메뉴 건너뛰기




Volumn 369, Issue 2, 2003, Pages 199-211

Ceramide: Second messenger or modulator of membrane structure and dynamics?

Author keywords

Apoptosis; Diacylglycerol; Lipid raft; Sphingolipid; Vesicular trafficking

Indexed keywords

DIFFUSION; FUSION REACTIONS; LIPIDS; MEMBRANES; METABOLISM; TOPOLOGY;

EID: 0037440032     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021528     Document Type: Review
Times cited : (402)

References (178)
  • 1
    • 0033974782 scopus 로고    scopus 로고
    • Ceramide in the eukaryotic stress response
    • Hannun, Y. A. and Luberto, C. (2000) Ceramide in the eukaryotic stress response. Trends Cell Biol. 10, 73-80
    • (2000) Trends Cell Biol. , vol.10 , pp. 73-80
    • Hannun, Y.A.1    Luberto, C.2
  • 2
    • 0344349001 scopus 로고    scopus 로고
    • Signalling sphingomyelinases: Which, where, how and why?
    • Levade, T. and Jaffrézou, J.-P. (1999) Signalling sphingomyelinases: which, where, how and why? Biochim. Biophys. Acta 1438, 1-17
    • (1999) Biochim. Biophys. Acta , vol.1438 , pp. 1-17
    • Levade, T.1    Jaffrézou, J.-P.2
  • 3
    • 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. and Kolesnick, R. (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    Kolesnick, R.6
  • 4
    • 0034013476 scopus 로고    scopus 로고
    • The role of de novo ceramide synthesis in chemotherapy-induced apoptosis
    • Perry, D. K. (2000) The role of de novo ceramide synthesis in chemotherapy-induced apoptosis. Ann. N.Y. Acad. Sci. 905, 91-96
    • (2000) Ann. N.Y. Acad. Sci. , vol.905 , pp. 91-96
    • Perry, D.K.1
  • 5
    • 0031757668 scopus 로고    scopus 로고
    • Ceramides in apoptosis - Does it really matter?
    • Hofmann, K. and Dixit, V. M. (1998) Ceramides in apoptosis - does it really matter? Trends Biochem. Sci. 23, 374-377
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 374-377
    • Hofmann, K.1    Dixit, V.M.2
  • 7
    • 0034308223 scopus 로고    scopus 로고
    • Ceramide as a second messenger: Sticky solutions to sticky problems
    • Venkataraman, K. and Futerman, A. H. (2000) Ceramide as a second messenger: sticky solutions to sticky problems. Trends Cell Biol. 10, 408-412
    • (2000) Trends Cell Biol. , vol.10 , pp. 408-412
    • Venkataraman, K.1    Futerman, A.H.2
  • 8
    • 0032869856 scopus 로고    scopus 로고
    • Functional analysis of acid and neutral sphingomyelinases in vitro and in vivo
    • Stoffel, W. (1999) Functional analysis of acid and neutral sphingomyelinases in vitro and in vivo. Chem. Phys. Lipids 102, 107-121
    • (1999) Chem. Phys. Lipids , vol.102 , pp. 107-121
    • Stoffel, W.1
  • 9
    • 0034738011 scopus 로고    scopus 로고
    • Physiology and pathophysiology of sphingolipid metabolism and signalling
    • Huwiler, A., Kolter, T., Pfeilschifter, J. and Sandhoff, K. (2000) Physiology and pathophysiology of sphingolipid metabolism and signalling. Biochim. Biophys. Acta 1485, 63-99
    • (2000) Biochim. Biophys. Acta , vol.1485 , pp. 63-99
    • Huwiler, A.1    Kolter, T.2    Pfeilschifter, J.3    Sandhoff, K.4
  • 10
    • 0039518668 scopus 로고    scopus 로고
    • Structure and functional properties of diacylglycerols in membranes
    • Goni, F. M. and Alonso, A. (1999) Structure and functional properties of diacylglycerols in membranes. Prog. Lipid Res. 38, 1-48
    • (1999) Prog. Lipid Res. , vol.38 , pp. 1-48
    • Goni, F.M.1    Alonso, A.2
  • 11
    • 0033884050 scopus 로고    scopus 로고
    • Compartmentalization of ceramide signalling: Physical foundations and biological effects
    • Kolesnick, R. N., Goni, F. M. and Alonso, A. (2000) Compartmentalization of ceramide signalling: 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
  • 12
    • 0030868488 scopus 로고    scopus 로고
    • Lipid microdomains in dimyristoylphosphatidylcholine-ceramide liposomes
    • Holopainen, J. M., Lehtonen, J. Y. A. and Kinnunen, P. K. J. (1997) Lipid microdomains in dimyristoylphosphatidylcholine-ceramide liposomes. Chem. Phys. Lipids 88, 1-13
    • (1997) Chem. Phys. Lipids , vol.88 , pp. 1-13
    • Holopainen, J.M.1    Lehtonen, J.Y.A.2    Kinnunen, P.K.J.3
  • 13
    • 0032535156 scopus 로고    scopus 로고
    • Sphingomyelinase induces lipid microdomain formation in a fluid phosphatidylcholine/sphingomyelin membrane
    • Holopainen, J. M., Subramanian, M. and Kinnunen, P. K. J. (1998) Sphingomyelinase induces lipid microdomain formation in a fluid phosphatidylcholine/sphingomyelin membrane. Biochemistry 37, 17562-17570
    • (1998) Biochemistry , vol.37 , pp. 17562-17570
    • Holopainen, J.M.1    Subramanian, M.2    Kinnunen, P.K.J.3
  • 14
    • 0023145301 scopus 로고
    • Quantitative contributions of cholesterol and the individual classes of phospholipids and their degree of fatty acyl (un)saturation to membrane fluidity measured by fluorescence polarization
    • van Blitterswijk, W. J., van der Meer, B. W. and Hilkmann, H. (1987) Quantitative contributions of cholesterol and the individual classes of phospholipids and their degree of fatty acyl (un)saturation to membrane fluidity measured by fluorescence polarization. Biochemistry 26, 1746-1756
    • (1987) Biochemistry , vol.26 , pp. 1746-1756
    • Van Blitterswijk, W.J.1    Van Der Meer, B.W.2    Hilkmann, H.3
  • 15
    • 0035830645 scopus 로고    scopus 로고
    • Interaction of ceramides with phosphatidylcholine, sphingomyelin and sphingomyelin/cholesterol bilayers
    • Massey, J. B. (2001) Interaction of ceramides with phosphatidylcholine, sphingomyelin and sphingomyelin/cholesterol bilayers. Biochim. Biophys. Acta 1510, 167-184
    • (2001) Biochim. Biophys. Acta , vol.1510 , pp. 167-184
    • Massey, J.B.1
  • 16
    • 0034142110 scopus 로고    scopus 로고
    • Sphingolipid signalling domains: Floating on rafts or burried in caves?
