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Volumn 9, Issue 2, 2008, Pages 139-150

Principles of bioactive lipid signalling: Lessons from sphingolipids

Author keywords

[No Author keywords available]

Indexed keywords

CERAMIDE; CERAMIDE 1 PHOSPHATE; SPHINGOLIPID; SPHINGOSINE; SPHINGOSINE 1 PHOSPHATE;

EID: 38549152194     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2329     Document Type: Review
Times cited : (2717)

References (118)
  • 1
    • 84960994832 scopus 로고
    • 32P into phospholipids of pancreas slices
    • Earliest study to demonstrate agonist-induced turnover of inositol phospholipids
    • 32P into phospholipids of pancreas slices. J. Biol. Chem. 203, 967-977 (1953). Earliest study to demonstrate agonist-induced turnover of inositol phospholipids.
    • (1953) J. Biol. Chem , vol.203 , pp. 967-977
    • Hokin, M.R.1    Hokin, L.E.2
  • 2
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • An excellent review, by a pioneer in the field on bioactive lipids, that discusses the discovery of activation of PKC by DAG
    • Nishizuka, Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 258, 607-614 (1992). An excellent review, by a pioneer in the field on bioactive lipids, that discusses the discovery of activation of PKC by DAG.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 3
    • 30044449982 scopus 로고    scopus 로고
    • Resolution of inflammation: The beginning programs the end
    • Serhan, C. N. & Savill, J. Resolution of inflammation: the beginning programs the end. Nature Immunol. 6, 1191-1197 (2005).
    • (2005) Nature Immunol , vol.6 , pp. 1191-1197
    • Serhan, C.N.1    Savill, J.2
  • 4
    • 0033792671 scopus 로고    scopus 로고
    • Effects of sphingosine and other sphingolipids on protein kinase C
    • Smith, E. R., Merrill, A. H., Obeid, L. M. & Hannun, Y. A. Effects of sphingosine and other sphingolipids on protein kinase C. Methods Enzymol. 312, 361-373 (2000).
    • (2000) Methods Enzymol , vol.312 , pp. 361-373
    • Smith, E.R.1    Merrill, A.H.2    Obeid, L.M.3    Hannun, Y.A.4
  • 5
    • 0027511687 scopus 로고    scopus 로고
    • Obeid, L. M., Linardic, C. M., Karolak, L. A. & Hannun, Y. A. Programmed cell death induced by ceramide. Science 259, 1769-1771 (1993). A landmark study that implicated ceramide in apoptosis.
    • Obeid, L. M., Linardic, C. M., Karolak, L. A. & Hannun, Y. A. Programmed cell death induced by ceramide. Science 259, 1769-1771 (1993). A landmark study that implicated ceramide in apoptosis.
  • 6
    • 0029562453 scopus 로고
    • Role of ceramide in cellular senescence
    • The first study to implicate ceramide in cellular senescence
    • Venable, M. E., Lee, J. Y., Smyth, M. J., Bielawska, A. & Obeid, L. M. Role of ceramide in cellular senescence. J. Biol. Chem. 270, 30701-30708 (1995). The first study to implicate ceramide in cellular senescence.
    • (1995) J. Biol. Chem , vol.270 , pp. 30701-30708
    • Venable, M.E.1    Lee, J.Y.2    Smyth, M.J.3    Bielawska, A.4    Obeid, L.M.5
  • 7
    • 3242696730 scopus 로고    scopus 로고
    • Physiological and pathological actions of sphingosine 1-phosphate
    • Hla, T. Physiological and pathological actions of sphingosine 1-phosphate. Semin. Cell Dev. Biol. 15, 513-520 (2004).
    • (2004) Semin. Cell Dev. Biol , vol.15 , pp. 513-520
    • Hla, T.1
  • 8
    • 27844517355 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate and ceramide 1-phosphate: Expanding roles in cell signaling
    • Chalfant, C. E. & Spiegel, S. Sphingosine 1-phosphate and ceramide 1-phosphate: expanding roles in cell signaling. J. Cell Sci. 118, 4605-4612 (2005).
    • (2005) J. Cell Sci , vol.118 , pp. 4605-4612
    • Chalfant, C.E.1    Spiegel, S.2
  • 9
    • 2342418547 scopus 로고    scopus 로고
    • Ceramide kinase is a mediator of calcium-dependent degranulation in mast cells
    • Mitsutake, S. et al. Ceramide kinase is a mediator of calcium-dependent degranulation in mast cells. J. Biol. Chem. 279, 17570-17577 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 17570-17577
    • Mitsutake, S.1
  • 10
    • 22544464177 scopus 로고    scopus 로고
    • Ceramide 1-phosphate, a mediator of phagocytosis
    • Hinkovska-Galcheva, V. et al. Ceramide 1-phosphate, a mediator of phagocytosis. J. Biol. Chem. 280, 26612-26621 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 26612-26621
    • Hinkovska-Galcheva, V.1
  • 11
    • 0027355755 scopus 로고
    • Metabolic effects of inhibiting glucosylceramide synthesis with PDMP and other substances
    • Radin, N. S., Shayman, J.A. & Inokuchi, J.-I. Metabolic effects of inhibiting glucosylceramide synthesis with PDMP and other substances. Adv. Lipid Res. 26, 183-211 (1993).
    • (1993) Adv. Lipid Res , vol.26 , pp. 183-211
    • Radin, N.S.1    Shayman, J.A.2    Inokuchi, J.-I.3
  • 13
    • 0037135626 scopus 로고    scopus 로고
    • The ceramide-centric universe of lipid-mediated cell regulation: Stress encounters of the lipid kind
    • Hannun, Y. A. & Obeid, L. M. The ceramide-centric universe of lipid-mediated cell regulation: stress encounters of the lipid kind. J. Biol. Chem. 277, 25847-25850 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 25847-25850
    • Hannun, Y.A.1    Obeid, L.M.2
  • 14
    • 0035212942 scopus 로고    scopus 로고
    • Regulation of de novo sphingolipid biosynthesis and the toxic consequences of its disruption
    • Linn, S. C. et al. Regulation of de novo sphingolipid biosynthesis and the toxic consequences of its disruption. Biochem. Soc. Trans. 29, 831-835 (2001).
    • (2001) Biochem. Soc. Trans , vol.29 , pp. 831-835
    • Linn, S.C.1
  • 15
    • 33748746334 scopus 로고    scopus 로고
    • When do Lasses (longevity assurance genes) become CerS (ceramide synthases)?: Insights into the regulation of ceramide synthesis
    • Pewzner-Jung, Y., Ben-Dor, S. & Futerman, A. H. When do Lasses (longevity assurance genes) become CerS (ceramide synthases)?: insights into the regulation of ceramide synthesis. J. Biol. Chem. 281, 25001-25005 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 25001-25005
    • Pewzner-Jung, Y.1    Ben-Dor, S.2    Futerman, A.H.3
  • 16
    • 0033744991 scopus 로고    scopus 로고
    • Further characterization of rat dihydroceramide desaturase: Tissue distribution, subcellular localization, and substrate specificity
    • Causeret, C., Geeraert, L., Van der Hoeven, G., Mannaerts, G. P. & van Veldhoven, P. P. Further characterization of rat dihydroceramide desaturase: tissue distribution, subcellular localization, and substrate specificity. Lipids 35, 1117-1125 (2000).
