메뉴 건너뛰기




Volumn 1758, Issue 12, 2006, Pages 2049-2056

Ceramide 1-phosphate/ceramide, a switch between life and death

Author keywords

Apoptosis; Cell proliferation; Ceramide 1 phosphate; Phosphatidylinositol 3 kinase; Sphingomyelinases; Sphingosine 1 phosphate

Indexed keywords

CERAMIDE 1 PHOSPHATE; CERAMIDE DERIVATIVE; CERAMIDE KINASE; ENZYME;

EID: 33845292007     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.05.011     Document Type: Review
Times cited : (157)

References (120)
  • 1
    • 0036469777 scopus 로고    scopus 로고
    • Apoptotic DNA fragmentation and tissue homeostasis
    • Zhang J., and Xu M. Apoptotic DNA fragmentation and tissue homeostasis. Trends Cell Biol. 12 (2002) 84-89
    • (2002) Trends Cell Biol. , vol.12 , pp. 84-89
    • Zhang, J.1    Xu, M.2
  • 2
    • 0033593572 scopus 로고    scopus 로고
    • Cell death in development
    • Vaux D.L., and Korsmeyer S.J. Cell death in development. Cell 96 (1999) 245-254
    • (1999) Cell , vol.96 , pp. 245-254
    • Vaux, D.L.1    Korsmeyer, S.J.2
  • 3
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson C.B. Apoptosis in the pathogenesis and treatment of disease. Science 267 (1995) 1456-1462
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 4
    • 0025283928 scopus 로고
    • An update of the enzymology and regulation of sphingomyelin metabolism
    • Merrill A.H., and Jones D.D. An update of the enzymology and regulation of sphingomyelin metabolism. Biochim. Biophys. Acta 1044 (1990) 1-12
    • (1990) Biochim. Biophys. Acta , vol.1044 , pp. 1-12
    • Merrill, A.H.1    Jones, D.D.2
  • 5
    • 0026022563 scopus 로고
    • Cell regulation by sphingosine and more complex sphingolipids
    • Merrill A.H. Cell regulation by sphingosine and more complex sphingolipids. J. Bioenerg. Biomembr. 23 (1991) 83-104
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 83-104
    • Merrill, A.H.1
  • 7
    • 0037135536 scopus 로고    scopus 로고
    • De novo sphingolipid biosynthesis: a necessary, but dangerous, pathway
    • Merril A.H. De novo sphingolipid biosynthesis: a necessary, but dangerous, pathway. J. Biol. Chem. 277 (2002) 25843-25846
    • (2002) J. Biol. Chem. , vol.277 , pp. 25843-25846
    • Merril, A.H.1
  • 8
    • 0029862561 scopus 로고    scopus 로고
    • Sphingolipid metabolism and cell growth regulation
    • Spiegel S., and Merrill A.H. Sphingolipid metabolism and cell growth regulation. FASEB J. 10 (1996) 1388-1397
    • (1996) FASEB J. , vol.10 , pp. 1388-1397
    • Spiegel, S.1    Merrill, A.H.2
  • 9
    • 0023555012 scopus 로고
    • 1,2-Diacylglycerols but not phorbol esters stimulate sphingomyelin hydrolysis in GH3 pituitary cells
    • Kolesnick R.N. 1,2-Diacylglycerols but not phorbol esters stimulate sphingomyelin hydrolysis in GH3 pituitary cells. J. Biol. Chem. 262 (1987) 16759-16762
    • (1987) J. Biol. Chem. , vol.262 , pp. 16759-16762
    • Kolesnick, R.N.1
  • 10
    • 0025185675 scopus 로고
    • Characterization of a ceramide kinase activity from human leukemia (HL-60) cells
    • Kolesnick R.N., and Hemer M.R. Characterization of a ceramide kinase activity from human leukemia (HL-60) cells. J. Biol. Chem 265 (1990) 18803-18808
    • (1990) J. Biol. Chem , vol.265 , pp. 18803-18808
    • Kolesnick, R.N.1    Hemer, M.R.2
  • 11
    • 0028297068 scopus 로고
    • The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling
    • Kolesnick R., and Golde D.W. The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling. Cell 77 (1994) 325-328
    • (1994) Cell , vol.77 , pp. 325-328
    • Kolesnick, R.1    Golde, D.W.2
  • 12
    • 0033884050 scopus 로고    scopus 로고
    • Compartmentalization of ceramide signalling. Physical foundations and biological effects
    • Kolesnick R.N., Goñi F.M., and Alonso A. Compartmentalization of ceramide signalling. Physical foundations and biological effects. J. Cell. Physiol. 184 (2002) 285-300
    • (2002) J. Cell. Physiol. , vol.184 , pp. 285-300
    • Kolesnick, R.N.1    Goñi, F.M.2    Alonso, A.3
  • 13
    • 0022974603 scopus 로고
    • Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets
    • Hannun Y.A., Loomis C.R., Merrill A.H., and Bell R.M. Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets. J. Biol. Chem. 261 (1986) 12604-12609
    • (1986) J. Biol. Chem. , vol.261 , pp. 12604-12609
    • Hannun, Y.A.1    Loomis, C.R.2    Merrill, A.H.3    Bell, R.M.4
  • 14
    • 0027994349 scopus 로고
    • The sphingomyelin cycle and the second messenger function of ceramide
    • Hannun Y.A. The sphingomyelin cycle and the second messenger function of ceramide. J. Biol. Chem. 269 (1994) 3125-3128
    • (1994) J. Biol. Chem. , vol.269 , pp. 3125-3128
    • Hannun, Y.A.1
  • 15
    • 0028855405 scopus 로고
    • Ceramide: an intracellular signal for apoptosis
    • Hannun Y.A., and Obeid L.M. Ceramide: an intracellular signal for apoptosis. Trends Biochem. Sci. 20 (1995) 73-79
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 73-79
    • Hannun, Y.A.1    Obeid, L.M.2
  • 16
    • 0030448021 scopus 로고    scopus 로고
    • Functions of ceramide in coordinating cellular responses to stress
    • Hannun Y.A. Functions of ceramide in coordinating cellular responses to stress. Science 274 (1996) 1855-1859
    • (1996) Science , vol.274 , pp. 1855-1859
    • Hannun, Y.A.1
  • 17
    • 0037135626 scopus 로고    scopus 로고
    • The ceramide-centric Universe of lipid-mediated cell regulation: stress encounters of the lipid kind
    • Hannun Y.A., and Obeid L.M. The ceramide-centric Universe of lipid-mediated cell regulation: stress encounters of the lipid kind. J. Biol. Chem. 277 (2002) 25847-25850
    • (2002) J. Biol. Chem. , vol.277 , pp. 25847-25850
    • Hannun, Y.A.1    Obeid, L.M.2
  • 18
    • 0032532298 scopus 로고    scopus 로고
    • Ceramide can induce cell death in sensory neurons, whereas ceramide analogues and sphingosine promote survival
    • Ping S.E., and Barrett G.L. Ceramide can induce cell death in sensory neurons, whereas ceramide analogues and sphingosine promote survival. J. Neurosci. Res. 54 (1998) 206-213