    • Dobrowsky, R. T. (2000) Sphingolipid signalling domains: floating on rafts or burried in caves? Cell. Signalling 12, 81-90
    • (2000) Cell. Signalling , vol.12 , pp. 81-90
    • Dobrowsky, R.T.1
  • 17
    • 0035340071 scopus 로고    scopus 로고
    • A neutral sphingomyelinase resides in sphingolipid-enriched microdomains and is inhibited by the caveolin-scaffolding domain: Potential implications in tumour necrosis factor signalling
    • Veldman, R. J., Maestre, N., Aduib, O. M., Medin, J. A., Salvayre, R. and Levade, T. (2001) A neutral sphingomyelinase resides in sphingolipid-enriched microdomains and is inhibited by the caveolin-scaffolding domain: potential implications in tumour necrosis factor signalling. Biochem. J. 355, 859-868
    • (2001) Biochem. J. , vol.355 , pp. 859-868
    • Veldman, R.J.1    Maestre, N.2    Aduib, O.M.3    Medin, J.A.4    Salvayre, R.5    Levade, T.6
  • 19
    • 0030743667 scopus 로고    scopus 로고
    • Measurements of spontaneous transfer and transbilayer movement of BODIPY-labeled lipids in lipid vesicles
    • Bai, J. and Pagano, R. E. (1997) Measurements of spontaneous transfer and transbilayer movement of BODIPY-labeled lipids in lipid vesicles. Biochemistry 36, 8840-8848
    • (1997) Biochemistry , vol.36 , pp. 8840-8848
    • Bai, J.1    Pagano, R.E.2
  • 23
    • 0036195136 scopus 로고    scopus 로고
    • An essential role for membrane rafts in the initiation of Fas/CD95-triggered cell death in mouse thymocytes
    • Hueber, A.-O., Bernard, A.-M., Herincs, Z., Couzinet, A. and He, H.-T. (2002) An essential role for membrane rafts in the initiation of Fas/CD95-triggered cell death in mouse thymocytes. EMBO Rep. 3, 190-196
    • (2002) EMBO Rep. , vol.3 , pp. 190-196
    • Hueber, A.-O.1    Bernard, A.-M.2    Herincs, Z.3    Couzinet, A.4    He, H.-T.5
  • 24
    • 0344588823 scopus 로고    scopus 로고
    • 2-ceramide may be responsible for its ability to inhibit platelet aggregation
    • 2-ceramide may be responsible for its ability to inhibit platelet aggregation. Biochemistry 37, 2059-2069
    • (1998) Biochemistry , vol.37 , pp. 2059-2069
    • Simon C.G., Jr.1    Gear, A.R.L.2
  • 25
    • 0032939644 scopus 로고    scopus 로고
    • Ceramides in phospholipid membranes: Effects on bilayer stability and transition to nonlamellar phases
    • Veiga, M. P., Arrondo, J. L., Goni, F. M. and 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
  • 26
    • 0034602178 scopus 로고    scopus 로고
    • Glucosylceramide synthase does not attenuate the ceramide pool accumulating during apoptosis induced by CD95 or anti-cancer regimens
    • Tepper, A. D., Diks, S. H., van Blitterswijk, W. J. and Borst, J. (2000) Glucosylceramide synthase does not attenuate the ceramide pool accumulating during apoptosis induced by CD95 or anti-cancer regimens. J. Biol. Chem. 275, 34810-34817
    • (2000) J. Biol. Chem. , vol.275 , pp. 34810-34817
    • Tepper, A.D.1    Diks, S.H.2    Van Blitterswijk, W.J.3    Borst, J.4
  • 27
    • 0034141357 scopus 로고    scopus 로고
    • Lipid metabolic changes caused by short-chain ceramides and the connection with apoptosis
    • Allan, D. (2000) Lipid metabolic changes caused by short-chain ceramides and the connection with apoptosis. Biochem. J. 345, 603-610
    • (2000) Biochem. J. , vol.345 , pp. 603-610
    • Allan, D.1
  • 28
    • 0141793247 scopus 로고    scopus 로고
    • Inhibition of phosphatidylcholine and phosphatidylethanolamine biosynthesis in rat-2 fibroblasts by cell-permeable ceramides
    • Bladergroen, B. A., Bussiere, M., Klein, W., Geelen, M. J. H., van Golde, L. M. G. and Houweling, M. (1999) Inhibition of phosphatidylcholine and phosphatidylethanolamine biosynthesis in rat-2 fibroblasts by cell-permeable ceramides. Eur. J. Biochem. 264, 152-160
    • (1999) Eur. J. Biochem. , vol.264 , pp. 152-160
    • Bladergroen, B.A.1    Bussiere, M.2    Klein, W.3    Geelen, M.J.H.4    Van Golde, L.M.G.5    Houweling, M.6
  • 31
    • 0035688703 scopus 로고    scopus 로고
    • Lipid metabolism and vesicle trafficking: More than just greasing the transport machinery
    • McMaster, C. R. (2001) Lipid metabolism and vesicle trafficking: more than just greasing the transport machinery. Biochem. Cell Biol. 79, 681-692
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 681-692
    • McMaster, C.R.1
  • 32
    • 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. and van Blitterswijk, W. J. (2002) Alkyl-lysophospholipid accumulates in lipid rafts and induces apoptosis via raft-dependent endocytosis and inhibition of phosphatidylcholine synthesis. J. Biol. Chem. 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
  • 35
    • 0037066756 scopus 로고    scopus 로고
    • Biochemical mechanisms of the generation of endogenous long chain ceramide in response to exogenous short chain ceramide in the A549 human lung adenocarcinoma cell line
    • Ogretmen, B., Pettus, B. J., Rossi, M. J., Wood, R., Usta, J., Szulc, Z., Bielawska, A., Obeid, L. M. and Hannun, Y. A. (2002) Biochemical mechanisms of the generation of endogenous long chain ceramide in response to exogenous short chain ceramide in the A549 human lung adenocarcinoma cell line. J. Biol. Chem. 277, 12960-12969
    • (2002) J. Biol. Chem. , vol.277 , pp. 12960-12969
    • Ogretmen, B.1    Pettus, B.J.2    Rossi, M.J.3    Wood, R.4    Usta, J.5    Szulc, Z.6    Bielawska, A.7    Obeid, L.M.8    Hannun, Y.A.9
  • 36
    • 0034612304 scopus 로고    scopus 로고
    • Ceramide interaction with the respiratory chain of heart mitochondria
    • Di Paola, M., Cocco, T. and Lorusso, M. (2000) Ceramide interaction with the respiratory chain of heart mitochondria. Biochemistry 39, 6660-6668
    • (2000) Biochemistry , vol.39 , pp. 6660-6668
    • Di Paola, M.1    Cocco, T.2    Lorusso, M.3
  • 37
    • 0029981159 scopus 로고    scopus 로고
    • Different effects of enzyme-generated ceramides and diacylglycerols in phospholipid membrane fusion and leakage
    • Ruiz-Arguello, M. B., Basanez, G., Goni, F. M. and 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
  • 38
    • 0033525685 scopus 로고    scopus 로고
    • Ceramide induces cytochrome c release from isolated mitochondria; importance of mitochondrial redox state
    • Ghafourifar, P., Klein, S. D., Schucht, O., Schenk, U., Pruschy, M., Rocha, S. and Richter, C. (1999) Ceramide induces cytochrome c release from isolated mitochondria; importance of mitochondrial redox state. J. Biol. Chem. 274, 6080-6084
    • (1999) J. Biol. Chem. , vol.274 , pp. 6080-6084
    • Ghafourifar, P.1    Klein, S.D.2    Schucht, O.3    Schenk, U.4    Pruschy, M.5    Rocha, S.6    Richter, C.7
  • 39
    • 0037023765 scopus 로고    scopus 로고
    • Membrane restructuring via ceramide results in enhanced solute efflux
    • Montes, L. R., Ruiz-Arguello, M. B., Goni, F. M. and Alonso, A. (2002) Membrane restructuring via ceramide results in enhanced solute efflux. J. Biol. Chem. 277, 11788-11794
    • (2002) J. Biol. Chem. , vol.277 , pp. 11788-11794
    • Montes, L.R.1    Ruiz-Arguello, M.B.2    Goni, F.M.3    Alonso, A.4
  • 40
    • 0034623715 scopus 로고    scopus 로고
    • 16-ceramide form large stable channels. Implications for apoptosis
    • 16-ceramide form large stable channels. Implications for apoptosis. J. Biol. Chem. 275, 38640-38644
    • (2000) J. Biol. Chem. , vol.275 , pp. 38640-38644
    • Siskind, L.J.1    Colombini, M.2
  • 41
    • 0037178790 scopus 로고    scopus 로고