    • (2000) Lipids , vol.35 , pp. 1117-1125
    • Causeret, C.1    Geeraert, L.2    Van der Hoeven, G.3    Mannaerts, G.P.4    van Veldhoven, P.P.5
  • 17
    • 30344439710 scopus 로고    scopus 로고
    • Substrate specificity of human ceramide kinase
    • Wijesinghe, D. S. et al. Substrate specificity of human ceramide kinase. J. Lipid Res. 46, 2706-2716 (2005).
    • (2005) J. Lipid Res , vol.46 , pp. 2706-2716
    • Wijesinghe, D.S.1
  • 19
    • 33749576963 scopus 로고    scopus 로고
    • The multigenic sphingomyelin synthase family
    • Tafesse, F. G., Ternes, P. & Holthuis, J. C. The multigenic sphingomyelin synthase family. J. Biol. Chem. 281, 29421-29425 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 29421-29425
    • Tafesse, F.G.1    Ternes, P.2    Holthuis, J.C.3
  • 20
    • 0034444166 scopus 로고    scopus 로고
    • Traveling for the glycosphingolipid path
    • Hakomori, S. Traveling for the glycosphingolipid path. Glycoconj. J. 17, 627-647 (2000).
    • (2000) Glycoconj. J , vol.17 , pp. 627-647
    • Hakomori, S.1
  • 21
    • 0032080795 scopus 로고    scopus 로고
    • Glucosylceramide synthase and glycosphingolipid synthesis
    • Ichikawa, S. & Hirabayashi, Y. Glucosylceramide synthase and glycosphingolipid synthesis. Trends Cell Biol. 8, 198-202 (1998).
    • (1998) Trends Cell Biol , vol.8 , pp. 198-202
    • Ichikawa, S.1    Hirabayashi, Y.2
  • 22
    • 2342570273 scopus 로고    scopus 로고
    • Acid and neutral sphingomyelinases: Roles and mechanisms of regulation
    • Marchesini, N. & Hannun, Y. A. Acid and neutral sphingomyelinases: roles and mechanisms of regulation. Biochem. Cell Biol. 82, 27-44 (2004).
    • (2004) Biochem. Cell Biol , vol.82 , pp. 27-44
    • Marchesini, N.1    Hannun, Y.A.2
  • 23
    • 33748665711 scopus 로고    scopus 로고
    • Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and S1P
    • Xu, R. et al. Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and S1P. FASEB J. 20, 1813-1825 (2006).
    • (2006) FASEB J , vol.20 , pp. 1813-1825
    • Xu, R.1
  • 24
    • 31544460932 scopus 로고    scopus 로고
    • Identification of a novel amidase motif in neutral ceramidase
    • Galadari, S. et al. Identification of a novel amidase motif in neutral ceramidase. Biochem. J. 393, 687-695 (2006).
    • (2006) Biochem. J , vol.393 , pp. 687-695
    • Galadari, S.1
  • 26
    • 0141445962 scopus 로고    scopus 로고
    • Role of human sphingosine-1-phosphate phosphatase 1 in the regulation of intra-and extracellular sphingosine-1- phosphate levels and cell viability
    • Johnson, K. R. et al. Role of human sphingosine-1-phosphate phosphatase 1 in the regulation of intra-and extracellular sphingosine-1- phosphate levels and cell viability. J. Biol. Chem. 278, 34541-34547 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 34541-34547
    • Johnson, K.R.1
  • 27
    • 14844284989 scopus 로고    scopus 로고
    • Lipid phosphate phosphatases and related proteins: Signaling functions in development, cell division, and cancer
    • Brindley, D. N. Lipid phosphate phosphatases and related proteins: signaling functions in development, cell division, and cancer. J. Cell Biochem. 92, 900-912 (2004).
    • (2004) J. Cell Biochem , vol.92 , pp. 900-912
    • Brindley, D.N.1
  • 28
    • 17744367455 scopus 로고    scopus 로고
    • Integral membrane lipid phosphatases/phosphotransferases: Common structure and diverse functions
    • Sigal, Y. J., McDermott, M. I. & Morris, A. J. Integral membrane lipid phosphatases/phosphotransferases: common structure and diverse functions. Biochem. J. 387, 281-293 (2005).
    • (2005) Biochem. J , vol.387 , pp. 281-293
    • Sigal, Y.J.1    McDermott, M.I.2    Morris, A.J.3
  • 29
    • 34247617182 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate lyase in immunity and cancer: Silencing the siren
    • Bandhuvula, P. & Saba, J. D. Sphingosine-1-phosphate lyase in immunity and cancer: silencing the siren. Trends Mol. Med. 13, 210-217 (2007).
    • (2007) Trends Mol. Med , vol.13 , pp. 210-217
    • Bandhuvula, P.1    Saba, J.D.2
  • 30
    • 33746271951 scopus 로고    scopus 로고
    • Simultaneous quantitative analysis of bioactive sphingolipids by high-performance liquid chromatography-tandem mass spectrometry
    • Bielawski, J., Szulc, Z. M., Hannun, Y. A. & Bielawska, A. Simultaneous quantitative analysis of bioactive sphingolipids by high-performance liquid chromatography-tandem mass spectrometry. Methods 39, 82-91 (2006).
    • (2006) Methods , vol.39 , pp. 82-91
    • Bielawski, J.1    Szulc, Z.M.2    Hannun, Y.A.3    Bielawska, A.4
  • 31
    • 19444380734 scopus 로고    scopus 로고
    • Sphingolipidomics: High-throughput, structure-specific, and quantitative analysis of sphingolipids by liquid chromatography tandem mass spectrometry
    • A comprehensive and cutting-edge review on mass spectrometry methodology to analyse the sphingolipidome
    • Merrill, A. H. Jr, Sullards, M. C., Allegood, J. C., Kelly, S. & Wang, E. Sphingolipidomics: high-throughput, structure-specific, and quantitative analysis of sphingolipids by liquid chromatography tandem mass spectrometry. Methods 36, 207-224 (2005). A comprehensive and cutting-edge review on mass spectrometry methodology to analyse the sphingolipidome.
    • (2005) Methods , vol.36 , pp. 207-224
    • Merrill Jr, A.H.1    Sullards, M.C.2    Allegood, J.C.3    Kelly, S.4    Wang, E.5
  • 32
    • 0033994563 scopus 로고    scopus 로고
    • Characterization of sphingomyelinase activity released by thrombin-stimulated platelets
    • Romiti, E. et al. Characterization of sphingomyelinase activity released by thrombin-stimulated platelets. Mol. Cell. Biochem. 205, 75-81 (2000).
