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Volumn 6, Issue 10, 2011, Pages

β-lapachone significantly increases the effect of ionizing radiation to cause mitochondrial apoptosis via JNK activation in cancer cells

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS INDUCING FACTOR; BETA LAPACHONE; CASPASE 3; CASPASE 8; CASPASE 9; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN BAX; REACTIVE OXYGEN METABOLITE; STRESS ACTIVATED PROTEIN KINASE; AIFM1 PROTEIN, HUMAN; ANTINEOPLASTIC AGENT; BETA-LAPACHONE; NAPHTHOQUINONE; NQO1 PROTEIN, HUMAN; RADIOSENSITIZING AGENT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE);

EID: 80053590637     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025976     Document Type: Article
Times cited : (33)

References (56)
  • 1
    • 0034009970 scopus 로고    scopus 로고
    • NAD(P)H:quinone oxidoreductase activity is the principal determinant of beta-lapachone cytotoxicity
    • Pink JJ, Planchon SM, Tagliarino C, Varnes ME, Siegel D, et al. (2000) NAD(P)H:quinone oxidoreductase activity is the principal determinant of beta-lapachone cytotoxicity. J Biol Chem 275: 5416-5424.
    • (2000) J Biol Chem , vol.275 , pp. 5416-5424
    • Pink, J.J.1    Planchon, S.M.2    Tagliarino, C.3    Varnes, M.E.4    Siegel, D.5
  • 2
    • 0034653956 scopus 로고    scopus 로고
    • Activation of cysteine protease in MCF-7 and T47D breast cancer cells during β-lapachone mediated apoptosis
    • Pink JJ, Wuerzberger-Davis S, Tagliarino C, Planchon SM, Yang X, et al. (2000) Activation of cysteine protease in MCF-7 and T47D breast cancer cells during β-lapachone mediated apoptosis. Exp Cell Res 255: 144-155.
    • (2000) Exp Cell Res , vol.255 , pp. 144-155
    • Pink, J.J.1    Wuerzberger-Davis, S.2    Tagliarino, C.3    Planchon, S.M.4    Yang, X.5
  • 3
    • 19944393198 scopus 로고    scopus 로고
    • Susceptibility of cancer cells to β-lapachone is enhanced by ionizing radiation
    • Park HJ, Ahn KJ, Ahn SD, Choi E, Lee SW, et al. (2005) Susceptibility of cancer cells to β-lapachone is enhanced by ionizing radiation. Int J Radiat Oncol Biol Phys 61: 212-219.
    • (2005) Int J Radiat Oncol Biol Phys , vol.61 , pp. 212-219
    • Park, H.J.1    Ahn, K.J.2    Ahn, S.D.3    Choi, E.4    Lee, S.W.5
  • 4
    • 0024532122 scopus 로고
    • Inhibition of potentially lethal DNA damage repair in human tumor cells by beta-lapachone, an activator of topoisomerase 1
    • Boothman DA, Trask DK, Pardee AB, (1989) Inhibition of potentially lethal DNA damage repair in human tumor cells by beta-lapachone, an activator of topoisomerase 1. Cancer Res 49: 605-612.
    • (1989) Cancer Res , vol.49 , pp. 605-612
    • Boothman, D.A.1    Trask, D.K.2    Pardee, A.B.3
  • 6
    • 0030828019 scopus 로고    scopus 로고
    • Cooperative interception of neuronal apoptosis by BCL-2 and BAG-1 expression: prevention of caspase activation and reduced production of reactive oxygen species
    • Schulz JB, Bremen D, Reed JC, Lommatzsch J, Takayama S, et al. (1997) Cooperative interception of neuronal apoptosis by BCL-2 and BAG-1 expression: prevention of caspase activation and reduced production of reactive oxygen species. J Neurochem 69: 2075-2086.