    • Ceramide channels increase the permeability of the mitochondrial outer membrane to small proteins
    • Siskind, L. J., Kolesnick, R. N. and 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
  • 42
    • 0141861184 scopus 로고    scopus 로고
    • Morphological changes induced by phospholipase C and by sphingomyelinase on large unilamellar vesicles: A cryo-transmission electronmicroscopy study of liposome fusion
    • Basanez, G., Ruiz-Arguello, M. B., Alonso, A., Goni, F. M., Karlsson, G. and Edwards, K. (1997) Morphological changes induced by phospholipase C and by sphingomyelinase on large unilamellar vesicles: a cryo-transmission electronmicroscopy study of liposome fusion. Biophys. J. 72, 2630-2637
    • (1997) Biophys. J. , vol.72 , pp. 2630-2637
    • Basanez, G.1    Ruiz-Arguello, M.B.2    Alonso, A.3    Goni, F.M.4    Karlsson, G.5    Edwards, K.6
  • 43
    • 0034087155 scopus 로고    scopus 로고
    • Vectorial budding of vesicles by asymmetrical enzymatic formation of ceramide in giant liposomes
    • Holopainen, J. M., Angelova, M. I. and Kinnunen, P. K. J. (2000) Vectorial budding of vesicles by asymmetrical enzymatic formation of ceramide in giant liposomes. Biophys. J. 78, 830-838
    • (2000) Biophys. J. , vol.78 , pp. 830-838
    • Holopainen, J.M.1    Angelova, M.I.2    Kinnunen, P.K.J.3
  • 48
    • 0034717903 scopus 로고    scopus 로고
    • Sphingolipid transport in eukaryotic cells
    • van Meer, G. and Holthuis, J. C. M. (2000) Sphingolipid transport in eukaryotic cells. Biochim. Biophys. Acta 1486, 145-170
    • (2000) Biochim. Biophys. Acta , vol.1486 , pp. 145-170
    • Van Meer, G.1    Holthuis, J.C.M.2
  • 49
    • 0027978352 scopus 로고
    • Identification of a distinct pool of sphingomyelin involved in the sphingomyelin cycle
    • Linardic, C. M. and Hannun, Y. A. (1994) Identification of a distinct pool of sphingomyelin involved in the sphingomyelin cycle. J. Biol. Chem. 269, 23530-23537
    • (1994) J. Biol. Chem. , vol.269 , pp. 23530-23537
    • Linardic, C.M.1    Hannun, Y.A.2
  • 50
    • 0029873839 scopus 로고    scopus 로고
    • Comparative study of the metabolic pools of sphingomyelin and phosphatidylcholine sensitive to tumor necrosis factor
    • Andrieu, N., Salvayre, R. and Levade, T. (1996) Comparative study of the metabolic pools of sphingomyelin and phosphatidylcholine sensitive to tumor necrosis factor. Eur. J. Biochem. 236, 738-745
    • (1996) Eur. J. Biochem. , vol.236 , pp. 738-745
    • Andrieu, N.1    Salvayre, R.2    Levade, T.3
  • 54
    • 0032079524 scopus 로고    scopus 로고
    • Glutathione regulation of neutral sphingomyelinase in tumor necrosis factor-alpha-induced cell death
    • Liu, B., Andrieu-Abadie, N., Levade, T., Zhang, P., Obeid, L. M. and Hannun, Y. A. (1998) Glutathione regulation of neutral sphingomyelinase in tumor necrosis factor-alpha-induced cell death. J. Biol. Chem. 273, 11313-11320
    • (1998) J. Biol. Chem. , vol.273 , pp. 11313-11320
    • Liu, B.1    Andrieu-Abadie, N.2    Levade, T.3    Zhang, P.4    Obeid, L.M.5    Hannun, Y.A.6
  • 55
    • 0037163870 scopus 로고    scopus 로고
    • Bcl-xL interrupts oxidative activation of neutral sphingomyelinase
    • Okamoto, Y., Obeid, L. M. and Hannun, Y. A. (2002) Bcl-xL interrupts oxidative activation of neutral sphingomyelinase. FEBS Lett. 530, 104-108
    • (2002) FEBS Lett. , vol.530 , pp. 104-108
    • Okamoto, Y.1    Obeid, L.M.2    Hannun, Y.A.3
  • 56
    • 0030893370 scopus 로고    scopus 로고
    • Expression of neutral sphingomyelinase identifies a distinct pool of sphingomyelin involved in apoptosis
    • Zhang, P., Liu, B., Jenkins, G. M., Hannun, Y. A. and Obeid, L. M. (1997) Expression of neutral sphingomyelinase identifies a distinct pool of sphingomyelin involved in apoptosis. J. Biol. Chem. 272, 9609-9612
    • (1997) J. Biol. Chem. , vol.272 , pp. 9609-9612
    • Zhang, P.1    Liu, B.2    Jenkins, G.M.3    Hannun, Y.A.4    Obeid, L.M.5
  • 57
    • 0028055154 scopus 로고
    • Conversion of diacylglycerol to phosphatidylcholine on the basolateral surface of epithelial (Madin-Darby Canine Kidney) cells
    • van Helvoort, A., van't Hof, W., Ritsema, T., Sandra, A. and van Meer, G. (1994) Conversion of diacylglycerol to phosphatidylcholine on the basolateral surface of epithelial (Madin-Darby Canine Kidney) cells. J. Biol. Chem. 269, 1763-1769
    • (1994) J. Biol. Chem. , vol.269 , pp. 1763-1769
    • Van Helvoort, A.1    Van't Hof, W.2    Ritsema, T.3    Sandra, A.4    Van Meer, G.5
  • 59
    • 0032571251 scopus 로고    scopus 로고
    • CD95 (Fas/APO-1) induces ceramide formation and apoptosis in the absence of a functional acid sphingomyelinase
    • Boesen-de Cock, J. G., Tepper, A. D., de Vries, E., van Blitterswijk, W. J. and Borst, J. (1998) CD95 (Fas/APO-1) induces ceramide formation and apoptosis in the absence of a functional acid sphingomyelinase. J. Biol. Chem. 273, 7560-7565
    • (1998) J. Biol. Chem. , vol.273 , pp. 7560-7565
    • Boesen-De Cock, J.G.1    Tepper, A.D.2    De Vries, E.3    Van Blitterswijk, W.J.4    Borst, J.5
  • 60
    • 0032536876 scopus 로고    scopus 로고
    • Acidic sphingomyelinase (ASM) is necessary for Fas-induced GD3 ganglioside accumulation and efficient apoptosis in lymphoid cells
    • De Maria, R., Rippo, M. R., Schuchman, E. H. and Testi, R. (1997) Acidic sphingomyelinase (ASM) is necessary for Fas-induced GD3 ganglioside accumulation and efficient apoptosis in lymphoid cells. J. Exp. Med. 187, 897-902
    • (1997) J. Exp. Med. , vol.187 , pp. 897-902
    • De Maria, R.1    Rippo, M.R.2    Schuchman, E.H.3    Testi, R.4
  • 65
    • 0033965898 scopus 로고    scopus 로고
    • Caveolin 1-mediated regulation of receptor tyrosine kinase-associated phosphatidylinositol 3-kinase activity by ceramide
    • Zundel, W., Swiersz, L. M. and Giaccia, A. (2000) Caveolin 1-mediated regulation of receptor tyrosine kinase-associated phosphatidylinositol 3-kinase activity by ceramide. Mol. Cell. Biol. 20, 1507-1514
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1507-1514
    • Zundel, W.1    Swiersz, L.M.2    Giaccia, A.3
  • 66
    • 0035807229 scopus 로고    scopus 로고
    • The role of ceramide in receptor- and stress-induced apoptosis studied in acidic ceramidase-deficient Farber disease cells
    • Burek, C., Roth, J., Koch, H.-G., Harzer, K., Los, M. and Schulze-Osthoff, K. (2001) The role of ceramide in receptor- and stress-induced apoptosis studied in acidic ceramidase-deficient Farber disease cells. Oncogene 20, 6493-6502
    • (2001) Oncogene , vol.20 , pp. 6493-6502
    • Burek, C.1    Roth, J.2    Koch, H.-G.3    Harzer, K.4    Los, M.5    Schulze-Osthoff, K.6
  • 67
    • 0034017357 scopus 로고    scopus 로고
    • Perturbation of membrane microdomains reduces mitogenic signaling and increases susceptibility to apoptosis after T cell receptor stimulation
    • Nix, M. and Stoffel, W. (2000) Perturbation of membrane microdomains reduces mitogenic signaling and increases susceptibility to apoptosis after T cell receptor stimulation. Cell Death Differ. 7, 413-424
    • (2000) Cell Death Differ , vol.7 , pp. 413-424
    • Nix, M.1    Stoffel, W.2
  • 68
    • 0030448021 scopus 로고    scopus 로고
    • Functions of ceramide in coordinating cellular responses to stress
    • Hannun, Y. A. (1996) Functions of ceramide in coordinating cellular responses to stress. Science 274, 1855-1859
    • (1996) Science , vol.274 , pp. 1855-1859
    • Hannun, Y.A.1
  • 69
    • 0030774818 scopus 로고    scopus 로고
