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Volumn 12, Issue 2, 2007, Pages 395-409

The marine sphingolipid-derived compound ES 285 triggers an atypical cell death pathway

Author keywords

Apoptosis; Marine derived compounds anti tumoral drugs; Sphingolipid derivatives

Indexed keywords

ES 285; MARCKS PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE B; PROTEIN KINASE C; SPHINGOLIPID; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 33846514589     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-006-0573-z     Document Type: Article
Times cited : (58)

References (62)
  • 1
    • 0036021010 scopus 로고    scopus 로고
    • Ecteinascidin 743: A novel anticancer drug with a unique mechanism of action
    • Aune GJ, Furuta T, Pommier Y (2002) Ecteinascidin 743: a novel anticancer drug with a unique mechanism of action. Anticancer Drugs 13:545-555
    • (2002) Anticancer Drugs , vol.13 , pp. 545-555
    • Aune, G.J.1    Furuta, T.2    Pommier, Y.3
  • 3
    • 0036738085 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate as a therapeutic agent
    • Spiegel S, Kolesnick R (2002) Sphingosine 1-phosphate as a therapeutic agent. Leukemia 16:1596-1602
    • (2002) Leukemia , vol.16 , pp. 1596-1602
    • Spiegel, S.1    Kolesnick, R.2
  • 4
    • 0037162061 scopus 로고    scopus 로고
    • Lipid phosphate phosphatases regulate signal transduction through glycerolipids and sphingolipids
    • Brindley DN, English D, Pilquil C, Buri K, Ling ZC (2002) Lipid phosphate phosphatases regulate signal transduction through glycerolipids and sphingolipids. Biochim Biophys Acta 1582:33-44
    • (2002) Biochim Biophys Acta , vol.1582 , pp. 33-44
    • Brindley, D.N.1    English, D.2    Pilquil, C.3    Buri, K.4    Ling, Z.C.5
  • 5
    • 0033604620 scopus 로고    scopus 로고
    • Bioactive lysophospholipids and their G protein-coupled receptors
    • Moolenaar WH (1999) Bioactive lysophospholipids and their G protein-coupled receptors. Exp Cell Res 253:230-238
    • (1999) Exp Cell Res , vol.253 , pp. 230-238
    • Moolenaar, W.H.1
  • 6
    • 0037162084 scopus 로고    scopus 로고
    • Structure-activity relationships of lysophosphatidic acid analogs
    • Lynch KR, Macdonald TL (2002) Structure-activity relationships of lysophosphatidic acid analogs. Biochim Biophys Acta 1582:289-294
    • (2002) Biochim Biophys Acta , vol.1582 , pp. 289-294
    • Lynch, K.R.1    Macdonald, T.L.2
  • 7
    • 0037201970 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate: Dual messenger functions
    • Payne SG, Milstien S, Spiegel S (2002) Sphingosine-1-phosphate: dual messenger functions. FEBS Lett 531:54-57
    • (2002) FEBS Lett , vol.531 , pp. 54-57
    • Payne, S.G.1    Milstien, S.2    Spiegel, S.3
  • 8
    • 0024428410 scopus 로고
    • Lysophosphatidate-induced cell proliferation: Identification and dissection of signaling pathways mediated by G proteins
    • van Corven EJ, Groenink A, Jalink K, Eichholtz T, Moolenaar WH (1989) Lysophosphatidate-induced cell proliferation: identification and dissection of signaling pathways mediated by G proteins. Cell 59:45-54
    • (1989) Cell , vol.59 , pp. 45-54
    • van Corven, E.J.1    Groenink, A.2    Jalink, K.3    Eichholtz, T.4    Moolenaar, W.H.5
  • 9
    • 0035895989 scopus 로고    scopus 로고
    • Lysophosphatidic acid-induced mitogenesis is regulated by lipid phosphate phosphatases and is Edg-receptor independent
