pp. 2154-2160
    • Fang, L.1    Moore, X.L.2    Gao, X.M.3    Dart, A.M.4    Lim, Y.L.5    Du, X.J.6
  • 134
    • 67349140952 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor delta regulates mitofusin 2 expression in the heart
    • Li Y, Yin R, Liu J, Wang P, Wu S, Luo J, Zhelyabovska O, Yang Q. Peroxisome proliferator-activated receptor delta regulates mitofusin 2 expression in the heart. J Mol Cell Cardiol. 2009;46:876-882.
    • (2009) J Mol Cell Cardiol , vol.46 , pp. 876-882
    • Li, Y.1    Yin, R.2    Liu, J.3    Wang, P.4    Wu, S.5    Luo, J.6    Zhelyabovska, O.7    Yang, Q.8
  • 136
    • 77951716870 scopus 로고    scopus 로고
    • ERMES-mediated ER-mitochondria contacts: Molecular hubs for the regulation of mitochondrial biology
    • Kornmann B, Walter P. ERMES-mediated ER-mitochondria contacts: molecular hubs for the regulation of mitochondrial biology. J Cell Sci. 2010;123:1389-1393.
    • (2010) J Cell Sci , vol.123 , pp. 1389-1393
    • Kornmann, B.1    Walter, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.