    • (2000) Mol. Cell. Biochem , vol.205 , pp. 75-81
    • Romiti, E.1
  • 33
    • 7244250153 scopus 로고    scopus 로고
    • Sphingosine kinase 1 is an intracellular effector of phosphatidic acid
    • Delon, C. et al. Sphingosine kinase 1 is an intracellular effector of phosphatidic acid. J. Biol. Chem. 279, 44763-44774 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 44763-44774
    • Delon, C.1
  • 34
    • 21844477032 scopus 로고    scopus 로고
    • Rapid transbilayer movement of ceramides in phospholipid vesicles and in human erythrocytes
    • Lopez-Montero, I. et al. Rapid transbilayer movement of ceramides in phospholipid vesicles and in human erythrocytes. J. Biol. Chem. 280, 25811-25819 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 25811-25819
    • Lopez-Montero, I.1
  • 35
    • 0025826305 scopus 로고
    • Use of D-erythro-sphingosine as a pharmacologic inhibitor of protein kinase C in human platelets
    • Khan, W. A. et al. Use of D-erythro-sphingosine as a pharmacologic inhibitor of protein kinase C in human platelets. Biochem. J. 278, 387-392 (1991).
    • (1991) Biochem. J , vol.278 , pp. 387-392
    • Khan, W.A.1
  • 36
    • 13144254221 scopus 로고    scopus 로고
    • Tumor necrosis factor-α induces adhesion molecule expression through the sphingosine kinase pathway
    • An important study that first demonstrated the activation of sphingosine kinase by TNFα
    • Xia, P. et al. Tumor necrosis factor-α induces adhesion molecule expression through the sphingosine kinase pathway. Proc. Natl Acad. Sci. USA 95, 14196-14201 (1998). An important study that first demonstrated the activation of sphingosine kinase by TNFα.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14196-14201
    • Xia, P.1
  • 37
    • 0041703016 scopus 로고    scopus 로고
    • Pettus, B. J. et al. The sphingosine kinase 1/sphingosine-1- phosphate pathway mediates COX-2 induction and PGE2 production in response to TNF-α. FASEB J. 17, 1411-1421 (2003). An important study that implicates the SK1-S1P pathway in inflammation.
    • Pettus, B. J. et al. The sphingosine kinase 1/sphingosine-1- phosphate pathway mediates COX-2 induction and PGE2 production in response to TNF-α. FASEB J. 17, 1411-1421 (2003). An important study that implicates the SK1-S1P pathway in inflammation.
  • 38
    • 0035976579 scopus 로고    scopus 로고
    • Lysophospholipids - receptor revelations
    • Hla, T., Lee, M. J., Ancellin, N., Paik, J. H. & Kluk, M. J. Lysophospholipids - receptor revelations. Science 294, 1875-1878 (2001).
    • (2001) Science , vol.294 , pp. 1875-1878
    • Hla, T.1    Lee, M.J.2    Ancellin, N.3    Paik, J.H.4    Kluk, M.J.5
  • 39
    • 0035929556 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane regulator regulates uptake of sphingoid base phosphates and lysophosphatidic acid: Modulation of cellular activity of sphingosine 1-phosphate
    • Boujaoude, L. C. et al. Cystic fibrosis transmembrane regulator regulates uptake of sphingoid base phosphates and lysophosphatidic acid: modulation of cellular activity of sphingosine 1-phosphate. J. Biol. Chem. 276, 35258-35264 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 35258-35264
    • Boujaoude, L.C.1
  • 40
    • 33750832270 scopus 로고    scopus 로고
    • Role of ABCC1 in export of sphingosine-1- phosphate from mast cells
    • Mitra, P. et al. Role of ABCC1 in export of sphingosine-1- phosphate from mast cells. Proc. Natl Acad. Sci. USA 103, 16394-16399 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 16394-16399
    • Mitra, P.1
  • 41
    • 0347611095 scopus 로고    scopus 로고
    • Hanada, K. et al. Molecular machinery for nonvesicular trafficking of ceramide. Nature 426, 803-809 (2003). A breakthrough study on the discovery of ceramide transfer protein.
    • Hanada, K. et al. Molecular machinery for nonvesicular trafficking of ceramide. Nature 426, 803-809 (2003). A breakthrough study on the discovery of ceramide transfer protein.
  • 42
    • 34347379940 scopus 로고    scopus 로고
    • Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein
    • Fugmann, T. et al. Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein. J. Cell Biol. 178, 15-22 (2007).
    • (2007) J. Cell Biol , vol.178 , pp. 15-22
    • Fugmann, T.1
  • 43
    • 1542723736 scopus 로고    scopus 로고
    • The structural requirements for ceramide activation of serine-threonine protein phosphatases
    • Chalfant, C. E., Szulc, Z., Roddy, P., Bielawska, A. & Hannun, Y. A. The structural requirements for ceramide activation of serine-threonine protein phosphatases. J. Lipid Res. 45, 496-506 (2004).
    • (2004) J. Lipid Res , vol.45 , pp. 496-506
    • Chalfant, C.E.1    Szulc, Z.2    Roddy, P.3    Bielawska, A.4    Hannun, Y.A.5
  • 44
    • 0028934811 scopus 로고
    • Rb as a downstream target for a ceramide-dependent pathway of growth arrest
    • Dbaibo, G. et al. Rb as a downstream target for a ceramide-dependent pathway of growth arrest. Proc. Natl Acad. Sci. USA 92, 1347-1351 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1347-1351
    • Dbaibo, G.1
  • 45
    • 15844387528 scopus 로고    scopus 로고
    • Ceramide inactivates cellular protein kinase Ca
    • Lee, J. Y., Hannun, Y. A. & Obeid, L. M. Ceramide inactivates cellular protein kinase Ca. J. Biol. Chem. 271, 13169-13174 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 13169-13174
    • Lee, J.Y.1    Hannun, Y.A.2    Obeid, L.M.3
  • 46
    • 0032569026 scopus 로고    scopus 로고
    • Inhibition of Akt kinase by cell-permeable ceramide and its implications for ceramide-induced apoptosis
    • Zhou, H. L., Summers, S. K., Birnbaum, M. J. & Pittman, R. N. Inhibition of Akt kinase by cell-permeable ceramide and its implications for ceramide-induced apoptosis. J. Biol. Chem. 273, 16568-16575 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 16568-16575
    • Zhou, H.L.1    Summers, S.K.2    Birnbaum, M.J.3    Pittman, R.N.4
  • 47
    • 0029003788 scopus 로고
    • PKCζ is a molecular switch in signal transduction of TNF-α, bifunctionally regulated by ceramide and arachidonic acid
    • Müller, G. et al. PKCζ is a molecular switch in signal transduction of TNF-α, bifunctionally regulated by ceramide and arachidonic acid. EMBO J. 14, 1961-1969 (1995).