    • Hooks SB, Santos WL, Im DS, Heise CE, Macdonald TL, Lynch KR (2001) Lysophosphatidic acid-induced mitogenesis is regulated by lipid phosphate phosphatases and is Edg-receptor independent. J Biol Chem 276:4611-4621
    • (2001) J Biol Chem , vol.276 , pp. 4611-4621
    • Hooks, S.B.1    Santos, W.L.2    Im, D.S.3    Heise, C.E.4    Macdonald, T.L.5    Lynch, K.R.6
  • 10
    • 0033609118 scopus 로고    scopus 로고
    • Schwann cell survival mediated by the signaling phospholipid lysophosphatidic acid
    • Weiner JA, Chun J (1999) Schwann cell survival mediated by the signaling phospholipid lysophosphatidic acid. Proc Natl Acad Sci USA 96:5233-5238
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5233-5238
    • Weiner, J.A.1    Chun, J.2
  • 11
    • 0033564744 scopus 로고    scopus 로고
    • Induction and suppression of endothelial cell apoptosis by sphingolipids: A possible in vitro model for cell-cell interactions between platelets and endothelial cells
    • Hisano N, Yatomi Y, Satoh K et al (1999) Induction and suppression of endothelial cell apoptosis by sphingolipids: a possible in vitro model for cell-cell interactions between platelets and endothelial cells. Blood 93:4293-4299
    • (1999) Blood , vol.93 , pp. 4293-4299
    • Hisano, N.1    Yatomi, Y.2    Satoh, K.3
  • 12
    • 0030049359 scopus 로고    scopus 로고
    • Lysophosphatidic acid-induced neurite retraction in PC12 cells: Neurite- protective effects of cyclic AMP signaling
    • Tigyi G, Fischer DJ, Sebok A, Marshall F, Dyer DL, Miledi R (1996) Lysophosphatidic acid-induced neurite retraction in PC12 cells: neurite- protective effects of cyclic AMP signaling. J Neurochem 66:549-558
    • (1996) J Neurochem , vol.66 , pp. 549-558
    • Tigyi, G.1    Fischer, D.J.2    Sebok, A.3    Marshall, F.4    Dyer, D.L.5    Miledi, R.6
  • 13
    • 0036318531 scopus 로고    scopus 로고
    • Fukushima N, Weiner JA, Kaushal Det al (2002) Lysophosphatidic acid influences the morphology and motility of young, postmitotic cortical neurons. Mol Cell Neurosci 20:271-282
    • Fukushima N, Weiner JA, Kaushal Det al (2002) Lysophosphatidic acid influences the morphology and motility of young, postmitotic cortical neurons. Mol Cell Neurosci 20:271-282
  • 14
    • 0000315614 scopus 로고    scopus 로고
    • Dissociation of LPA-induced cytoskeletal contraction from stress fiber formation by differential localization of RhoA
    • Kranenburg O, Poland M, Gebbink M, Oomen L, Moolenaar WH (1997) Dissociation of LPA-induced cytoskeletal contraction from stress fiber formation by differential localization of RhoA. J Cell Sci 110:2417-2427
    • (1997) J Cell Sci , vol.110 , pp. 2417-2427
    • Kranenburg, O.1    Poland, M.2    Gebbink, M.3    Oomen, L.4    Moolenaar, W.H.5
  • 15
    • 0033135378 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate stimulates fibronectin matrix assembly through a Rho-dependent signal pathway
    • Zhang Q, Peyruchaud O, French KJ, Magnusson MK, Mosher DF (1999) Sphingosine 1-phosphate stimulates fibronectin matrix assembly through a Rho-dependent signal pathway. Blood 93:2984-2990
    • (1999) Blood , vol.93 , pp. 2984-2990
    • Zhang, Q.1    Peyruchaud, O.2    French, K.J.3    Magnusson, M.K.4    Mosher, D.F.5
  • 16
    • 0030048805 scopus 로고    scopus 로고
