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Volumn 32, Issue 12, 2007, Pages 2103-2113

Curcumin suppressed anti-apoptotic signals and activated cysteine proteases for apoptosis in human malignant glioblastoma U87MG cells

Author keywords

Apoptosis; Bcl 2 proteins; Caspases; Curcumin; Glioblastoma

Indexed keywords

CALPAIN; CASPASE 3; CASPASE 8; CASPASE 9; CURCUMIN; CYSTEINE PROTEINASE; CYTOCHROME C; FODRIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN 1; POLYPHENOL DERIVATIVE; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BID; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; TRYPAN BLUE;

EID: 35848949333     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11064-007-9376-z     Document Type: Article
Times cited : (90)

References (74)
  • 2
    • 0034899448 scopus 로고    scopus 로고
    • Antiangiogenic and antitumor effects of a protein kinase Cβ inhibitor in human T98G glioblastoma multiforme xenografts
    • Teicher BA, Menon K, Alvarez E et al (2001) Antiangiogenic and antitumor effects of a protein kinase Cβ inhibitor in human T98G glioblastoma multiforme xenografts. Clin Cancer Res 7:634-640
    • (2001) Clin Cancer Res , vol.7 , pp. 634-640
    • Teicher, B.A.1    Menon, K.2    Alvarez, E.3
  • 3
    • 0037843576 scopus 로고    scopus 로고
    • Use of a vaccine strain of measles virus genetically engineered to produce carcinoembryonic antigen as a novel therapeutic agent against glioblastoma multiforme
    • Phuong LK, Allen C, Peng KW et al (2003) Use of a vaccine strain of measles virus genetically engineered to produce carcinoembryonic antigen as a novel therapeutic agent against glioblastoma multiforme. Cancer Res 63:2462-2469
    • (2003) Cancer Res , vol.63 , pp. 2462-2469
    • Phuong, L.K.1    Allen, C.2    Peng, K.W.3
  • 4
    • 0033051463 scopus 로고    scopus 로고
    • Inhibition of drug-induced DNA fragmentation, but not cell death, of glioma cells by non-caspase protease inhibitors
    • Eitel K, Wagenknecht B, Weller M (1999) Inhibition of drug-induced DNA fragmentation, but not cell death, of glioma cells by non-caspase protease inhibitors. Cancer Lett 142:11-16
    • (1999) Cancer Lett , vol.142 , pp. 11-16
    • Eitel, K.1    Wagenknecht, B.2    Weller, M.3
  • 5
    • 33749380913 scopus 로고    scopus 로고
    • PTEN enhances TNF-induced apoptosis through modulation of nuclear factor kappa B signaling pathway in human glioma cells
    • Koul D, Takada Y, Shen R et al (2006) PTEN enhances TNF-induced apoptosis through modulation of nuclear factor kappa B signaling pathway in human glioma cells. Biochem Biophys Res Commun 350:463-471
    • (2006) Biochem Biophys Res Commun , vol.350 , pp. 463-471
    • Koul, D.1    Takada, Y.2    Shen, R.3
  • 6
    • 2442480795 scopus 로고    scopus 로고
    • Multiple cell death pathways as regulators of tumour initiation and progression
    • Jaattela M (2004) Multiple cell death pathways as regulators of tumour initiation and progression. Oncogene 23:2746-2756
    • (2004) Oncogene , vol.23 , pp. 2746-2756
    • Jaattela, M.1
  • 7
    • 0032510679 scopus 로고    scopus 로고
    • Drug resistance of human glioblastoma cells conferred by a tumor-specific mutant epidermal growth factor receptor through modulation of Bcl-xL and caspase-3-like proteases
    • Nagane M, Levitzki A, Gazit A et al (1998) Drug resistance of human glioblastoma cells conferred by a tumor-specific mutant epidermal growth factor receptor through modulation of Bcl-xL and caspase-3-like proteases. Proc Natl Acad Sci USA 95:5724-5729
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5724-5729
    • Nagane, M.1    Levitzki, A.2    Gazit, A.3
  • 8
    • 1642517370 scopus 로고    scopus 로고
    • Induction of thymidine phosphorylase in both irradiated and shielded, contralateral human U87MG glioma xenografts: Implications for a dual modality treatment using capecitabine and irradiation
