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Volumn 96, Issue 2, 2005, Pages 83-92

Phytosphingosine induced mitochondria-involved apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; CASPASE 8; CASPASE 9; CYTOCHROME C; DNA FRAGMENT; OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; PHYTOSPHINGOSINE; PROTEIN BCL 2; PROTEIN KINASE B; PROTEIN P70; SPHINGANINE; SPHINGOLIPID; CASPASE; DRUG DERIVATIVE; SPHINGOSINE;

EID: 15844395370     PISSN: 13479032     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1349-7006.2005.00012.x     Document Type: Article
Times cited : (55)

References (39)
  • 1
    • 0032567877 scopus 로고    scopus 로고
    • The thiol crosslinking agent diamide overcomes the apoptosis-inhibitory effect of Bcl-2 by enforcing mitochondrial permeability transition
    • Zamzami N, Marzo I, Susin SA, Brenner C, Larochette N, Marchetti P, Reed J, Kofler R, Kroemer G. The thiol crosslinking agent diamide overcomes the apoptosis-inhibitory effect of Bcl-2 by enforcing mitochondrial permeability transition. Oncogene 1998; 16: 1055-63.
    • (1998) Oncogene , vol.16 , pp. 1055-1063
    • Zamzami, N.1    Marzo, I.2    Susin, S.A.3    Brenner, C.4    Larochette, N.5    Marchetti, P.6    Reed, J.7    Kofler, R.8    Kroemer, G.9
  • 2
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita M, Shimizu S, Ito T, Chittenden T, Lutz RJ, Matsuda H, Tsujimoto Y. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proceedings Natl Acad Sci USA 1998; 95: 14681-6.
    • (1998) Proceedings Natl. Acad. Sci. USA , vol.95 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6    Tsujimoto, Y.7
  • 3
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 1996; 86: 147-57.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 6
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C, Fang M, Li Y, Li L, Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000; 102: 33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 7
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997; 91: 479-89.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 8
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H, Henzel WJ, Liu X, Lutschg A, Wang X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 1997; 90: 405-13.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 10
    • 0034665512 scopus 로고    scopus 로고
    • Immunosuppressant FTY720 induces apoptosis by direct induction of permeability transition and release of cytochrome c from mitochondria
    • Nagahara Y, Ikekita M, Shinomiya T. Immunosuppressant FTY720 induces apoptosis by direct induction of permeability transition and release of cytochrome c from mitochondria. J Immunol 2000; 165: 3250-9.
    • (2000) J. Immunol. , vol.165 , pp. 3250-3259
    • Nagahara, Y.1    Ikekita, M.2    Shinomiya, T.3
  • 11
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X, Budihardjo I, Zou H, Slaughter C, Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998; 94: 481-90.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 12
    • 0034074486 scopus 로고    scopus 로고
    • Protein kinases as mediators of phosphoinositide 3-kinase signaling
    • Toker A. Protein kinases as mediators of phosphoinositide 3-kinase signaling. Mol Pharmacol 2000; 57: 652-8.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 652-658
    • Toker, A.1
  • 14
    • 0034983918 scopus 로고    scopus 로고
    • Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase
    • Gottlob K, Majewski N, Kennedy S, Kandel E, Robey RB, Hay N. Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase. Genes Dev 2001; 15: 1406-18.
    • (2001) Genes Dev. , vol.15 , pp. 1406-1418
    • Gottlob, K.1    Majewski, N.2    Kennedy, S.3    Kandel, E.4    Robey, R.B.5    Hay, N.6
  • 15
    • 0036510541 scopus 로고    scopus 로고
    • Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis
    • Pastorino JG, Shulga N, Hoek JB. Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis. J Biol Chem 2002; 277: 7610-8.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7610-7618
    • Pastorino, J.G.1    Shulga, N.2    Hoek, J.B.3
  • 17
    • 0028855405 scopus 로고
    • Ceramide: An intracellular signal for apoptosis
    • Hannun YA, Obeid LM. Ceramide: an intracellular signal for apoptosis. Trends Biochem Sci 1995; 20: 73-7.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 73-77
    • Hannun, Y.A.1    Obeid, L.M.2
  • 18
    • 0034943309 scopus 로고    scopus 로고
    • Role of AKT kinase in sphingosine-induced apoptosis in human hepatoma cells
    • Chang HC, Tsai LH, Chuang LY, Hung WC. Role of AKT kinase in sphingosine-induced apoptosis in human hepatoma cells. J Cell Physiol 2001; 188: 188-93.