    • Serum-induced membrane depolarization in quiescent fibroblasts: Activation of a chloride conductance through the G protein-coupled LPA receptor
    • Postma FR, Jalink K, Hengeveld T et al (1996) Serum-induced membrane depolarization in quiescent fibroblasts: activation of a chloride conductance through the G protein-coupled LPA receptor. Embo J 15:63-72
    • (1996) Embo J , vol.15 , pp. 63-72
    • Postma, F.R.1    Jalink, K.2    Hengeveld, T.3
  • 17
    • 0032577246 scopus 로고    scopus 로고
    • Selectivity of sphingosine-induced apoptosis. Lack of activity of DL- erythyrodihydrosphingosine
    • Sakakura C, Sweeney EA, Shirahama T et al (1998) Selectivity of sphingosine-induced apoptosis. Lack of activity of DL- erythyrodihydrosphingosine. Biochem Biophys Res Commun 246:827-830
    • (1998) Biochem Biophys Res Commun , vol.246 , pp. 827-830
    • Sakakura, C.1    Sweeney, E.A.2    Shirahama, T.3
  • 18
    • 0035233927 scopus 로고    scopus 로고
    • Modulation of protein kinase C in antitumor treatment
    • Hofmann J (2001) Modulation of protein kinase C in antitumor treatment. Rev Physiol Biochem Pharmacol 142:1-96
    • (2001) Rev Physiol Biochem Pharmacol , vol.142 , pp. 1-96
    • Hofmann, J.1
  • 19
    • 0031058595 scopus 로고    scopus 로고
    • Protein kinase C: A worthwhile target for anticancer drugs?
    • Caponigro F, French RC, Kaye SB (1997) Protein kinase C: a worthwhile target for anticancer drugs? Anticancer Drugs 8:26-33
    • (1997) Anticancer Drugs , vol.8 , pp. 26-33
    • Caponigro, F.1    French, R.C.2    Kaye, S.B.3
  • 20
    • 0027536464 scopus 로고
    • Protein kinase C: A novel target for inhibiting gastric cancer cell invasion
    • Schwartz GK, Jiang J, Kelsen D, Albino AP (1993) Protein kinase C: a novel target for inhibiting gastric cancer cell invasion. J Natl Cancer Inst 85:402-407
    • (1993) J Natl Cancer Inst , vol.85 , pp. 402-407
    • Schwartz, G.K.1    Jiang, J.2    Kelsen, D.3    Albino, A.P.4
  • 21
    • 0029564320 scopus 로고
    • Protein kinase C and skin tumor promotion
    • Marks F, Gschwendt M (1995) Protein kinase C and skin tumor promotion. Mutat Res 333:161-172
    • (1995) Mutat Res , vol.333 , pp. 161-172
    • Marks, F.1    Gschwendt, M.2
  • 22
    • 0036773777 scopus 로고    scopus 로고
    • Protein kinase C isotypes and their specific functions: Prologue
    • Ohno S, Nishizuka Y (2002) Protein kinase C isotypes and their specific functions: prologue. J Biochem (Tokyo) 132:509-511
    • (2002) J Biochem (Tokyo) , vol.132 , pp. 509-511
    • Ohno, S.1    Nishizuka, Y.2
  • 23
    • 0036856263 scopus 로고    scopus 로고
    • Protein kinase C gamma (PKC gamma): Function of neuron specific isotype
    • Saito N, Shirai Y (2002) Protein kinase C gamma (PKC gamma): function of neuron specific isotype. J Biochem (Tokyo) 132:683-687
    • (2002) J Biochem (Tokyo) , vol.132 , pp. 683-687
    • Saito, N.1    Shirai, Y.2
  • 24
    • 0036855463 scopus 로고    scopus 로고
    • Protein kinase C alpha (PKC alpha): Regulation and biological function
    • Nakashima S (2002) Protein kinase C alpha (PKC alpha): regulation and biological function. J Biochem (Tokyo) 132:669-675
    • (2002) J Biochem (Tokyo) , vol.132 , pp. 669-675
    • Nakashima, S.1
  • 25
    • 0036177115 scopus 로고    scopus 로고
    • Targeting protein kinase C: New therapeutic opportunities against high-grade malignant gliomas?