    • Blanquicett C, Gillespie GY, Nabors LB et al (2002) Induction of thymidine phosphorylase in both irradiated and shielded, contralateral human U87MG glioma xenografts: implications for a dual modality treatment using capecitabine and irradiation. Mol Cancer Ther 1:1139-1145
    • (2002) Mol Cancer Ther , vol.1 , pp. 1139-1145
    • Blanquicett, C.1    Gillespie, G.Y.2    Nabors, L.B.3
  • 9
    • 0037434422 scopus 로고    scopus 로고
    • α-Tocopheryl succinate sensitises a T lymphoma cell line to TRAIL-induced apoptosis by suppressing NFκB activation
    • Dalen H, Neuzil J (2003) α-Tocopheryl succinate sensitises a T lymphoma cell line to TRAIL-induced apoptosis by suppressing NFκB activation. Br J Cancer 88:153-158
    • (2003) Br J Cancer , vol.88 , pp. 153-158
    • Dalen, H.1    Neuzil, J.2
  • 10
    • 0037439685 scopus 로고    scopus 로고
    • Apoptosis caused by chemotherapeutic inhibition of nuclear factor kappa B activation
    • Biswas DK, Martin KJ, McAlister C et al (2003) Apoptosis caused by chemotherapeutic inhibition of nuclear factor kappa B activation. Cancer Res 63:290-295
    • (2003) Cancer Res , vol.63 , pp. 290-295
    • Biswas, D.K.1    Martin, K.J.2    McAlister, C.3
  • 11
    • 20944447769 scopus 로고    scopus 로고
    • Apoptosis related to telomere instability and cell cycle alterations in human glioma cells treated by new highly selective G-quadruplex ligands
    • Pennarun G, Granotier C, Gauthier LR et al (2005) Apoptosis related to telomere instability and cell cycle alterations in human glioma cells treated by new highly selective G-quadruplex ligands. Oncogene 24:2917-2928
    • (2005) Oncogene , vol.24 , pp. 2917-2928
    • Pennarun, G.1    Granotier, C.2    Gauthier, L.R.3
  • 12
    • 33645783756 scopus 로고    scopus 로고
    • Glioma: What is the role of c-Myc, hsp90 and telomerase?
    • Shervington A, Cruickshanks N, Wright H et al (2006) Glioma: what is the role of c-Myc, hsp90 and telomerase? Mol Cell Biochem 283:1-9
    • (2006) Mol Cell Biochem , vol.283 , pp. 1-9
    • Shervington, A.1    Cruickshanks, N.2    Wright, H.3
  • 13
    • 0038333197 scopus 로고    scopus 로고
    • Paclitaxel-induced apoptosis in BJAB cells proceeds via a death receptor-independent, caspases-3/-8-driven mitochondrial amplification loop
    • von Haefen C, Wieder T, Essmann F et al (2003) Paclitaxel-induced apoptosis in BJAB cells proceeds via a death receptor-independent, caspases-3/-8-driven mitochondrial amplification loop. Oncogene 22:2236-2247
    • (2003) Oncogene , vol.22 , pp. 2236-2247
    • Von Haefen, C.1    Wieder, T.2    Essmann, F.3
  • 14
    • 16844377506 scopus 로고    scopus 로고
    • Recent advances in understanding the cell death pathways activated by anticancer therapy
    • Kim R (2005) Recent advances in understanding the cell death pathways activated by anticancer therapy. Cancer 103:1551-1560
    • (2005) Cancer , vol.103 , pp. 1551-1560
    • Kim, R.1
  • 15
    • 0033521905 scopus 로고    scopus 로고
    • Apoptosis: A cellular poison cupboard
    • Earnshaw WC (1999) Apoptosis: A cellular poison cupboard. Nature 397:387-389
    • (1999) Nature , vol.397 , pp. 387-389
    • Earnshaw, W.C.1
  • 16
    • 15144345497 scopus 로고    scopus 로고
    • Pro-caspase-3 is a major physiologic target of caspase-8
    • Stennicke HR, Jurgensmeier JM, Shin H, et al (1998) Pro-caspase-3 is a major physiologic target of caspase-8. J Biol Chem 273:27084-27090
    • (1998) J Biol Chem , vol.273 , pp. 27084-27090
    • Stennicke, H.R.1    Jurgensmeier, J.M.2    Shin, H.3
  • 17
    • 0033535350 scopus 로고    scopus 로고
    • Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis
    • Desagher S, Osen-Sand A, Nichols A et al (1999) Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J Cell Biol 144:891-901
    • (1999) J Cell Biol , vol.144 , pp. 891-901
    • Desagher, S.1    Osen-Sand, A.2    Nichols, A.3
  • 18
    • 1842767259 scopus 로고    scopus 로고
    • Mitochondrial regulation of apoptotic cell death
    • Orrenius S (2004) Mitochondrial regulation of apoptotic cell death. Toxicol Lett 149:19-23