    • (1998) J. Neurosci. Res. , vol.54 , pp. 206-213
    • Ping, S.E.1    Barrett, G.L.2
  • 19
    • 0033215974 scopus 로고    scopus 로고
    • Ceramide signaling downstream of p75 neurotrophin receptor mediates the effects of nerve growth factor on outgrowth of cultured hippocampal neurons
    • Brann A.B., Scott R., Neuberger Y., Abulafia D., Boldin S., Fainzilber M., and Futerman A.H. Ceramide signaling downstream of p75 neurotrophin receptor mediates the effects of nerve growth factor on outgrowth of cultured hippocampal neurons. J. Neurosci. 19 (1999) 8199-8206
    • (1999) J. Neurosci. , vol.19 , pp. 8199-8206
    • Brann, A.B.1    Scott, R.2    Neuberger, Y.3    Abulafia, D.4    Boldin, S.5    Fainzilber, M.6    Futerman, A.H.7
  • 20
    • 0030026613 scopus 로고    scopus 로고
    • Ceramide protects hippocampal neurons against exicitotoxic and oxidative insults, and amyloid beta-peptaide toxicity
    • Goodman Y., and Mattson M.P. Ceramide protects hippocampal neurons against exicitotoxic and oxidative insults, and amyloid beta-peptaide toxicity. J. Neurochem. 66 (1996) 869-872
    • (1996) J. Neurochem. , vol.66 , pp. 869-872
    • Goodman, Y.1    Mattson, M.P.2
  • 21
    • 13444274563 scopus 로고    scopus 로고
    • Activation of serine-threonine protein phosphatase-1 is required for ceramide-induced survival of sympathetic neurons
    • Plummer G., Perreault K.R., Holmes C.F., and Posse de Chaves E.I. Activation of serine-threonine protein phosphatase-1 is required for ceramide-induced survival of sympathetic neurons. Biochem. J. 385 Pt 3 (2005) 685-693
    • (2005) Biochem. J. , vol.385 , Issue.PART 3 , pp. 685-693
    • Plummer, G.1    Perreault, K.R.2    Holmes, C.F.3    Posse de Chaves, E.I.4
  • 22
    • 0242712151 scopus 로고    scopus 로고
    • Inhibition of rat sympathetic neuron apoptosis by ceramide. Role of p75NTR in ceramide generation
    • Song M.S., and Posse de Chaves E.I. Inhibition of rat sympathetic neuron apoptosis by ceramide. Role of p75NTR in ceramide generation. Neuropharmacology 45 (2003) 1130-1150
    • (2003) Neuropharmacology , vol.45 , pp. 1130-1150
    • Song, M.S.1    Posse de Chaves, E.I.2
  • 23
    • 0025003424 scopus 로고
    • Role of ceramide as a lipid mediator of 1 alpha,25-dihydroxyvitamin D3-induced HL-60 cell differentiation.
    • Okazaki T., Bielawska A., Bell R.M., and Hannun Y.A. Role of ceramide as a lipid mediator of 1 alpha,25-dihydroxyvitamin D3-induced HL-60 cell differentiation. J. Biol. Chem. 265 (1990) 15823-15831
    • (1990) J. Biol. Chem. , vol.265 , pp. 15823-15831
    • Okazaki, T.1    Bielawska, A.2    Bell, R.M.3    Hannun, Y.A.4
  • 24
    • 0025889011 scopus 로고
    • Characterization of a ceramide-activated protein kinase: stimulation by tumor necrosis factor alpha.
    • Mathias S., Dressler K., and Kolesnick R. Characterization of a ceramide-activated protein kinase: stimulation by tumor necrosis factor alpha. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 10009-10013
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 10009-10013
    • Mathias, S.1    Dressler, K.2    Kolesnick, R.3
  • 25
    • 0027488403 scopus 로고
    • Ceramide: a novel second messenger
    • Mathias S., and Kolesnick R. Ceramide: a novel second messenger. Adv. Lipid Res. 25 (1993) 65-90
    • (1993) Adv. Lipid Res. , vol.25 , pp. 65-90
    • Mathias, S.1    Kolesnick, R.2
  • 26
    • 0026560014 scopus 로고
    • Tumor necrosis factor-alpha activates the sphingomyelin signal transduction pathway in a cell-free system
    • Dressler K.A., Mathias S., and Kolesnick R.N. Tumor necrosis factor-alpha activates the sphingomyelin signal transduction pathway in a cell-free system. Science 255 (1992) 1715-1718
    • (1992) Science , vol.255 , pp. 1715-1718
    • Dressler, K.A.1    Mathias, S.2    Kolesnick, R.N.3
  • 27
    • 0032489435 scopus 로고    scopus 로고
    • Modulation of cell signalling by ceramides
    • Gómez-Muñoz A. Modulation of cell signalling by ceramides. Biochim. Biophys. Acta 1391 (1998) 92-109
    • (1998) Biochim. Biophys. Acta , vol.1391 , pp. 92-109
    • Gómez-Muñoz, A.1
  • 29
    • 0242574357 scopus 로고    scopus 로고
    • Raft ceramide in molecular medicine
    • Gulbins E., and Kolesnick R. Raft ceramide in molecular medicine. Oncogene 22 (2003) 7070-7077
    • (2003) Oncogene , vol.22 , pp. 7070-7077
    • Gulbins, E.1    Kolesnick, R.2
  • 30
    • 0036295566 scopus 로고    scopus 로고
    • Protein kinase C and lipid-induced insulin resistance in skeletal muscle
    • Schmitz-Peiffer C. Protein kinase C and lipid-induced insulin resistance in skeletal muscle. Ann. N. Y. Acad. Sci. 967 (2002) 146-157
    • (2002) Ann. N. Y. Acad. Sci. , vol.967 , pp. 146-157
    • Schmitz-Peiffer, C.1
  • 32
    • 4344614649 scopus 로고    scopus 로고
    • Regulation of insulin action by ceramide: dual mechanisms linking ceramide accumulation to the inhibition of Akt/Protein kinase B
    • Stratford S., Hoehn K.L., Liu F., and Summers S.A. Regulation of insulin action by ceramide: dual mechanisms linking ceramide accumulation to the inhibition of Akt/Protein kinase B. J. Biol. Chem. 279 (2004) 36608-36615
    • (2004) J. Biol. Chem. , vol.279 , pp. 36608-36615
    • Stratford, S.1    Hoehn, K.L.2    Liu, F.3    Summers, S.A.4
  • 34
    • 0027434784 scopus 로고
    • The role of sphingosine in cell growth regulation and transmembrane signaling
    • Spiegel S., Olivera A., and Carlson R.O. The role of sphingosine in cell growth regulation and transmembrane signaling. Adv. Lipid Res. 25 (1993) 105-127
    • (1993) Adv. Lipid Res. , vol.25 , pp. 105-127
    • Spiegel, S.1    Olivera, A.2    Carlson, R.O.3
  • 35
    • 0029996139 scopus 로고    scopus 로고
    • Signal transduction through lipid second messengers
    • Spiegel S., Foster D., and Kolesnick R. Signal transduction through lipid second messengers. Curr. Opin. Cell Biol. 8 (1996) 159-167
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 159-167
