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Volumn 1813, Issue 4, 2011, Pages 551-557

Apoptosis-induced changes in mitochondrial lipids

Author keywords

Apoptosis; Bcl 2; Bid; Cardiolipin; Death receptor; Lysophosphatidyl choline; Membrane lipids; Mitochondria; MOMP

Indexed keywords

CARDIOLIPIN; CASPASE; MEMBRANE LIPID; PHOSPHOLIPID;

EID: 79952698118     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2010.09.014     Document Type: Review
Times cited : (70)

References (100)
  • 1
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G., Galluzzi L., Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol. Rev. 2007, 87:99-163.
    • (2007) Physiol. Rev. , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 3
    • 1842680755 scopus 로고    scopus 로고
    • Membrane lipids and cell death: an overview
    • Cristea I.M., Degli Esposti M. Membrane lipids and cell death: an overview. Chem. Phys. Lipids 2004, 129:133-160.
    • (2004) Chem. Phys. Lipids , vol.129 , pp. 133-160
    • Cristea, I.M.1    Degli Esposti, M.2
  • 4
    • 51449112852 scopus 로고    scopus 로고
    • Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes
    • Schlame M. Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes. J. Lipid Res. 2008, 49:1607-1620.
    • (2008) J. Lipid Res. , vol.49 , pp. 1607-1620
    • Schlame, M.1
  • 5
    • 70349524664 scopus 로고    scopus 로고
    • Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis
    • Schug Z.T., Gottlieb E. Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis. Biochim. Biophys. Acta 2009, 1788:2022-2031.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2022-2031
    • Schug, Z.T.1    Gottlieb, E.2
  • 6
    • 52049104392 scopus 로고    scopus 로고
    • Organelle intermixing and membrane scrambling in cell death
    • Degli Esposti M. Organelle intermixing and membrane scrambling in cell death. Meth. Enzymol. 2008, 442:421-438.
    • (2008) Meth. Enzymol. , vol.442 , pp. 421-438
    • Degli Esposti, M.1
  • 7
    • 0041423663 scopus 로고    scopus 로고
    • Apoptosis, giving phosphatidylserine recognition an assist with a twist
    • Fadok V.A., Henson P.M. Apoptosis, giving phosphatidylserine recognition an assist with a twist. Curr. Biol. 2003, 13:R655-R657.
    • (2003) Curr. Biol. , vol.13
    • Fadok, V.A.1    Henson, P.M.2
  • 8
    • 33748745926 scopus 로고    scopus 로고
    • Cell migration and signaling specificity is determined by the phosphatidylserine recognition motif of Rac1
    • Finkielstein C.V., Overduin M., Capelluto D.G. Cell migration and signaling specificity is determined by the phosphatidylserine recognition motif of Rac1. J. Biol. Chem. 2006, 281:27317-27326.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27317-27326
    • Finkielstein, C.V.1    Overduin, M.2    Capelluto, D.G.3
  • 10
    • 0036270432 scopus 로고    scopus 로고
    • Citicoline: neuroprotective mechanisms in cerebral ischemia
    • Adibhatla R.M., Hatcher J.F., Dempsey R.J. Citicoline: neuroprotective mechanisms in cerebral ischemia. J. Neurochem. 2002, 80:12-23.
    • (2002) J. Neurochem. , vol.80 , pp. 12-23
    • Adibhatla, R.M.1    Hatcher, J.F.2    Dempsey, R.J.3
  • 12
    • 70350374353 scopus 로고    scopus 로고
    • Suppression of mitochondrial function by oxidatively truncated phospholipids is reversible, aided by bid, and suppressed by Bcl-XL
    • Chen R., Feldstein A.E., McIntyre T.M. Suppression of mitochondrial function by oxidatively truncated phospholipids is reversible, aided by bid, and suppressed by Bcl-XL. J. Biol. Chem. 2009, 284:26297-26308.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26297-26308
    • Chen, R.1    Feldstein, A.E.2    McIntyre, T.M.3
  • 14
    • 0036750174 scopus 로고    scopus 로고
    • Application of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry for monitoring the digestion of phosphatidylcholine by pancreatic phospholipase A(2)
    • Petkovi' M., Müller J., Müller M., Schiller J., Arnold K., Arnhold J. Application of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry for monitoring the digestion of phosphatidylcholine by pancreatic phospholipase A(2). Anal. Biochem. 2002, 308:61-70.