    • da Rocha AB, Mans DR, Regner A, Schwartsmann G (2002) Targeting protein kinase C: new therapeutic opportunities against high-grade malignant gliomas? Oncologist 7:17-33
    • (2002) Oncologist , vol.7 , pp. 17-33
    • da Rocha, A.B.1    Mans, D.R.2    Regner, A.3    Schwartsmann, G.4
  • 26
    • 0036905264 scopus 로고    scopus 로고
    • Move over protein kinase C, you've got company: Alternative cellular effectors of diacylglycerol and phorbol esters
    • Brose N, Rosenmund C (2002) Move over protein kinase C, you've got company: alternative cellular effectors of diacylglycerol and phorbol esters. J Cell Sci 115:4399-4411
    • (2002) J Cell Sci , vol.115 , pp. 4399-4411
    • Brose, N.1    Rosenmund, C.2
  • 27
    • 0031984081 scopus 로고    scopus 로고
    • The role of protein kinase C in G1 and G2/M phases of the cell cycle (review)
    • Fishman DD, Segal S, Livneh E (1998) The role of protein kinase C in G1 and G2/M phases of the cell cycle (review). Int J Oncol 12:181-186
    • (1998) Int J Oncol , vol.12 , pp. 181-186
    • Fishman, D.D.1    Segal, S.2    Livneh, E.3
  • 28
    • 0037246123 scopus 로고    scopus 로고
    • Regulation of cell apoptosis by protein kinase c delta
    • Brodie C, Blumberg PM (2003) Regulation of cell apoptosis by protein kinase c delta. Apoptosis 8:19-27
    • (2003) Apoptosis , vol.8 , pp. 19-27
    • Brodie, C.1    Blumberg, P.M.2
  • 29
    • 0344114246 scopus 로고
    • Specificity and mechanism of protein kinase C activation by sn-1,2-diacylglycerols
    • Ganong BR, Loomis CR, Hannun YA, Bell RM (1986) Specificity and mechanism of protein kinase C activation by sn-1,2-diacylglycerols. Proc Natl Acad Sci USA 83:1184-1188
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 1184-1188
    • Ganong, B.R.1    Loomis, C.R.2    Hannun, Y.A.3    Bell, R.M.4
  • 30
    • 0036560847 scopus 로고    scopus 로고
    • Diacylglycerol kinases: Emerging downstream regulators in cell signaling systems
    • Kanoh H, Yamada K, Sakane F (2002) Diacylglycerol kinases: emerging downstream regulators in cell signaling systems. J Biochem (Tokyo) 131:629-633
    • (2002) J Biochem (Tokyo) , vol.131 , pp. 629-633
    • Kanoh, H.1    Yamada, K.2    Sakane, F.3
  • 31
    • 0032849088 scopus 로고    scopus 로고
    • New insights into the regulation of protein kinase C and novel phorbol ester receptors
    • Ron D, Kazanietz MG (1999) New insights into the regulation of protein kinase C and novel phorbol ester receptors. Faseb J 13:1658-1676
    • (1999) Faseb J , vol.13 , pp. 1658-1676
    • Ron, D.1    Kazanietz, M.G.2
  • 32
    • 0034713935 scopus 로고    scopus 로고
    • Importance of protein kinase C targeting for the phosphorylation of its substrate, myristoylated alanine-rich C-kinase substrate
    • Ohmori S, Sakai N, Shirai Y et al (2000) Importance of protein kinase C targeting for the phosphorylation of its substrate, myristoylated alanine-rich C-kinase substrate. J Biol Chem 275:26449-26457
    • (2000) J Biol Chem , vol.275 , pp. 26449-26457
    • Ohmori, S.1    Sakai, N.2    Shirai, Y.3
  • 33
    • 0023025483 scopus 로고
    • Phorbol ester binding and activation of protein kinase C on triton X-100 mixed micelles containing phosphatidylserine
    • Hannun YA, Bell RM (1986) Phorbol ester binding and activation of protein kinase C on triton X-100 mixed micelles containing phosphatidylserine. J Biol Chem 261:9341-9347