    • (2004) Toxicol Lett , vol.149 , pp. 19-23
    • Orrenius, S.1
  • 19
    • 3042679658 scopus 로고    scopus 로고
    • Smac induces cytochrome c release and apoptosis independently from Bax/Bcl-xL in a strictly caspase-3-dependent manner in human carcinoma cells
    • Hasenjager A, Gillissen B, Muller A et al (2004) Smac induces cytochrome c release and apoptosis independently from Bax/Bcl-xL in a strictly caspase-3-dependent manner in human carcinoma cells. Oncogene 23:4523-4535
    • (2004) Oncogene , vol.23 , pp. 4523-4535
    • Hasenjager, A.1    Gillissen, B.2    Muller, A.3
  • 20
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G, Reed JC (2000) Mitochondrial control of cell death. Nat Med 6:513-519
    • (2000) Nat Med , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 21
    • 0035937420 scopus 로고    scopus 로고
    • Cell death inhibition: Keeping caspases in check
    • Goyal L (2001) Cell death inhibition: keeping caspases in check. Cell 104:805-808
    • (2001) Cell , vol.104 , pp. 805-808
    • Goyal, L.1
  • 22
    • 0036186039 scopus 로고    scopus 로고
    • Involvement of caspases and calpains in cerebrocortical neuronal cell death is stimulus-dependent
    • Moore JD, Rothwell NJ, Gibson RM (2002) Involvement of caspases and calpains in cerebrocortical neuronal cell death is stimulus-dependent. Br J Pharmacol 135:1069-1077
    • (2002) Br J Pharmacol , vol.135 , pp. 1069-1077
    • Moore, J.D.1    Rothwell, N.J.2    Gibson, R.M.3
  • 23
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • Sakahira H, Enari M, Nagata S (1998) Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. Nature 391:96-99
    • (1998) Nature , vol.391 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 24
    • 2442621492 scopus 로고    scopus 로고
    • Role of AIF in caspase-dependent and caspase-independent cell death
    • Cregan SP, Dawson VL, Slack RS (2004) Role of AIF in caspase-dependent and caspase-independent cell death. Oncogene 23:2785-2796
    • (2004) Oncogene , vol.23 , pp. 2785-2796
    • Cregan, S.P.1    Dawson, V.L.2    Slack, R.S.3
  • 25
    • 0036252496 scopus 로고    scopus 로고
    • Growth inhibition, cell-cycle arrest and apoptosis in human T-cell leukemia by the isothiocyanate sulforaphane
    • Fimognari C, Nusse M, Cesari R et al (2002) Growth inhibition, cell-cycle arrest and apoptosis in human T-cell leukemia by the isothiocyanate sulforaphane. Carcinogenesis 23:581-586
    • (2002) Carcinogenesis , vol.23 , pp. 581-586
    • Fimognari, C.1    Nusse, M.2    Cesari, R.3
  • 26
    • 0033980370 scopus 로고    scopus 로고
    • Progress in cancer chemoprevention: Development of diet-derived chemopreventive agents
    • Kelloff GJ, Crowell JA, Steele VE et al (2000) Progress in cancer chemoprevention: development of diet-derived chemopreventive agents. J Nutr 130:467S-471S
    • (2000) J Nutr , vol.130
    • Kelloff, G.J.1    Crowell, J.A.2    Steele, V.E.3
  • 27
    • 16844371915 scopus 로고    scopus 로고
    • Induction of apoptosis by curcumin and its implications for cancer therapy
    • Karunagaran D, Rashmi R, Kumar TR (2005) Induction of apoptosis by curcumin and its implications for cancer therapy. Curr Cancer Drug Targets 5:117-129
    • (2005) Curr Cancer Drug Targets , vol.5 , pp. 117-129
    • Karunagaran, D.1    Rashmi, R.2    Kumar, T.R.3
  • 28
    • 33748433166 scopus 로고    scopus 로고
    • Curcumin activated both receptor-mediated and mitochondria-mediated proteolytic pathways for apoptosis in human glioblastoma T98G cells
    • Karmakar S, Banik NL, Patel SJ et al (2006) Curcumin activated both receptor-mediated and mitochondria-mediated proteolytic pathways for apoptosis in human glioblastoma T98G cells. Neurosci Lett 407:53-58
    • (2006) Neurosci Lett , vol.407 , pp. 53-58
    • Karmakar, S.1    Banik, N.L.2    Patel, S.J.3
  • 29
    • 84873487776 scopus 로고    scopus 로고
    • Induction of Apoptosis in Tumor Cells by Natural Phenolic Compounds