    • (1997) J Neurochem , vol.69 , pp. 2075-2086
    • Schulz, J.B.1    Bremen, D.2    Reed, J.C.3    Lommatzsch, J.4    Takayama, S.5
  • 7
    • 13544276189 scopus 로고    scopus 로고
    • Phytosphingosine in combination with ionizing radiation enhances apoptotic cell death in radiation-resistant cancer cells through ROS-dependent and -independent AIF release
    • Park MT, Kim MJ, Kang YH, Choi SY, Lee JH, et al. (2005) Phytosphingosine in combination with ionizing radiation enhances apoptotic cell death in radiation-resistant cancer cells through ROS-dependent and-independent AIF release. Blood 105: 1724-1733.
    • (2005) Blood , vol.105 , pp. 1724-1733
    • Park, M.T.1    Kim, M.J.2    Kang, Y.H.3    Choi, S.Y.4    Lee, J.H.5
  • 8
    • 10844264632 scopus 로고    scopus 로고
    • Caspase-independent cell death by arsenic trioxide in human cervical cancer cells: reactive oxygen species-mediated poly(ADP-ribose) polymerase-1 activation signals apoptosis-inducing factor release from mitochondria
    • Kang YH, Yi MJ, Kim MJ, Park MT, Bae S, et al. (2004) Caspase-independent cell death by arsenic trioxide in human cervical cancer cells: reactive oxygen species-mediated poly(ADP-ribose) polymerase-1 activation signals apoptosis-inducing factor release from mitochondria. Cancer Res 64: 8960-8967.
    • (2004) Cancer Res , vol.64 , pp. 8960-8967
    • Kang, Y.H.1    Yi, M.J.2    Kim, M.J.3    Park, M.T.4    Bae, S.5
  • 10
    • 0035900676 scopus 로고    scopus 로고
    • Reactive oxygen species are downstream products of TRAF-mediated signal transduction
    • Chandel NS, Schumacker PT, Arch RH, (2001) Reactive oxygen species are downstream products of TRAF-mediated signal transduction. J Biol Chem 276: 42728-42736.
    • (2001) J Biol Chem , vol.276 , pp. 42728-42736
    • Chandel, N.S.1    Schumacker, P.T.2    Arch, R.H.3
  • 11
    • 58149140268 scopus 로고    scopus 로고
    • Involvement of endoplasmic reticulum stress and activation of MAP kinases in beta-lapachone-induced human prostate cancer cell apoptosis
    • Lien YC, Kung HN, Lu KS, Jeng CJ, Chau YP, (2008) Involvement of endoplasmic reticulum stress and activation of MAP kinases in beta-lapachone-induced human prostate cancer cell apoptosis. Histol Histopathol 23: 1299-1308.
    • (2008) Histol Histopathol , vol.23 , pp. 1299-1308
    • Lien, Y.C.1    Kung, H.N.2    Lu, K.S.3    Jeng, C.J.4    Chau, Y.P.5
  • 12
    • 0033635733 scopus 로고    scopus 로고
    • BH3-Only proteins-essential initiators of apoptotic cell death
    • Huang DC, Strasser A, (2000) BH3-Only proteins-essential initiators of apoptotic cell death. Cell 103: 839-842.
    • (2000) Cell , vol.103 , pp. 839-842
    • Huang, D.C.1    Strasser, A.2
  • 13
    • 0036258111 scopus 로고    scopus 로고
    • The IARC TP53 database: new online mutation analysis and recommendations to users
    • Olivier M, Eeles R, Hollstein M, Khan MA, Harris CC, et al. (2002) The IARC TP53 database: new online mutation analysis and recommendations to users. Hum Mutat 19: 607-614.
    • (2002) Hum Mutat , vol.19 , pp. 607-614
    • Olivier, M.1    Eeles, R.2    Hollstein, M.3    Khan, M.A.4    Harris, C.C.5
  • 14
    • 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, et al. (2003) 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 278: 50624-50634.
    • (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
  • 15
    • 0037469097 scopus 로고    scopus 로고
    • Calpain-induced Bax-cleavage product is a more potent inducer of apoptotic cell death than wild-type Bax
    • Toyota H, Yanase N, Yoshimoto T, Moriyama M, Sudo T, et al. (2003) Calpain-induced Bax-cleavage product is a more potent inducer of apoptotic cell death than wild-type Bax. Cancer Lett 189: 221-230.