    • (1995) EMBO J , vol.14 , pp. 1961-1969
    • Müller, G.1
  • 48
    • 0036479251 scopus 로고    scopus 로고
    • Ceramide-induced inhibition of Akt is mediated through protein kinase Cζ: Implications for growth arrest
    • Bourbon, N. A., Sandirasegarane, L. & Kester, M. Ceramide-induced inhibition of Akt is mediated through protein kinase Cζ: implications for growth arrest. J. Biol. Chem. 277, 3286-3292 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 3286-3292
    • Bourbon, N.A.1    Sandirasegarane, L.2    Kester, M.3
  • 49
    • 0343742670 scopus 로고    scopus 로고
    • Kinase suppressor of Ras is ceramide-activated protein kinase
    • Zhang, Y. H. et al. Kinase suppressor of Ras is ceramide-activated protein kinase. Cell 89, 63-72 (1997).
    • (1997) Cell , vol.89 , pp. 63-72
    • Zhang, Y.H.1
  • 50
    • 2442661614 scopus 로고    scopus 로고
    • Cathepsin D links TNF-induced acid sphingomyelinase to Bid-mediated caspase-9 and -3 activation
    • Heinrich, M. et al. Cathepsin D links TNF-induced acid sphingomyelinase to Bid-mediated caspase-9 and -3 activation. Cell Death Differ. 11, 550-563 (2004).
    • (2004) Cell Death Differ , vol.11 , pp. 550-563
    • Heinrich, M.1
  • 51
    • 22544468543 scopus 로고    scopus 로고
    • Direct binding to ceramide activates protein kinase Cζ before the formation of a proapoptotic complex with PAR-4 in differentiating stem cells
    • Wang, G. et al. Direct binding to ceramide activates protein kinase Cζ before the formation of a proapoptotic complex with PAR-4 in differentiating stem cells. J. Biol. Chem. 280, 26415-26424 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 26415-26424
    • Wang, G.1
  • 52
    • 0037162038 scopus 로고    scopus 로고
    • Plasma lipoproteins behave as carriers of extracellular sphingosine 1-phosphate: Is this an atherogenic mediator or an anti-atherogenic mediator?
    • Okajima, F. Plasma lipoproteins behave as carriers of extracellular sphingosine 1-phosphate: is this an atherogenic mediator or an anti-atherogenic mediator? Biochim. Biophys. Acta 1582, 132-137 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1582 , pp. 132-137
    • Okajima, F.1
  • 53
    • 0032489574 scopus 로고    scopus 로고
    • Lee, M. J. et al. Sphingosine-1-phosphate as a ligand for the G protein coupled receptor EDG-1. Science 279, 1552-1555 (1998). The first study to identify and characterize an S1P receptor.
    • Lee, M. J. et al. Sphingosine-1-phosphate as a ligand for the G protein coupled receptor EDG-1. Science 279, 1552-1555 (1998). The first study to identify and characterize an S1P receptor.
  • 54
    • 0029148660 scopus 로고
    • Ceramide synthase mediates daunorubicin-induced apoptosis: An alternative mechanism for generating death signals
    • An important study implicating ceramide synthase in chemotherapy-induced apoptosis
    • Bose, R. et al. Ceramide synthase mediates daunorubicin-induced apoptosis: an alternative mechanism for generating death signals. Cell 82, 405-414 (1995). An important study implicating ceramide synthase in chemotherapy-induced apoptosis.
    • (1995) Cell , vol.82 , pp. 405-414
    • Bose, R.1
  • 55
    • 0034708594 scopus 로고    scopus 로고
    • Serine palmitoyltransferase regulates de novo ceramide generation during etoposide-induced apoptosis
    • Perry, D. K. et al. Serine palmitoyltransferase regulates de novo ceramide generation during etoposide-induced apoptosis. J. Biol. Chem. 275, 9078-9084 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 9078-9084
    • Perry, D.K.1
  • 56
    • 0038352072 scopus 로고    scopus 로고
    • BcR-induced apoptosis involves differential regulation of C16 and C24-ceramide formation and sphingolipid-dependent activation of the proteasome
    • Kroesen, B. J. et al. BcR-induced apoptosis involves differential regulation of C16 and C24-ceramide formation and sphingolipid-dependent activation of the proteasome. J. Biol. Chem. 278, 14723-14731 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 14723-14731
    • Kroesen, B.J.1
  • 57
    • 0037066727 scopus 로고    scopus 로고
    • De novo ceramide regulates the alternative splicing of caspase 9 and Bcl-x in A549 lung adenocarcinoma cells. Dependence on protein phosphatase-1
    • Chalfant, C. E. et al. De novo ceramide regulates the alternative splicing of caspase 9 and Bcl-x in A549 lung adenocarcinoma cells. Dependence on protein phosphatase-1. J. Biol. Chem. 277, 12587-12595 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 12587-12595
    • Chalfant, C.E.1
  • 58
    • 0023836942 scopus 로고
    • Kinetics of long-chain (sphingoid) base biosynthesis in intact LM cells: Effects of varying the extracellular concentrations of serine and fatty acid precursors of this pathway
    • Merrill, A. H. Jr, Wang, E. & Mullins, R. E. Kinetics of long-chain (sphingoid) base biosynthesis in intact LM cells: effects of varying the extracellular concentrations of serine and fatty acid precursors of this pathway. Biochemistry 27, 340-345 (1988).
    • (1988) Biochemistry , vol.27 , pp. 340-345
    • Merrill Jr, A.H.1    Wang, E.2    Mullins, R.E.3
  • 59
    • 34249697044 scopus 로고    scopus 로고
    • Selective substrate supply in the regulation of yeast de novo sphingolipid synthesis
    • Cowart, L. A. & Hannun, Y. A. Selective substrate supply in the regulation of yeast de novo sphingolipid synthesis. J. Biol. Chem. 282, 12330-12340 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 12330-12340
    • Cowart, L.A.1    Hannun, Y.A.2
  • 60
    • 33748309395 scopus 로고    scopus 로고
    • Functions and metabolism of sphingolipids in Saccharomyces cerevisiae
    • Dickson, R. C., Sumanasekera, C. & Lester, R. L. Functions and metabolism of sphingolipids in Saccharomyces cerevisiae. Prog. Lipid Res. 45, 447-465 (2006).
    • (2006) Prog. Lipid Res , vol.45 , pp. 447-465
    • Dickson, R.C.1    Sumanasekera, C.2    Lester, R.L.3
  • 61
    • 0035929636 scopus 로고    scopus 로고
    • Phytosphingosine as a specific inhibitor of growth and nutrient import in Saccharomyces cerevisiae
    • Chung, N., Mao, C., Heitman, J., Hannun, Y. A. & Obeid, L. M. Phytosphingosine as a specific inhibitor of growth and nutrient import in Saccharomyces cerevisiae. J. Biol. Chem. 276, 35614-35621 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 35614-35621
    • Chung, N.1    Mao, C.2    Heitman, J.3    Hannun, Y.A.4    Obeid, L.M.5
  • 62
    • 0035803482 scopus 로고    scopus 로고
    • Sphingoid base signaling via Pkh kinases is required for endocytosis in yeast
    • Friant, S., Lombardi, R., Schmelzle, T., Hall, M. N. & Riezman, H. Sphingoid base signaling via Pkh kinases is required for endocytosis in yeast. EMBO J. 20, 6783-6792 (2001).