    • (1986) J Biol Chem , vol.261 , pp. 9341-9347
    • Hannun, Y.A.1    Bell, R.M.2
  • 34
    • 0020645583 scopus 로고
    • 2+-dependent protein phosphorylation system in various types of leukemic cells from human patients and in human leukemic cell lines HL60 and K562, and its inhibition by alkyl-lysophospholipid
    • 2+-dependent protein phosphorylation system in various types of leukemic cells from human patients and in human leukemic cell lines HL60 and K562, and its inhibition by alkyl-lysophospholipid. Cancer Res 43:2955-2961
    • (1983) Cancer Res , vol.43 , pp. 2955-2961
    • Helfman, D.M.1    Barnes, K.C.2    Kinkade Jr, J.M.3    Vogler, W.R.4    Shoji, M.5    Kuo, J.F.6
  • 35
    • 0022273858 scopus 로고
    • 2+-dependent protein kinase and phosphorylation of leukemic cell proteins by CP-46,665-1, a novel antineoplastic lipoidal amine
    • 2+-dependent protein kinase and phosphorylation of leukemic cell proteins by CP-46,665-1, a novel antineoplastic lipoidal amine. Biochem Biophys Res Commun 127:590-595
    • (1985) Biochem Biophys Res Commun , vol.127 , pp. 590-595
    • Shoji, M.1    Vogler, W.R.2    Kuo, J.F.3
  • 36
    • 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 (1986) Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets. J Biol Chem 261:12604-12609
    • (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
  • 37
    • 0028818393 scopus 로고
    • Partial inhibition of multidrug resistance by safingol is independent of modulation of P-glycoprotein substrate activities and correlated with inhibition of protein kinase C
    • Sachs CW, Safa AR, Harrison SD, Fine RL (1995) Partial inhibition of multidrug resistance by safingol is independent of modulation of P-glycoprotein substrate activities and correlated with inhibition of protein kinase C. J Biol Chem 270:26639-26648
    • (1995) J Biol Chem , vol.270 , pp. 26639-26648
    • Sachs, C.W.1    Safa, A.R.2    Harrison, S.D.3    Fine, R.L.4
  • 38
    • 0027510002 scopus 로고
    • Inhibitors of protein kinase C. 3. Potent and highly selective bisindolylmaleimides by conformational restriction
    • Bit RA, Davis PD, Elliott LH et al (1993) Inhibitors of protein kinase C. 3. Potent and highly selective bisindolylmaleimides by conformational restriction. J Med Chem 36:21-29
    • (1993) J Med Chem , vol.36 , pp. 21-29
    • Bit, R.A.1    Davis, P.D.2    Elliott, L.H.3
  • 39
    • 0025942516 scopus 로고
    • The bisindolylmaleimide GF 109203X is a potent and selective inhibitor of protein kinase C
    • Toullec D, Pianetti P, Coste H et al (1991) The bisindolylmaleimide GF 109203X is a potent and selective inhibitor of protein kinase C. J Biol Chem 266:15771-15781
    • (1991) J Biol Chem , vol.266 , pp. 15771-15781
    • Toullec, D.1    Pianetti, P.2    Coste, H.3
  • 40
    • 0036738085 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate as a therapeutic agent
    • Spiegel S, Kolesnick R (2002) Sphingosine 1-phosphate as a therapeutic agent. Leukemia 16:1596-1602
    • (2002) Leukemia , vol.16 , pp. 1596-1602
    • Spiegel, S.1    Kolesnick, R.2
  • 41
    • 0037162061 scopus 로고    scopus 로고
    • Lipid phosphate phosphatases regulate signal transduction through glycerolipids and sphingolipids