    • (2002) Anal. Biochem. , vol.308 , pp. 61-70
    • Petkovi', M.1    Müller, J.2    Müller, M.3    Schiller, J.4    Arnold, K.5    Arnhold, J.6
  • 15
    • 33749415625 scopus 로고    scopus 로고
    • Mitochondrial phospholipids of rat skeletal muscle are less polyunsaturated than whole tissue phospholipids: implications for protection against oxidative stress
    • Tsalouhidou S., Argyrou C., Theofilidis G., Karaoglanidis D., Orfanidou E., Nikolaidis M.G., Petridou A., Mougios V. Mitochondrial phospholipids of rat skeletal muscle are less polyunsaturated than whole tissue phospholipids: implications for protection against oxidative stress. J. Anim. Sci. 2006, 84:2818-2825.
    • (2006) J. Anim. Sci. , vol.84 , pp. 2818-2825
    • Tsalouhidou, S.1    Argyrou, C.2    Theofilidis, G.3    Karaoglanidis, D.4    Orfanidou, E.5    Nikolaidis, M.G.6    Petridou, A.7    Mougios, V.8
  • 16
    • 0032496143 scopus 로고    scopus 로고
    • Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss
    • Cai J., Jones D.P. Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss. J. Biol. Chem. 1998, 273:11401-11404.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11401-11404
    • Cai, J.1    Jones, D.P.2
  • 17
    • 0035869341 scopus 로고    scopus 로고
    • Evidence for redox regulation of cytochrome C release during programmed neuronal death: antioxidant effects of protein synthesis and caspase inhibition
    • Kirkland R.A., Franklin J.L. Evidence for redox regulation of cytochrome C release during programmed neuronal death: antioxidant effects of protein synthesis and caspase inhibition. J. Neurosci. 2001, 21:1949-1963.
    • (2001) J. Neurosci. , vol.21 , pp. 1949-1963
    • Kirkland, R.A.1    Franklin, J.L.2
  • 18
    • 12344303128 scopus 로고    scopus 로고
    • Cytochrome c release is required for phosphatidylserine peroxidation during Fas-triggered apoptosis in lung epithelial A549 cells
    • Jiang J., Kini V., Belikova N., Serinkan B.F., Borisenko G.G., Tyurina Y.Y., Tyurin V.A., Kagan V.E. Cytochrome c release is required for phosphatidylserine peroxidation during Fas-triggered apoptosis in lung epithelial A549 cells. Lipids 2004, 39:1133-1142.
    • (2004) Lipids , vol.39 , pp. 1133-1142
    • Jiang, J.1    Kini, V.2    Belikova, N.3    Serinkan, B.F.4    Borisenko, G.G.5    Tyurina, Y.Y.6    Tyurin, V.A.7    Kagan, V.E.8
  • 20
    • 26444453262 scopus 로고    scopus 로고
    • Mitochondrial ceramide and the induction of apoptosis
    • Siskind L.J. Mitochondrial ceramide and the induction of apoptosis. J. Bioenerg. Biomembr. 2005, 37:143-153.
    • (2005) J. Bioenerg. Biomembr. , vol.37 , pp. 143-153
    • Siskind, L.J.1
  • 21
    • 77953811195 scopus 로고    scopus 로고
    • Ceramide channels and their role in mitochondria-mediated apoptosis
    • Colombini M. Ceramide channels and their role in mitochondria-mediated apoptosis. Biochim. Biophys. Acta 2010, 1797:1239-1244.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1239-1244
    • Colombini, M.1
  • 22
    • 22544470314 scopus 로고    scopus 로고
    • Caspase-dependent and -independent activation of acid sphingomyelinase signaling
    • Rotolo J.A., Zhang J., Donepudi M., Lee H., Fuks Z., Kolesnick R. Caspase-dependent and -independent activation of acid sphingomyelinase signaling. J. Biol. Chem. 2005, 280:26425-26434.