    • CD95/Fas-induced ceramide formation proceeds with slow kinetics and is not blocked by caspase-3/CPP32 inhibition
    • Tepper, A. D., Boesen-de Cock, J. G., de Vries, E., Borst, J. and van Blitterswijk, W. J. (1997) CD95/Fas-induced ceramide formation proceeds with slow kinetics and is not blocked by caspase-3/CPP32 inhibition. J. Biol. Chem. 272, 24308-24312
    • (1997) J. Biol. Chem. , vol.272 , pp. 24308-24312
    • Tepper, A.D.1    Boesen-De Cock, J.G.2    De Vries, E.3    Borst, J.4    Van Blitterswijk, W.J.5
  • 70
    • 0032900335 scopus 로고    scopus 로고
    • Ordering of ceramide formation, caspase activation, and mitochondrial changes during CD95- and DNA damage-induced apoptosis
    • Tepper, A. D., de Vries, E., van Blitterswijk, W. J. and Borst, J. (1999) Ordering of ceramide formation, caspase activation, and mitochondrial changes during CD95- and DNA damage-induced apoptosis. J. Clin. Invest. 103, 971-978
    • (1999) J. Clin. Invest. , vol.103 , pp. 971-978
    • Tepper, A.D.1    De Vries, E.2    Van Blitterswijk, W.J.3    Borst, J.4
  • 71
    • 0034631827 scopus 로고    scopus 로고
    • Sphingomyelin hydrolysis to ceramide during the execution phase of apoptosis results from phospholipid scrambling and alters cell-surface morphology
    • Tepper, A. D., Ruurs, P., Wiedmer, T., Sims, P., Borst, J. and van Blitterswijk, W. J. (2000) Sphingomyelin hydrolysis to ceramide during the execution phase of apoptosis results from phospholipid scrambling and alters cell-surface morphology. J. Cell Biol. 150, 155-164
    • (2000) J. Cell Biol. , vol.150 , pp. 155-164
    • Tepper, A.D.1    Ruurs, P.2    Wiedmer, T.3    Sims, P.4    Borst, J.5    Van Blitterswijk, W.J.6
  • 72
  • 73
    • 0040737621 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and expression of a novel human neutral sphingomyelinase
    • Chatterjee, S., Han, H., Rollins, S. and Cleveland, T. (1999) Molecular cloning, characterization, and expression of a novel human neutral sphingomyelinase. J. Biol. Chem. 274, 37407-37412
    • (1999) J. Biol. Chem. , vol.274 , pp. 37407-37412
    • Chatterjee, S.1    Han, H.2    Rollins, S.3    Cleveland, T.4
  • 75
    • 0034811417 scopus 로고    scopus 로고
    • Effect of overexpression of a neutral sphingomyelinase on CD95-induced ceramide production and apoptosis
    • Tepper, A. D., Ruurs, P., Borst, J. and van Blitterswijk, W. J. (2001) Effect of overexpression of a neutral sphingomyelinase on CD95-induced ceramide production and apoptosis. Biochem. Biophys. Res. Commun. 280, 634-639
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 634-639
    • Tepper, A.D.1    Ruurs, P.2    Borst, J.3    Van Blitterswijk, W.J.4
  • 76
    • 0035074269 scopus 로고    scopus 로고
    • Apoptosis: Caspases orchestrate the ROCK n' bleb
    • Leverrier, Y. and Ridley, A. J. (2001) Apoptosis: caspases orchestrate the ROCK n' bleb. Nat. Cell Biol. 3, E91-E93
    • (2001) Nat. Cell Biol. , vol.3
    • Leverrier, Y.1    Ridley, A.J.2
  • 77
    • 0032959608 scopus 로고    scopus 로고
    • Lipid regulators of membrane traffic through the Golgi complex
    • Roth, M. G. (1999) Lipid regulators of membrane traffic through the Golgi complex. Trends Cell Biol. 9, 174-179
    • (1999) Trends Cell Biol. , vol.9 , pp. 174-179
    • Roth, M.G.1
  • 78
    • 0037059448 scopus 로고    scopus 로고
    • Slick recruitment to the Golgi
    • Bankaitis, V. A. (2002) Slick recruitment to the Golgi. Science 295, 290-291
    • (2002) Science , vol.295 , pp. 290-291
    • Bankaitis, V.A.1
  • 79
    • 0035830496 scopus 로고    scopus 로고
    • Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network
    • Liljedahl, M., Maeda, Y., Cotanzi, A., Ayala, I., van Lint, J. and Mathotra, V. (2001) Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network. Cell 104, 409-420
    • (2001) Cell , vol.104 , pp. 409-420
    • Liljedahl, M.1    Maeda, Y.2    Cotanzi, A.3    Ayala, I.4    Van Lint, J.5    Mathotra, V.6
  • 80
    • 0037059451 scopus 로고    scopus 로고
    • Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane
    • Baron, C. L. and Malhotra, V. (2002) Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane. Science 295, 325-328
    • (2002) Science , vol.295 , pp. 325-328
    • Baron, C.L.1    Malhotra, V.2
  • 82
    • 0035158785 scopus 로고    scopus 로고
    • Phosphatidylcholine synthesis influences the diacylglycerol homeostasis required for Sec14p-dependent Golgi function and cell growth
    • Henneberry, A. L., Lagace, T. A., Ridgway, N. D. and McMaster, C. R. (2001) Phosphatidylcholine synthesis influences the diacylglycerol homeostasis required for Sec14p-dependent Golgi function and cell growth. Mol. Biol. Cell 12, 511-520
    • (2001) Mol. Biol. Cell , vol.12 , pp. 511-520
    • Henneberry, A.L.1    Lagace, T.A.2    Ridgway, N.D.3    McMaster, C.R.4
  • 83
    • 0032486257 scopus 로고    scopus 로고
    • Sphingomyelin synthase, a potential regulator of intracellular levels of ceramide and diacylglycerol during SV40 transformation. Does sphingomyelin synthase account for the putative phosphatidylcholine-specific phospholipase C?
    • Luberto, C. and Hannun, Y. A. (1998) Sphingomyelin synthase, a potential regulator of intracellular levels of ceramide and diacylglycerol during SV40 transformation. Does sphingomyelin synthase account for the putative phosphatidylcholine-specific phospholipase C? J. Biol. Chem. 273, 14550-14559
    • (1998) J. Biol. Chem. , vol.273 , pp. 14550-14559
    • Luberto, C.1    Hannun, Y.A.2
  • 84
    • 0034640391 scopus 로고    scopus 로고
    • Differential effects of sphingomyelin hydrolysis and resynthesis on the activation of NF-κB in normal and SV40-transformed human fibroblasts
    • Luberto, C., Yoo, D. S., Suidan, H. S., Bartoli, G. M. and Hannun, Y. A. (2000) Differential effects of sphingomyelin hydrolysis and resynthesis on the activation of NF-κB in normal and SV40-transformed human fibroblasts. J. Biol. Chem. 275, 14760-14766
    • (2000) J. Biol. Chem. , vol.275 , pp. 14760-14766
    • Luberto, C.1    Yoo, D.S.2    Suidan, H.S.3    Bartoli, G.M.4    Hannun, Y.A.5
  • 85
    • 0034726106 scopus 로고    scopus 로고
    • Cell type specific localization of sphingomyelin biosynthesis
    • Sadeghlar, F., Sandhoff, K. and van Echten-Deckert, G. (2000) Cell type specific localization of sphingomyelin biosynthesis. FEBS Lett. 478, 9-12
    • (2000) FEBS Lett. , vol.478 , pp. 9-12
    • Sadeghlar, F.1    Sandhoff, K.2    Van Echten-Deckert, G.3
  • 86
    • 0032126336 scopus 로고    scopus 로고
    • The tumour necrosis factor-sensitive pool of sphingomyelin is resynthesized in a distinct compartment of the plasma membrane
    • Andrieu-Abadie, N., Carpentier, S., Salvayre, R. and Levade, T. (1998) The tumour necrosis factor-sensitive pool of sphingomyelin is resynthesized in a distinct compartment of the plasma membrane. Biochem J. 333, 91-97
    • (1998) Biochem J. , vol.333 , pp. 91-97
    • Andrieu-Abadie, N.1    Carpentier, S.2    Salvayre, R.3    Levade, T.4
  • 88
    • 0032055909 scopus 로고    scopus 로고
    • Utilization of phosphatidylcholine and production of diradylglycerol as a consequence of sphingomyelin synthesis
    • Sillence, D. J. and Allan, D. (1998) Utilization of phosphatidylcholine and production of diradylglycerol as a consequence of sphingomyelin synthesis. Biochem. J. 331, 251-256
    • (1998) Biochem. J. , vol.331 , pp. 251-256
    • Sillence, D.J.1    Allan, D.2
  • 89
    • 0026458406 scopus 로고