    • (2003) Cancer Lett , vol.189 , pp. 221-230
    • Toyota, H.1    Yanase, N.2    Yoshimoto, T.3    Moriyama, M.4    Sudo, T.5
  • 16
    • 33644998898 scopus 로고    scopus 로고
    • Gefitinib, a selective EGFR tyrosine kinase inhibitor, induces apoptosis through activation of Bax in human gallbladder adenocarcinoma cells
    • Ariyama H, Qin B, Baba E, Tanaka R, Mitsugi K, et al. (2006) Gefitinib, a selective EGFR tyrosine kinase inhibitor, induces apoptosis through activation of Bax in human gallbladder adenocarcinoma cells. J Cell Biochem 97: 724-734.
    • (2006) J Cell Biochem , vol.97 , pp. 724-734
    • Ariyama, H.1    Qin, B.2    Baba, E.3    Tanaka, R.4    Mitsugi, K.5
  • 17
    • 0141481980 scopus 로고    scopus 로고
    • Cleavage of Bax to p18 Bax accelerates stress-induced apoptosis, and a cathepsin-like protease may rapidly degrade p18 Bax
    • Cao X, Deng X, May WS, (2003) Cleavage of Bax to p18 Bax accelerates stress-induced apoptosis, and a cathepsin-like protease may rapidly degrade p18 Bax. Blood 102: 2605-2614.
    • (2003) Blood , vol.102 , pp. 2605-2614
    • Cao, X.1    Deng, X.2    May, W.S.3
  • 18
    • 34548206759 scopus 로고    scopus 로고
    • Upregulation of NAD(P)H:Quinone Oxidoreductase By Radiation Potentiates the Effect of Bioreductive β-Lapachone on Cancer Cells
    • Choi EK, Terai K, Ji IM, Kook YH, Park KH, et al. (2007) Upregulation of NAD(P)H:Quinone Oxidoreductase By Radiation Potentiates the Effect of Bioreductive β-Lapachone on Cancer Cells. Neoplasia 9: 634-642.
    • (2007) Neoplasia , vol.9 , pp. 634-642
    • Choi, E.K.1    Terai, K.2    Ji, I.M.3    Kook, Y.H.4    Park, K.H.5
  • 19
    • 0033539487 scopus 로고    scopus 로고
    • Potent inhibition of tumor survival in vivo by beta-lapachone plus Taxol: Combining drugs imposes different artificial checkpoints
    • Li CJ, Li YZ, Pinto AV, Pardee AB, (1999) Potent inhibition of tumor survival in vivo by beta-lapachone plus Taxol: Combining drugs imposes different artificial checkpoints. Proc Natl Acad Sci USA 96: 13369-13374.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13369-13374
    • Li, C.J.1    Li, Y.Z.2    Pinto, A.V.3    Pardee, A.B.4
  • 20
    • 0021347851 scopus 로고
    • Beta-lapachone greatly enhances MMS lethality to human fibroblasts
    • Boorstein RJ, Pardee AB, (1984) Beta-lapachone greatly enhances MMS lethality to human fibroblasts. Biochem Biophys Res Commun 47: 828-834.
    • (1984) Biochem Biophys Res Commun , vol.47 , pp. 828-834
    • Boorstein, R.J.1    Pardee, A.B.2
  • 21
    • 0036109069 scopus 로고    scopus 로고
    • Chemosensitivity of human prostate cancer cells PC3 and LNCaP to genistein isoflavone and beta-lapachone
    • Kumi-Diaka J, (2002) Chemosensitivity of human prostate cancer cells PC3 and LNCaP to genistein isoflavone and beta-lapachone. Biol Cell 94: 37-44.
    • (2002) Biol Cell , vol.94 , pp. 37-44
    • Kumi-Diaka, J.1
  • 22
    • 73349107095 scopus 로고    scopus 로고
    • Cisplatin enhances the anticancer effect of beta-lapachone by upregulating NQO1
    • Terai K, Dong GZ, Oh ET, Park MT, Gu Y, et al. (2009) Cisplatin enhances the anticancer effect of beta-lapachone by upregulating NQO1. Anticancer Drugs 20: 901-909.