    • (2005) J. Biol. Chem. , vol.280 , pp. 26425-26434
    • Rotolo, J.A.1    Zhang, J.2    Donepudi, M.3    Lee, H.4    Fuks, Z.5    Kolesnick, R.6
  • 25
    • 67849133020 scopus 로고    scopus 로고
    • Cardiolipin-enriched raft-like microdomains are essential activating platforms for apoptotic signals on mitochondria
    • Sorice M., Manganelli V., Matarrese P., Tinari A., Misasi R., Malorni W., Garofalo T. Cardiolipin-enriched raft-like microdomains are essential activating platforms for apoptotic signals on mitochondria. FEBS Lett. 2009, 583:2447-2450.
    • (2009) FEBS Lett. , vol.583 , pp. 2447-2450
    • Sorice, M.1    Manganelli, V.2    Matarrese, P.3    Tinari, A.4    Misasi, R.5    Malorni, W.6    Garofalo, T.7
  • 27
    • 0041355315 scopus 로고    scopus 로고
    • Saturated fatty acid-induced apoptosis in MDA-MB-231 breast cancer cells. A role for cardiolipin
    • Hardy S., El-Assaad W., Przybytkowski E., Joly E., Prentki M., Langelier Y. Saturated fatty acid-induced apoptosis in MDA-MB-231 breast cancer cells. A role for cardiolipin. J. Biol. Chem. 2003, 278:31861-31870.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31861-31870
    • Hardy, S.1    El-Assaad, W.2    Przybytkowski, E.3    Joly, E.4    Prentki, M.5    Langelier, Y.6
  • 28
    • 0035851186 scopus 로고    scopus 로고
    • Decreased cardiolipin synthesis corresponds with cytochrome c release in palmitate-induced cardiomyocyte apoptosis
    • Ostrander D.B., Sparagna G.C., Amoscato A.A., McMillin J.B., Dowhan W. Decreased cardiolipin synthesis corresponds with cytochrome c release in palmitate-induced cardiomyocyte apoptosis. J. Biol. Chem. 2001, 276:38061-38067.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38061-38067
    • Ostrander, D.B.1    Sparagna, G.C.2    Amoscato, A.A.3    McMillin, J.B.4    Dowhan, W.5
  • 30
    • 0348038751 scopus 로고    scopus 로고
    • Proapoptotic Bid binds to monolysocardiolipin, a new molecular connection between mitochondrial membranes and cell death
    • Degli Esposti M., Cristea I.M., Gaskell S.J., Nakao Y., Dive C. Proapoptotic Bid binds to monolysocardiolipin, a new molecular connection between mitochondrial membranes and cell death. Cell Death Differ. 2003, 10:1300-1309.
    • (2003) Cell Death Differ. , vol.10 , pp. 1300-1309
    • Degli Esposti, M.1    Cristea, I.M.2    Gaskell, S.J.3    Nakao, Y.4    Dive, C.5
  • 31
    • 45849117232 scopus 로고    scopus 로고
    • Unravelling the bcl-2 apoptosis code with a simple model system
    • Basañez G., Hardwick J.M. Unravelling the bcl-2 apoptosis code with a simple model system. PLoS Biol. 2008, 6:e154.
    • (2008) PLoS Biol. , vol.6
    • Basañez, G.1    Hardwick, J.M.2
  • 32
    • 0037203313 scopus 로고    scopus 로고
    • Phosphatidylcholine and cell death
    • Cui Z., Houweling M. Phosphatidylcholine and cell death. Biochim. Biophys. Acta 2002, 1585:87-96.
    • (2002) Biochim. Biophys. Acta , vol.1585 , pp. 87-96
    • Cui, Z.1    Houweling, M.2
  • 33
    • 0036723844 scopus 로고    scopus 로고
    • Erucylphosphocholine-induced apoptosis in glioma cells: involvement of death receptor signalling and caspase activation
    • Kugler W., Erdlenbruch B., Junemann A., Heinemann D., Eibl H., Lakomek M. Erucylphosphocholine-induced apoptosis in glioma cells: involvement of death receptor signalling and caspase activation. J. Neurochem. 2002, 82:1160-1170.