    • Roy M, Chakraborty S, Siddiqi M et al (2002) Induction of Apoptosis in Tumor Cells by Natural Phenolic Compounds. Asian Pac J Cancer Prev 3:61-67
    • (2002) Asian Pac J Cancer Prev , vol.3 , pp. 61-67
    • Roy, M.1    Chakraborty, S.2    Siddiqi, M.3
  • 30
    • 7644223910 scopus 로고    scopus 로고
    • NFκB and IκBα kinase are constitutively active in human pancreatic cells, and their down-regulation by curcumin (diferuloylmethane) is associated with the suppression of proliferation and the induction of apoptosis
    • Li L, Aggarwal BB, Shishodia S et al (2004) NFκB and IκBα kinase are constitutively active in human pancreatic cells, and their down-regulation by curcumin (diferuloylmethane) is associated with the suppression of proliferation and the induction of apoptosis. Cancer 101:2351-2362
    • (2004) Cancer , vol.101 , pp. 2351-2362
    • Li, L.1    Aggarwal, B.B.2    Shishodia, S.3
  • 31
    • 0042169007 scopus 로고    scopus 로고
    • Molecular mechanisms of curcumin-induced cytotoxicity: Induction of apoptosis through generation of reactive oxygen species, down regulation of Bcl-xL and IAP, the release of cytochrome c and inhibition of Akt
    • Woo JH, Kim YH, Choi YJ et al (2003) Molecular mechanisms of curcumin-induced cytotoxicity: induction of apoptosis through generation of reactive oxygen species, down regulation of Bcl-xL and IAP, the release of cytochrome c and inhibition of Akt. Carcinogenesis 24:1199-1208
    • (2003) Carcinogenesis , vol.24 , pp. 1199-1208
    • Woo, J.H.1    Kim, Y.H.2    Choi, Y.J.3
  • 33
    • 0036195104 scopus 로고    scopus 로고
    • Curcumin (diferuloylmethane) induces apoptosis through activation of caspase-8, Bid cleavage, and cytochrome c release: Its suppression by ectopic expression of Bcl-2 and Bcl-xL
    • Anto RJ, Mukhopadhyay A, Denning K et al (2002) Curcumin (diferuloylmethane) induces apoptosis through activation of caspase-8, Bid cleavage, and cytochrome c release: its suppression by ectopic expression of Bcl-2 and Bcl-xL. Carcinogenesis 23:143-150
    • (2002) Carcinogenesis , vol.23 , pp. 143-150
    • Anto, R.J.1    Mukhopadhyay, A.2    Denning, K.3
  • 34
    • 19344368071 scopus 로고    scopus 로고
    • Chemopreventive and therapeutic effects of curcumin
    • Duvoix A, Blasius R, Delhalle S et al (2005) Chemopreventive and therapeutic effects of curcumin. Cancer Lett 223:181-190
    • (2005) Cancer Lett , vol.223 , pp. 181-190
    • Duvoix, A.1    Blasius, R.2    Delhalle, S.3
  • 35
    • 19344367506 scopus 로고    scopus 로고
    • Anti-tumor effects of curcumin, alone or in combination with cisplatin or doxorubicin, on human hepatic cancer cells. Analysis of their possible relationship to changes in NFκB activation levels and in IAP gene expression
    • Notarbartolo M, Poma P, Perri D et al (2005) Anti-tumor effects of curcumin, alone or in combination with cisplatin or doxorubicin, on human hepatic cancer cells. Analysis of their possible relationship to changes in NFκB activation levels and in IAP gene expression. Cancer Lett 224: 53-65
    • (2005) Cancer Lett , vol.224 , pp. 53-65
    • Notarbartolo, M.1    Poma, P.2    Perri, D.3
  • 36
    • 0023677360 scopus 로고
    • Calcium-activated neutral proteinase in rat brain myelin and subcellular fractions
    • Chakrabarti AK, Yoshida Y, Powers JM et al (1988) Calcium-activated neutral proteinase in rat brain myelin and subcellular fractions. J Neurosci Res 20:351-358
    • (1988) J Neurosci Res , vol.20 , pp. 351-358
    • Chakrabarti, A.K.1    Yoshida, Y.2    Powers, J.M.3
  • 37
    • 33746422972 scopus 로고    scopus 로고
    • Activation of multiple molecular mechanisms for apoptosis in human malignant glioblastoma T98G and U87MG cells treated with sulforaphane
    • Karmakar S, Weinberg MS, Banik NL et al (2006) Activation of multiple molecular mechanisms for apoptosis in human malignant glioblastoma T98G and U87MG cells treated with sulforaphane. Neuroscience 141:1265-1280
    • (2006) Neuroscience , vol.141 , pp. 1265-1280