    • TNF activates NF-kappa B by phosphatidylcholine-specific phospholipase C-induced "acidic" sphingomyelin breakdown
    • Schutze, S., Potthoff, K., Machleidt, T., Berkovic, D., Wiegmann, K. and Kronke, M. (1992) TNF activates NF-kappa B by phosphatidylcholine-specific phospholipase C-induced "acidic" sphingomyelin breakdown. Cell 71, 765-776
    • (1992) Cell , vol.71 , pp. 765-776
    • Schutze, S.1    Potthoff, K.2    Machleidt, T.3    Berkovic, D.4    Wiegmann, K.5    Kronke, M.6
  • 90
    • 0036471395 scopus 로고    scopus 로고
    • Cell-permeable ceramides preferentially inhibit coated vesicle formation and exocytosis in CHO compared to MDCK cells by preventing the membrane association of ADP-ribosylation factor
    • Abousalham, A., Hobman, T. C., Dewald, J., Garbutt, M. and Brindley, D. N. (2002) Cell-permeable ceramides preferentially inhibit coated vesicle formation and exocytosis in CHO compared to MDCK cells by preventing the membrane association of ADP-ribosylation factor. Biochem. J. 361, 653-661
    • (2002) Biochem. J. , vol.361 , pp. 653-661
    • Abousalham, A.1    Hobman, T.C.2    Dewald, J.3    Garbutt, M.4    Brindley, D.N.5
  • 91
    • 0000255378 scopus 로고    scopus 로고
    • Expression of glucosylceramide synthase, converting ceramide to glucosylceramide, confers adriamycin resistance in human breast cancer cells
    • Liu, Y.-Y., Han, T.-Y., Giuliano, A. E. and Cabot, M. C. (1999) Expression of glucosylceramide synthase, converting ceramide to glucosylceramide, confers adriamycin resistance in human breast cancer cells. J. Biol. Chem. 274, 1140-1146
    • (1999) J. Biol. Chem. , vol.274 , pp. 1140-1146
    • Liu, Y.-Y.1    Han, T.-Y.2    Giuliano, A.E.3    Cabot, M.C.4
  • 92
    • 0033231485 scopus 로고    scopus 로고
    • Glycosylation of ceramide potentiates cellular resistance to tumor necrosis factor-alpha-induced apoptosis
    • Liu, Y.-Y., Han, T.-Y., Giuliano, A. E., Ichikawa, S., Hirabayashi, Y. and Cabot, M. C. (1999) Glycosylation of ceramide potentiates cellular resistance to tumor necrosis factor-alpha-induced apoptosis. Exp. Cell Res. 252, 464-470
    • (1999) Exp. Cell Res. , vol.252 , pp. 464-470
    • Liu, Y.-Y.1    Han, T.-Y.2    Giuliano, A.E.3    Ichikawa, S.4    Hirabayashi, Y.5    Cabot, M.C.6
  • 93
    • 0033565728 scopus 로고    scopus 로고
    • Multidrug resistance modulators and doxorubicin synergise to elevate ceramide levels and elicit apoptosis in drug-resistant cancer cells
    • Lucci, A., Han, T.-Y., Liu, Y.-Y., Giuliano, A. E. and Cabot, M. C. (1999) Multidrug resistance modulators and doxorubicin synergise to elevate ceramide levels and elicit apoptosis in drug-resistant cancer cells. Cancer 86, 300-311
    • (1999) Cancer , vol.86 , pp. 300-311
    • Lucci, A.1    Han, T.-Y.2    Liu, Y.-Y.3    Giuliano, A.E.4    Cabot, M.C.5
  • 94
    • 0036633148 scopus 로고    scopus 로고
    • Enhanced de novo ceramide generation through activation of serine palmitoyltransferase by the P-glycoprotein antagonist SDZ PSC 833 in breast cancer cells
    • Wang, H., Giuliano, A. E. and Cabot, M. C. (2002) Enhanced de novo ceramide generation through activation of serine palmitoyltransferase by the P-glycoprotein antagonist SDZ PSC 833 in breast cancer cells. Mol. Cancer Therap. 1, 719-726
    • (2002) Mol. Cancer Therap. , vol.1 , pp. 719-726
    • Wang, H.1    Giuliano, A.E.2    Cabot, M.C.3
  • 95
    • 0035313233 scopus 로고    scopus 로고
    • Potentiation of okadaic acid-induced ceramide elevation but not apoptosis by inhibition of glucosylceramide synthase in human neuroepithelioma cells
    • Di Bartolomeo, S. and Spinedi, A. (2001) Potentiation of okadaic acid-induced ceramide elevation but not apoptosis by inhibition of glucosylceramide synthase in human neuroepithelioma cells. Biochem. Pharmacol. 61, 851-856
    • (2001) Biochem. Pharmacol. , vol.61 , pp. 851-856
    • Di Bartolomeo, S.1    Spinedi, A.2
  • 96
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondria as the central control point of apoptosis
    • Desagher, S. and Martinou, J.-C. (2000) Mitochondria as the central control point of apoptosis. Trends Cell Biol. 10, 369-377
    • (2000) Trends Cell Biol. , vol.10 , pp. 369-377
    • Desagher, S.1    Martinou, J.-C.2
  • 97
    • 0035910473 scopus 로고    scopus 로고
    • Occurrence of ceramides and neutral glycolipids with unusual long-chain base composition in purified rat liver mitochondria
    • Ardail, D., Popa, I., Alcantara, K., Pons, A., Zanetta, J. P., Louisot, P., Thomas, L. and Portoukalian, J. (2001) Occurrence of ceramides and neutral glycolipids with unusual long-chain base composition in purified rat liver mitochondria. FEBS Lett. 488, 160-164
    • (2001) FEBS Lett. , vol.488 , pp. 160-164
    • Ardail, D.1    Popa, I.2    Alcantara, K.3    Pons, A.4    Zanetta, J.P.5    Louisot, P.6    Thomas, L.7    Portoukalian, J.8
  • 98
    • 0031470335 scopus 로고    scopus 로고
    • Import of lipids into mitochondria
    • Daum, G. and Vance, J. E. (1997) Import of lipids into mitochondria. Prog. Lipid Res. 36, 103-130
    • (1997) Prog. Lipid Res. , vol.36 , pp. 103-130
    • Daum, G.1    Vance, J.E.2
  • 99
    • 0034618102 scopus 로고    scopus 로고
    • Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisae
    • Prinz, W. A., Grzyb, L., Veenhuis, M., Kahana, J. A., Silver, P. A. and Rapoport, A. (2000) Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisae. J. Cell Biol. 150, 461-474
    • (2000) J. Cell Biol. , vol.150 , pp. 461-474
    • Prinz, W.A.1    Grzyb, L.2    Veenhuis, M.3    Kahana, J.A.4    Silver, P.A.5    Rapoport, A.6
  • 100
    • 0035956989 scopus 로고    scopus 로고
    • Organellar relationships in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography
    • Marsh, B. J., Mastronarde, D. N., Buttle, K. F., Howell, K. E. and McIntosh, J. R. (2001) Organellar relationships in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography. Proc. Natl. Acad. Sci. U.S.A. 98, 2399-2406
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2399-2406
    • Marsh, B.J.1    Mastronarde, D.N.2    Buttle, K.F.3    Howell, K.E.4    McIntosh, J.R.5
  • 101
    • 1842330849 scopus 로고    scopus 로고
    • Direct effect of ceramide on the mitochondrial electron transport chain leads to generation of reactive oxygen species. Role of mitochondrial glutathione
    • Garcia-Ruiz, C., Colell, A., Mari, M., Morales, A. and Fernandez-Checa, J. C. (1997) Direct effect of ceramide on the mitochondrial electron transport chain leads to generation of reactive oxygen species. Role of mitochondrial glutathione. J. Biol. Chem. 272, 11369-11377
    • (1997) J. Biol. Chem. , vol.272 , pp. 11369-11377
    • Garcia-Ruiz, C.1    Colell, A.2    Mari, M.3    Morales, A.4    Fernandez-Checa, J.C.5
  • 104
    • 0035907364 scopus 로고    scopus 로고
    • Biochemical characterization of the reverse activity of rat brain ceramidase. A CoA-independent and fumonisin B1-insensitive ceramide synthase
    • El Bawab, S., Birbes, H., Roddy, P., Szulc, Z. M., Bielawska, A. and Hannun, Y. A. (2001) Biochemical characterization of the reverse activity of rat brain ceramidase. A CoA-independent and fumonisin B1-insensitive ceramide synthase. J. Biol. Chem. 276, 16758-16766
    • (2001) J. Biol. Chem. , vol.276 , pp. 16758-16766
    • El Bawab, S.1    Birbes, H.2    Roddy, P.3    Szulc, Z.M.4    Bielawska, A.5    Hannun, Y.A.6
  • 105
    • 0035199418 scopus 로고    scopus 로고
