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Volumn 6, Issue 6, 2011, Pages

Mitochondrial ceramide-rich macrodomains functionalize bax upon irradiation

Author keywords

[No Author keywords available]

Indexed keywords

CERAMIDE; CYTOCHROME C; FUMONISIN B1; PROTEIN BAX; SPHINGOSINE ACYLTRANSFERASE; DIHYDROCERAMIDE DESATURASE; FUMONISIN; OXIDOREDUCTASE;

EID: 79958763461     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019783     Document Type: Article
Times cited : (132)

References (78)
  • 1
    • 53349098893 scopus 로고    scopus 로고
    • Ceramide biogenesis is required for radiation-induced apoptosis in the germ line of C. elegans
    • Deng X, Yin X, Allan R, Lu DD, Maurer CW, et al. (2008) Ceramide biogenesis is required for radiation-induced apoptosis in the germ line of C. elegans. Science 322: 110-115.
    • (2008) Science , vol.322 , pp. 110-115
    • Deng, X.1    Yin, X.2    Allan, R.3    Lu, D.D.4    Maurer, C.W.5
  • 2
    • 0034869026 scopus 로고    scopus 로고
    • Conformational change of Bax: a question of life or death
    • Roucou X, Martinou JC, (2001) Conformational change of Bax: a question of life or death. Cell Death Differ 8: 875-877.
    • (2001) Cell Death Differ , vol.8 , pp. 875-877
    • Roucou, X.1    Martinou, J.C.2
  • 3
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: coregulation of dimer formation and intracellular localization
    • Suzuki M, Youle RJ, Tjandra N, (2000) Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103: 645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 4
    • 5244224827 scopus 로고    scopus 로고
    • X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death
    • Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, et al. (1996) X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. Nature 381: 335-341.
    • (1996) Nature , vol.381 , pp. 335-341
    • Muchmore, S.W.1    Sattler, M.2    Liang, H.3    Meadows, R.P.4    Harlan, J.E.5
  • 6
    • 0037147239 scopus 로고    scopus 로고
    • Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature
    • Basanez G, Sharpe JC, Galanis J, Brandt TB, Hardwick JM, et al. (2002) Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature. J Biol Chem 277: 49360-49365.
    • (2002) J Biol Chem , vol.277 , pp. 49360-49365
    • Basanez, G.1    Sharpe, J.C.2    Galanis, J.3    Brandt, T.B.4    Hardwick, J.M.5
  • 7
    • 3142746012 scopus 로고    scopus 로고
    • Lipidic pore formation by the concerted action of proapoptotic BAX and tBID
    • Terrones O, Antonsson B, Yamaguchi H, Wang HG, Liu J, et al. (2004) Lipidic pore formation by the concerted action of proapoptotic BAX and tBID. J Biol Chem 279: 30081-30091.
    • (2004) J Biol Chem , vol.279 , pp. 30081-30091
    • Terrones, O.1    Antonsson, B.2    Yamaguchi, H.3    Wang, H.G.4    Liu, J.5
  • 8
    • 0029917541 scopus 로고    scopus 로고
    • Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2
    • Zha H, Aime-Sempe C, Sato T, Reed JC, (1996) Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2. J Biol Chem 271: 7440-7444.
    • (1996) J Biol Chem , vol.271 , pp. 7440-7444
    • Zha, H.1    Aime-Sempe, C.2    Sato, T.3    Reed, J.C.4
  • 10
    • 61349188950 scopus 로고    scopus 로고
    • Diversity and complexity of ceramide generation after exposure of jurkat leukemia cells to irradiation
    • Ardail D, Maalouf M, Boivin A, Chapet O, Bodennec J, (2009) Diversity and complexity of ceramide generation after exposure of jurkat leukemia cells to irradiation. Int J Radiat Oncol Biol Phys 73: 1211-1218.
    • (2009) Int J Radiat Oncol Biol Phys , vol.73 , pp. 1211-1218
    • Ardail, D.1    Maalouf, M.2    Boivin, A.3    Chapet, O.4    Bodennec, J.5
  • 11
    • 15944425766 scopus 로고    scopus 로고
    • A mitochondrial pool of sphingomyelin is involved in TNFalpha-induced Bax translocation to mitochondria
    • Birbes H, Luberto C, Hsu YT, El Bawab S, Hannun YA, et al. (2005) A mitochondrial pool of sphingomyelin is involved in TNFalpha-induced Bax translocation to mitochondria. Biochem J 386 (Pt 3): 445-451.