    • (2002) J. Neurochem. , vol.82 , pp. 1160-1170
    • Kugler, W.1    Erdlenbruch, B.2    Junemann, A.3    Heinemann, D.4    Eibl, H.5    Lakomek, M.6
  • 34
    • 77953617179 scopus 로고    scopus 로고
    • Lysosomal membrane permeabilization and cathepsin release is a Bax/Bak-dependent, amplifying event of apoptosis in fibroblasts and monocytes
    • Oberle C., Huai J., Reinheckel T., Tacke M., Rassner M., Ekert P.G., Buellesbach J., Borner C. Lysosomal membrane permeabilization and cathepsin release is a Bax/Bak-dependent, amplifying event of apoptosis in fibroblasts and monocytes. Cell Death Differ. 2010, 17:1167-1178.
    • (2010) Cell Death Differ. , vol.17 , pp. 1167-1178
    • Oberle, C.1    Huai, J.2    Reinheckel, T.3    Tacke, M.4    Rassner, M.5    Ekert, P.G.6    Buellesbach, J.7    Borner, C.8
  • 35
    • 44349165818 scopus 로고    scopus 로고
    • Shotgun lipidomics reveals the temporally dependent, highly diversified cardiolipin profile in the mammalian brain: temporally coordinated postnatal diversification of cardiolipin molecular species with neuronal remodeling
    • Cheng H., Mancuso D.J., Jiang X., Guan S., Yang J., Yang K., Sun G., Gross R.W., Han X. Shotgun lipidomics reveals the temporally dependent, highly diversified cardiolipin profile in the mammalian brain: temporally coordinated postnatal diversification of cardiolipin molecular species with neuronal remodeling. Biochemistry 2008, 47:5869-5880.
    • (2008) Biochemistry , vol.47 , pp. 5869-5880
    • Cheng, H.1    Mancuso, D.J.2    Jiang, X.3    Guan, S.4    Yang, J.5    Yang, K.6    Sun, G.7    Gross, R.W.8    Han, X.9
  • 36
    • 0037085029 scopus 로고    scopus 로고
    • Sequence and functional similarities between pro-apoptotic Bid and plant lipid transfer proteins
    • Degli Esposti M. Sequence and functional similarities between pro-apoptotic Bid and plant lipid transfer proteins. Biochim. Biophys. Acta 2002, 1553:331-340.
    • (2002) Biochim. Biophys. Acta , vol.1553 , pp. 331-340
    • Degli Esposti, M.1
  • 39
    • 0034795258 scopus 로고    scopus 로고
    • Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity
    • Degli Esposti M., Erler J.T., Hickman J.A., Dive C. Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity. Mol. Cell. Biol. 2001, 21:7268-7276.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7268-7276
    • Degli Esposti, M.1    Erler, J.T.2    Hickman, J.A.3    Dive, C.4
  • 42
    • 0037605881 scopus 로고    scopus 로고
    • Phospholipase A2 (PLA2) enzymes in membrane trafficking: mediators of membrane shape and function
    • Brown W.J., Chambers K., Doody A. Phospholipase A2 (PLA2) enzymes in membrane trafficking: mediators of membrane shape and function. Traffic 2003, 4:214-221.
    • (2003) Traffic , vol.4 , pp. 214-221
    • Brown, W.J.1    Chambers, K.2    Doody, A.3
  • 43
    • 0344119435 scopus 로고    scopus 로고
    • Prefission constriction of Golgi tubular carriers driven by local lipid metabolism: a theoretical model
    • Shemesh T., Luini A., Malhotra V., Burger K.N., Kozlov M.M. Prefission constriction of Golgi tubular carriers driven by local lipid metabolism: a theoretical model. Biophys. J. 2003, 85:3813-3827.
    • (2003) Biophys. J. , vol.85 , pp. 3813-3827
    • Shemesh, T.1    Luini, A.2    Malhotra, V.3    Burger, K.N.4    Kozlov, M.M.5
  • 44
    • 0036710546 scopus 로고    scopus 로고
    • Membrane fusion: the process and its energy suppliers
    • Basañez G. Membrane fusion: the process and its energy suppliers. Cell. Mol. Life Sci. 2002, 59:1478-1490.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1478-1490
    • Basañez, G.1
  • 45
    • 0037147239 scopus 로고    scopus 로고
    • Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature
    • Basañez G., Sharpe J.C., Galanis J., Brandt T.B., Hardwick J.M., Zimmerberg J. Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature. J. Biol. Chem. 2002, 277:49360-49365.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49360-49365
    • Basañez, G.1    Sharpe, J.C.2    Galanis, J.3    Brandt, T.B.4    Hardwick, J.M.5    Zimmerberg, J.6
  • 46
    • 0036847178 scopus 로고    scopus 로고
    • Membrane perturbations induced by the apoptotic Bax protein
    • Epand R.F., Martinou J.C., Montessuit S., Epand R.M. Membrane perturbations induced by the apoptotic Bax protein. Biochem. J. 2002, 367:849-855.