    • Brindley DN, English D, Pilquil C, Buri K, Ling ZC (2002) Lipid phosphate phosphatases regulate signal transduction through glycerolipids and sphingolipids. Biochim Biophys Acta 1582:33-44
    • (2002) Biochim Biophys Acta , vol.1582 , pp. 33-44
    • Brindley, D.N.1    English, D.2    Pilquil, C.3    Buri, K.4    Ling, Z.C.5
  • 42
    • 0035210589 scopus 로고    scopus 로고
    • Selective ligands for lysophosphatidic acid receptor subtypes: Gaining control over the endothelial differentiation gene family
    • Tigyi G (2001) Selective ligands for lysophosphatidic acid receptor subtypes: gaining control over the endothelial differentiation gene family. Mol Pharmacol 60:1161-1164
    • (2001) Mol Pharmacol , vol.60 , pp. 1161-1164
    • Tigyi, G.1
  • 43
  • 44
    • 0026472164 scopus 로고
    • The MARCKS brothers: A family of protein kinase C substrates
    • Aderem A (1992) The MARCKS brothers: a family of protein kinase C substrates. Cell 71:713-716
    • (1992) Cell , vol.71 , pp. 713-716
    • Aderem, A.1
  • 45
    • 0027392102 scopus 로고
    • The MARCKS family of cellular protein kinase C substrates
    • Blackshear PJ (1993) The MARCKS family of cellular protein kinase C substrates. J Biol Chem 268:1501-1504
    • (1993) J Biol Chem , vol.268 , pp. 1501-1504
    • Blackshear, P.J.1
  • 46
    • 0026073476 scopus 로고
    • Effects of protein kinase C activators and inhibitors on membrane properties, synaptic responses, and cholinergic actions in CA1 subfield of rat hippocampus in situ and in vitro
    • Agopyan N, Agopyan I (1991) Effects of protein kinase C activators and inhibitors on membrane properties, synaptic responses, and cholinergic actions in CA1 subfield of rat hippocampus in situ and in vitro. Synapse 7:193-206
    • (1991) Synapse , vol.7 , pp. 193-206
    • Agopyan, N.1    Agopyan, I.2
  • 47
    • 0035023432 scopus 로고    scopus 로고
    • Pleiotypic mechanisms of cellular responses to biologically active lysophospholipids
    • Goetzl EJ (2001) Pleiotypic mechanisms of cellular responses to biologically active lysophospholipids. Prostaglandins 64:11-20
    • (2001) Prostaglandins , vol.64 , pp. 11-20
    • Goetzl, E.J.1
  • 49
    • 0036209077 scopus 로고    scopus 로고
    • Novel "nonkinase" phorbol ester receptors: The C1 domain connection
    • Kazanietz MG (2002) Novel "nonkinase" phorbol ester receptors: the C1 domain connection. Mol Pharmacol 61:759-767
    • (2002) Mol Pharmacol , vol.61 , pp. 759-767
    • Kazanietz, M.G.1
  • 50
    • 0034930391 scopus 로고    scopus 로고
    • Signaling pathways and effector mechanisms pre-programmed cell death
    • Blatt NB, Glick GD (2001) Signaling pathways and effector mechanisms pre-programmed cell death. Bioorg Med Chem 9:1371-1384
    • (2001) Bioorg Med Chem , vol.9 , pp. 1371-1384
    • Blatt, N.B.1    Glick, G.D.2
  • 51
    • 0035525733 scopus 로고    scopus 로고
    • Cellular stress response and apoptosis in cancer therapy
    • Herr I, Debatin KM (2001) Cellular stress response and apoptosis in cancer therapy. Blood 98:2603-2614
    • (2001) Blood , vol.98 , pp. 2603-2614
    • Herr, I.1    Debatin, K.M.2
  • 52
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta SR, Dudek H, Tao X et al (1997) Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91:231-241