    • (2005) Biochem J , vol.386 , Issue.Pt 3 , pp. 445-451
    • Birbes, H.1    Luberto, C.2    Hsu, Y.T.3    El Bawab, S.4    Hannun, Y.A.5
  • 12
    • 2442711625 scopus 로고    scopus 로고
    • Mitochondrial ceramide increases in UV-irradiated HeLa cells and is mainly derived from hydrolysis of sphingomyelin
    • Dai Q, Liu J, Chen J, Durrant D, McIntyre TM, et al. (2004) Mitochondrial ceramide increases in UV-irradiated HeLa cells and is mainly derived from hydrolysis of sphingomyelin. Oncogene 23: 3650-3658.
    • (2004) Oncogene , vol.23 , pp. 3650-3658
    • Dai, Q.1    Liu, J.2    Chen, J.3    Durrant, D.4    McIntyre, T.M.5
  • 14
    • 79958740220 scopus 로고
    • Phospholipid synthesis in a membrane fraction associated with mitochondria
    • Vance JE, (1990) Phospholipid synthesis in a membrane fraction associated with mitochondria. Mitochondrion 6: 11825.
    • (1990) Mitochondrion , vol.6 , pp. 11825
    • Vance, J.E.1
  • 15
    • 77951665317 scopus 로고    scopus 로고
    • Ceramide and activated Bax act synergistically to permeabilize the mitochondrial outer membrane
    • Ganesan V, Perera MN, Colombini D, Datskovskiy D, Chadha K, et al. (2010) Ceramide and activated Bax act synergistically to permeabilize the mitochondrial outer membrane. Apoptosis 15: 553-562.
    • (2010) Apoptosis , vol.15 , pp. 553-562
    • Ganesan, V.1    Perera, M.N.2    Colombini, D.3    Datskovskiy, D.4    Chadha, K.5
  • 16
    • 0033615649 scopus 로고    scopus 로고
    • Functional consequences of the sustained or transient activation by Bax of the mitochondrial permeability transition pore
    • Pastorino JG, Tafani M, Rothman RJ, Marcinkeviciute A, Hoek JB, et al. (1999) Functional consequences of the sustained or transient activation by Bax of the mitochondrial permeability transition pore. J Biol Chem 274: 31734-31739.
    • (1999) J Biol Chem , vol.274 , pp. 31734-31739
    • Pastorino, J.G.1    Tafani, M.2    Rothman, R.J.3    Marcinkeviciute, A.4    Hoek, J.B.5
  • 17
    • 20144367155 scopus 로고    scopus 로고
    • Acid Sphingomyelinase is Indispensable for UV Light-induced Bax Conformational Change at the Mitochondrial Membrane
    • Kashkar H, Wiegmann K, Yazdanpanah B, Haubert D, Kronke M, (2005) Acid Sphingomyelinase is Indispensable for UV Light-induced Bax Conformational Change at the Mitochondrial Membrane. J Biol Chem 280: 20804-20813.
    • (2005) J Biol Chem , vol.280 , pp. 20804-20813
    • Kashkar, H.1    Wiegmann, K.2    Yazdanpanah, B.3    Haubert, D.4    Kronke, M.5
  • 19
    • 0242574357 scopus 로고    scopus 로고
    • Raft ceramide in molecular medicine
    • Gulbins E, Kolesnick R, (2003) Raft ceramide in molecular medicine. Oncogene 22: 7070-7077.
    • (2003) Oncogene , vol.22 , pp. 7070-7077
    • Gulbins, E.1    Kolesnick, R.2
  • 21
    • 0036285870 scopus 로고    scopus 로고
    • Pore-forming toxins
    • Gilbert RJ, (2002) Pore-forming toxins. Cell Mol Life Sci 59: 832-844.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 832-844
    • Gilbert, R.J.1
  • 22
    • 0035028838 scopus 로고    scopus 로고
    • Raft membrane domains: from a liquid-ordered membrane phase to a site of pathogen attack
    • van der Goot FG, Harder T, (2001) Raft membrane domains: from a liquid-ordered membrane phase to a site of pathogen attack. Semin Immunol 13: 89-97.
    • (2001) Semin Immunol , vol.13 , pp. 89-97
    • van der Goot, F.G.1    Harder, T.2
  • 23
    • 0037134485 scopus 로고    scopus 로고
    • Heliothis virescens and Manduca sexta lipid rafts are involved in Cry1A toxin binding to the midgut epithelium and subsequent pore formation
    • Zhuang M, Oltean DI, Gomez I, Pullikuth AK, Soberon M, et al. (2002) Heliothis virescens and Manduca sexta lipid rafts are involved in Cry1A toxin binding to the midgut epithelium and subsequent pore formation. J Biol Chem 277: 13863-13872.