    • (2001) EMBO J , vol.20 , pp. 6783-6792
    • Friant, S.1    Lombardi, R.2    Schmelzle, T.3    Hall, M.N.4    Riezman, H.5
  • 63
    • 33644851220 scopus 로고    scopus 로고
    • Sphingoid base is required for translation initiation during heat stress in Saccharomyces cerevisiae
    • Meier, K. D., Deloche, O., Kajiwara, K., Funato, K. & Riezman, H. Sphingoid base is required for translation initiation during heat stress in Saccharomyces cerevisiae. Mol. Biol. Cell 17, 1164-1175 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1164-1175
    • Meier, K.D.1    Deloche, O.2    Kajiwara, K.3    Funato, K.4    Riezman, H.5
  • 64
    • 0345374579 scopus 로고    scopus 로고
    • Minireview: Weapons of lean body mass destruction: the role of ectopic lipids in the metabolic syndrome
    • Unger, R. H. Minireview: weapons of lean body mass destruction: the role of ectopic lipids in the metabolic syndrome. Endocrinology 144, 5159-5165 (2003).
    • (2003) Endocrinology , vol.144 , pp. 5159-5165
    • Unger, R.H.1
  • 65
    • 33847332202 scopus 로고    scopus 로고
    • Inhibition of ceramide synthesis ameliorates glucocorticoid-, saturated-fat-, and obesity-induced insulin resistance
    • An important study that implicates ceramide in insulin resistance
    • Holland, W. L. et al. Inhibition of ceramide synthesis ameliorates glucocorticoid-, saturated-fat-, and obesity-induced insulin resistance. Cell Metab. 5, 167-179 (2007). An important study that implicates ceramide in insulin resistance.
    • (2007) Cell Metab , vol.5 , pp. 167-179
    • Holland, W.L.1
  • 66
    • 22544470314 scopus 로고    scopus 로고
    • Caspase-dependent and -independent activation of acid sphingomyelinase signaling
    • Rotolo, J. A. et al. Caspase-dependent and -independent activation of acid sphingomyelinase signaling. J. Biol. Chem. 280, 26425-26434 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 26425-26434
    • Rotolo, J.A.1
  • 67
    • 0035808364 scopus 로고    scopus 로고
    • Cell autonomous apoptosis defects in acid sphingomyelinase knockout fibroblasts
    • Lozano, J. et al. Cell autonomous apoptosis defects in acid sphingomyelinase knockout fibroblasts. J. Biol. Chem. 276, 442-448 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 442-448
    • Lozano, J.1
  • 68
    • 0038626211 scopus 로고    scopus 로고
    • Tumor response to radiotherapy regulated by endothelial cell apoptosis
    • Garcia-Barros, M. et al. Tumor response to radiotherapy regulated by endothelial cell apoptosis. Science 300, 1155-1159 (2003).
    • (2003) Science , vol.300 , pp. 1155-1159
    • Garcia-Barros, M.1
  • 69
    • 38049098527 scopus 로고    scopus 로고
    • A novel role for protein kinase Cδ-mediated phosphorylation of acid sphingomyelinase in UV light-induced mitochondrial injury
    • 13 Aug, doi:10.1096/fj.07-8967com
    • Zeidan, Y. H., Wu, B. X., Jenkins, R. W., Obeid, L. M. & Hannun, Y. A. A novel role for protein kinase Cδ-mediated phosphorylation of acid sphingomyelinase in UV light-induced mitochondrial injury. FASEB J. 13 Aug 2007 (doi:10.1096/fj.07-8967com).
    • (2007) FASEB J
    • Zeidan, Y.H.1    Wu, B.X.2    Jenkins, R.W.3    Obeid, L.M.4    Hannun, Y.A.5
  • 70
    • 22544476850 scopus 로고    scopus 로고
    • Rhinoviruses infect human epithelial cells via ceramide-enriched membrane platforms
    • Grassme, H., Riehle, A., Wilker, B. & Gulbins, E. Rhinoviruses infect human epithelial cells via ceramide-enriched membrane platforms. J. Biol. Chem. 280, 26256-26262 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 26256-26262
    • Grassme, H.1    Riehle, A.2    Wilker, B.3    Gulbins, E.4
  • 71
    • 33746917065 scopus 로고    scopus 로고
    • Acid ceramidase but not acid sphingomyelinase is required for tumor necrosis factor-a-induced PGE2 production
    • Zeidan, Y. H. et al. Acid ceramidase but not acid sphingomyelinase is required for tumor necrosis factor-a-induced PGE2 production. J. Biol. Chem. 281, 24695-24703 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 24695-24703
    • Zeidan, Y.H.1
  • 72
    • 34249657837 scopus 로고    scopus 로고
    • Activation of acid sphingomyelinase by protein kinase Cδ-mediated phosphorylation
    • Zeidan, Y. H. & Hannun, Y. A. Activation of acid sphingomyelinase by protein kinase Cδ-mediated phosphorylation. J. Biol. Chem. 282, 11549-11561 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 11549-11561
    • Zeidan, Y.H.1    Hannun, Y.A.2
  • 73
    • 0034708831 scopus 로고    scopus 로고
    • Role of acidic sphingomyelinase in Fas/CD95-mediated cell death
    • Lin, T. et al. Role of acidic sphingomyelinase in Fas/CD95-mediated cell death. J. Biol. Chem. 275, 8657-8663 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 8657-8663
    • Lin, T.1
  • 74
    • 0034017357 scopus 로고    scopus 로고
    • Perturbation of membrane microdomains reduces mitogenic signaling and increases susceptibility to apoptosis after T cell receptor stimulation
    • Nix, M. & Stoffel, W. Perturbation of membrane microdomains reduces mitogenic signaling and increases susceptibility to apoptosis after T cell receptor stimulation. Cell Death Differ. 7, 413-424 (2000).
    • (2000) Cell Death Differ , vol.7 , pp. 413-424
    • Nix, M.1    Stoffel, W.2
  • 75
    • 34250799092 scopus 로고    scopus 로고
    • Reactive nitrogen and oxygen species activate different sphingomyelinases to induce apoptosis in airway epithelial cells
    • Castillo, S. S., Levy, M., Thaikoottathil, J. V. & Goldkorn, T. Reactive nitrogen and oxygen species activate different sphingomyelinases to induce apoptosis in airway epithelial cells. Exp. Cell Res. 313, 2680-2686 (2007).