    • Selective hydrolysis of a mitochondrial pool of sphingomyelin induces apoptosis
    • Birbes, H., El Bawab, S., Hannun, Y. A. and Obeid, L. M. (2001) Selective hydrolysis of a mitochondrial pool of sphingomyelin induces apoptosis. FASEB J. 14, 2669-2679
    • (2001) FASEB J. , vol.14 , pp. 2669-2679
    • Birbes, H.1    El Bawab, S.2    Hannun, Y.A.3    Obeid, L.M.4
  • 107
    • 0034306169 scopus 로고    scopus 로고
    • Cardiolipin provides specificity for targeting of tBid to mitochondria
    • Lutter, M., Fang, M., Luo, X., Nishijima, M., Xie, X. and Wang, X. (2000) Cardiolipin provides specificity for targeting of tBid to mitochondria. Nat. Cell Biol. 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
  • 110
    • 0036479053 scopus 로고    scopus 로고
    • Mitochondria as sensors of sphingolipids
    • Tomassini, B. and Testi, R. (2002) Mitochondria as sensors of sphingolipids. Biochimie 84, 123-129
    • (2002) Biochimie , vol.84 , pp. 123-129
    • Tomassini, B.1    Testi, R.2
  • 113
    • 0037189948 scopus 로고    scopus 로고
    • Ceramide generated by acidic sphingomyelinase contributes to tumor necrosis factor-α-mediated apoptosis in human colon HT-29 cells through glycosphingolipid formation. Possible role of ganglioside GD3
    • Colell, A., Morales, A., Fernandez-Checa, J. C. and Garcia-Ruiz, C. (2002) Ceramide generated by acidic sphingomyelinase contributes to tumor necrosis factor-α-mediated apoptosis in human colon HT-29 cells through glycosphingolipid formation. Possible role of ganglioside GD3. FEBS Lett. 526, 135-141
    • (2002) FEBS Lett. , vol.526 , pp. 135-141
    • Colell, A.1    Morales, A.2    Fernandez-Checa, J.C.3    Garcia-Ruiz, C.4
  • 114
    • 0035423556 scopus 로고    scopus 로고
    • Roles of lipid rafts in membrane transport
    • Ikonen, E. (2001) Roles of lipid rafts in membrane transport. Curr. Opin. Cell Biol. 13, 470-477
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 470-477
    • Ikonen, E.1
  • 117
    • 0343883506 scopus 로고    scopus 로고
    • Direct interaction of GD3 ganglioside with mitochondria generates reactive oxygen species followed by mitochondrial permeability transition, cytochrome c release, and caspase activation
    • Garcia-Ruiz, C., Colell, A., Paris, R. and Fernandez-Checa, J. C. (2000) Direct interaction of GD3 ganglioside with mitochondria generates reactive oxygen species followed by mitochondrial permeability transition, cytochrome c release, and caspase activation. FASEB J. 14, 847-858
    • (2000) FASEB J. , vol.14 , pp. 847-858
    • Garcia-Ruiz, C.1    Colell, A.2    Paris, R.3    Fernandez-Checa, J.C.4
  • 118
    • 0032514918 scopus 로고    scopus 로고
    • BAD enables ceramide to signal apoptosis via Ras and Raf-1
    • Basu, S., Bayoumy, S., Zhang, Y., Lozano, J. and Kolesnick, R. (1998) BAD enables ceramide to signal apoptosis via Ras and Raf-1. J. Biol. Chem. 273, 30419-30426
    • (1998) J. Biol. Chem. , vol.273 , pp. 30419-30426
    • Basu, S.1    Bayoumy, S.2    Zhang, Y.3    Lozano, J.4    Kolesnick, R.5
  • 119
    • 0037030465 scopus 로고    scopus 로고
    • Ceramide induces mitochondrial activation and apoptosis via a Bax-dependent pathway in human carcinoma cells
    • von Haefen, C., Wieder, T., Gillissen, B., Starck, L., Graupner, V., Dorken, B. and Daniel, P. T. (2002) Ceramide induces mitochondrial activation and apoptosis via a Bax-dependent pathway in human carcinoma cells. Oncogene 21, 4009-4019
    • (2002) Oncogene , vol.21 , pp. 4009-4019
    • Von Haefen, C.1    Wieder, T.2    Gillissen, B.3    Starck, L.4    Graupner, V.5    Dorken, B.6    Daniel, P.T.7
  • 120
    • 0036533631 scopus 로고    scopus 로고
    • Segregation of Bad from lipid rafts is implicated in the induction of apoptosis
    • Ayllon, V., Fleischer, A., Cayla, X., Garcia, A. and Rebollo, A. (2002) Segregation of Bad from lipid rafts is implicated in the induction of apoptosis. J. Immunol. 168, 3387-3393
    • (2002) J. Immunol. , vol.168 , pp. 3387-3393
    • Ayllon, V.1    Fleischer, A.2    Cayla, X.3    Garcia, A.4    Rebollo, A.5
  • 121
    • 0027965006 scopus 로고
    • Protein kinase C ζ isoform is critical for κB-dependent promoter activation by sphingomyelinase
    • Lozano, J., Berra, E., Municio, M. M., Diaz-Meco, M. T., Dominguez, I., Sanz, L. and Moscat, J. (1994) Protein kinase C ζ isoform is critical for κB-dependent promoter activation by sphingomyelinase. J. Biol. Chem. 269, 19200-19202
    • (1994) J. Biol. Chem. , vol.269 , pp. 19200-19202
    • Lozano, J.1    Berra, E.2    Municio, M.M.3    Diaz-Meco, M.T.4    Dominguez, I.5    Sanz, L.6    Moscat, J.7
  • 122
    • 0029003788 scopus 로고
    • PKCζ is a molecular switch in signal transduction of TNF-α, bifunctionally regulated by ceramide and arachidonic acid
    • Muller, G., Ayoub, M., Storz, P., Rennecke, J., Fabbro, D. and Pfizenmaier, K. (1995) PKCζ is a molecular switch in signal transduction of TNF-α, bifunctionally regulated by ceramide and arachidonic acid. EMBO J. 14, 1961-1969
    • (1995) EMBO J. , vol.14 , pp. 1961-1969
    • Muller, G.1    Ayoub, M.2    Storz, P.3    Rennecke, J.4    Fabbro, D.5    Pfizenmaier, K.6
  • 125
    • 0035116903 scopus 로고    scopus 로고
    • Kinase suppressor of Ras is necessary for tumor necrosis factor α activation of extracellular signal-regulated kinase/mitogen-activated protein kinase in intestinal epithelial cells
    • Yan, F. and Polk, D. B. (2001) Kinase suppressor of Ras is necessary for tumor necrosis factor α activation of extracellular signal-regulated kinase/mitogen-activated protein kinase in intestinal epithelial cells. Cancer Res. 61, 963-969
    • (2001) Cancer Res. , vol.61 , pp. 963-969
    • Yan, F.1    Polk, D.B.2
  • 127
  • 128
    • 0037151038 scopus 로고    scopus 로고
    • A functional role for the B56 alpha-subunit of protein phosphatase 2A in ceramide-mediated regulation of Bcl2 phosphorylation status and function
    • Ruvolo, P. P., Clark, W., Mumby, M., Gao, F. and May, W. S. (2002) A functional role for the B56 alpha-subunit of protein phosphatase 2A in ceramide-mediated regulation of Bcl2 phosphorylation status and function. J. Biol. Chem. 277, 22847-22852
    • (2002) J. Biol. Chem. , vol.277 , pp. 22847-22852
    • Ruvolo, P.P.1    Clark, W.2    Mumby, M.3    Gao, F.4    May, W.S.5
  • 129
    • 0035253856 scopus 로고    scopus 로고
    • t-SNARE dephosphorylation promotes SNARE assembly and exocytosis in yeast
    • Marash, M. and Gerst, J. E. (2001) t-SNARE dephosphorylation promotes SNARE assembly and exocytosis in yeast. EMBO J. 20, 411-421
    • (2001) EMBO J. , vol.20 , pp. 411-421
    • Marash, M.1    Gerst, J.E.2
  • 130
    • 0033575310 scopus 로고    scopus 로고
    • Long-chain ceramides activate protein phosphatase-1 and protein phosphatase-2A. Activation is stereospecific and regulated by phosphatidic acid
    • Chalfant, C. E., Kishikawa, K., Mumby, M. C., Kamibayashi, C., Bielawska, A. and Hannun, Y. A. (1999) Long-chain ceramides activate protein phosphatase-1 and protein phosphatase-2A. Activation is stereospecific and regulated by phosphatidic acid. J. Biol. Chem. 274, 20313-20317
    • (1999) J. Biol. Chem. , vol.274 , pp. 20313-20317
    • Chalfant, C.E.1    Kishikawa, K.2    Mumby, M.C.3    Kamibayashi, C.4    Bielawska, A.5    Hannun, Y.A.6
  • 131
    • 0035977067 scopus 로고    scopus 로고
    • FAS activation induces dephosphorylation of SR proteins. Dependence on the de novo generation of ceramide and activation of protein phosphatase-1