    • (2002) Biochem. J. , vol.367 , pp. 849-855
    • Epand, R.F.1    Martinou, J.C.2    Montessuit, S.3    Epand, R.M.4
  • 47
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes R., Desagher S., Antonsson B., Martinou J.C. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol. Cell. Biol. 2000, 20:929-935.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 48
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells
    • Antonsson B., Montessuit S., Sanchez B., Martinou J.C. Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. J. Biol. Chem. 2001, 276:11615-11623.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11615-11623
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 51
    • 33645978129 scopus 로고    scopus 로고
    • The mechanism of pore formation by bacterial toxins
    • Tilley S.J., Saibil H.R. The mechanism of pore formation by bacterial toxins. Curr. Opin. Struct. Biol. 2006, 16:230-236.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 230-236
    • Tilley, S.J.1    Saibil, H.R.2
  • 52
    • 0034725630 scopus 로고    scopus 로고
    • The destabilization of lipid membranes induced by the C-terminal fragment of caspase 8-cleaved bid is inhibited by the N-terminal fragment
    • Kudla G., Montessuit S., Eskes R., Berrier C., Martinou J.C., Ghazi A., Antonsson B. The destabilization of lipid membranes induced by the C-terminal fragment of caspase 8-cleaved bid is inhibited by the N-terminal fragment. J. Biol. Chem. 2000, 275:22713-22718.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22713-22718
    • Kudla, G.1    Montessuit, S.2    Eskes, R.3    Berrier, C.4    Martinou, J.C.5    Ghazi, A.6    Antonsson, B.7
  • 53
    • 12844266796 scopus 로고    scopus 로고
    • Conformational changes in BID, a pro-apoptotic BCL-2 family member, upon membrane binding. A site-directed spin labeling study
    • Oh K.J., Barbuto S., Meyer N., Kim R.S., Collier R.J., Korsmeyer S.J. Conformational changes in BID, a pro-apoptotic BCL-2 family member, upon membrane binding. A site-directed spin labeling study. J. Biol. Chem. 2005, 280:753-767.
    • (2005) J. Biol. Chem. , vol.280 , pp. 753-767
    • Oh, K.J.1    Barbuto, S.2    Meyer, N.3    Kim, R.S.4    Collier, R.J.5    Korsmeyer, S.J.6
  • 54
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: coregulation of dimer formation and intracellular localization
    • Suzuki M., Youle R.J., Tjandra N. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 2000, 103:645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 56
    • 1542465184 scopus 로고    scopus 로고
    • Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis
    • Yethon J.A., Epand R.F., Leber B., Epand R.M., Andrews D.W. Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis. J. Biol. Chem. 2003, 278:48935-48941.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48935-48941
    • Yethon, J.A.1    Epand, R.F.2    Leber, B.3    Epand, R.M.4    Andrews, D.W.5
  • 58
    • 34247497716 scopus 로고    scopus 로고
    • Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes
    • Leber B., Lin J., Andrews D.W. Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes. Apoptosis 2007, 12:897-911.
    • (2007) Apoptosis , vol.12 , pp. 897-911
    • Leber, B.1    Lin, J.2    Andrews, D.W.3
  • 59
    • 57149135309 scopus 로고    scopus 로고
    • Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax
    • Lovell J.F., Billen L.P., Bindner S., Shamas-Din A., Fradin C., Leber B., Andrews D.W. 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
  • 60
    • 42149094346 scopus 로고    scopus 로고
    • Contributions to Bax insertion and oligomerization of lipids of the mitochondrial outer membrane
    • Lucken-Ardjomande S., Montessuit S., Martinou J.C. Contributions to Bax insertion and oligomerization of lipids of the mitochondrial outer membrane. Cell Death Differ. 2008, 15:929-937.