    • (2007) Exp. Cell Res , vol.313 , pp. 2680-2686
    • Castillo, S.S.1    Levy, M.2    Thaikoottathil, J.V.3    Goldkorn, T.4
  • 76
    • 13244259440 scopus 로고    scopus 로고
    • Selective inhibition of juxtanuclear translocation of protein kinase C βII by a negative feedback mechanism involving ceramide formed from the salvage pathway
    • Becker, K. P., Kitatani, K., Idkowiak-Baldys, J., Bielawski, J. & Hannun, Y. A. Selective inhibition of juxtanuclear translocation of protein kinase C βII by a negative feedback mechanism involving ceramide formed from the salvage pathway. J. Biol. Chem. 280, 2606-2612 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 2606-2612
    • Becker, K.P.1    Kitatani, K.2    Idkowiak-Baldys, J.3    Bielawski, J.4    Hannun, Y.A.5
  • 77
    • 33749009744 scopus 로고    scopus 로고
    • The extended family of neutral sphingomyelinases
    • Clarke, C. J. et al. The extended family of neutral sphingomyelinases. Biochemistry 45, 11247-11256 (2006).
    • (2006) Biochemistry , vol.45 , pp. 11247-11256
    • Clarke, C.J.1
  • 79
    • 0038529730 scopus 로고    scopus 로고
    • Biochemical properties of mammalian neutral sphingomyelinase 2 and its role in sphingolipid metabolism
    • Marchesini, N., Luberto, C. & Hannun, Y. A. Biochemical properties of mammalian neutral sphingomyelinase 2 and its role in sphingolipid metabolism. J. Biol. Chem. 278, 13775-13783 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 13775-13783
    • Marchesini, N.1    Luberto, C.2    Hannun, Y.A.3
  • 80
    • 23044482222 scopus 로고    scopus 로고
    • A deletion in the gene encoding sphingomyelin phosphodiesterase 3 (Smpd3) results in osteogenesis and dentinogenesis imperfecta in the mouse
    • Aubin, I. et al. A deletion in the gene encoding sphingomyelin phosphodiesterase 3 (Smpd3) results in osteogenesis and dentinogenesis imperfecta in the mouse. Nature Genet. 37, 803-805 (2005).
    • (2005) Nature Genet , vol.37 , pp. 803-805
    • Aubin, I.1
  • 81
    • 34547653109 scopus 로고    scopus 로고
    • Neutral sphingomyelinase (SMPD3) deficiency causes a novel form of chondrodysplasia and dwarfism that is rescued by Col2A1-driven smpd3 transgene expression
    • Stoffel, W. et al. Neutral sphingomyelinase (SMPD3) deficiency causes a novel form of chondrodysplasia and dwarfism that is rescued by Col2A1-driven smpd3 transgene expression. Am. J. Pathol. 171,153-161 (2007).
    • (2007) Am. J. Pathol , vol.171 , pp. 153-161
    • Stoffel, W.1
  • 82
    • 4444272893 scopus 로고    scopus 로고
    • Expression of neutral sphingomyelinase-2 (NSMase-2) in primary rat hepatocytes modulates IL-β-induced JNK activation
    • Karakashian, A. A., Giltiay, N. V., Smith, G. M. & Nikolova-Karakashian, M. N. Expression of neutral sphingomyelinase-2 (NSMase-2) in primary rat hepatocytes modulates IL-β-induced JNK activation. FASEB J. 18, 968-970 (2004).
    • (2004) FASEB J , vol.18 , pp. 968-970
    • Karakashian, A.A.1    Giltiay, N.V.2    Smith, G.M.3    Nikolova-Karakashian, M.N.4
  • 83
    • 33644819311 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase activation by tumor necrosis factor α through neutral sphingomyelinase 2, sphingosine kinase 1, and sphingosine 1 phosphate receptors: A novel pathway relevant to the pathophysiology of endothelium
    • De Palma, C., Meacci, E., Perrotta, C., Bruni, P. & Clementi, E. Endothelial nitric oxide synthase activation by tumor necrosis factor α through neutral sphingomyelinase 2, sphingosine kinase 1, and sphingosine 1 phosphate receptors: a novel pathway relevant to the pathophysiology of endothelium. Arterioscler. Thromb. Vasc. Biol. 26, 99-105 (2006).
    • (2006) Arterioscler. Thromb. Vasc. Biol , vol.26 , pp. 99-105
    • De Palma, C.1    Meacci, E.2    Perrotta, C.3    Bruni, P.4    Clementi, E.5
  • 84
    • 34547520207 scopus 로고    scopus 로고
    • Rutkute, K., Karakashian, A. A., Giltiay, N. V., Dobierzewska, A. & Nikolova-Karakashian, M. N. Aging in rat causes hepatic hyperresponsiveness to interleukin-1β which is mediated by neutral sphingomyelinase-2. Hepatology 46, 1166-1176 (2007). A crucial study that demonstrates a role for ceramide and sphingomyelin in ageing in vivo.
    • Rutkute, K., Karakashian, A. A., Giltiay, N. V., Dobierzewska, A. & Nikolova-Karakashian, M. N. Aging in rat causes hepatic hyperresponsiveness to interleukin-1β which is mediated by neutral sphingomyelinase-2. Hepatology 46, 1166-1176 (2007). A crucial study that demonstrates a role for ceramide and sphingomyelin in ageing in vivo.
  • 85
    • 33847719144 scopus 로고    scopus 로고
    • Role for neutral sphingomyelinase-2 in tumor necrosis factor α-stimulated expression of vascular cell adhesion molecule-1 (VCAM) and intercellular adhesion molecule-1 (ICAM) in lung epithelial cells: P38 MAPK is an upstream regulator of nSMase2
    • Clarke, C. J., Truong, T. G. & Hannun, Y. A. Role for neutral sphingomyelinase-2 in tumor necrosis factor α-stimulated expression of vascular cell adhesion molecule-1 (VCAM) and intercellular adhesion molecule-1 (ICAM) in lung epithelial cells: p38 MAPK is an upstream regulator of nSMase2. J. Biol. Chem. 282, 1384-1396 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 1384-1396
    • Clarke, C.J.1    Truong, T.G.2    Hannun, Y.A.3
  • 86
    • 28644451007 scopus 로고    scopus 로고
    • Regulation of cholesterol and sphingomyelin metabolism by amyloid-â and presenilin
    • Grimm, M. O. et al. Regulation of cholesterol and sphingomyelin metabolism by amyloid-â and presenilin. Nature Cell Biol. 7, 1118-1123 (2005).
    • (2005) Nature Cell Biol , vol.7 , pp. 1118-1123
    • Grimm, M.O.1
  • 87
    • 23244468383 scopus 로고    scopus 로고
    • Amyloid-β peptide enhances tumor necrosis factor-α-induced iNOS through neutral sphingomyelinase/ceramide pathway in oligodendrocytes
    • Zeng, C. et al. Amyloid-β peptide enhances tumor necrosis factor-α-induced iNOS through neutral sphingomyelinase/ceramide pathway in oligodendrocytes. J. Neurochem. 94, 703-712 (2005).