    • Spiegel, S.1    Foster, D.2    Kolesnick, R.3
  • 36
    • 0037135572 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate, a key cell signaling molecule
    • Spiegel S., and Milstien S. Sphingosine 1-phosphate, a key cell signaling molecule. J. Biol. Chem. 277 (2002) 25851-25854
    • (2002) J. Biol. Chem. , vol.277 , pp. 25851-25854
    • Spiegel, S.1    Milstien, S.2
  • 37
    • 0038218405 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate: an enigmatic signalling lipid
    • Spiegel S., and Milstien S. Sphingosine-1-phosphate: an enigmatic signalling lipid. Nat. Rev., Mol. Cell Biol. 4 (2003) 397-407
    • (2003) Nat. Rev., Mol. Cell Biol. , vol.4 , pp. 397-407
    • Spiegel, S.1    Milstien, S.2
  • 38
    • 0029014026 scopus 로고
    • Short-chain ceramide 1-phosphates are novel stimulators of DNA synthesis and cell division: antagonism by cell-permeable ceramides
    • Gómez-Muñoz A., Duffy P.A., Martin A., O'Brien L., Byun H.S., Bittman R., and Brindley D.N. Short-chain ceramide 1-phosphates are novel stimulators of DNA synthesis and cell division: antagonism by cell-permeable ceramides. Mol. Pharmacol. 47 (1995) 883-889
    • (1995) Mol. Pharmacol. , vol.47 , pp. 883-889
    • Gómez-Muñoz, A.1    Duffy, P.A.2    Martin, A.3    O'Brien, L.4    Byun, H.S.5    Bittman, R.6    Brindley, D.N.7
  • 39
    • 0030788162 scopus 로고    scopus 로고
    • Stimulation of DNA synthesis by natural ceramide 1-phosphate
    • Gómez-Muñoz A., Frago L., Alvarez L., and Varela-Nieto I. Stimulation of DNA synthesis by natural ceramide 1-phosphate. Biochem. J. 325 (1997) 435-440
    • (1997) Biochem. J. , vol.325 , pp. 435-440
    • Gómez-Muñoz, A.1    Frago, L.2    Alvarez, L.3    Varela-Nieto, I.4
  • 40
    • 1642403610 scopus 로고    scopus 로고
    • Ceramide-1-phosphate: a novel regulator of cell activation
    • Gómez-Muñoz A. Ceramide-1-phosphate: a novel regulator of cell activation. FEBS Lett. 562 (2004) 5-10
    • (2004) FEBS Lett. , vol.562 , pp. 5-10
    • Gómez-Muñoz, A.1
  • 41
    • 0037201939 scopus 로고    scopus 로고
    • Sphingomyelinases: enzymology and membrane activity
    • Goñi F.M., and Alonso A. Sphingomyelinases: enzymology and membrane activity. FEBS Lett. 531 (2002) 38-46
    • (2002) FEBS Lett. , vol.531 , pp. 38-46
    • Goñi, F.M.1    Alonso, A.2
  • 42
    • 0037201936 scopus 로고    scopus 로고
    • Role of sphingomyelin and ceramide in modulating rafts: do biophysical properties determine biologic outcome?
    • Cremesti A.E., Goñi F.M., and Kolesnick R.N. Role of sphingomyelin and ceramide in modulating rafts: do biophysical properties determine biologic outcome?. FEBS Lett. 531 (2002) 47-53
    • (2002) FEBS Lett. , vol.531 , pp. 47-53
    • Cremesti, A.E.1    Goñi, F.M.2    Kolesnick, R.N.3
  • 43
    • 19444380734 scopus 로고    scopus 로고
    • Sphingolipidomics: high-throughput, structure-specific, and quantitative analysis of sphingolipids by liquid chromatography tandem mass spectrometry
    • Merrill A.H., Sullards M.C., Allegood J.C., Kelly S., and Wang E. Sphingolipidomics: high-throughput, structure-specific, and quantitative analysis of sphingolipids by liquid chromatography tandem mass spectrometry. Methods 36 (2005) 207-224
    • (2005) Methods , vol.36 , pp. 207-224
    • Merrill, A.H.1    Sullards, M.C.2    Allegood, J.C.3    Kelly, S.4    Wang, E.5
  • 44
    • 0037685044 scopus 로고    scopus 로고
    • Observation of different ceramide species from crude cellular extracts by normal-phase high-performance liquid chromatography coupled to atmospheric pressure chemical ionization mass spectrometry
    • Pettus B.J., Bielawska A., Kroesen B.-J., Moeller P.D.R., Szulc Z.M., Hannun Y.A., and Busman M. Observation of different ceramide species from crude cellular extracts by normal-phase high-performance liquid chromatography coupled to atmospheric pressure chemical ionization mass spectrometry. Rapid Commun. Mass Spectrom. 17 (2003) 1203-1211
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 1203-1211
    • Pettus, B.J.1    Bielawska, A.2    Kroesen, B.-J.3    Moeller, P.D.R.4    Szulc, Z.M.5    Hannun, Y.A.6    Busman, M.7
  • 45
    • 0035007113 scopus 로고    scopus 로고
    • Sphingolipid metabolism: roles in signal transduction and disruption by fumonisins
    • Merrill A.H., Sullards M.C., Voss K.A., and Riley R.T. Sphingolipid metabolism: roles in signal transduction and disruption by fumonisins. Environ. Health Perspect. 109 (2001) 283-289
    • (2001) Environ. Health Perspect. , vol.109 , pp. 283-289
    • Merrill, A.H.1    Sullards, M.C.2    Voss, K.A.3    Riley, R.T.4
  • 46
    • 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. Sphingomyelin turnover induced by vitamin D3 in HL-60 cells. Role in cell differentiation. J. Biol. Chem. 264 (1989) 19076-19080
    • (1989) J. Biol. Chem. , vol.264 , pp. 19076-19080
    • Okazaki, T.1    Bell, R.M.2    Hannun, Y.A.3
  • 48
    • 0028838235 scopus 로고
    • Phosphorylation of Raf by ceramide-activated protein kinase
    • Yao B., Zhang Y., Delikat S., Mathias S., Basu S., and Kolesnick R. Phosphorylation of Raf by ceramide-activated protein kinase. Nature 378 (1995) 307-310
    • (1995) Nature , vol.378 , pp. 307-310
    • Yao, B.1    Zhang, Y.2    Delikat, S.3    Mathias, S.4    Basu, S.5    Kolesnick, R.6
  • 49
    • 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., Galdari S., Kroesen B.J., Pettus B.J., and Hannun Y.A. 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 (2001) 44848-44855
    • (2001) J. Biol. Chem. , vol.276 , pp. 44848-44855
    • Chalfant, C.E.1    Ogretmen, B.2    Galdari, S.3    Kroesen, B.J.4    Pettus, B.J.5    Hannun, Y.A.6
  • 50
    • 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., and Hannun Y.A. The structural requirements for ceramide activation of serine-threonine protein phosphatases. J. Lipid Res. 45 (2004) 496-506
    • (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
  • 51
    • 0026723048 scopus 로고