    • (2008) Cell Death Differ. , vol.15 , pp. 929-937
    • Lucken-Ardjomande, S.1    Montessuit, S.2    Martinou, J.C.3
  • 61
    • 39449130146 scopus 로고    scopus 로고
    • Bax activation and stress-induced apoptosis delayed by the accumulation of cholesterol in mitochondrial membranes
    • Lucken-Ardjomande S., Montessuit S., Martinou J.C. Bax activation and stress-induced apoptosis delayed by the accumulation of cholesterol in mitochondrial membranes. Cell Death Differ. 2008, 15:484-493.
    • (2008) Cell Death Differ. , vol.15 , pp. 484-493
    • Lucken-Ardjomande, S.1    Montessuit, S.2    Martinou, J.C.3
  • 62
    • 70350025502 scopus 로고    scopus 로고
    • Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis
    • Dewson G., Kluck R.M. Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis. J. Cell Sci. 2009, 122:2801-2808.
    • (2009) J. Cell Sci. , vol.122 , pp. 2801-2808
    • Dewson, G.1    Kluck, R.M.2
  • 63
    • 77952760990 scopus 로고    scopus 로고
    • Understanding detergent effects on lipid membranes: a model study of lysolipids
    • Henriksen J.R., Andresen T.L., Feldborg L.N., Duelund L., Ipsen J.H. Understanding detergent effects on lipid membranes: a model study of lysolipids. Biophys. J. 2010, 98:2199-2205.
    • (2010) Biophys. J. , vol.98 , pp. 2199-2205
    • Henriksen, J.R.1    Andresen, T.L.2    Feldborg, L.N.3    Duelund, L.4    Ipsen, J.H.5
  • 64
    • 0034534795 scopus 로고    scopus 로고
    • Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis
    • Zha J., Weiler S., Oh K.J., Wei M.C., Korsmeyer S.J. Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis. Science 2000, 290:1761-1765.
    • (2000) Science , vol.290 , pp. 1761-1765
    • Zha, J.1    Weiler, S.2    Oh, K.J.3    Wei, M.C.4    Korsmeyer, S.J.5
  • 66
    • 70349954755 scopus 로고    scopus 로고
    • Interaction of the alpha-helical H6 peptide from the pro-apoptotic protein tBid with cardiolipin
    • Petit P.X., Dupaigne P., Pariselli F., Gonzalvez F., Etienne F., Rameau C., Bernard S. Interaction of the alpha-helical H6 peptide from the pro-apoptotic protein tBid with cardiolipin. FEBS J. 2009, 276:6338-6354.
    • (2009) FEBS J. , vol.276 , pp. 6338-6354
    • Petit, P.X.1    Dupaigne, P.2    Pariselli, F.3    Gonzalvez, F.4    Etienne, F.5    Rameau, C.6    Bernard, S.7
  • 68
    • 0037131168 scopus 로고    scopus 로고
    • Alkyl-lysophospholipid accumulates in lipid rafts and induces apoptosis via raft-dependent endocytosis and inhibition of phosphatidylcholine synthesis
    • Van der Luit A.H., Budde M., Ruurs P., Verheij M., Van Blitterswijk W.J. Alkyl-lysophospholipid accumulates in lipid rafts and induces apoptosis via raft-dependent endocytosis and inhibition of phosphatidylcholine synthesis. J. Biol. Chem. 2002, 277:39541-39547.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39541-39547
    • Van der Luit, A.H.1    Budde, M.2    Ruurs, P.3    Verheij, M.4    Van Blitterswijk, W.J.5
  • 69
    • 0141456089 scopus 로고    scopus 로고
    • Different modes of internalization of apoptotic alkyl-lysophospholipid and cell-rescuing lysophosphatidylcholine
    • Van der Luit A.H., Budde M., Verheij M., Van Blitterswijk W.J. Different modes of internalization of apoptotic alkyl-lysophospholipid and cell-rescuing lysophosphatidylcholine. Biochem. J. 2003, 374:747-753.
    • (2003) Biochem. J. , vol.374 , pp. 747-753
    • Van der Luit, A.H.1    Budde, M.2    Verheij, M.3    Van Blitterswijk, W.J.4
  • 70
    • 63049084604 scopus 로고    scopus 로고
    • Lysophosphatidylcholine protects cerebellar granule neurons from apoptotic cell death
    • Ikeno Y., Cheon S.H., Konno N., Nakamura A., Kitamoto K., Arioka M. Lysophosphatidylcholine protects cerebellar granule neurons from apoptotic cell death. J. Neurosci. Res. 2009, 87:190-199.