    • Karmakar, S.1    Weinberg, M.S.2    Banik, N.L.3
  • 38
    • 33645846638 scopus 로고    scopus 로고
    • Inhibition of calpain and caspase-3 prevented apoptosis and preserved electrophysiological properties of voltage-gated and ligand-gated ion channels in rat primary cortical neurons exposed to glutamate
    • Ray SK, Karmakar S, Nowak MW et al (2006) Inhibition of calpain and caspase-3 prevented apoptosis and preserved electrophysiological properties of voltage-gated and ligand-gated ion channels in rat primary cortical neurons exposed to glutamate. Neuroscience 139:577-595
    • (2006) Neuroscience , vol.139 , pp. 577-595
    • Ray, S.K.1    Karmakar, S.2    Nowak, M.W.3
  • 39
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • Gavrieli Y, Sherman Y, Ben-Sasson SA (1992) Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. J Cell Biol 119:493-501
    • (1992) J Cell Biol , vol.119 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 40
    • 0014311556 scopus 로고
    • Nondroplet ultrastructural demonstration of cytochrome oxidase activity with a polymerizing osmiophilic reagent, diaminobenzidine (DAB)
    • Seligman AM, Karnovsky MJ, Wasserkrug HL et al (1968) Nondroplet ultrastructural demonstration of cytochrome oxidase activity with a polymerizing osmiophilic reagent, diaminobenzidine (DAB). J Cell Biol 38:1-14
    • (1968) J Cell Biol , vol.38 , pp. 1-14
    • Seligman, A.M.1    Karnovsky, M.J.2    Wasserkrug, H.L.3
  • 41
    • 33947174588 scopus 로고    scopus 로고
    • Garlic compounds induced calpain and intrinsic caspase cascade for apoptosis in human malignant neuroblastoma SH-SY5Y cells
    • Karmakar S, Banik NL, Patel SJ et al (2007) Garlic compounds induced calpain and intrinsic caspase cascade for apoptosis in human malignant neuroblastoma SH-SY5Y cells. Apoptosis 12:671-684
    • (2007) Apoptosis , vol.12 , pp. 671-684
    • Karmakar, S.1    Banik, N.L.2    Patel, S.J.3
  • 42
    • 33947136015 scopus 로고    scopus 로고
    • 5-Aminolevulinic acid-based photodynamic therapy suppressed survival factors and activated proteases for apoptosis in human glioblastoma U87MG cells
    • Karmakar S, Banik NL, Patel SJ et al (2007) 5-Aminolevulinic acid-based photodynamic therapy suppressed survival factors and activated proteases for apoptosis in human glioblastoma U87MG cells. Neurosci Lett 415:242-247
    • (2007) Neurosci Lett , vol.415 , pp. 242-247
    • Karmakar, S.1    Banik, N.L.2    Patel, S.J.3
  • 43
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 44
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A, Dixit VM (1998) Death receptors: signaling and modulation. Science 281:1305-1308
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 45
    • 0033534446 scopus 로고    scopus 로고
    • Caspase cleaved Bid targets mitochondria and is required for cytochrome c release, while Bcl-xL prevents this release but not tumor necrosis factor-R1/Fas death
    • Gross A, Yin XM, Wang K et al (1999) Caspase cleaved Bid targets mitochondria and is required for cytochrome c release, while Bcl-xL prevents this release but not tumor necrosis factor-R1/Fas death. J Biol Chem 274:1156-1163
    • (1999) J Biol Chem , vol.274 , pp. 1156-1163
    • Gross, A.1    Yin, X.M.2    Wang, K.3
  • 46
    • 33646492469 scopus 로고    scopus 로고
    • Inhibition of telomerase activity and induction of apoptosis by curcumin in K562 cells
    • Chakraborty S, Ghosh U, Bhattacharyya NP et al (2006) Inhibition of telomerase activity and induction of apoptosis by curcumin in K562 cells. Mutat Res 596:81-90
    • (2006) Mutat Res , vol.596 , pp. 81-90
    • Chakraborty, S.1    Ghosh, U.2    Bhattacharyya, N.P.3
  • 47
    • 18844461634 scopus 로고    scopus 로고
    • Curcumin enhances Vinorelbine mediated apoptosis in NSCLC cells by the mitochondrial pathway
    • Sen S, Sharma H, Singh N (2005) Curcumin enhances Vinorelbine mediated apoptosis in NSCLC cells by the mitochondrial pathway. Biochem Biophys Res Commun 331:1245-1252