    • (2009) Anticancer Drugs , vol.20 , pp. 901-909
    • Terai, K.1    Dong, G.Z.2    Oh, E.T.3    Park, M.T.4    Gu, Y.5
  • 23
    • 78049311247 scopus 로고    scopus 로고
    • Prostate cancer radiosensitization through poly (ADP-Ribose) polymerase-1 hyperactivation
    • Dong Y, Bey EA, Li LS, Kabbani W, Yan J, et al. (2010) Prostate cancer radiosensitization through poly (ADP-Ribose) polymerase-1 hyperactivation. Cancer Res 70: 8088-8096.
    • (2010) Cancer Res , vol.70 , pp. 8088-8096
    • Dong, Y.1    Bey, E.A.2    Li, L.S.3    Kabbani, W.4    Yan, J.5
  • 24
    • 0035969989 scopus 로고    scopus 로고
    • Regulation of p53 stability and p53-dependent apoptosis by NADH quinine oxidoreductase 1
    • Asher G, Lotem J, Cohen B, Sachs L, Shaul Y, (2001) Regulation of p53 stability and p53-dependent apoptosis by NADH quinine oxidoreductase 1. Proc Natl Acad Sci USA 98: 1188-1193.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1188-1193
    • Asher, G.1    Lotem, J.2    Cohen, B.3    Sachs, L.4    Shaul, Y.5
  • 25
    • 5444240961 scopus 로고    scopus 로고
    • Contribution of NAD(P)H:quinone oxidoreductase 1 to protection against carcinogenesis, and regulation of its gene by the Nrf2 basic-region leucine zipper and the arylhydrocarbon receptor basic helix-loop-helix transcription factors
    • Nioi P, Hayes JD, (2004) Contribution of NAD(P)H:quinone oxidoreductase 1 to protection against carcinogenesis, and regulation of its gene by the Nrf2 basic-region leucine zipper and the arylhydrocarbon receptor basic helix-loop-helix transcription factors. Mutat Res 555: 149-171.
    • (2004) Mutat Res , vol.555 , pp. 149-171
    • Nioi, P.1    Hayes, J.D.2
  • 28
  • 29
    • 0035943598 scopus 로고    scopus 로고
    • Specific residues within the alpha 2 integrin subunit cytoplasmic domain regulate migration and cell cycle progression via distinct MAPK pathways
    • Klekotka PA, Santoro SA, Wang H, Zutter MM, (2001) Specific residues within the alpha 2 integrin subunit cytoplasmic domain regulate migration and cell cycle progression via distinct MAPK pathways. J Biol Chem 276: 32353-32361.
    • (2001) J Biol Chem , vol.276 , pp. 32353-32361
    • Klekotka, P.A.1    Santoro, S.A.2    Wang, H.3    Zutter, M.M.4
  • 30
    • 2342562556 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases in apoptosis regulation
    • Wada T, Penninger JM, (2004) Mitogen-activated protein kinases in apoptosis regulation. Oncogene 23: 2838-2849.
    • (2004) Oncogene , vol.23 , pp. 2838-2849
    • Wada, T.1    Penninger, J.M.2
  • 31
    • 0033730196 scopus 로고    scopus 로고
    • Sequential activation of ERK and repression of JNK by scatter factor/hepatocyte growth factor in madin-darby canine kidney epithelial cells
    • Paumelle R, Tulasne D, Leroy C, Coll J, Vandenbunder B, et al. (2000) Sequential activation of ERK and repression of JNK by scatter factor/hepatocyte growth factor in madin-darby canine kidney epithelial cells. Mol Biol Cell 11: 3751-3763.
    • (2000) Mol Biol Cell , vol.11 , pp. 3751-3763
    • Paumelle, R.1    Tulasne, D.2    Leroy, C.3    Coll, J.4    Vandenbunder, B.5
  • 32
    • 0042355729 scopus 로고    scopus 로고
    • Activation of ERK induces phosphorylation of MAPK phosphatase-7, a JNK specific phosphatase, at Ser-446
    • Masuda K, Shima H, Katagiri C, Kikuchi K, (2003) Activation of ERK induces phosphorylation of MAPK phosphatase-7, a JNK specific phosphatase, at Ser-446. J Biol Chem 278: 32448-32456.