    • (2009) J. Neurosci. Res. , vol.87 , pp. 190-199
    • Ikeno, Y.1    Cheon, S.H.2    Konno, N.3    Nakamura, A.4    Kitamoto, K.5    Arioka, M.6
  • 71
    • 0041829104 scopus 로고    scopus 로고
    • Distinct regulation of cytosolic phospholipase A2 phosphorylation, translocation, proteolysis and activation by tumour necrosis factor-receptor subtypes
    • Jupp O.J., Vandenabeele P., MacEwan D.J. Distinct regulation of cytosolic phospholipase A2 phosphorylation, translocation, proteolysis and activation by tumour necrosis factor-receptor subtypes. Biochem. J. 2003, 374:453-461.
    • (2003) Biochem. J. , vol.374 , pp. 453-461
    • Jupp, O.J.1    Vandenabeele, P.2    MacEwan, D.J.3
  • 72
    • 2342584674 scopus 로고    scopus 로고
    • Clearance of apoptotic cells: getting rid of the corpses
    • Lauber K., Blumenthal S.G., Waibel M., Wesselborg S. Clearance of apoptotic cells: getting rid of the corpses. Mol. Cell 2004, 14:277-287.
    • (2004) Mol. Cell , vol.14 , pp. 277-287
    • Lauber, K.1    Blumenthal, S.G.2    Waibel, M.3    Wesselborg, S.4
  • 73
    • 73949096361 scopus 로고    scopus 로고
    • Mechanisms underlying neutrophil-mediated monocyte recruitment
    • Soehnlein O., Lindbom L., Weber C. Mechanisms underlying neutrophil-mediated monocyte recruitment. Blood 2009, 114:4613-4623.
    • (2009) Blood , vol.114 , pp. 4613-4623
    • Soehnlein, O.1    Lindbom, L.2    Weber, C.3
  • 74
    • 0345803935 scopus 로고    scopus 로고
    • Remodeling of cardiolipin by phospholipid transacylation
    • Xu Y., Kelley R.I., Blanck T.J., Schlame M. Remodeling of cardiolipin by phospholipid transacylation. J. Biol. Chem. 2003, 278:51380-51385.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51380-51385
    • Xu, Y.1    Kelley, R.I.2    Blanck, T.J.3    Schlame, M.4
  • 76
    • 0032562796 scopus 로고    scopus 로고
    • Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations
    • Hsu Y.T., Youle R.J. Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations. J. Biol. Chem. 1998, 273:10777-10783.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10777-10783
    • Hsu, Y.T.1    Youle, R.J.2
  • 78
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • Schlame M., Rua D., Greenberg M.L. The biosynthesis and functional role of cardiolipin. Prog. Lipid Res. 2000, 39:257-288.
    • (2000) Prog. Lipid Res. , vol.39 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 81
    • 42049102578 scopus 로고    scopus 로고
    • Role of phospholipid scramblase 3 in the regulation of tumor necrosis factor-alpha-induced apoptosis
    • Liu J., Epand R.F., Durrant D., Grossman D., Chi N.W., Epand R.M., Lee R.M. Role of phospholipid scramblase 3 in the regulation of tumor necrosis factor-alpha-induced apoptosis. Biochemistry 2008, 47:4518-4529.
    • (2008) Biochemistry , vol.47 , pp. 4518-4529
    • Liu, J.1    Epand, R.F.2    Durrant, D.3    Grossman, D.4    Chi, N.W.5    Epand, R.M.6    Lee, R.M.7
  • 83
    • 0037115740 scopus 로고    scopus 로고
    • Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein
    • Roucou X., Montessuit S., Antonsson B., Martinou J.C. Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein. Biochem. J. 2002, 368:915-921.
    • (2002) Biochem. J. , vol.368 , pp. 915-921
    • Roucou, X.1    Montessuit, S.2    Antonsson, B.3    Martinou, J.C.4
  • 84
    • 45349094984 scopus 로고    scopus 로고
    • Mitochondrial dynamics and apoptosis
    • Suen D.F., Norris K.L., Youle R.J. Mitochondrial dynamics and apoptosis. Genes Dev. 2008, 22:1577-1590.