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 1245-1252
    • Sen, S.1    Sharma, H.2    Singh, N.3
  • 48
    • 33244476761 scopus 로고    scopus 로고
    • Antiproliferation and apoptosis induced by curcumin in human ovarian cancer cells
    • Shi M, Cai Q, Yao L (2006) Antiproliferation and apoptosis induced by curcumin in human ovarian cancer cells. Cell Biol Int 30:221-226
    • (2006) Cell Biol Int , vol.30 , pp. 221-226
    • Shi, M.1    Cai, Q.2    Yao, L.3
  • 49
    • 33344461738 scopus 로고    scopus 로고
    • Curcumin induces apoptosis via inhibition of PI3-kinase/Akt pathway in acute T cell leukemias
    • Hussain AR, Al-Rasheed M, Manogaran PS et al (2006) Curcumin induces apoptosis via inhibition of PI3-kinase/Akt pathway in acute T cell leukemias. Apoptosis 11:245-254
    • (2006) Apoptosis , vol.11 , pp. 245-254
    • Hussain, A.R.1    Al-Rasheed, M.2    Manogaran, P.S.3
  • 50
    • 28444464762 scopus 로고    scopus 로고
    • Chemosensitization of hormone-refractory prostate cancer cells by curcumin to TRAIL-induced apoptosis
    • Deeb DD, Jiang H, Gao X et al (2005) Chemosensitization of hormone-refractory prostate cancer cells by curcumin to TRAIL-induced apoptosis. J Exp Ther Oncol 5:81-91
    • (2005) J Exp Ther Oncol , vol.5 , pp. 81-91
    • Deeb, D.D.1    Jiang, H.2    Gao, X.3
  • 51
    • 0037388691 scopus 로고    scopus 로고
    • A comprehensive search for DNA amplification in lung cancer identifies inhibitors of apoptosis cIAP1 and cIAP2 as candidate oncogenes
    • Dai Z, Zhu WG, Morrison CD et al (2003) A comprehensive search for DNA amplification in lung cancer identifies inhibitors of apoptosis cIAP1 and cIAP2 as candidate oncogenes. Hum Mol Genet 12:791-801
    • (2003) Hum Mol Genet , vol.12 , pp. 791-801
    • Dai, Z.1    Zhu, W.G.2    Morrison, C.D.3
  • 52
    • 30444437867 scopus 로고    scopus 로고
    • Curcumin (diferuloylmethane) inhibits constitutive active NFκB, leading to suppression of cell growth of human T-cell leukemia virus type I-infected T-cell lines and primary adult T-cell leukemia cells
    • Tomita M, Kawakami H, Uchihara JN et al (2006) Curcumin (diferuloylmethane) inhibits constitutive active NFκB, leading to suppression of cell growth of human T-cell leukemia virus type I-infected T-cell lines and primary adult T-cell leukemia cells. Int J Cancer 118:765-772
    • (2006) Int J Cancer , vol.118 , pp. 765-772
    • Tomita, M.1    Kawakami, H.2    Uchihara, J.N.3
  • 53
    • 33748207614 scopus 로고    scopus 로고
    • Resistance to apoptosis of HCW-2 cells can be overcome by curcumin- or vincristine-induced mitotic catastrophe
    • Magalska A, Sliwinska M, Szczepanowska J et al (2006) Resistance to apoptosis of HCW-2 cells can be overcome by curcumin- or vincristine-induced mitotic catastrophe. Int J Cancer 119:1811-1818
    • (2006) Int J Cancer , vol.119 , pp. 1811-1818
    • Magalska, A.1    Sliwinska, M.2    Szczepanowska, J.3
  • 54
    • 1242307957 scopus 로고    scopus 로고
    • Ectopic expression of Hsp70 confers resistance and silencing its expression sensitizes human colon cancer cells to curcumin-induced apoptosis
    • Rashmi R, Kumar S, Karunagaran D (2004) Ectopic expression of Hsp70 confers resistance and silencing its expression sensitizes human colon cancer cells to curcumin-induced apoptosis. Carcinogenesis 25:179-187
    • (2004) Carcinogenesis , vol.25 , pp. 179-187
    • Rashmi, R.1    Kumar, S.2    Karunagaran, D.3
  • 55
    • 0034616942 scopus 로고    scopus 로고
    • Identification of Diablo, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen AM, Ekert PG, Pakusch M et al (2000) Identification of Diablo, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 102:43-53
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3
  • 56
    • 10944247878 scopus 로고    scopus 로고
    • Neutralization of Smac/Diablo by inhibitors of apoptosis (IAPs). a caspase-independent mechanism for apoptotic inhibition