    • (2002) J Biol Chem , vol.277 , pp. 13863-13872
    • Zhuang, M.1    Oltean, D.I.2    Gomez, I.3    Pullikuth, A.K.4    Soberon, M.5
  • 24
    • 0033523767 scopus 로고    scopus 로고
    • Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin
    • Abrami L, van Der Goot FG, (1999) Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin. J Cell Biol 147: 175-184.
    • (1999) J Cell Biol , vol.147 , pp. 175-184
    • Abrami, L.1    van Der Goot, F.G.2
  • 25
    • 33644943981 scopus 로고    scopus 로고
    • Detergent-resistant membranes are platforms for actinoporin pore-forming activity on intact cells
    • Alegre-Cebollada J, Rodriguez-Crespo I, Gavilanes JG, del Pozo AM, (2006) Detergent-resistant membranes are platforms for actinoporin pore-forming activity on intact cells. Febs J 273: 863-871.
    • (2006) Febs J , vol.273 , pp. 863-871
    • Alegre-Cebollada, J.1    Rodriguez-Crespo, I.2    Gavilanes, J.G.3    del Pozo, A.M.4
  • 26
    • 0037072947 scopus 로고    scopus 로고
    • Association of Helicobacter pylori vacuolating toxin (VacA) with lipid rafts
    • Schraw W, Li Y, McClain MS, van der Goot FG, Cover TL, (2002) Association of Helicobacter pylori vacuolating toxin (VacA) with lipid rafts. J Biol Chem 277: 34642-34650.
    • (2002) J Biol Chem , vol.277 , pp. 34642-34650
    • Schraw, W.1    Li, Y.2    McClain, M.S.3    van der Goot, F.G.4    Cover, T.L.5
  • 27
    • 77951910348 scopus 로고    scopus 로고
    • Ceramide-rich platforms in transmembrane signaling
    • Stancevic B, Kolesnick R, (2010) Ceramide-rich platforms in transmembrane signaling. FEBS Lett 584: 1728-1740.
    • (2010) FEBS Lett , vol.584 , pp. 1728-1740
    • Stancevic, B.1    Kolesnick, R.2
  • 28
    • 0142095498 scopus 로고    scopus 로고
    • Host defense against Pseudomonas aeruginosa requires ceramide-rich membrane rafts
    • Grassme H, Jendrossek V, Riehle A, von Kurthy G, Berger J, et al. (2003) Host defense against Pseudomonas aeruginosa requires ceramide-rich membrane rafts. Nat Med 9: 322-330.
    • (2003) Nat Med , vol.9 , pp. 322-330
    • Grassme, H.1    Jendrossek, V.2    Riehle, A.3    von Kurthy, G.4    Berger, J.5
  • 29
    • 22544470314 scopus 로고    scopus 로고
    • Caspase-dependent and -independent activation of acid sphingomyelinase signaling
    • Rotolo JA, Zhang J, Donepudi M, Lee H, Fuks Z, et al. (2005) Caspase-dependent and-independent activation of acid sphingomyelinase signaling. J Biol Chem 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
  • 32
    • 0029148660 scopus 로고
    • Ceramide synthase mediates daunorubicin-induced apoptosis: an alternative mechanism for generating death signals
    • Bose R, Verheij M, Haimovitz-Friedman A, Scotto K, Fuks Z, et al. (1995) Ceramide synthase mediates daunorubicin-induced apoptosis: an alternative mechanism for generating death signals. Cell 82: 405-414.
    • (1995) Cell , vol.82 , pp. 405-414
    • Bose, R.1    Verheij, M.2    Haimovitz-Friedman, A.3    Scotto, K.4    Fuks, Z.5
  • 33
    • 0030741528 scopus 로고    scopus 로고
    • Cytochrome c activation of CPP32-like proteolysis plays a critical role in a Xenopus cell-free apoptosis system
    • Kluck RM, Martin SJ, Hoffman BM, Zhou JS, Green DR, et al. (1997) Cytochrome c activation of CPP32-like proteolysis plays a critical role in a Xenopus cell-free apoptosis system. Embo J 16: 4639-4649.