    • Ceramide stimulates a cytosolic protein phosphatase
    • Dobrowsky R.T., and Hannun Y.A. Ceramide stimulates a cytosolic protein phosphatase. J. Biol. Chem. 267 (1992) 5048-5051
    • (1992) J. Biol. Chem. , vol.267 , pp. 5048-5051
    • Dobrowsky, R.T.1    Hannun, Y.A.2
  • 52
    • 0027965006 scopus 로고
    • Protein kinase C zeta isoform is critical for kappa B-dependent promoter activation by sphingomyelinase
    • Lozano J., Berra E., Municio M.M., Diaz-Meco M.T., Dominguez I., Sanz L., and Moscat J. Protein kinase C zeta isoform is critical for kappa B-dependent promoter activation by sphingomyelinase. J. Biol. Chem. 265 (1994) 19200-19202
    • (1994) J. Biol. Chem. , vol.265 , 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
  • 56
    • 0029890361 scopus 로고    scopus 로고
    • Role of ceramide in stimulation of the transcription of cytosolic phospholipase A2 and cyclooxigenase 2
    • Hayakawa M., Jayadev S., Tsujimoto M., Hannun Y.A., and Fumiaki I. Role of ceramide in stimulation of the transcription of cytosolic phospholipase A2 and cyclooxigenase 2. Biochem. Biophys. Res. Commun. 220 (1996) 681-686
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 681-686
    • Hayakawa, M.1    Jayadev, S.2    Tsujimoto, M.3    Hannun, Y.A.4    Fumiaki, I.5
  • 57
    • 0036479251 scopus 로고    scopus 로고
    • Ceramide-induced inhibition of Akt is mediated through protein kinase Cζ
    • Bourbon N.A., Sandirasegarane L., and Kester M. Ceramide-induced inhibition of Akt is mediated through protein kinase Cζ. J. Biol. Chem. 277 (2002) 3286-3292
    • (2002) J. Biol. Chem. , vol.277 , pp. 3286-3292
    • Bourbon, N.A.1    Sandirasegarane, L.2    Kester, M.3
  • 58
    • 0034607914 scopus 로고    scopus 로고
    • Ceramide inhibits protein kinase B/Akt by promoting dephosphorylation of Ser 473
    • Schubert K.M., Scheid M.P., and Duronio V. Ceramide inhibits protein kinase B/Akt by promoting dephosphorylation of Ser 473. J. Biol. Chem. 275 (2000) 13330-13335
    • (2000) J. Biol. Chem. , vol.275 , pp. 13330-13335
    • Schubert, K.M.1    Scheid, M.P.2    Duronio, V.3
  • 59
    • 0028339322 scopus 로고
    • Cell-permeable ceramides inhibit the stimulation of DNA synthesis and phospholipase D activity by phosphatidate and lysophosphatidate in rat fibroblasts
    • Gómez-Muñoz A., Martin A., O'Brien L., and Brindley D.N. Cell-permeable ceramides inhibit the stimulation of DNA synthesis and phospholipase D activity by phosphatidate and lysophosphatidate in rat fibroblasts. J. Biol. Chem. 269 (1994) 8937-8943
    • (1994) J. Biol. Chem. , vol.269 , pp. 8937-8943
    • Gómez-Muñoz, A.1    Martin, A.2    O'Brien, L.3    Brindley, D.N.4
  • 60
    • 0028825719 scopus 로고
    • Interaction of ceramides, sphingosine, and sphingosine 1-phosphate in regulating DNA synthesis and phospholipase D activity
    • Gómez-Muñoz A., Waggoner D.W., O'Brien L., and Brindley D.N. Interaction of ceramides, sphingosine, and sphingosine 1-phosphate in regulating DNA synthesis and phospholipase D activity. J. Biol. Chem. 270 (1995) 26318-26325
    • (1995) J. Biol. Chem. , vol.270 , pp. 26318-26325
    • Gómez-Muñoz, A.1    Waggoner, D.W.2    O'Brien, L.3    Brindley, D.N.4
  • 61
    • 0031012382 scopus 로고    scopus 로고
    • Cell permeable ceramides prevent the activation of phospholipase D by ADP-ribosylation factor and Rho A
    • Abousalham A., Liossis C., O'Brien L., and Brindley D.N. Cell permeable ceramides prevent the activation of phospholipase D by ADP-ribosylation factor and Rho A. J. Biol. Chem. 272 (1997) 1069-1075
    • (1997) J. Biol. Chem. , vol.272 , pp. 1069-1075
    • Abousalham, A.1    Liossis, C.2    O'Brien, L.3    Brindley, D.N.4
  • 62
    • 0031051559 scopus 로고    scopus 로고
    • Changing J774A.1 cells to new medium perturbs multiple signaling pathways, including the modulation of protein kinase C by endogenous sphingoid bases
    • Smith E.R., Jones P.L., Boss J.M., and Merrill A.H. Changing J774A.1 cells to new medium perturbs multiple signaling pathways, including the modulation of protein kinase C by endogenous sphingoid bases. J. Biol. Chem. 272 (1997) 5640-5646
    • (1997) J. Biol. Chem. , vol.272 , pp. 5640-5646
    • Smith, E.R.1    Jones, P.L.2    Boss, J.M.3    Merrill, A.H.4
  • 63
    • 0026654779 scopus 로고
    • Effects of sphingosine, albumin and unsaturated fatty acids on the activation and translocation of phosphatidate phosphohydrolases in rat hepatocytes
    • Gómez-Muñoz A., Hamza E.H., and Brindley D.N. Effects of sphingosine, albumin and unsaturated fatty acids on the activation and translocation of phosphatidate phosphohydrolases in rat hepatocytes. Biochim. Biophys. Acta 1127 (1992) 49-56
    • (1992) Biochim. Biophys. Acta , vol.1127 , pp. 49-56
    • Gómez-Muñoz, A.1    Hamza, E.H.2    Brindley, D.N.3
  • 64
    • 0025774977 scopus 로고
    • Plasma membrane fractions from rat liver contain a phosphatidate phosphohydrolase distinct from that in the endoplasmic reticulum and cytosol
    • Jamal Z., Martin A., Gomez-Muñoz A., and Brindley D.N. Plasma membrane fractions from rat liver contain a phosphatidate phosphohydrolase distinct from that in the endoplasmic reticulum and cytosol. J. Biol. Chem. 266 (1991) 2988-2996
    • (1991) J. Biol. Chem. , vol.266 , pp. 2988-2996
    • Jamal, Z.1    Martin, A.2    Gomez-Muñoz, A.3    Brindley, D.N.4
  • 65
    • 0028486763 scopus 로고
    • Activation of endothelial cell phospholipase D by sphingosine and sphingosine 1-phosphate
    • Natarajan V., Jayaram H.N., and Scribner W.M. Activation of endothelial cell phospholipase D by sphingosine and sphingosine 1-phosphate. Am. J. Respir. Cell Mol. Biol. 11 (1994) 221-229
    • (1994) Am. J. Respir. Cell Mol. Biol. , vol.11 , pp. 221-229
    • Natarajan, V.1    Jayaram, H.N.2    Scribner, W.M.3
  • 66
    • 0024412757 scopus 로고
    • Different effects of sphingosine, R59022 and anionic amphiphiles on two diacylglycerol kinase isozymes purified from porcine thymus cytosol.