    • Chalfant, C. E., Ogretmen, B., Galadari, S. H., Kroesen, B. J., Pettus, B. J. and Hannun, Y. A. (2001) FAS activation induces dephosphorylation of SR proteins. Dependence on the de novo generation of ceramide and activation of protein phosphatase-1. J. Biol. Chem. 276, 44848-44855
    • (2001) J. Biol. Chem. , vol.276 , pp. 44848-44855
    • Chalfant, C.E.1    Ogretmen, B.2    Galadari, S.H.3    Kroesen, B.J.4    Pettus, B.J.5    Hannun, Y.A.6
  • 133
    • 0034634596 scopus 로고    scopus 로고
    • Ceramide directly activates protein kinase C ζ to regulate a stress-activated protein kinase signaling complex
    • Bourbon, N. A., Yun, J. and Kester, M. (2000) Ceramide directly activates protein kinase C ζ to regulate a stress-activated protein kinase signaling complex. J. Biol. Chem. 275, 35617-35623
    • (2000) J. Biol. Chem. , vol.275 , pp. 35617-35623
    • Bourbon, N.A.1    Yun, J.2    Kester, M.3
  • 134
    • 0028979464 scopus 로고
    • Crystal structure of the Cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester
    • Zhang, G., Kazanietz, M. G., Blumberg, P. M. and Hurley, J. H. (1995) Crystal structure of the Cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester. Cell 81, 917-924
    • (1995) Cell , vol.81 , pp. 917-924
    • Zhang, G.1    Kazanietz, M.G.2    Blumberg, P.M.3    Hurley, J.H.4
  • 135
    • 0028447767 scopus 로고
    • Solution structure of a cysteine rich domain of rat protein kinase C
    • Hommel, U., Zurini, M. and Luyten, M. (1994) Solution structure of a cysteine rich domain of rat protein kinase C. Nat. Struct. Biol. 1, 383-387
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 383-387
    • Hommel, U.1    Zurini, M.2    Luyten, M.3
  • 136
    • 0032521767 scopus 로고    scopus 로고
    • Hypothesis: Ceramide conditionally activates atypical protein kinases C, Raf-1 and KSR through binding to their cysteine-rich domains
    • van Blitterswijk, W. J. (1998) Hypothesis: ceramide conditionally activates atypical protein kinases C, Raf-1 and KSR through binding to their cysteine-rich domains. Biochem. J. 331, 679-680
    • (1998) Biochem. J. , vol.331 , pp. 679-680
    • Van Blitterswijk, W.J.1
  • 137
    • 0031037134 scopus 로고    scopus 로고
    • Interleukin 1-β-induced protein kinase C-ζ activation is mimicked by exogenous phospholipase D
    • Limatola, C., Barabino, B., Nista, A. and Santoni, A. (1997) Interleukin 1-β-induced protein kinase C-ζ activation is mimicked by exogenous phospholipase D. Biochem. J. 321, 497-501
    • (1997) Biochem. J. , vol.321 , pp. 497-501
    • Limatola, C.1    Barabino, B.2    Nista, A.3    Santoni, A.4
  • 138
    • 0030846622 scopus 로고    scopus 로고
    • Ceramide-induced translocation of protein kinase C ζ in primary cultures of astrocytes
    • Galve-Roperh, I., Haro, A. and Diaz-Laviada, I. (1997) Ceramide-induced translocation of protein kinase C ζ in primary cultures of astrocytes. FEBS Lett. 415, 271-274
    • (1997) FEBS Lett. , vol.415 , pp. 271-274
    • Galve-Roperh, I.1    Haro, A.2    Diaz-Laviada, I.3
  • 141
    • 0034617281 scopus 로고    scopus 로고
    • A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta) and PKC-related kinase 2 by PDK1
    • Balendran, A., Biondi, R. M., Cheung, P. C., Casamayor, A., Deak, M. and Alessi, D. R. (2000) A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta) and PKC-related kinase 2 by PDK1. J. Biol. Chem. 275, 20806-20813
    • (2000) J. Biol. Chem. , vol.275 , pp. 20806-20813
    • Balendran, A.1    Biondi, R.M.2    Cheung, P.C.3    Casamayor, A.4    Deak, M.5    Alessi, D.R.6
  • 143
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta, S. R., Dudek, H., Tao, X., Masters, S., Fu, H., Gotoh, Y. and Greenberg, M. E. (1997) Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91, 231-241
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 144
    • 0036479251 scopus 로고    scopus 로고
    • Ceramide-induced inhibition of Akt is mediated through protein kinase C ζ. Implications for growth arrest
    • Bourbon, N. A., Sandirasegarane, L. and Kester, M. (2002) Ceramide-induced inhibition of Akt is mediated through protein kinase C ζ. Implications for growth arrest. J. Biol. Chem. 277, 3286-3292
    • (2002) J. Biol. Chem. , vol.277 , pp. 3286-3292
    • Bourbon, N.A.1    Sandirasegarane, L.2    Kester, M.3
  • 147
    • 0035487315 scopus 로고    scopus 로고
    • A role for protein phosphatase 2A-like activity, but not atypical protein kinase Cζ, in the inhibition of protein kinase B/Akt and glycogen synthesis by palmitate
    • Cazzolli, R., Carpenter, L., Biden, T. J. and Schmitz-Peiffer, C. (2001) A role for protein phosphatase 2A-like activity, but not atypical protein kinase Cζ, in the inhibition of protein kinase B/Akt and glycogen synthesis by palmitate. Diabetes 50, 2210-2218
    • (2001) Diabetes , vol.50 , pp. 2210-2218
    • Cazzolli, R.1    Carpenter, L.2    Biden, T.J.3    Schmitz-Peiffer, C.4
  • 148
    • 0035281991 scopus 로고    scopus 로고
    • Ceramide dissociates 3′-phosphoinositide production from pleckstrin homology domain translocation
    • Stratford, S., DeWald, D. B. and Summers, S. A. (2001) Ceramide dissociates 3′-phosphoinositide production from pleckstrin homology domain translocation. Biochem. J. 354, 359-368
    • (2001) Biochem. J. , vol.354 , pp. 359-368
    • Stratford, S.1    DeWald, D.B.2    Summers, S.A.3
  • 150
    • 0033081893 scopus 로고    scopus 로고
    • Atypical PKCζ is activated by ceramide, resulting in coactivation of NF-kappaB/JNK kinase and cell survival
    • Wang, Y. M., Seibenhener, M. L., Vandenplas, M. L. and Wooten, M. W. (1999) Atypical PKCζ is activated by ceramide, resulting in coactivation of NF-kappaB/JNK kinase and cell survival. J. Neurosci. Res. 55, 293-302
    • (1999) J. Neurosci. Res. , vol.55 , pp. 293-302
    • Wang, Y.M.1    Seibenhener, M.L.2    Vandenplas, M.L.3    Wooten, M.W.4
  • 151
    • 0033105530 scopus 로고    scopus 로고
    • A phosphatidylcholine-specific phospholipase C regulates activation of p42/44 mitogen-activated protein kinases in lipopolysaccharide-stimulated human alveolar macrophages
    • Monick, M. M., Carter, A. B., Gudmundsson, G., Mallampalli, R., Powers, L. S. and Hunninghake, G. W. (1999) A phosphatidylcholine-specific phospholipase C regulates activation of p42/44 mitogen-activated protein kinases in lipopolysaccharide-stimulated human alveolar macrophages. J. Immunol. 162, 3005-3012
    • (1999) J. Immunol. , vol.162 , pp. 3005-3012
    • Monick, M.M.1    Carter, A.B.2    Gudmundsson, G.3    Mallampalli, R.4    Powers, L.S.5    Hunninghake, G.W.6
  • 152
    • 0034668121 scopus 로고    scopus 로고
    • Protein kinase C zeta plays a central role in activation of the p42/44 mitogen-activated protein kinase by endotoxin in alveolar macrophages
    • Monick, M. M., Carter, A. B., Flaherty, D. M., Peterson, M. W. and Hunninghake, G. W. (2000) Protein kinase C zeta plays a central role in activation of the p42/44 mitogen-activated protein kinase by endotoxin in alveolar macrophages. J. Immunol. 165, 4632-4639
    • (2000) J. Immunol. , vol.165 , pp. 4632-4639
    • Monick, M.M.1    Carter, A.B.2    Flaherty, D.M.3    Peterson, M.W.4    Hunninghake, G.W.5
  • 155
    • 12244277466 scopus 로고    scopus 로고
    • Caspase-dependent initiation of apoptosis and necrosis by the Fas receptor in lymphoid cells: Onset of necrosis is associated with delayed ceramide increase