    • (1997) Embo J , vol.16 , pp. 4639-4649
    • Kluck, R.M.1    Martin, S.J.2    Hoffman, B.M.3    Zhou, J.S.4    Green, D.R.5
  • 34
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis
    • Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD, (1997) The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275: 1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 35
    • 0035866785 scopus 로고    scopus 로고
    • Induction of the mitochondrial permeability transition mediates the killing of HeLa cells by staurosporine
    • Tafani M, Minchenko DA, Serroni A, Farber JL, (2001) Induction of the mitochondrial permeability transition mediates the killing of HeLa cells by staurosporine. Cancer Res 61: 2459-2466.
    • (2001) Cancer Res , vol.61 , pp. 2459-2466
    • Tafani, M.1    Minchenko, D.A.2    Serroni, A.3    Farber, J.L.4
  • 36
    • 0025273937 scopus 로고
    • Phospholipid synthesis in a membrane fraction associated with mitochondria
    • Vance JE, (1990) Phospholipid synthesis in a membrane fraction associated with mitochondria. J Biol Chem 265: 7248-7256.
    • (1990) J Biol Chem , vol.265 , pp. 7248-7256
    • Vance, J.E.1
  • 37
    • 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 JC, (2001) Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. J Biol Chem 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
  • 38
    • 0038025230 scopus 로고    scopus 로고
    • Association of Bax and Bak homo-oligomers in mitochondria. Bax requirement for Bak reorganization and cytochrome c release
    • Mikhailov V, Mikhailova M, Degenhardt K, Venkatachalam MA, White E, et al. (2003) Association of Bax and Bak homo-oligomers in mitochondria. Bax requirement for Bak reorganization and cytochrome c release. J Biol Chem 278: 5367-5376.
    • (2003) J Biol Chem , vol.278 , pp. 5367-5376
    • Mikhailov, V.1    Mikhailova, M.2    Degenhardt, K.3    Venkatachalam, M.A.4    White, E.5
  • 39
    • 0027278513 scopus 로고
    • Inhibition of sphingolipid synthesis affects axonal outgrowth in cultured hippocampal neurons
    • Harel R, Futerman AH, (1993) Inhibition of sphingolipid synthesis affects axonal outgrowth in cultured hippocampal neurons. J Biol Chem 268: 14476-14481.
    • (1993) J Biol Chem , vol.268 , pp. 14476-14481
    • Harel, R.1    Futerman, A.H.2
  • 40
    • 0027447521 scopus 로고
    • Ganglioside expression on human malignant melanoma assessed by quantitative immune thin-layer chromatography
    • Hamilton WB, Helling F, Lloyd KO, Livingston PO, (1993) Ganglioside expression on human malignant melanoma assessed by quantitative immune thin-layer chromatography. Int J Cancer 53: 566-573.
    • (1993) Int J Cancer , vol.53 , pp. 566-573
    • Hamilton, W.B.1    Helling, F.2    Lloyd, K.O.3    Livingston, P.O.4
  • 41
    • 0016618177 scopus 로고
    • Lecithin-sphingomyelin ratio in amniotic fluid, as assessed by a modified thin-layer chromatographic method in which a commercial pre-coated plate is used
    • Mallikarjuneswara VR, (1975) Lecithin-sphingomyelin ratio in amniotic fluid, as assessed by a modified thin-layer chromatographic method in which a commercial pre-coated plate is used. Clin Chem 21: 260-263.
    • (1975) Clin Chem , vol.21 , pp. 260-263
    • Mallikarjuneswara, V.R.1
  • 42
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: coregulation of dimer formation and intracellular localization
    • Suzuki M, Youle RJ, Tjandra N, (2000) Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103: 645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 43
    • 0038581115 scopus 로고    scopus 로고
    • Ceramide inhibits the potassium channel Kv1.3 by the formation of membrane platforms
    • Bock J, Szabo I, Gamper N, Adams C, Gulbins E, (2003) Ceramide inhibits the potassium channel Kv1.3 by the formation of membrane platforms. Biochem Biophys Res Commun 305: 890-897.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 890-897
    • Bock, J.1    Szabo, I.2    Gamper, N.3    Adams, C.4    Gulbins, E.5
  • 44
    • 0033535350 scopus 로고    scopus 로고
    • Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis
    • Desagher S, Osen-Sand A, Nichols A, Eskes R, Montessuit S, et al. (1999) Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J Cell Biol 144: 891-901.
    • (1999) J Cell Biol , vol.144 , pp. 891-901
    • Desagher, S.1    Osen-Sand, A.2    Nichols, A.3    Eskes, R.4    Montessuit, S.5
  • 45
    • 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 JC, (2000) Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol Cell Biol 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
  • 46
    • 0032487583 scopus 로고    scopus 로고
    • Bax-induced cytochrome C release from mitochondria is independent of the permeability transition pore but highly dependent on Mg2+ ions
    • Eskes R, Antonsson B, Osen-Sand A, Montessuit S, Richter C, et al. (1998) Bax-induced cytochrome C release from mitochondria is independent of the permeability transition pore but highly dependent on Mg2+ ions. J Cell Biol 143: 217-224.