    • (2005) J. Neurochem , vol.94 , pp. 703-712
    • Zeng, C.1
  • 88
    • 0030792143 scopus 로고    scopus 로고
    • cca1 is required for formation of growth-arrested confluent monolayer of rat 3Y1 cells
    • Hayashi, Y., Kiyono, T., Fujita, M. & Ishibashi, M. cca1 is required for formation of growth-arrested confluent monolayer of rat 3Y1 cells. J. Biol. Chem. 272, 18082-18086 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 18082-18086
    • Hayashi, Y.1    Kiyono, T.2    Fujita, M.3    Ishibashi, M.4
  • 89
    • 2942532249 scopus 로고    scopus 로고
    • Role for mammalian neutral sphingomyelinase 2 in confluence-induced growth arrest of MCF7 cells
    • Marchesini, N. et al. Role for mammalian neutral sphingomyelinase 2 in confluence-induced growth arrest of MCF7 cells. J. Biol. Chem. 279, 25101-25111 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 25101-25111
    • Marchesini, N.1
  • 90
    • 33947363813 scopus 로고    scopus 로고
    • Analysis of membrane topology of neutral sphingomyelinase 2
    • Tani, M. & Hannun, Y. A. Analysis of membrane topology of neutral sphingomyelinase 2. FEBS Lett. 581, 1323-1328 (2007).
    • (2007) FEBS Lett , vol.581 , pp. 1323-1328
    • Tani, M.1    Hannun, Y.A.2
  • 91
    • 0038218405 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate: An enigmatic signalling lipid
    • Spiegel, S. & Milstien, S. Sphingosine-1-phosphate: an enigmatic signalling lipid. Nature Rev. Mol. Cell Biol. 4, 397-407 (2003).
    • (2003) Nature Rev. Mol. Cell Biol , vol.4 , pp. 397-407
    • Spiegel, S.1    Milstien, S.2
  • 92
    • 0037144434 scopus 로고    scopus 로고
    • PKC-dependent activation of sphingosine kinase 1 and translocation to the plasma membrane. Extracellular release of sphingosine-1-phosphate induced by phorbol 12-myristate 13-acetate (PMA)
    • Johnson, K. R., Becker, K. P., Facchinetti, M. M., Hannun, Y. A. & Obeid, L. M. PKC-dependent activation of sphingosine kinase 1 and translocation to the plasma membrane. Extracellular release of sphingosine-1-phosphate induced by phorbol 12-myristate 13-acetate (PMA). J. Biol. Chem. 277, 35257-35262 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 35257-35262
    • Johnson, K.R.1    Becker, K.P.2    Facchinetti, M.M.3    Hannun, Y.A.4    Obeid, L.M.5
  • 93
    • 0032540010 scopus 로고    scopus 로고
    • FcaγRI coupling to phospholipase D initiates sphingosine kinase-mediated calcium mobilization and vesicular trafficking
    • Melendez, A., Floto, R. A., Gillooly, D. J., Harnett, M. M. & Allen, J. M. FcaγRI coupling to phospholipase D initiates sphingosine kinase-mediated calcium mobilization and vesicular trafficking. J. Biol. Chem. 273, 9393-9402 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 9393-9402
    • Melendez, A.1    Floto, R.A.2    Gillooly, D.J.3    Harnett, M.M.4    Allen, J.M.5
  • 94
    • 0142105397 scopus 로고    scopus 로고
    • Activation of sphingosine kinase 1 by ERK1/2-mediated phosphorylation
    • Pitson, S. M. et al. Activation of sphingosine kinase 1 by ERK1/2-mediated phosphorylation. EMBO J. 22, 5491-5500 (2003).
    • (2003) EMBO J , vol.22 , pp. 5491-5500
    • Pitson, S.M.1
  • 95
    • 2442699980 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate receptors: Receptor specificity versus functional redundancy
    • Taha, T. A., Argraves, K. M. & Obeid, L. M. Sphingosine-1-phosphate receptors: receptor specificity versus functional redundancy. Biochim. Biophys. Acta 1682, 48-55 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1682 , pp. 48-55
    • Taha, T.A.1    Argraves, K.M.2    Obeid, L.M.3
  • 96
    • 0037040908 scopus 로고    scopus 로고
    • Sphingosine kinase interacts with TRAF2 and dissects tumor necrosis factor-α signaling
    • Xia, P. et al. Sphingosine kinase interacts with TRAF2 and dissects tumor necrosis factor-α signaling. J. Biol. Chem. 277, 7996-8003 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 7996-8003
    • Xia, P.1
  • 97
    • 22144486976 scopus 로고    scopus 로고
    • Basal and induced sphingosine kinase 1 activity in A549 carcinoma cells: Function in cell survival and IL-1β and TNF-α induced production of inflammatory mediators
    • Billich, A. et al. Basal and induced sphingosine kinase 1 activity in A549 carcinoma cells: function in cell survival and IL-1β and TNF-α induced production of inflammatory mediators. Cell Signal. 17, 1203-1217 (2005).
    • (2005) Cell Signal , vol.17 , pp. 1203-1217
    • Billich, A.1
  • 98
    • 0033615537 scopus 로고    scopus 로고
    • Vascular endothelial cell adherens junction assembly and morphogenesis induced by sphingosine-1-phosphate
    • Lee, M. J. et al. Vascular endothelial cell adherens junction assembly and morphogenesis induced by sphingosine-1-phosphate. Cell 99, 301-312 (1999).
    • (1999) Cell , vol.99 , pp. 301-312
    • Lee, M.J.1
  • 99
    • 0033783522 scopus 로고    scopus 로고
    • Edg-1, the G protein-coupled receptor for sphingosine-1-phosphate, is essential for vascular maturation
    • Liu, Y. et al. Edg-1, the G protein-coupled receptor for sphingosine-1-phosphate, is essential for vascular maturation. J. Clin. Invest. 106, 951-961 (2000).
    • (2000) J. Clin. Invest , vol.106 , pp. 951-961
    • Liu, Y.1
  • 100
    • 28544437478 scopus 로고    scopus 로고
    • Essential role for sphingosine kinases in neural and vascular development
    • Mizugishi, K. et al. Essential role for sphingosine kinases in neural and vascular development. Mol. Cell. Biol. 25, 11113-11121 (2005).
    • (2005) Mol. Cell. Biol , vol.25 , pp. 11113-11121
    • Mizugishi, K.1
  • 101
    • 33947147730 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate signaling in the cardiovascular system
    • Peters, S. L. & Alewijnse, A. E. Sphingosine-1-phosphate signaling in the cardiovascular system. Curr. Opin. Pharmacol. 7, 186-192 (2007).
    • (2007) Curr. Opin. Pharmacol , vol.7 , pp. 186-192
    • Peters, S.L.1    Alewijnse, A.E.2
  • 102
    • 0141566600 scopus 로고    scopus 로고
    • Egress: A receptorregulated step in lymphocyte trafficking
    • Rosen, H., Sanna, G. & Alfonso, C. Egress: a receptorregulated step in lymphocyte trafficking. Immunol. Rev. 195, 160-177 (2003).