    • (2003) J Biol Chem , vol.278 , pp. 32448-32456
    • Masuda, K.1    Shima, H.2    Katagiri, C.3    Kikuchi, K.4
  • 33
    • 17644397417 scopus 로고    scopus 로고
    • Phosphorylation of Ser-446 determines stability of MKP-7
    • Katagiri C, Masuda K, Urano T, Yamashita K, Araki Y, et al. (2005) Phosphorylation of Ser-446 determines stability of MKP-7. J Biol Chem 280: 14716-14722.
    • (2005) J Biol Chem , vol.280 , pp. 14716-14722
    • Katagiri, C.1    Masuda, K.2    Urano, T.3    Yamashita, K.4    Araki, Y.5
  • 34
    • 73649089980 scopus 로고    scopus 로고
    • ERK and cell death: mechanisms of ERK-induced cell death-apoptosis, autophagy and senescence
    • Cagnol S, Chambard JC, (2010) ERK and cell death: mechanisms of ERK-induced cell death-apoptosis, autophagy and senescence. FEBS J 277: 2-21.
    • (2010) FEBS J , vol.277 , pp. 2-21
    • Cagnol, S.1    Chambard, J.C.2
  • 35
    • 0035065836 scopus 로고    scopus 로고
    • ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis
    • Tobiume K, Matsuzawa A, Takahashi T, Nishitoh H, Morita K, et al. (2001) ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis. EMBO Rep 2: 222-228.
    • (2001) EMBO Rep , vol.2 , pp. 222-228
    • Tobiume, K.1    Matsuzawa, A.2    Takahashi, T.3    Nishitoh, H.4    Morita, K.5
  • 36
    • 2242445273 scopus 로고    scopus 로고
    • Role of glutaredoxin in metabolic oxidative stress. Glutaredoxin as a sensor of oxidative stress mediated by H2 O2
    • Song JJ, Rhee JG, Suntharalingam M, Walsh SA, Spitz DR, et al. (2002) Role of glutaredoxin in metabolic oxidative stress. Glutaredoxin as a sensor of oxidative stress mediated by H2 O2. J Biol Chem 277: 46566-46575.
    • (2002) J Biol Chem , vol.277 , pp. 46566-46575
    • Song, J.J.1    Rhee, J.G.2    Suntharalingam, M.3    Walsh, S.A.4    Spitz, D.R.5
  • 37
    • 77949699981 scopus 로고    scopus 로고
    • Roles of NADPH oxidases in cisplatin-induced reactive oxygen species generation and ototoxicity
    • Kim HJ, Lee JH, Kim SJ, Oh GS, Moon HD, et al. (2010) Roles of NADPH oxidases in cisplatin-induced reactive oxygen species generation and ototoxicity. J Neurosci 30: 3933-3946.
    • (2010) J Neurosci , vol.30 , pp. 3933-3946
    • Kim, H.J.1    Lee, J.H.2    Kim, S.J.3    Oh, G.S.4    Moon, H.D.5
  • 38
    • 33845630668 scopus 로고    scopus 로고
    • Anti-inflammatory effect of interleukin-10 on human neutrophil respiratory burst involves inhibition of GM-CSF-induced p47PHOX phosphorylation through a decrease in ERK1/2 activity
    • Dang PM, Elbim C, Marie JC, Chiandotto M, Gougerot-Pocidalo MA, et al. (2006) Anti-inflammatory effect of interleukin-10 on human neutrophil respiratory burst involves inhibition of GM-CSF-induced p47PHOX phosphorylation through a decrease in ERK1/2 activity. FASEB J 20: 1504-1506.
    • (2006) FASEB J , vol.20 , pp. 1504-1506
    • Dang, P.M.1    Elbim, C.2    Marie, J.C.3    Chiandotto, M.4    Gougerot-Pocidalo, M.A.5
  • 39
    • 84862833343 scopus 로고    scopus 로고
    • Endoplasmic Reticulum Stress-Induced JNK Activation Is a Critical Event Leading to Mitochondria-Mediated Cell Death Caused by β-Lapachone Treatment
    • Lee H, Park MT, Choi BH, Oh ET, Song MJ, et al. (2011) Endoplasmic Reticulum Stress-Induced JNK Activation Is a Critical Event Leading to Mitochondria-Mediated Cell Death Caused by β-Lapachone Treatment. PLoS One 6: e21533.