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3
  • 53
    • 0031053586 scopus 로고    scopus 로고
    • Dudek H, Datta SR, Franke TF et al (1997) Regulation of neuronal survival by the serine-threonine protein kinase Akt. Science 275:661-665
    • Dudek H, Datta SR, Franke TF et al (1997) Regulation of neuronal survival by the serine-threonine protein kinase Akt. Science 275:661-665
  • 55
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • Earnshaw WC, Martins LM, Kaufmann SH (1999) Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu Rev Biochem 68:383-424
    • (1999) Annu Rev Biochem , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 57
    • 0023635624 scopus 로고    scopus 로고
    • Wilson E, Rice WG, Kinkade JM, Jr., Merrill AH, Jr., Arnold RR, Lambeth JD (1987) Protein kinase C inhibition by sphingoid long-chain bases: effects on secretion in human neutrophils. Arch Biochem Biophys 259:204-214
    • Wilson E, Rice WG, Kinkade JM, Jr., Merrill AH, Jr., Arnold RR, Lambeth JD (1987) Protein kinase C inhibition by sphingoid long-chain bases: effects on secretion in human neutrophils. Arch Biochem Biophys 259:204-214
  • 58
    • 1842843860 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program
    • Rao RV, Ellerby HM, Bredesen DE (2004) Coupling endoplasmic reticulum stress to the cell death program. Cell Death Differ 11:372-380
    • (2004) Cell Death Differ , vol.11 , pp. 372-380
    • Rao, R.V.1    Ellerby, H.M.2    Bredesen, D.E.3
  • 59
    • 1342305497 scopus 로고    scopus 로고
    • Caspase-12 and ER-stress-mediated apoptosis: The story so far
    • Szegezdi E, Fitzgerald U, Samali A (2003) Caspase-12 and ER-stress-mediated apoptosis: the story so far. Ann NY Acad Sci 1010:186-194
    • (2003) Ann NY Acad Sci , vol.1010 , pp. 186-194
    • Szegezdi, E.1    Fitzgerald, U.2    Samali, A.3
  • 60
    • 1242269804 scopus 로고    scopus 로고
    • Apoptosis induced by endoplasmic reticulum stress depends on activation of caspase-3 via caspase-12
    • Hitomi J, Katayama T, Taniguchi M, Honda A, Imaizumi K, Tohyama M (2004) Apoptosis induced by endoplasmic reticulum stress depends on activation of caspase-3 via caspase-12. Neurosci Lett 357:127-130
    • (2004) Neurosci Lett , vol.357 , pp. 127-130
    • Hitomi, J.1    Katayama, T.2    Taniguchi, M.3    Honda, A.4    Imaizumi, K.5    Tohyama, M.6
  • 61
    • 0037314856 scopus 로고    scopus 로고
    • Phytosphingosine induces apoptotic cell death via caspase 8 activation and Bax translocation in human cancer cells
    • Park MT, Kang JA, Choi JA et al (2003) Phytosphingosine induces apoptotic cell death via caspase 8 activation and Bax translocation in human cancer cells. Clin Cancer Res 9:878-885
    • (2003) Clin Cancer Res , vol.9 , pp. 878-885
    • Park, M.T.1    Kang, J.A.2    Choi, J.A.3
  • 62
    • 6944241423 scopus 로고    scopus 로고
    • Sphingosine-dependent apoptosis: A unified concept based on multiple mechanisms operating in concert
    • Suzuki E, Handa K, Toledo MS, Hakomori S (2004) Sphingosine-dependent apoptosis: a unified concept based on multiple mechanisms operating in concert. Proc Natl Acad Sci USA 101:14788-14793
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14788-14793
    • Suzuki, E.1    Handa, K.2    Toledo, M.S.3    Hakomori, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.