    • Sakane F., Yamada K., and Kanoh H. Different effects of sphingosine, R59022 and anionic amphiphiles on two diacylglycerol kinase isozymes purified from porcine thymus cytosol. FEBS Lett. 255 (1989) 409-413
    • (1989) FEBS Lett. , vol.255 , pp. 409-413
    • Sakane, F.1    Yamada, K.2    Kanoh, H.3
  • 67
    • 0027302925 scopus 로고
    • Sphingosine activates cellular diacylglycerol kinase in intact Jurkat cells, a human T-cell line.
    • Yamada K., Sakane F., Imai S.I., and Kanoh H. Sphingosine activates cellular diacylglycerol kinase in intact Jurkat cells, a human T-cell line. Biochim. Biophys. Acta 1169 (1993) 217-224
    • (1993) Biochim. Biophys. Acta , vol.1169 , pp. 217-224
    • Yamada, K.1    Sakane, F.2    Imai, S.I.3    Kanoh, H.4
  • 68
    • 0029079324 scopus 로고
    • Sphingosine-1-phosphate rapidly activates the mitogen-activated protein kinase pathway by a G protein-dependent mechanism
    • Wu J., Spiegel S., and Sturgill T.W. Sphingosine-1-phosphate rapidly activates the mitogen-activated protein kinase pathway by a G protein-dependent mechanism. J. Biol. Chem. 270 (1995) 11484-11488
    • (1995) J. Biol. Chem. , vol.270 , pp. 11484-11488
    • Wu, J.1    Spiegel, S.2    Sturgill, T.W.3
  • 71
    • 27844517355 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate and ceramide-1-phosphate: expanding roles in cell signaling
    • Chalfant C., and Spiegel S. Sphingosine-1-phosphate and ceramide-1-phosphate: expanding roles in cell signaling. J. Cell Sci. 118 (2005) 4605-4612
    • (2005) J. Cell Sci. , vol.118 , pp. 4605-4612
    • Chalfant, C.1    Spiegel, S.2
  • 72
    • 30344435318 scopus 로고    scopus 로고
    • Ceramide-1-phosphate: the "missing" link in eicosanoid biosynthesis and inflammation
    • Lamour N.F., and Chalfant C. Ceramide-1-phosphate: the "missing" link in eicosanoid biosynthesis and inflammation. Mol. Interv. 5 (2005) 358-367
    • (2005) Mol. Interv. , vol.5 , pp. 358-367
    • Lamour, N.F.1    Chalfant, C.2
  • 75
    • 0025168334 scopus 로고
    • Ceramide-1-phosphate, a novel phospholipid in human leukemia (HL-60) cells
    • Dressler K.A., and Kolesnick R.N. Ceramide-1-phosphate, a novel phospholipid in human leukemia (HL-60) cells. J. Biol. Chem. 265 (1990) 14917-14921
    • (1990) J. Biol. Chem. , vol.265 , pp. 14917-14921
    • Dressler, K.A.1    Kolesnick, R.N.2
  • 76
    • 0024373904 scopus 로고
    • Synaptic vesicle ceramide kinase. A calcium-stimulated lipid kinase that copurifies with brain synaptic vesicles.