    • Hetz, C. A., Hunn, M., Rojas, P., Torres, V., Leyton, L. and Quest, A. F. G. (2002) Caspase-dependent initiation of apoptosis and necrosis by the Fas receptor in lymphoid cells: onset of necrosis is associated with delayed ceramide increase. J. Cell. Sci. 115, 4671-4683
    • (2002) J. Cell. Sci. , vol.115 , pp. 4671-4683
    • Hetz, C.A.1    Hunn, M.2    Rojas, P.3    Torres, V.4    Leyton, L.5    Quest, A.F.G.6
  • 157
    • 0031577667 scopus 로고
    • Differential effects of sphingomyelinase and cell-permeable ceramide analogs on proliferation of Swiss 3T3 fibroblasts
    • Olivera, A., Romanowski, A., Rani, C. S. S. and Spiegel, S. (1977) Differential effects of sphingomyelinase and cell-permeable ceramide analogs on proliferation of Swiss 3T3 fibroblasts. Biochim. Biophys. Acta 1348, 311-323
    • (1977) Biochim. Biophys. Acta , vol.1348 , pp. 311-323
    • Olivera, A.1    Romanowski, A.2    Rani, C.S.S.3    Spiegel, S.4
  • 158
    • 0024795059 scopus 로고
    • Sphingomyelin turnover induced by vitamin D3 in HL-60 cells. Role in cell differentiation
    • Okazaki, T., Bell, R. M. and Hannun, Y. A. (1989) Sphingomyelin turnover induced by vitamin D3 in HL-60 cells. Role in cell differentiation. J. Biol. Chem. 264, 19076-19080
    • (1989) J. Biol. Chem. , vol.264 , pp. 19076-19080
    • Okazaki, T.1    Bell, R.M.2    Hannun, Y.A.3
  • 159
    • 0028108788 scopus 로고
    • Activation of the sphingomyelin cycle through the low-affinity neurotrophin receptor
    • Dobrowsky, R. T., Werner, M. H., Castellino, A. M., Chao, M. V. and Hannun, Y. A. (1994) Activation of the sphingomyelin cycle through the low-affinity neurotrophin receptor. Science 265, 1596-1599
    • (1994) Science , vol.265 , pp. 1596-1599
    • Dobrowsky, R.T.1    Werner, M.H.2    Castellino, A.M.3    Chao, M.V.4    Hannun, Y.A.5
  • 161
    • 0035192726 scopus 로고    scopus 로고
    • Tumor necrosis factor-α induces stress fiber formation through ceramide production: Role of sphingosine kinase
    • Hanna, A. N., Berthiaume, L. G., Kikuchi, Y., Begg, D., Bourgoin, S. and Brindley, D. N. (2001) Tumor necrosis factor-α induces stress fiber formation through ceramide production: role of sphingosine kinase. Mol. Biol. Cell 12, 3618-3630
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3618-3630
    • Hanna, A.N.1    Berthiaume, L.G.2    Kikuchi, Y.3    Begg, D.4    Bourgoin, S.5    Brindley, D.N.6
  • 162
    • 0037155796 scopus 로고    scopus 로고
    • Nerve growth factor-induced p75-mediated death of cultured hippocampal neurons is age-dependent and transduced through ceramide generated by neutral sphingomyelinase
    • Brann, A. B., Tcherpakov, M., Williams, I. M., Futerman, A. H. and Fainzilber, M. (2002) Nerve growth factor-induced p75-mediated death of cultured hippocampal neurons is age-dependent and transduced through ceramide generated by neutral sphingomyelinase. J. Biol. Chem. 277, 9812-9818
    • (2002) J. Biol. Chem. , vol.277 , pp. 9812-9818
    • Brann, A.B.1    Tcherpakov, M.2    Williams, I.M.3    Futerman, A.H.4    Fainzilber, M.5
  • 164
    • 0036201098 scopus 로고    scopus 로고
    • IL-1 stimulates ceramide accumulation without inducing apoptosis in intestinal epithelial cells
    • Homaidan, F. R., El-Sabban, M. E., Chakroun, I., El-Sibai, M. and Dbaibo, G. S. (2002) IL-1 stimulates ceramide accumulation without inducing apoptosis in intestinal epithelial cells. Mediators Inflamm. 11, 39-45
    • (2002) Mediators Inflamm. , vol.11 , pp. 39-45
    • Homaidan, F.R.1    El-Sabban, M.E.2    Chakroun, I.3    El-Sibai, M.4    Dbaibo, G.S.5
  • 165
    • 0033064288 scopus 로고    scopus 로고
    • Relationships of apoptotic signaling mediated by ceramide and TNF-alpha in U937 cells
    • Karasavvas, N. and Zakeri, Z. (1999) Relationships of apoptotic signaling mediated by ceramide and TNF-alpha in U937 cells. Cell Death Differ. 6, 115-123
    • (1999) Cell Death Differ. , vol.6 , pp. 115-123
    • Karasavvas, N.1    Zakeri, Z.2
  • 166
    • 0035053367 scopus 로고    scopus 로고
    • Cell line dependent involvement of ceramide in ultraviolet light-induced apoptosis
    • Chatterjee, M. and Wu, S. (2001) Cell line dependent involvement of ceramide in ultraviolet light-induced apoptosis. Mol. Cell. Biochem. 219, 21-27
    • (2001) Mol. Cell. Biochem. , vol.219 , pp. 21-27
    • Chatterjee, M.1    Wu, S.2
  • 169
    • 0034661482 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate signalling in mammalian cells
    • Pyne, S. and Pyne, N. J. (2000) Sphingosine 1-phosphate signalling in mammalian cells. Biochem. J. 349, 385-402
    • (2000) Biochem. J. , vol.349 , pp. 385-402
    • Pyne, S.1    Pyne, N.J.2
  • 170
  • 171
    • 0034733910 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate: Signalling inside and out
    • Spiegel, S. and Milstien, S. (2000) Sphingosine-1-phosphate: signalling inside and out. FEBS Lett. 476, 55-57
    • (2000) FEBS Lett. , vol.476 , pp. 55-57
    • Spiegel, S.1    Milstien, S.2
  • 172
    • 0037119991 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate phosphohydrolase in regulation of sphingolipid metabolism and apoptosis
    • Le Stunff, H., Galve-Roperh, I., Peterson, C., Milstien, S. and Spiegel, S. (2002) Sphingosine-1-phosphate phosphohydrolase in regulation of sphingolipid metabolism and apoptosis. J. Cell Biol. 158, 1039-1049
    • (2002) J. Cell Biol. , vol.158 , pp. 1039-1049
    • Le Stunff, H.1    Galve-Roperh, I.2    Peterson, C.3    Milstien, S.4    Spiegel, S.5
  • 173
    • 85047683702 scopus 로고    scopus 로고
    • Protein kinase Cδ amplifies ceramide formation via mitochondrial signalling in prostate cancer cells
    • Sumitomo, M., Ohba, M., Asakuma, J., Asano, T., Kuroki, T., Asano, T. and Hayakawa, M. (2002) Protein kinase Cδ amplifies ceramide formation via mitochondrial signalling in prostate cancer cells. J. Clin. Invest. 109, 827-836
    • (2002) J. Clin. Invest. , vol.109 , pp. 827-836
    • Sumitomo, M.1    Ohba, M.2    Asakuma, J.3    Asano, T.4    Kuroki, T.5    Asano, T.6    Hayakawa, M.7
  • 176
    • 0035817629 scopus 로고    scopus 로고
    • Clathrin-dependent and -independent internalization of plasma membrane sphingolipids initiates two Golgi targeting pathways
    • Puri, V., Watanabe, R., Singh, R. D., Dominguez, M., Brown, J. C., Wheatley, C. L., Marks, D. L. and Pagano, R. E. (2001) Clathrin-dependent and -independent internalization of plasma membrane sphingolipids initiates two Golgi targeting pathways. J. Cell Biol. 154, 535-547
    • (2001) J. Cell Biol. , vol.154 , pp. 535-547
    • Puri, V.1    Watanabe, R.2    Singh, R.D.3    Dominguez, M.4    Brown, J.C.5    Wheatley, C.L.6    Marks, D.L.7    Pagano, R.E.8
  • 177
    • 0034685807 scopus 로고    scopus 로고
    • Characterization of rapid membrane internalization and recycling
    • Hao, M. and Maxfield, F. R. (2000) Characterization of rapid membrane internalization and recycling. J. Biol. Chem. 275, 15279-15286
    • (2000) J. Biol. Chem. , vol.275 , pp. 15279-15286
    • Hao, M.1    Maxfield, F.R.2
  • 178
    • 0031661695 scopus 로고    scopus 로고
    • Variations among cell lines in the synthesis of sphingolipids in de novo and recycling pathways
    • Gillard, B. K., Clement, R. G. and Marcus, D. M. (1998) Variations among cell lines in the synthesis of sphingolipids in de novo and recycling pathways. Glycobiology 8, 885-890
    • (1998) Glycobiology , vol.8 , pp. 885-890
    • Gillard, B.K.1    Clement, R.G.2    Marcus, D.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.