    • (1998) J Cell Biol , vol.143 , pp. 217-224
    • Eskes, R.1    Antonsson, B.2    Osen-Sand, A.3    Montessuit, S.4    Richter, C.5
  • 47
    • 77953728877 scopus 로고    scopus 로고
    • Ceramide synthases 2, 5, and 6 confer distinct roles in radiation-induced apoptosis in HeLa cells
    • Mesicek J, Lee H, Feldman T, Jiang X, Skobeleva A, et al. (2010) Ceramide synthases 2, 5, and 6 confer distinct roles in radiation-induced apoptosis in HeLa cells. Cell Signal 22: 1300-1307.
    • (2010) Cell Signal , vol.22 , pp. 1300-1307
    • Mesicek, J.1    Lee, H.2    Feldman, T.3    Jiang, X.4    Skobeleva, A.5
  • 48
    • 1542465944 scopus 로고    scopus 로고
    • Molecular and cell biology of phosphatidylserine and phosphatidylethanolamine metabolism
    • Vance JE, (2003) Molecular and cell biology of phosphatidylserine and phosphatidylethanolamine metabolism. Prog Nucleic Acid Res Mol Biol 75: 69-111.
    • (2003) Prog Nucleic Acid Res Mol Biol , vol.75 , pp. 69-111
    • Vance, J.E.1
  • 49
    • 0029055754 scopus 로고
    • Evidence that phosphatidylserine is imported into mitochondria via a mitochondria-associated membrane and that the majority of mitochondrial phosphatidylethanolamine is derived from decarboxylation of phosphatidylserine
    • Shiao YJ, Lupo G, Vance JE, (1995) Evidence that phosphatidylserine is imported into mitochondria via a mitochondria-associated membrane and that the majority of mitochondrial phosphatidylethanolamine is derived from decarboxylation of phosphatidylserine. J Biol Chem 270: 11190-11198.
    • (1995) J Biol Chem , vol.270 , pp. 11190-11198
    • Shiao, Y.J.1    Lupo, G.2    Vance, J.E.3
  • 50
    • 0034602158 scopus 로고    scopus 로고
    • Phosphatidylserine synthase-1 and -2 are localized to mitochondria-associated membranes
    • Stone SJ, Vance JE, (2000) Phosphatidylserine synthase-1 and-2 are localized to mitochondria-associated membranes. J Biol Chem 275: 34534-34540.
    • (2000) J Biol Chem , vol.275 , pp. 34534-34540
    • Stone, S.J.1    Vance, J.E.2
  • 51
    • 42949105726 scopus 로고    scopus 로고
    • Ceramide synthesis in the endoplasmic reticulum can permeabilize mitochondria to proapoptotic proteins
    • Stiban J, Caputo L, Colombini M, (2008) Ceramide synthesis in the endoplasmic reticulum can permeabilize mitochondria to proapoptotic proteins. J Lipid Res 49: 625-634.
    • (2008) J Lipid Res , vol.49 , pp. 625-634
    • Stiban, J.1    Caputo, L.2    Colombini, M.3
  • 52
    • 33845987513 scopus 로고    scopus 로고
    • Protein kinase C-induced activation of a ceramide/protein phosphatase 1 pathway leading to dephosphorylation of p38 MAPK
    • Kitatani K, Idkowiak-Baldys J, Bielawski J, Taha TA, Jenkins RW, et al. (2006) Protein kinase C-induced activation of a ceramide/protein phosphatase 1 pathway leading to dephosphorylation of p38 MAPK. J Biol Chem 281: 36793-36802.
    • (2006) J Biol Chem , vol.281 , pp. 36793-36802
    • Kitatani, K.1    Idkowiak-Baldys, J.2    Bielawski, J.3    Taha, T.A.4    Jenkins, R.W.5
  • 53
    • 0027787984 scopus 로고
    • Fumonisin B1 inhibits sphingosine (sphinganine) N-acyltransferase and de novo sphingolipid biosynthesis in cultured neurons in situ
    • Merrill AH Jr, van Echten G, Wang E, Sandhoff K, (1993) Fumonisin B1 inhibits sphingosine (sphinganine) N-acyltransferase and de novo sphingolipid biosynthesis in cultured neurons in situ. J Biol Chem 268: 27299-27306.