    • Wilkinson JC, Wilkinson AS, Scott FL (2004) Neutralization of Smac/Diablo by inhibitors of apoptosis (IAPs). A caspase-independent mechanism for apoptotic inhibition. J Biol Chem 279:51082-51090
    • (2004) J Biol Chem , vol.279 , pp. 51082-51090
    • Wilkinson, J.C.1    Wilkinson, A.S.2    Scott, F.L.3
  • 57
    • 0035803568 scopus 로고    scopus 로고
    • Apoptosis-associated release of Smac/Diablo from mitochondria requires active caspases and is blocked by Bcl-2
    • Adrain C, Creagh EM, Martin SJ (1996) Apoptosis-associated release of Smac/Diablo from mitochondria requires active caspases and is blocked by Bcl-2. EMBO J 20:6627-6636
    • (1996) EMBO J , vol.20 , pp. 6627-6636
    • Adrain, C.1    Creagh, E.M.2    Martin, S.J.3
  • 58
    • 0030698127 scopus 로고    scopus 로고
    • The cIAP1 and cIAP2 proteins are direct inhibitors of specific caspases
    • Roy N, Deveraux QL, Takahashi R et al (1997) The cIAP1 and cIAP2 proteins are direct inhibitors of specific caspases. EMBO J 16:6914-6925
    • (1997) EMBO J , vol.16 , pp. 6914-6925
    • Roy, N.1    Deveraux, Q.L.2    Takahashi, R.3
  • 59
    • 0032410818 scopus 로고    scopus 로고
    • The inhibitors of apoptosis (IAPs) and their emerging role in cancer
    • LaCasse EC, Baird S, Korneluk RG et al (1998) The inhibitors of apoptosis (IAPs) and their emerging role in cancer. Oncogene 17:3247-3259
    • (1998) Oncogene , vol.17 , pp. 3247-3259
    • Lacasse, E.C.1    Baird, S.2    Korneluk, R.G.3
  • 60
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins-suppressors of apoptosis
    • Deveraux QL, Reed JC (1999) IAP family proteins-suppressors of apoptosis. Genes Dev 13:239-252
    • (1999) Genes Dev , vol.13 , pp. 239-252
    • Deveraux, Q.L.1    Reed, J.C.2
  • 61
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NFκB in preventing TNF-α-induced cell death
    • Beg AA, Baltimore D (1996) An essential role for NFκB in preventing TNF-α-induced cell death. Science 274:782-784
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 62
    • 0036624741 scopus 로고    scopus 로고
    • Biologic sequelae of nuclear factor kappa B blockade in multiple myeloma: Therapeutic applications
    • Mitsiades N, Mitsiades CS, Poulaki V et al (2002) Biologic sequelae of nuclear factor kappa B blockade in multiple myeloma: therapeutic applications. Blood 99:4079-4086
    • (2002) Blood , vol.99 , pp. 4079-4086
    • Mitsiades, N.1    Mitsiades, C.S.2    Poulaki, V.3
  • 63
    • 1942486873 scopus 로고    scopus 로고
    • NFκB-mediated IAP expression induces resistance of intestinal epithelial cells to apoptosis after polyamine depletion
    • Zou T, Rao JN, Guo X et al (2004) NFκB-mediated IAP expression induces resistance of intestinal epithelial cells to apoptosis after polyamine depletion. Am J Physiol Cell Physiol 286:C1009-C1018
    • (2004) Am J Physiol Cell Physiol , vol.286
    • Zou, T.1    Rao, J.N.2    Guo, X.3
  • 64
    • 0031810458 scopus 로고    scopus 로고
    • Inhibition of nuclear factor kappa B activation attenuates apoptosis resistance in lymphoid cells
    • Jeremias I, Kupatt C, Baumann B et al (1998) Inhibition of nuclear factor kappa B activation attenuates apoptosis resistance in lymphoid cells. Blood 91:4624-4631
    • (1998) Blood , vol.91 , pp. 4624-4631
    • Jeremias, I.1    Kupatt, C.2    Baumann, B.3
  • 65
    • 0032508414 scopus 로고    scopus 로고
    • NFκB anti-apoptosis: Induction of TRAF1 and TRAF2 and cIAP1 and cIAP2 to suppress caspase-8 activation
    • Wang CY, Mayo MW, Korneluk RG et al (1998) NFκB anti-apoptosis: induction of TRAF1 and TRAF2 and cIAP1 and cIAP2 to suppress caspase-8 activation. Science 281:1680-1683
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3
  • 66
    • 0037305821 scopus 로고    scopus 로고
    • Curcumin (diferuloylmethane) down-regulates the constitutive activation of NFκB and IκBα kinase in human multiple myeloma cells, leading to suppression of proliferation and induction of apoptosis