    • (2003) Immunol. Rev , vol.195 , pp. 160-177
    • Rosen, H.1    Sanna, G.2    Alfonso, C.3
  • 103
    • 3142588813 scopus 로고    scopus 로고
    • New immunosuppressants with potential implication in multiple sclerosis
    • Gonsette, R. E. New immunosuppressants with potential implication in multiple sclerosis. J. Neurol. Sci. 223, 87-93 (2004).
    • (2004) J. Neurol. Sci , vol.223 , pp. 87-93
    • Gonsette, R.E.1
  • 104
    • 33645801577 scopus 로고    scopus 로고
    • Loss of sphingosine kinase-1 activates the intrinsic pathway of programmed cell death: Modulation of sphingolipid levels and the induction of apoptosis
    • Taha, T. A. et al. Loss of sphingosine kinase-1 activates the intrinsic pathway of programmed cell death: modulation of sphingolipid levels and the induction of apoptosis. FASEB J. 20, 482-484 (2006).
    • (2006) FASEB J , vol.20 , pp. 482-484
    • Taha, T.A.1
  • 105
    • 12144287654 scopus 로고    scopus 로고
    • Ceramide 1-phosphate is a direct activator of cytosolic phospholipase A2
    • Pettus, B. J. et al. Ceramide 1-phosphate is a direct activator of cytosolic phospholipase A2. J. Biol. Chem. 279, 11320-11326 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 11320-11326
    • Pettus, B.J.1
  • 106
    • 28844493023 scopus 로고    scopus 로고
    • 2+-dependent activation of ceramide kinase as a calcium sensor
    • 2+-dependent activation of ceramide kinase as a calcium sensor. J. Biol. Chem. 280, 40436-40441 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 40436-40441
    • Mitsutake, S.1    Igarashi, Y.2
  • 107
    • 33845292007 scopus 로고    scopus 로고
    • Ceramide 1-phosphate/ceramide, a switch between life and death
    • Gomez-Munoz, A. Ceramide 1-phosphate/ceramide, a switch between life and death. Biochim. Biophys. Acta 1758, 2049-2056 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 2049-2056
    • Gomez-Munoz, A.1
  • 108
    • 0033058419 scopus 로고    scopus 로고
    • The human multidrug resistance protein MRP1 translocates sphingolipid analogs across the plasma membrane
    • Raggers, R. J., van Helvoort, A., Evers, R. & van Meer, G. The human multidrug resistance protein MRP1 translocates sphingolipid analogs across the plasma membrane. J. Cell Sci. 112, 415-422 (1999).
    • (1999) J. Cell Sci , vol.112 , pp. 415-422
    • Raggers, R.J.1    van Helvoort, A.2    Evers, R.3    van Meer, G.4
  • 109
    • 33646356745 scopus 로고    scopus 로고
    • The CLN9 protein, a regulator of dihydroceramide synthase
    • Schulz, A. et al. The CLN9 protein, a regulator of dihydroceramide synthase. J. Biol. Chem. 281, 2784-2794 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 2784-2794
    • Schulz, A.1
  • 110
    • 34447115107 scopus 로고    scopus 로고
    • Involvement of dihydroceramide desaturase in cell cycle progression in human neuroblastoma cells
    • Kraveka, J. M. et al. Involvement of dihydroceramide desaturase in cell cycle progression in human neuroblastoma cells. J. Biol. Chem. 282, 16718-16728 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 16718-16728
    • Kraveka, J.M.1
  • 111
    • 33845336495 scopus 로고    scopus 로고
    • Ceramides and other bioactive sphingolipid backbones in health and disease: Lipidomic analysis, metabolism and roles in membrane structure, dynamics, signaling and autophagy
    • Zheng, W. et al. Ceramides and other bioactive sphingolipid backbones in health and disease: lipidomic analysis, metabolism and roles in membrane structure, dynamics, signaling and autophagy. Biochim. Biophys. Acta 1758, 1864-1884 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1864-1884
    • Zheng, W.1
  • 112
    • 0037321393 scopus 로고    scopus 로고
    • Role of the G-protein-coupled receptor GPR12 as high-affinity receptor for sphingosylphosphorylcholine and its expression and function in brain development
    • Ignatov, A. et al. Role of the G-protein-coupled receptor GPR12 as high-affinity receptor for sphingosylphosphorylcholine and its expression and function in brain development. J. Neurosci. 23, 907-914 (2003).
    • (2003) J. Neurosci , vol.23 , pp. 907-914
    • Ignatov, A.1
  • 113
    • 34547149529 scopus 로고    scopus 로고
    • Translational aspects of sphingolipid metabolism
    • Zeidan, Y. H. & Hannun, Y. A. Translational aspects of sphingolipid metabolism. Trends Mol. Med. 13, 327-336 (2007).
    • (2007) Trends Mol. Med , vol.13 , pp. 327-336
    • Zeidan, Y.H.1    Hannun, Y.A.2
  • 114
    • 0037375586 scopus 로고    scopus 로고
    • Designing anticancer drugs via the achilles heel: Ceramide, allylic ketones, and mitochondria
    • Radin, N. S. Designing anticancer drugs via the achilles heel: ceramide, allylic ketones, and mitochondria. Bioorg. Med. Chem. 11, 2123-2142 (2003).
    • (2003) Bioorg. Med. Chem , vol.11 , pp. 2123-2142
    • Radin, N.S.1
  • 115
    • 31644443192 scopus 로고    scopus 로고
    • Ceramides in insulin resistance and lipotoxicity
    • Summers, S. A. Ceramides in insulin resistance and lipotoxicity. Prog. Lipid Res. 45, 42-72 (2006).
    • (2006) Prog. Lipid Res , vol.45 , pp. 42-72
    • Summers, S.A.1
  • 116
    • 33744807983 scopus 로고    scopus 로고
    • The sphingosine and diacylglycerol kinase superfamily of signaling kinases: Localization as a key to signaling function
    • Wattenberg, B. W., Pitson, S. M. & Raben, D. M. The sphingosine and diacylglycerol kinase superfamily of signaling kinases: localization as a key to signaling function. J. Lipid Res. 47, 1128-1139 (2006).
    • (2006) J. Lipid Res , vol.47 , pp. 1128-1139
    • Wattenberg, B.W.1    Pitson, S.M.2    Raben, D.M.3
  • 117
    • 13444283465 scopus 로고    scopus 로고
    • Simulation and validation of modelled sphingolipid metabolism in Saccharomyces cerevisiae
    • Alvarez-Vasquez, F. et al. Simulation and validation of modelled sphingolipid metabolism in Saccharomyces cerevisiae. Nature 433, 425-430 (2005).
    • (2005) Nature , vol.433 , pp. 425-430
    • Alvarez-Vasquez, F.1
  • 118
    • 34548498611 scopus 로고    scopus 로고
    • Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide
    • D'Angelo, G. et al. Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide. Nature 449, 62-67 (2007).
    • (2007) Nature , vol.449 , pp. 62-67
    • D'Angelo, G.1


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