    • (1993) J Biol Chem , vol.268 , pp. 27299-27306
    • Merrill Jr., A.H.1    van Echten, G.2    Wang, E.3    Sandhoff, K.4
  • 54
    • 0033581014 scopus 로고    scopus 로고
    • Ataxia telangiectasia-mutated gene product inhibits DNA damage-induced apoptosis via ceramide synthase
    • Liao WC, Haimovitz-Friedman A, Persaud RS, McLoughlin M, Ehleiter D, et al. (1999) Ataxia telangiectasia-mutated gene product inhibits DNA damage-induced apoptosis via ceramide synthase. J Biol Chem 274: 17908-17917.
    • (1999) J Biol Chem , vol.274 , pp. 17908-17917
    • Liao, W.C.1    Haimovitz-Friedman, A.2    Persaud, R.S.3    McLoughlin, M.4    Ehleiter, D.5
  • 55
    • 0037377677 scopus 로고    scopus 로고
    • De novo ceramide synthesis participates in the ultraviolet B irradiation-induced apoptosis in undifferentiated cultured human keratinocytes
    • Uchida Y, Nardo AD, Collins V, Elias PM, Holleran WM, (2003) De novo ceramide synthesis participates in the ultraviolet B irradiation-induced apoptosis in undifferentiated cultured human keratinocytes. J Invest Dermatol 120: 662-669.
    • (2003) J Invest Dermatol , vol.120 , pp. 662-669
    • Uchida, Y.1    Nardo, A.D.2    Collins, V.3    Elias, P.M.4    Holleran, W.M.5
  • 56
    • 0029848765 scopus 로고    scopus 로고
    • Structure-function comparisons of the proapoptotic protein Bax in yeast and mammalian cells
    • Zha H, Fisk HA, Yaffe MP, Mahajan N, Herman B, et al. (1996) Structure-function comparisons of the proapoptotic protein Bax in yeast and mammalian cells. Mol Cell Biol 16: 6494-6508.
    • (1996) Mol Cell Biol , vol.16 , pp. 6494-6508
    • Zha, H.1    Fisk, H.A.2    Yaffe, M.P.3    Mahajan, N.4    Herman, B.5
  • 57
    • 33845346790 scopus 로고    scopus 로고
    • Biophysics of sphingolipids I. Membrane properties of sphingosine, ceramides and other simple sphingolipids
    • Goni FM, Alonso A, (2006) Biophysics of sphingolipids I. Membrane properties of sphingosine, ceramides and other simple sphingolipids. Biochim Biophys Acta 1758: 1902-1921.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1902-1921
    • Goni, F.M.1    Alonso, A.2
  • 58
    • 0026317290 scopus 로고
    • Apical and basal Forssman antigen in MDCK II cells: a morphological and quantitative study
    • Butor C, Stelzer EH, Sonnenberg A, Davoust J, (1991) Apical and basal Forssman antigen in MDCK II cells: a morphological and quantitative study. Eur J Cell Biol 56: 269-285.
    • (1991) Eur J Cell Biol , vol.56 , pp. 269-285
    • Butor, C.1    Stelzer, E.H.2    Sonnenberg, A.3    Davoust, J.4
  • 59
    • 0032562796 scopus 로고    scopus 로고
    • Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations
    • Hsu YT, Youle RJ, (1998) Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations. J Biol Chem 273: 10777-10783.
    • (1998) J Biol Chem , vol.273 , pp. 10777-10783
    • Hsu, Y.T.1    Youle, R.J.2
  • 60
    • 0033884050 scopus 로고    scopus 로고
    • Compartmentalization of ceramide signaling: physical foundations and biological effects
    • Kolesnick RN, Goni FM, Alonso A, (2000) Compartmentalization of ceramide signaling: physical foundations and biological effects. J Cell Physiol 184: 285-300.
    • (2000) J Cell Physiol , vol.184 , pp. 285-300
    • Kolesnick, R.N.1    Goni, F.M.2    Alonso, A.3
  • 61
    • 0042335762 scopus 로고    scopus 로고
    • Ceramide-mediated clustering is required for CD95-DISC formation
    • Grassme H, Cremesti A, Kolesnick R, Gulbins E, (2003) Ceramide-mediated clustering is required for CD95-DISC formation. Oncogene 22: 5457-5470.