    • (2008) Genes Dev. , vol.22 , pp. 1577-1590
    • Suen, D.F.1    Norris, K.L.2    Youle, R.J.3
  • 85
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • Okamoto K., Shaw J.M. Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu. Rev. Genet. 2005, 39:503-536.
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 88
    • 77953526521 scopus 로고    scopus 로고
    • OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation
    • Ban T., Heymann J.A., Song Z., Hinshaw J.E., Chan D.C. OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation. Hum. Mol. Genet. 2010, 19:2113-2122.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 2113-2122
    • Ban, T.1    Heymann, J.A.2    Song, Z.3    Hinshaw, J.E.4    Chan, D.C.5
  • 89
    • 51049112309 scopus 로고    scopus 로고
    • Lipid localization in bacterial cells through curvature-mediated microphase separation
    • Mukhopadhyay R., Huang K.C., Wingreen N.S. Lipid localization in bacterial cells through curvature-mediated microphase separation. Biophys. J. 2008, 95:1034-1049.
    • (2008) Biophys. J. , vol.95 , pp. 1034-1049
    • Mukhopadhyay, R.1    Huang, K.C.2    Wingreen, N.S.3
  • 90
    • 0033956407 scopus 로고    scopus 로고
    • Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange
    • Mileykovskaya E., Dowhan W. Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange. J. Bacteriol. 2000, 182:1172-1175.
    • (2000) J. Bacteriol. , vol.182 , pp. 1172-1175
    • Mileykovskaya, E.1    Dowhan, W.2
  • 92
    • 33751395400 scopus 로고    scopus 로고
    • A curvature-mediated mechanism for localization of lipids to bacterial poles
    • Huang K.C., Mukhopadhyay R., Wingreen N.S. A curvature-mediated mechanism for localization of lipids to bacterial poles. PLoS Comput. Biol. 2006, 2:e151.
    • (2006) PLoS Comput. Biol. , vol.2
    • Huang, K.C.1    Mukhopadhyay, R.2    Wingreen, N.S.3
  • 94
    • 0043166392 scopus 로고    scopus 로고
    • Dynamics of mitochondrial morphology in healthy cells and during apoptosis
    • Karbowski M., Youle R.J. Dynamics of mitochondrial morphology in healthy cells and during apoptosis. Cell Death Differ. 2003, 10:1-11.
    • (2003) Cell Death Differ. , vol.10 , pp. 1-11
    • Karbowski, M.1    Youle, R.J.2
  • 95
    • 0033525749 scopus 로고    scopus 로고
    • Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists
    • McDonnell J.M., Fushman D., Milliman C., Korsmeyer S.J., Cowburn D. Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists. Cell 1999, 96:625-634.
    • (1999) Cell , vol.96 , pp. 625-634
    • McDonnell, J.M.1    Fushman, D.2    Milliman, C.3    Korsmeyer, S.J.4    Cowburn, D.5
  • 96
    • 0034306169 scopus 로고    scopus 로고
    • Cardiolipin provides specificity for targeting of tBid to mitochondria
    • Lutter M., Fang M., Luo X., Nishijima M., Xie X., Wang X. Cardiolipin provides specificity for targeting of tBid to mitochondria. Nat. Cell Biol. 2000, 2:754-761.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 754-761
    • Lutter, M.1    Fang, M.2    Luo, X.3    Nishijima, M.4    Xie, X.5    Wang, X.6
  • 98
    • 77954992376 scopus 로고    scopus 로고
    • Signaling LTPs: A new plant LTPs sub-family?
    • Pii Y., Pandolfini T., Crimi M. Signaling LTPs: A new plant LTPs sub-family?. Plant Signal Behav. 2010, 5:594-597.
    • (2010) Plant Signal Behav. , vol.5 , pp. 594-597
    • Pii, Y.1    Pandolfini, T.2    Crimi, M.3
  • 99
    • 70350703442 scopus 로고    scopus 로고
    • Lysophosphatidic acid in vascular development and disease
    • Teo S.T., Yung Y.C., Herr D.R., Chun J. Lysophosphatidic acid in vascular development and disease. IUBMB Life 2009, 61:791-799.
    • (2009) IUBMB Life , vol.61 , pp. 791-799
    • Teo, S.T.1    Yung, Y.C.2    Herr, D.R.3    Chun, J.4


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