    • (2001) J. Cell Physiol. , vol.188 , pp. 188-193
    • Chang, H.C.1    Tsai, L.H.2    Chuang, L.Y.3    Hung, W.C.4
  • 20
    • 0037401894 scopus 로고    scopus 로고
    • Intracellular signal transduction pathways activated by ceramide and its metabolites
    • Ruvolo PP. Intracellular signal transduction pathways activated by ceramide and its metabolites. Pharmacol Res 2003; 47: 383-92.
    • (2003) Pharmacol. Res. , vol.47 , pp. 383-392
    • Ruvolo, P.P.1
  • 21
    • 0022974603 scopus 로고
    • Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets
    • Hannun YA, Loomis CR, Merrill AH Jr, Bell RM. Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets. J Biol Chem 1986; 261: 12604-9.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12604-12609
    • Hannun, Y.A.1    Loomis, C.R.2    Merrill Jr., A.H.3    Bell, R.M.4
  • 22
    • 0023014094 scopus 로고
    • Inhibition of phorbol ester-dependent differentiation of human promyelocytic leukemic (HL-60) cells by sphinganine and other long-chain bases
    • Merrill AH Jr, Sereni AM, Stevens VL, Hannun YA, Bell RM, Kinkade JM Jr. Inhibition of phorbol ester-dependent differentiation of human promyelocytic leukemic (HL-60) cells by sphinganine and other long-chain bases. J Biol Chem 1986; 261: 12610-5.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12610-12615
    • Merrill Jr., A.H.1    Sereni, A.M.2    Stevens, V.L.3    Hannun, Y.A.4    Bell, R.M.5    Kinkade Jr., J.M.6
  • 23
    • 0033555814 scopus 로고    scopus 로고
    • Sphingosine blocks human polymorphonuclear leukocyte phagocytosis through inhibition of mitogen-activated protein kinase activation
    • Raeder EM, Mansfield PJ, Hinkovska-Galcheva V, Kjeldsen L, Shayman JA, Boxer LA. Sphingosine blocks human polymorphonuclear leukocyte phagocytosis through inhibition of mitogen-activated protein kinase activation. Blood 1999; 93: 686-93.
    • (1999) Blood , vol.93 , pp. 686-693
    • Raeder, E.M.1    Mansfield, P.J.2    Hinkovska-Galcheva, V.3    Kjeldsen, L.4    Shayman, J.A.5    Boxer, L.A.6
  • 25
    • 0033558227 scopus 로고    scopus 로고
    • Activation of caspase-3-like proteases in apoptosis induced by sphingosine and other long-chain bases in Hep3B hepatoma cells
    • Hung WC, Chang HC, Chuang LY. Activation of caspase-3-like proteases in apoptosis induced by sphingosine and other long-chain bases in Hep3B hepatoma cells. Biochem J 1999; 338 (1): 161-6.
    • (1999) Biochem. J. , vol.338 , Issue.1 , pp. 161-166
    • Hung, W.C.1    Chang, H.C.2    Chuang, L.Y.3
  • 26
    • 0037739755 scopus 로고    scopus 로고
    • A novel immunosuppressive agent FFY720 induced Akt dephosphorylation in leukemia cells
    • Matsuoka Y, Nagahara Y, Ikekita M, Shinomiya T. A novel immunosuppressive agent FFY720 induced Akt dephosphorylation in leukemia cells. Br J Pharmacol 2003; 138: 1303-12.