    • (2003) Oncogene , vol.22 , pp. 5457-5470
    • Grassme, H.1    Cremesti, A.2    Kolesnick, R.3    Gulbins, E.4
  • 62
    • 33748664357 scopus 로고    scopus 로고
    • TRAIL activates acid sphingomyelinase via a redox mechanism and releases ceramide to trigger apoptosis
    • Dumitru CA, Gulbins E, (2006) TRAIL activates acid sphingomyelinase via a redox mechanism and releases ceramide to trigger apoptosis. Oncogene 25: 5612-5625.
    • (2006) Oncogene , vol.25 , pp. 5612-5625
    • Dumitru, C.A.1    Gulbins, E.2
  • 63
    • 33745037188 scopus 로고    scopus 로고
    • Ceramide forms channels in mitochondrial outer membranes at physiologically relevant concentrations
    • Siskind LJ, Kolesnick R, Colombini D, (2006) Ceramide forms channels in mitochondrial outer membranes at physiologically relevant concentrations. Mitochondrion 6: 118-125.
    • (2006) Mitochondrion , vol.6 , pp. 118-125
    • Siskind, L.J.1    Kolesnick, R.2    Colombini, D.3
  • 64
    • 70349237249 scopus 로고    scopus 로고
    • Bax distribution into mitochondrial detergent-resistant microdomains is related to ceramide and cholesterol content in postischemic hearts
    • Martínez-Abundis E, Correa F, Pavón N, Zazueta C, (2009) Bax distribution into mitochondrial detergent-resistant microdomains is related to ceramide and cholesterol content in postischemic hearts. FEBS J 276: 5579-5588.
    • (2009) FEBS J , vol.276 , pp. 5579-5588
    • Martínez-Abundis, E.1    Correa, F.2    Pavón, N.3    Zazueta, C.4
  • 65
    • 33744921915 scopus 로고    scopus 로고
    • Lipid dependence of the channel properties of a colicin E1-lipid toroidal pore
    • Sobko AA, Kotova EA, Antonenko YN, Zakharov SD, Cramer WA, (2006) Lipid dependence of the channel properties of a colicin E1-lipid toroidal pore. J Biol Chem 281: 14408-14416.
    • (2006) J Biol Chem , vol.281 , pp. 14408-14416
    • Sobko, A.A.1    Kotova, E.A.2    Antonenko, Y.N.3    Zakharov, S.D.4    Cramer, W.A.5
  • 66
    • 0029981159 scopus 로고    scopus 로고
    • Different effects of enzyme-generated ceramides and diacylglycerols in phospholipid membrane fusion and leakage
    • Ruiz-Arguello MB, Basanez G, Goni FM, Alonso A, (1996) Different effects of enzyme-generated ceramides and diacylglycerols in phospholipid membrane fusion and leakage. J Biol Chem 271: 26616-26621.
    • (1996) J Biol Chem , vol.271 , pp. 26616-26621
    • Ruiz-Arguello, M.B.1    Basanez, G.2    Goni, F.M.3    Alonso, A.4
  • 67
    • 0032939644 scopus 로고    scopus 로고
    • Ceramides in phospholipid membranes: effects on bilayer stability and transition to nonlamellar phases
    • Veiga MP, Arrondo JL, Goni FM, Alonso A, (1999) Ceramides in phospholipid membranes: effects on bilayer stability and transition to nonlamellar phases. Biophys J 76: 342-350.
    • (1999) Biophys J , vol.76 , pp. 342-350
    • Veiga, M.P.1    Arrondo, J.L.2    Goni, F.M.3    Alonso, A.4
  • 68
    • 19444377889 scopus 로고    scopus 로고
    • Molecular associations and surface-active properties of short- and long-N-acyl chain ceramides
    • Sot J, Goni FM, Alonso A, (2005) Molecular associations and surface-active properties of short- and long-N-acyl chain ceramides. Biochim Biophys Acta 1711: 12-19.
    • (2005) Biochim Biophys Acta , vol.1711 , pp. 12-19
    • Sot, J.1    Goni, F.M.2    Alonso, A.3
  • 69
    • 33745812349 scopus 로고    scopus 로고
    • Protein phosphatase 2A enhances the proapoptotic function of Bax through dephosphorylation
    • Xin M, Deng X, (2006) Protein phosphatase 2A enhances the proapoptotic function of Bax through dephosphorylation. J Biol Chem 281: 18859-18867.
    • (2006) J Biol Chem , vol.281 , pp. 18859-18867
    • Xin, M.1    Deng, X.2
  • 70
    • 0035957921 scopus 로고    scopus 로고
    • Induction of apoptosis through B-cell receptor cross-linking occurs via de novo generated C16-ceramide and involves mitochondria
    • Kroesen BJ, Pettus B, Luberto C, Busman M, Sietsma H, et al. (2001) Induction of apoptosis through B-cell receptor cross-linking occurs via de novo generated C16-ceramide and involves mitochondria. J Biol Chem 276: 13606-13614.