    • Bajjalieh S.M., Martin T.F.J., and Floor E. Synaptic vesicle ceramide kinase. A calcium-stimulated lipid kinase that copurifies with brain synaptic vesicles. J. Biol. Chem. 264 (1989) 14354-14360
    • (1989) J. Biol. Chem. , vol.264 , pp. 14354-14360
    • Bajjalieh, S.M.1    Martin, T.F.J.2    Floor, E.3
  • 77
  • 79
    • 23644433676 scopus 로고    scopus 로고
    • The leucine 10 residue in the pleckstrin homology domain of ceramide kinase is crucial for its catalytic activity
    • Kim T.-J., Mitsutake S., Kato M., and Igarashi Y. The leucine 10 residue in the pleckstrin homology domain of ceramide kinase is crucial for its catalytic activity. FEBS Lett. 579 (2005) 4383-4388
    • (2005) FEBS Lett. , vol.579 , pp. 4383-4388
    • Kim, T.-J.1    Mitsutake, S.2    Kato, M.3    Igarashi, Y.4
  • 80
    • 33344456919 scopus 로고    scopus 로고
    • The interaction between the plekstrin homology domain of ceramide kinase and phosphatidylinositol 4,5-bisphosphate regulates the plasma membrane targeting and ceramide 1-phosphate levels
    • Kim T.-J., Mitsutake S., and Igarashi Y. The interaction between the plekstrin homology domain of ceramide kinase and phosphatidylinositol 4,5-bisphosphate regulates the plasma membrane targeting and ceramide 1-phosphate levels. Biochim. Biophys. Res Commun. 342 (2006) 611-617
    • (2006) Biochim. Biophys. Res Commun. , vol.342 , pp. 611-617
    • Kim, T.-J.1    Mitsutake, S.2    Igarashi, Y.3
  • 81
    • 10044236607 scopus 로고    scopus 로고
    • The role of sphingosine and ceramide kinases in inflammatory responses
    • Baumruker T., Bornancin F., and Billich A. The role of sphingosine and ceramide kinases in inflammatory responses. Immunol. Lett. 96 (2005) 175-185
    • (2005) Immunol. Lett. , vol.96 , pp. 175-185
    • Baumruker, T.1    Bornancin, F.2    Billich, A.3
  • 83
    • 0141755365 scopus 로고    scopus 로고
    • Ceramide kinase mediates cytokine- and calcium ionophore-induced arachidonic acid release
    • Pettus B.J., Bielawska A., Spiegel S., Roddy P., Hannun Y.A., and Chalfant C.E. Ceramide kinase mediates cytokine- and calcium ionophore-induced arachidonic acid release. J. Biol. Chem. 278 (2003) 38206-38213
    • (2003) J. Biol. Chem. , vol.278 , pp. 38206-38213
    • Pettus, B.J.1    Bielawska, A.2    Spiegel, S.3    Roddy, P.4    Hannun, Y.A.5    Chalfant, C.E.6
  • 84
    • 0346373649 scopus 로고    scopus 로고
    • Mutation of CERKL, a novel human ceramide kinase gene, causes autosomal recessive renitis pigmentosa (RP26)
    • Tuson M., Marfany G., and González-Duarte R. Mutation of CERKL, a novel human ceramide kinase gene, causes autosomal recessive renitis pigmentosa (RP26). Am. J. Hum. Genet. 74 (2004) 128-138
    • (2004) Am. J. Hum. Genet. , vol.74 , pp. 128-138
    • Tuson, M.1    Marfany, G.2    González-Duarte, R.3
  • 86
    • 0037219462 scopus 로고    scopus 로고
    • Ceramide 1-phosphate formation in neutrophils
    • Rile G., Yatomi Y., Takafuta T., and Ozaki Y. Ceramide 1-phosphate formation in neutrophils. Acta Haematol. 109 (2003) 76-83
    • (2003) Acta Haematol. , vol.109 , pp. 76-83
    • Rile, G.1    Yatomi, Y.2    Takafuta, T.3    Ozaki, Y.4
  • 87
    • 0036695440 scopus 로고    scopus 로고
    • Metabolic formation of ceramide-1-phosphate in cerebellar granule cells: evidence for the phosphorylation of ceramide by different metabolic pathways
    • Riboni L., Bassi R., Anelli V., and Viani P. Metabolic formation of ceramide-1-phosphate in cerebellar granule cells: evidence for the phosphorylation of ceramide by different metabolic pathways. Neurochem. Res. 27 (2002) 711-716
    • (2002) Neurochem. Res. , vol.27 , pp. 711-716
    • Riboni, L.1    Bassi, R.2    Anelli, V.3    Viani, P.4
  • 90
    • 20444371635 scopus 로고    scopus 로고
    • Ceramide-1-phosphate acts as a positive allosteric activator of group IV cytosolic phospholipase A2-alfa and enhances the interaction of the enzyme with phosphatidylcholine
    • Subramanian P., Stahelin R.V., Szulc Z., Bielawska A., Cho W., and Chalfant C. Ceramide-1-phosphate acts as a positive allosteric activator of group IV cytosolic phospholipase A2-alfa and enhances the interaction of the enzyme with phosphatidylcholine. J. Biol. Chem. 280 (2005) 17601-17607
    • (2005) J. Biol. Chem. , vol.280 , pp. 17601-17607
    • Subramanian, P.1    Stahelin, R.V.2    Szulc, Z.3    Bielawska, A.4    Cho, W.5    Chalfant, C.6
  • 91
    • 32144439190 scopus 로고    scopus 로고
    • Ceramide-1-phosphate activates cytosilic phospholipase 2-alfa directly and by PKC pathway
    • Nakamura H., Hirabayashi T., Shimuzu M., and Murayama T. Ceramide-1-phosphate activates cytosilic phospholipase 2-alfa directly and by PKC pathway. Biochem. Pharmacol. 71 (2006) 850-857
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 850-857
    • Nakamura, H.1    Hirabayashi, T.2    Shimuzu, M.3    Murayama, T.4
  • 92
    • 0842282983 scopus 로고    scopus 로고
    • Ceramide-1-phosphate blocks apoptosis through inhibition of acid sphingomyelinase in macrophages
    • Gómez-Muñoz A., Kong J.Y., Salh B., and Steinbrecher U.P. Ceramide-1-phosphate blocks apoptosis through inhibition of acid sphingomyelinase in macrophages. J. Lipid Res. 45 (2004) 99-105
    • (2004) J. Lipid Res. , vol.45 , pp. 99-105
    • Gómez-Muñoz, A.1    Kong, J.Y.2    Salh, B.3    Steinbrecher, U.P.4
  • 93
    • 0027350613 scopus 로고
    • Sphingomyelinase D: a pathogenic agent produced by bacteria and arthropodes
    • Truett A.P., and King L.E.J. Sphingomyelinase D: a pathogenic agent produced by bacteria and arthropodes. Adv. Lipid Res. 26 (1993) 275-289
    • (1993) Adv. Lipid Res. , vol.26 , pp. 275-289
    • Truett, A.P.1    King, L.E.J.2
  • 94
    • 27444432178 scopus 로고    scopus 로고
    • Brown recluse spider (Loxosceles reclusa) venom phospholipase D (PLD) generated lysophosphatidic acid (LPA)
    • Lee S., and Lynch K.R. Brown recluse spider (Loxosceles reclusa) venom phospholipase D (PLD) generated lysophosphatidic acid (LPA). Biochem. J. 391 (2005) 317-323
    • (2005) Biochem. J. , vol.391 , pp. 317-323
    • Lee, S.1    Lynch, K.R.2
  • 95
    • 0027430787 scopus 로고
    • Ceramide-1-phosphate phosphatase activity in brain
    • Shinghal R., Scheller R.H., and Bajjalieh S.M. Ceramide-1-phosphate phosphatase activity in brain. J. Neurochem. 61 (1993) 2279-2285
    • (1993) J. Neurochem. , vol.61 , pp. 2279-2285
    • Shinghal, R.1    Scheller, R.H.2    Bajjalieh, S.M.3