    • (2003) Br. J. Pharmacol. , vol.138 , pp. 1303-1312
    • Matsuoka, Y.1    Nagahara, Y.2    Ikekita, M.3    Shinomiya, T.4
  • 27
    • 0035839556 scopus 로고    scopus 로고
    • Akt down-regulation of p38 signaling provides a novel mechanism of vascular endothelial growth factor-mediated cytoprotection in endothelial cells
    • Gratton JP, Morales-Ruiz M, Kureishi Y, Fulton D, Walsh K, Sessa WC. Akt down-regulation of p38 signaling provides a novel mechanism of vascular endothelial growth factor-mediated cytoprotection in endothelial cells. J Biol Chem 2001; 276: 30359-65.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30359-30365
    • Gratton, J.P.1    Morales-Ruiz, M.2    Kureishi, Y.3    Fulton, D.4    Walsh, K.5    Sessa, W.C.6
  • 28
    • 0037134431 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase (PI3K) -Akt pathway suppresses Bax translocation to mitochondria
    • Tsuruta F, Masuyama N, Gotoh Y. The phosphatidylinositol 3-kinase (PI3K) -Akt pathway suppresses Bax translocation to mitochondria. J Biol Chem 2002; 277: 14040-7.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14040-14047
    • Tsuruta, F.1    Masuyama, N.2    Gotoh, Y.3
  • 30
    • 0034708482 scopus 로고    scopus 로고
    • Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site
    • Toker A, Newton AC. Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site. J Biol Chem 2000; 275: 8271-4.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8271-8274
    • Toker, A.1    Newton, A.C.2
  • 33
    • 0033811659 scopus 로고    scopus 로고
    • Deficiency of PTEN in Jurkat T cells causes constitutive localization of Itk to the plasma membrane and hyperresponsiveness to CD3 stimulation
    • Shan X, Czar MJ, Bunnel SC, Liu P, Liu Y, Schwartzberg PL, Wange RL. Deficiency of PTEN in Jurkat T cells causes constitutive localization of Itk to the plasma membrane and hyperresponsiveness to CD3 stimulation. Mol Cell Biol 2000; 20: 6945-57.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 6945-6957
    • Shan, X.1    Czar, M.J.2    Bunnel, S.C.3    Liu, P.4    Liu, Y.5    Schwartzberg, P.L.6    Wange, R.L.7
  • 34
    • 10744222950 scopus 로고    scopus 로고
    • Suppression of extracellular signal-related kinase and activation of p38 MAPK are two critical events leading to caspase-8- and mitochondria-mediated cell death in phytosphingosine-treated human cancer cells
    • Park MT, Choi JA, Kim MJ, Um HD, Bae S, Kang CM, Cho CK, Kang S, Chung HY, Lee YS, Lee SJ. Suppression of extracellular signal-related kinase and activation of p38 MAPK are two critical events leading to caspase-8- and mitochondria-mediated cell death in phytosphingosine-treated human cancer cells. J Biol Chem 2003; 278: 50624-34.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50624-50634
    • Park, M.T.1    Choi, J.A.2    Kim, M.J.3    Um, H.D.4    Bae, S.5    Kang, C.M.6    Cho, C.K.7    Kang, S.8    Chung, H.Y.9    Lee, Y.S.10    Lee, S.J.11
  • 35
    • 3042549655 scopus 로고    scopus 로고
    • The phosphorylation status and antiapoptotic activity of Bcl-2 are regulated by ERK and protein phosphatase 2A on the mitochondria
    • Tamura Y, Simizu S, Osada H. The phosphorylation status and antiapoptotic activity of Bcl-2 are regulated by ERK and protein phosphatase 2A on the mitochondria. FEBS Lett 2004; 569: 249-55.
    • (2004) FEBS Lett. , vol.569 , pp. 249-255
    • Tamura, Y.1    Simizu, S.2    Osada, H.3
  • 36
    • 0031662853 scopus 로고    scopus 로고
    • Sphingolipid functions in Saccharomyces cerevisiae: Comparison to mammals
    • Dickson RC. Sphingolipid functions in Saccharomyces cerevisiae: comparison to mammals. Annu Rev Biochem 1998; 67 27-48.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 27-48
    • Dickson, R.C.1
  • 38
    • 0028217554 scopus 로고
    • In vivo distribution of free long-chain sphingoid bases in the human stratum corneum by high-performance liquid chromatographic analysis of strippings
    • Flamand N, Justine P, Bernaud F, Rougier A, Gaetani Q. In vivo distribution of free long-chain sphingoid bases in the human stratum corneum by high-performance liquid chromatographic analysis of strippings. J Chromatogr B Biomed Appl 1994; 656: 65-71.
    • (1994) J. Chromatogr. B Biomed. Appl. , vol.656 , pp. 65-71
    • Flamand, N.1    Justine, P.2    Bernaud, F.3    Rougier, A.4    Gaetani, Q.5
  • 39
    • 0032497277 scopus 로고    scopus 로고
    • Phytosphingosine biosynthesis differs from sphingosine in fish leukocytes and involves a transfer of methyl groups from [3H-methyl]methionine precursor
    • Bodennec J, Zwingelstein G, Koul O, Brichon G, Portoukalian J. Phytosphingosine biosynthesis differs from sphingosine in fish leukocytes and involves a transfer of methyl groups from [3H-methyl]methionine precursor. Biochem Biophys Res Commun 1998; 250: 88-93.
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 88-93
    • Bodennec, J.1    Zwingelstein, G.2    Koul, O.3    Brichon, G.4    Portoukalian, J.5


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