    • Bharti AC, Donato N, Singh S et al (2003) Curcumin (diferuloylmethane) down-regulates the constitutive activation of NFκB and IκBα kinase in human multiple myeloma cells, leading to suppression of proliferation and induction of apoptosis. Blood 101:1053-1062
    • (2003) Blood , vol.101 , pp. 1053-1062
    • Bharti, A.C.1    Donato, N.2    Singh, S.3
  • 67
    • 30044446136 scopus 로고    scopus 로고
    • Curcumin (diferuloylmethane) down-regulates expression of cell proliferation and antiapoptotic and metastatic gene products through suppression of IκBα kinase and Akt activation
    • Aggarwal S, Ichikawa H, Takada Y et al (2006) Curcumin (diferuloylmethane) down-regulates expression of cell proliferation and antiapoptotic and metastatic gene products through suppression of IκBα kinase and Akt activation. Mol Pharmacol 69:195-206
    • (2006) Mol Pharmacol , vol.69 , pp. 195-206
    • Aggarwal, S.1    Ichikawa, H.2    Takada, Y.3
  • 68
    • 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 et al (2000) Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102:33-42
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3
  • 69
    • 17844392101 scopus 로고    scopus 로고
    • Human colon cancer cells lacking Bax resist curcumin-induced apoptosis and Bax requirement is dispensable with ectopic expression of Smac or downregulation of Bcl-xL
    • Rashmi R, Kumar S, Karunagaran D (2005) Human colon cancer cells lacking Bax resist curcumin-induced apoptosis and Bax requirement is dispensable with ectopic expression of Smac or downregulation of Bcl-xL. Carcinogenesis 26:713-723
    • (2005) Carcinogenesis , vol.26 , pp. 713-723
    • Rashmi, R.1    Kumar, S.2    Karunagaran, D.3
  • 70
    • 1242307957 scopus 로고    scopus 로고
    • Ectopic expression of Hsp70 confers resistance and silencing its expression sensitizes human colon cancer cells to curcumin-induced apoptosis
    • Rashmi R, Kumar S, Karunagaran D (2004) Ectopic expression of Hsp70 confers resistance and silencing its expression sensitizes human colon cancer cells to curcumin-induced apoptosis. Carcinogenesis 25:179-187
    • (2004) Carcinogenesis , vol.25 , pp. 179-187
    • Rashmi, R.1    Kumar, S.2    Karunagaran, D.3
  • 71
    • 18144407551 scopus 로고    scopus 로고
    • Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: Evidence from calpastatin mutant mice
    • Takano J, Tomioka M, Tsubuki S et al (2005) Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: evidence from calpastatin mutant mice. J Biol Chem 280:16175-16184
    • (2005) J Biol Chem , vol.280 , pp. 16175-16184
    • Takano, J.1    Tomioka, M.2    Tsubuki, S.3
  • 72
    • 0029854806 scopus 로고    scopus 로고
    • Non-erythroid α-spectrin breakdown by calpain and interleukin 1β-converting-enzyme-like protease(s) in apoptotic cells: Contributory roles of both protease families in neuronal apoptosis
    • Nath R, Raser KJ, Stafford D et al (1996) Non-erythroid α-spectrin breakdown by calpain and interleukin 1β-converting-enzyme-like protease(s) in apoptotic cells: contributory roles of both protease families in neuronal apoptosis. Biochem J 319:683-690
    • (1996) Biochem J , vol.319 , pp. 683-690
    • Nath, R.1    Raser, K.J.2    Stafford, D.3
  • 73
    • 0032575377 scopus 로고    scopus 로고
    • Simultaneous degradation of αiI- and βiI-spectrin by caspase 3 (CPP32) in apoptotic cells
    • Wang KK, Posmantur R, Nath R et al (1998) Simultaneous degradation of αII- and βII-spectrin by caspase 3 (CPP32) in apoptotic cells. J Biol Chem 273:22490-22497
    • (1998) J Biol Chem , vol.273 , pp. 22490-22497
    • Wang, K.K.1    Posmantur, R.2    Nath, R.3
  • 74
    • 0037648485 scopus 로고    scopus 로고
    • Cross-talk between calpain and caspase proteolytic systems during neuronal apoptosis
    • Neumar RW, Xu YA, Gada H et al (2003) Cross-talk between calpain and caspase proteolytic systems during neuronal apoptosis. J Biol Chem 278:14162-14167
    • (2003) J Biol Chem , vol.278 , pp. 14162-14167
    • Neumar, R.W.1    Xu, Y.A.2    Gada, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.