  • 96
    • 0027377618 scopus 로고
    • Detection and characterization of ceramide-1-phosphate phosphatase activity in rat liver plasma membrane
    • Boudker O., and Futerman A.H. Detection and characterization of ceramide-1-phosphate phosphatase activity in rat liver plasma membrane. J. Biol. Chem. 268 (1993) 22150-22155
    • (1993) J. Biol. Chem. , vol.268 , pp. 22150-22155
    • Boudker, O.1    Futerman, A.H.2
  • 97
    • 0029904257 scopus 로고    scopus 로고
    • Phosphatidate phosphohydrolase catalyzes the hydrolysis of ceramide-1-phosphate, lysophosphatidate, and sphingosine-1-phosphate
    • Waggoner D.W., Gomez-Muñoz A., Dewald J., and Brindley D.N. Phosphatidate phosphohydrolase catalyzes the hydrolysis of ceramide-1-phosphate, lysophosphatidate, and sphingosine-1-phosphate. J. Biol. Chem. 271 (1996) 16506-16509
    • (1996) J. Biol. Chem. , vol.271 , pp. 16506-16509
    • Waggoner, D.W.1    Gomez-Muñoz, A.2    Dewald, J.3    Brindley, D.N.4
  • 98
    • 0032544691 scopus 로고    scopus 로고
    • Mammalian lipid phosphate phosphohydrolases
    • Brindley D.N., and Waggoner D.W. Mammalian lipid phosphate phosphohydrolases. J. Biol. Chem. 273 (1998) 24281-24283
    • (1998) J. Biol. Chem. , vol.273 , pp. 24281-24283
    • Brindley, D.N.1    Waggoner, D.W.2
  • 99
    • 26844442547 scopus 로고    scopus 로고
    • Regulation of cell survival by lipid phosphatases involves the modulation of intracellular phosphatidic acid and sphingosine-1-phosphate pools
    • Long J., Darroch P., Wan K.F., Kong K.C., Ktistakis N., Pyne N.J., and Pyne S. Regulation of cell survival by lipid phosphatases involves the modulation of intracellular phosphatidic acid and sphingosine-1-phosphate pools. Biochem. J. 391 (2005) 25-32
    • (2005) Biochem. J. , vol.391 , pp. 25-32
    • Long, J.1    Darroch, P.2    Wan, K.F.3    Kong, K.C.4    Ktistakis, N.5    Pyne, N.J.6    Pyne, S.7
  • 100
    • 19944432760 scopus 로고    scopus 로고
    • Lipid phosphate phosphatase-1 regulates lysophosphatidic acid-induced calcium release, NF-κB activation and interleukin-8 secretion in human bronchial epithelial cells
    • Zhao Y., Zhang Y., Delikat S., Mathias S., Basu S., and Kolesnick R.N. Lipid phosphate phosphatase-1 regulates lysophosphatidic acid-induced calcium release, NF-κB activation and interleukin-8 secretion in human bronchial epithelial cells. Biochem. J. 385 (2005) 493-502
    • (2005) Biochem. J. , vol.385 , pp. 493-502
    • Zhao, Y.1    Zhang, Y.2    Delikat, S.3    Mathias, S.4    Basu, S.5    Kolesnick, R.N.6
  • 101
    • 22244478079 scopus 로고    scopus 로고
    • Cellular DNA replicases: components and dynamics at the replication fork
    • Johnson A., and O'Donell M. Cellular DNA replicases: components and dynamics at the replication fork. Annu. Rev. Biochem. 74 (2005) 283-315
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 283-315
    • Johnson, A.1    O'Donell, M.2
  • 102
    • 2642600056 scopus 로고    scopus 로고
    • Nerve growth factor and ceramides modulate cell death in the early developing inner ear.
    • Frago L.M., León Y., de la Rosa E.J., Gómez-Muñoz A., and Varela-Nieto I. Nerve growth factor and ceramides modulate cell death in the early developing inner ear. J. Cell Sci. 111 (1998) 549-556
    • (1998) J. Cell Sci. , vol.111 , pp. 549-556
    • Frago, L.M.1    León, Y.2    de la Rosa, E.J.3    Gómez-Muñoz, A.4    Varela-Nieto, I.5
  • 104
    • 19444377889 scopus 로고    scopus 로고
    • Molecular associations and surface-active properties of short- and long-N-acyl chain ceramides
    • Sot J., Goñi F.M., and Alonso A. Molecular associations and surface-active properties of short- and long-N-acyl chain ceramides. Biochim. Biophys. Acta 1711 (2005) 12-19
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 12-19
    • Sot, J.1    Goñi, F.M.2    Alonso, A.3
  • 106
    • 0032794361 scopus 로고    scopus 로고
    • N-acetyl- sphingenine-1-phosphate is a potent calcium mobilizing agent
    • Gijsbers S., Mannaerts G.P., Himpens B., and Van Veldhoven P.P. N-acetyl- sphingenine-1-phosphate is a potent calcium mobilizing agent. FEBS Lett. 453 (1999) 269-272
    • (1999) FEBS Lett. , vol.453 , pp. 269-272
    • Gijsbers, S.1    Mannaerts, G.P.2    Himpens, B.3    Van Veldhoven, P.P.4
  • 107
    • 0242501551 scopus 로고    scopus 로고
    • Ceramide 1-phosphate increases intracellular free calcium concentrations in thyroid FRTL-5 cells: evidence for an effect mediated by inositol 1,4,5-trisphosphate and intracellular sphingosine 1-phosphate
    • Hogback S., Leppimaki P., Rudnas B., Bjorklund S., Slotte J.P., and Tornquist K. Ceramide 1-phosphate increases intracellular free calcium concentrations in thyroid FRTL-5 cells: evidence for an effect mediated by inositol 1,4,5-trisphosphate and intracellular sphingosine 1-phosphate. Biochem. J. 370 (2003) 111-119
    • (2003) Biochem. J. , vol.370 , pp. 111-119
    • Hogback, S.1    Leppimaki, P.2    Rudnas, B.3    Bjorklund, S.4    Slotte, J.P.5    Tornquist, K.6
  • 108
    • 24344495483 scopus 로고    scopus 로고
    • Ceramide-1-phosphate induces Ca2+ mobilization in Jurkat T-cells by elevation of Ins(1,4,5)-P3 and activation of a store-operated calcium channel
    • Colina C., Flores A., Castillo C., del Rosario Garrido M., Israel A., DiPolo R., and Benaim G. Ceramide-1-phosphate induces Ca2+ mobilization in Jurkat T-cells by elevation of Ins(1,4,5)-P3 and activation of a store-operated calcium channel. Biochim. Biophys. Res. Commun. 336 (2005) 54-60
    • (2005) Biochim. Biophys. Res. Commun. , vol.336 , pp. 54-60
    • Colina, C.1    Flores, A.2    Castillo, C.3    del Rosario Garrido, M.4    Israel, A.5    DiPolo, R.6    Benaim, G.7
  • 109
    • 0033591231 scopus 로고    scopus 로고
    • Roles of the mitogen-activated protein kinase family in macrophage responses to colony stimulating factor-1 addition and withdrawal
    • Jaworowski A., Wilson N.J., Christy E., Byrne R., and Hamilton J.A. Roles of the mitogen-activated protein kinase family in macrophage responses to colony stimulating factor-1 addition and withdrawal. J. Biol. Chem. 274 (1999) 15127-15133
    • (1999) J. Biol. Chem. , vol.274 , pp. 15127-15133
    • Jaworowski, A.1    Wilson, N.J.2    Christy, E.3    Byrne, R.4    Hamilton, J.A.5
  • 110
    • 0042090272 scopus 로고    scopus 로고
    • Oxidized low density lipoprotein inhibits macrophage apoptosis by blocking ceramide generation thereby maintaining PKB activation and Bcl-XL levels.