    • (2011) PLoS One , vol.6
    • Lee, H.1    Park, M.T.2    Choi, B.H.3    Oh, E.T.4    Song, M.J.5
  • 40
    • 45049083557 scopus 로고    scopus 로고
    • Induction of apoptosis by cigarette smoke via ROS-dependent endoplasmic reticulum stress and CCAAT/enhancer-binding protein-homologous protein (CHOP)
    • Tagawa Y, Hiramatsu N, Kasai A, Hayakawa K, et al. (2008) Induction of apoptosis by cigarette smoke via ROS-dependent endoplasmic reticulum stress and CCAAT/enhancer-binding protein-homologous protein (CHOP). Free Radic Biol Med 45: 50-59.
    • (2008) Free Radic Biol Med , vol.45 , pp. 50-59
    • Tagawa, Y.1    Hiramatsu, N.2    Kasai, A.3    Hayakawa, K.4
  • 41
    • 33645156429 scopus 로고    scopus 로고
    • From acute ER stress to physiological roles of the Unfolded Protein Response
    • Wu J, Kaufman RJ, (2006) From acute ER stress to physiological roles of the Unfolded Protein Response. Cell Death Differ 13: 374-384.
    • (2006) Cell Death Differ , vol.13 , pp. 374-384
    • Wu, J.1    Kaufman, R.J.2
  • 42
    • 33645154135 scopus 로고    scopus 로고
    • Cellular response to endoplasmic reticulum stress: a matter of life or death
    • Boyce M, Yuan J, (2006) Cellular response to endoplasmic reticulum stress: a matter of life or death. Cell Death Differ 13: 363-373.
    • (2006) Cell Death Differ , vol.13 , pp. 363-373
    • Boyce, M.1    Yuan, J.2
  • 43
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, Walter P, (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8: 519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 44
    • 33748789479 scopus 로고    scopus 로고
    • Mediators of endoplasmic reticulum stress-induced apoptosis
    • Szegezdi E, Logue SE, Gorman AM, Samali A, (2006) Mediators of endoplasmic reticulum stress-induced apoptosis. EMBO Rep 7: 880-885.
    • (2006) EMBO Rep , vol.7 , pp. 880-885
    • Szegezdi, E.1    Logue, S.E.2    Gorman, A.M.3    Samali, A.4
  • 45
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • Malhotra JD, Kaufman RJ, (2007) The endoplasmic reticulum and the unfolded protein response. Semin Cell Dev Biol 18: 716-731.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 46
    • 4444253303 scopus 로고    scopus 로고
    • Survival and apoptosis signals in ER stress: the role of protein kinases
    • Kadowaki H, Nishitoh H, Ichijo H, (2004) Survival and apoptosis signals in ER stress: the role of protein kinases. J Chem Neuroana 28: 93-100.
    • (2004) J Chem Neuroana , vol.28 , pp. 93-100
    • Kadowaki, H.1    Nishitoh, H.2    Ichijo, H.3
  • 47
    • 54749084254 scopus 로고    scopus 로고
    • Coupling of endoplasmic reticulum stress to CDDO-Me-induced up-regulation of death receptor 5 via a CHOP-dependent mechanism involving JNK activation
    • Zou W, Yue P, Khuri FR, Sun SY, (2008) Coupling of endoplasmic reticulum stress to CDDO-Me-induced up-regulation of death receptor 5 via a CHOP-dependent mechanism involving JNK activation. Cancer Res 68: 7484-7492.
    • (2008) Cancer Res , vol.68 , pp. 7484-7492
    • Zou, W.1    Yue, P.2    Khuri, F.R.3    Sun, S.Y.4
  • 48
    • 33746845181 scopus 로고    scopus 로고
    • Cardiotoxicity of the cancer therapeutic agent imatinib mesylate
    • Kerkelä R, Grazette L, Yacobi R, Iliescu C, Patten R, et al. (2006) Cardiotoxicity of the cancer therapeutic agent imatinib mesylate. Nat Med 12: 908-916.