    • (2001) J Biol Chem , vol.276 , pp. 13606-13614
    • Kroesen, B.J.1    Pettus, B.2    Luberto, C.3    Busman, M.4    Sietsma, H.5
  • 71
    • 20744432465 scopus 로고    scopus 로고
    • Down-regulation of ATM protein sensitizes human prostate cancer cells to radiation-induced apoptosis
    • Truman JP, Gueven N, Lavin M, Leibel S, Kolesnick R, et al. (2005) Down-regulation of ATM protein sensitizes human prostate cancer cells to radiation-induced apoptosis. J Biol Chem 280: 23262-23272.
    • (2005) J Biol Chem , vol.280 , pp. 23262-23272
    • Truman, J.P.1    Gueven, N.2    Lavin, M.3    Leibel, S.4    Kolesnick, R.5
  • 72
    • 0036534724 scopus 로고    scopus 로고
    • De novo-synthesized ceramide is involved in cannabinoid-induced apoptosis
    • Gomez del Pulgar T, Velasco G, Sanchez C, Haro A, Guzman M, (2002) De novo-synthesized ceramide is involved in cannabinoid-induced apoptosis. Biochem J 363: 183-188.
    • (2002) Biochem J , vol.363 , pp. 183-188
    • del Gomez, P.T.1    Velasco, G.2    Sanchez, C.3    Haro, A.4    Guzman, M.5
  • 73
    • 0037379889 scopus 로고    scopus 로고
    • Significant role of ceramide pathway in experimental gastric ulcer formation in rats
    • Uehara K, Miura S, Takeuchi T, Taki T, Nakashita M, et al. (2003) Significant role of ceramide pathway in experimental gastric ulcer formation in rats. J Pharmacol Exp Ther 305: 232-239.
    • (2003) J Pharmacol Exp Ther , vol.305 , pp. 232-239
    • Uehara, K.1    Miura, S.2    Takeuchi, T.3    Taki, T.4    Nakashita, M.5
  • 75
    • 18844434417 scopus 로고    scopus 로고
    • Ceramide upregulation causes pulmonary cell apoptosis and emphysema-like disease in mice
    • Petrache I, Natarajan V, Zhen L, Medler TR, Richter AT, et al. (2005) Ceramide upregulation causes pulmonary cell apoptosis and emphysema-like disease in mice. Nat Med 11: 491-498.
    • (2005) Nat Med , vol.11 , pp. 491-498
    • Petrache, I.1    Natarajan, V.2    Zhen, L.3    Medler, T.R.4    Richter, A.T.5
  • 76
    • 21044450491 scopus 로고    scopus 로고
    • ATM regulates target switching to escalating doses of radiation in the intestines
    • Ch'ang HJ, Maj JG, Paris F, Xing HR, Zhang J, et al. (2005) ATM regulates target switching to escalating doses of radiation in the intestines. Nat Med 11: 484-490.
    • (2005) Nat Med , vol.11 , pp. 484-490
    • Ch'ang, H.J.1    Maj, J.G.2    Paris, F.3    Xing, H.R.4    Zhang, J.5
  • 77
    • 0037178790 scopus 로고    scopus 로고
    • Ceramide channels increase the permeability of the mitochondrial outer membrane to small proteins
    • Siskind LJ, Kolesnick RN, Colombini M, (2002) Ceramide channels increase the permeability of the mitochondrial outer membrane to small proteins. J Biol Chem 277: 26796-26803.
    • (2002) J Biol Chem , vol.277 , pp. 26796-26803
    • Siskind, L.J.1    Kolesnick, R.N.2    Colombini, M.3
  • 78
    • 0036119432 scopus 로고    scopus 로고
    • A matrix-assisted laser desorption ionization post-source decay (MALDI-PSD) analysis of proteins released from isolated liver mitochondria treated with recombinant truncated Bid
    • Van Loo G, Demol H, van Gurp M, Hoorelbeke B, Schotte P, et al. (2002) A matrix-assisted laser desorption ionization post-source decay (MALDI-PSD) analysis of proteins released from isolated liver mitochondria treated with recombinant truncated Bid. Cell Death Differ 9: 301-308.
    • (2002) Cell Death Differ , vol.9 , pp. 301-308
    • van Loo, G.1    Demol, H.2    van Gurp, M.3    Hoorelbeke, B.4    Schotte, P.5


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