    • Hundal R.S., Gómez-Muñoz A., K.J.Y., Salh B., Marotta A., Duronio V., and Steinbrecher U.P. Oxidized low density lipoprotein inhibits macrophage apoptosis by blocking ceramide generation thereby maintaining PKB activation and Bcl-XL levels. J. Biol. Chem. 278 (2003) 24399-24408
    • (2003) J. Biol. Chem. , vol.278 , Issue.27 , pp. 24399-24408
    • Hundal, R.S.1    Gómez-Muñoz, A.2    Kong, J.Y.3    Salh, B.4    Marotta, A.5    Duronio, V.6    Steinbrecher, U.P.7
  • 111
    • 0037468614 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate inhibits sphingomyelinase and blocks apoptosis in macrophages
    • Gómez-Muñoz A., Kong J., Salh B., and Steinbrecher U. Sphingosine-1-phosphate inhibits sphingomyelinase and blocks apoptosis in macrophages. FEBS Lett. 539 (2003) 56-60
    • (2003) FEBS Lett. , vol.539 , pp. 56-60
    • Gómez-Muñoz, A.1    Kong, J.2    Salh, B.3    Steinbrecher, U.4
  • 113
    • 2042499658 scopus 로고    scopus 로고
    • Acid sphingomyelinase and inhibition by phosphate ion: role of inhibition by phosphatidyl-myo-inositol 3,4,5-triphosphate in oligodendrocyte cell signaling
    • Testai F.D., Landek M.A., Goswami R., Ahmed M., and Dawson G. Acid sphingomyelinase and inhibition by phosphate ion: role of inhibition by phosphatidyl-myo-inositol 3,4,5-triphosphate in oligodendrocyte cell signaling. J. Neurochem. 89 (2004) 636-644
    • (2004) J. Neurochem. , vol.89 , pp. 636-644
    • Testai, F.D.1    Landek, M.A.2    Goswami, R.3    Ahmed, M.4    Dawson, G.5
  • 114
    • 0037088681 scopus 로고    scopus 로고
    • Phosphatidylinositol (3,4,5)P3 is essential but not sufficient for protein kinase B (PKB) activation; phosphatidylinositol (3,4)P2 is required for PKB phosphorylation at Ser-473: studies using cells from SH2-containing inositol-5-phosphatase knockout mice
    • Scheid M.P., Huber M., Damen J.E., Hughes M., Kang V., Neilsen P., Prestwich G.D., Krystal G., and Duronio V. Phosphatidylinositol (3,4,5)P3 is essential but not sufficient for protein kinase B (PKB) activation; phosphatidylinositol (3,4)P2 is required for PKB phosphorylation at Ser-473: studies using cells from SH2-containing inositol-5-phosphatase knockout mice. J. Biol. Chem. 277 (2002) 9027-9035
    • (2002) J. Biol. Chem. , vol.277 , pp. 9027-9035
    • Scheid, M.P.1    Huber, M.2    Damen, J.E.3    Hughes, M.4    Kang, V.5    Neilsen, P.6    Prestwich, G.D.7    Krystal, G.8    Duronio, V.9
  • 115
    • 0037862006 scopus 로고    scopus 로고
    • Unravelling the activation mechanisms of protein kinase B/Akt
    • Scheid M.P., and Woodgett J.R. Unravelling the activation mechanisms of protein kinase B/Akt. FEBS Lett. 546 (2003) 108-112
    • (2003) FEBS Lett. , vol.546 , pp. 108-112
    • Scheid, M.P.1    Woodgett, J.R.2
  • 116
    • 0030943057 scopus 로고    scopus 로고
    • cAMP stimulates protein kinase B in a wortmannin-insensitive manner
    • Sable C.L., Filippa N., Hemming B., and Van Obberghen E. cAMP stimulates protein kinase B in a wortmannin-insensitive manner. FEBS Lett. 409 (1997) 253-257
    • (1997) FEBS Lett. , vol.409 , pp. 253-257
    • Sable, C.L.1    Filippa, N.2    Hemming, B.3    Van Obberghen, E.4
  • 117
    • 0032997270 scopus 로고    scopus 로고
    • Mechanism of protein kinase B activation by cyclic AMP-dependent protein kinase B
    • Filippa N., Sable C.L., Filloux C., Hemmings B., and Van Obberghen E. Mechanism of protein kinase B activation by cyclic AMP-dependent protein kinase B. Mol. Cell. Biol. 19 (1999) 4989-5000
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4989-5000
    • Filippa, N.1    Sable, C.L.2    Filloux, C.3    Hemmings, B.4    Van Obberghen, E.5
  • 118
    • 33646344489 scopus 로고    scopus 로고
    • P2Y12 receptor signalling towards PKB proceeds through IGF-I receptor cross-talk and requires activation of Src, Pyk2 and Rap1
    • Van Kolen K., Gilany K., Moens L., Esmans E.L., and Slegers H. P2Y12 receptor signalling towards PKB proceeds through IGF-I receptor cross-talk and requires activation of Src, Pyk2 and Rap1. Cell. Signalling 18 (2006) 1169-1181
    • (2006) Cell. Signalling , vol.18 , pp. 1169-1181
    • Van Kolen, K.1    Gilany, K.2    Moens, L.3    Esmans, E.L.4    Slegers, H.5
  • 119
    • 0037326496 scopus 로고    scopus 로고
    • Programmed cell death in the developing inner ear is balanced by nerve growth factor and insulin-like growth factor I
    • Frago L., Cañón S., de la Rosa E.J., León Y., and Varela-Nieto I. Programmed cell death in the developing inner ear is balanced by nerve growth factor and insulin-like growth factor I. J. Cell Sci. 116 (2003) 475-486
    • (2003) J. Cell Sci. , vol.116 , pp. 475-486
    • Frago, L.1    Cañón, S.2    de la Rosa, E.J.3    León, Y.4    Varela-Nieto, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.