    • (2006) Nat Med , vol.12 , pp. 908-916
    • Kerkelä, R.1    Grazette, L.2    Yacobi, R.3    Iliescu, C.4    Patten, R.5
  • 50
    • 0035894881 scopus 로고    scopus 로고
    • Caspase-9 activation results in downstream caspase-8 activation and bid cleavage in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced Parkinson's disease
    • Viswanath V, Wu Y, Boonplueang R, Chen S, Stevenson FF, et al. (2001) Caspase-9 activation results in downstream caspase-8 activation and bid cleavage in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced Parkinson's disease. J Neurosci 21: 9519-9528.
    • (2001) J Neurosci , vol.21 , pp. 9519-9528
    • Viswanath, V.1    Wu, Y.2    Boonplueang, R.3    Chen, S.4    Stevenson, F.F.5
  • 51
    • 40449140034 scopus 로고    scopus 로고
    • The human carcinoembryonic antigen (CEA) GPI anchor mediates anoikis inhibition by inactivation of the intrinsic death pathway
    • Camacho-Leal P, Stanners CP, (2008) The human carcinoembryonic antigen (CEA) GPI anchor mediates anoikis inhibition by inactivation of the intrinsic death pathway. Oncogene 27: 1545-1553.
    • (2008) Oncogene , vol.27 , pp. 1545-1553
    • Camacho-Leal, P.1    Stanners, C.P.2
  • 52
    • 0034737736 scopus 로고    scopus 로고
    • Caspase-8 activation and bid cleavage contribute to MCF7 cellular execution in a caspase-3-dependent manner during staurosporine-mediated apoptosis
    • Tang D, Lahti JM, Kidd VJ, (2000) Caspase-8 activation and bid cleavage contribute to MCF7 cellular execution in a caspase-3-dependent manner during staurosporine-mediated apoptosis. J Biol Chem 275: 9303-9307.
    • (2000) J Biol Chem , vol.275 , pp. 9303-9307
    • Tang, D.1    Lahti, J.M.2    Kidd, V.J.3
  • 53
    • 0037069929 scopus 로고    scopus 로고
    • Chemotherapy: targeting the mitochondrial cell death pathway
    • Debatin KM, Poncet D, Kroemer G, (2002) Chemotherapy: targeting the mitochondrial cell death pathway. Oncogene 21: 8786-8803.
    • (2002) Oncogene , vol.21 , pp. 8786-8803
    • Debatin, K.M.1    Poncet, D.2    Kroemer, G.3
  • 54
    • 0034699353 scopus 로고    scopus 로고
    • Caspase-8/FLICE functions as an executioner caspase in anticancer drug-induced apoptosis
    • Engels IH, Stepczynska A, Stroh C, Lauber K, Berg C, et al. (2000) Caspase-8/FLICE functions as an executioner caspase in anticancer drug-induced apoptosis. Oncogene 19: 4563-4573.
    • (2000) Oncogene , vol.19 , pp. 4563-4573
    • Engels, I.H.1    Stepczynska, A.2    Stroh, C.3    Lauber, K.4    Berg, C.5
  • 55
    • 0034617449 scopus 로고    scopus 로고
    • Apoptosis-inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis
    • Daugas E, Nochy D, Ravagnan L, Loeffler M, Susin SA, et al. (2000) Apoptosis-inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis. FEBS Lett 476: 118-123.
    • (2000) FEBS Lett , vol.476 , pp. 118-123
    • Daugas, E.1    Nochy, D.2    Ravagnan, L.3    Loeffler, M.4    Susin, S.A.5
  • 56
    • 2442583335 scopus 로고    scopus 로고
    • Arsenic trioxide-induced death of neuroblastoma cells involves activation of Bax and does not require p53
    • Karlsson J, Øra I, Pörn-Ares I, Påhlman S, (2004) Arsenic trioxide-induced death of neuroblastoma cells involves activation of Bax and does not require p53. Clin Cancer Res 10: 3179-3188.
    • (2004) Clin Cancer Res , vol.10 , pp. 3179-3188
    • Karlsson, J.1    Øra, I.2    Pörn-Ares, I.3    Påhlman, S.4


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