메뉴 건너뛰기




Volumn 30, Issue 4, 2013, Pages 1929-1935

Cytochalasin B induces apoptosis through the mitochondrial apoptotic pathway in HeLa human cervical carcinoma cells

Author keywords

Apoptosis; Cell cycle arrest; Cytochalasin B; Mitochondrial pathway; Reactive oxygen species

Indexed keywords

CASPASE 3; CASPASE 9; CYTOCHALASIN B; DNA; PROTEIN BAX; PROTEIN BCL 2; REACTIVE OXYGEN METABOLITE;

EID: 84882566861     PISSN: 1021335X     EISSN: 17912431     Source Type: Journal    
DOI: 10.3892/or.2013.2617     Document Type: Article
Times cited : (22)

References (38)
  • 1
    • 0036478970 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species in cell death signaling
    • Fleury C, Mignotte B and Vayssière JL: Mitochondrial reactive oxygen species in cell death signaling. Biochimie 84: 131-141, 2002.
    • (2002) Biochimie , vol.84 , pp. 131-141
    • Fleury, C.1    Mignotte, B.2    Vayssière, J.L.3
  • 2
    • 0033178637 scopus 로고    scopus 로고
    • Stimulation of cardiac fibroblast proliferation by cerium: A superoxide anion-mediated response
    • Preeta R and Nair RR: Stimulation of cardiac fibroblast proliferation by cerium: a superoxide anion-mediated response. J Mol Cell Cardiol 31: 1573-1580, 1999.
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 1573-1580
    • Preeta, R.1    Nair, R.R.2
  • 3
    • 0028064339 scopus 로고
    • Differential proliferative responses of Syrian hamster embryo fibroblasts to paraquat-generated superoxide radicals depending on tumor suppressor gene function
    • Nicotera TM, Privalle C, Wang TC, et al: Differential proliferative responses of Syrian hamster embryo fibroblasts to paraquat-generated superoxide radicals depending on tumor suppressor gene function. Cancer Res 54: 3884-3888, 1994.
    • (1994) Cancer Res , vol.54 , pp. 3884-3888
    • Nicotera, T.M.1    Privalle, C.2    Wang, T.C.3
  • 4
    • 0025290814 scopus 로고
    • Kinetic evaluation of freemalondialdehyde and enzyme leakage as indices of iron damage in rat hepatocyte cultures
    • Morel I, Lescoat G, Cillard J, et al: Kinetic evaluation of freemalondialdehyde and enzyme leakage as indices of iron damage in rat hepatocyte cultures. Involvement of free radicals. Biochem Pharmacol 39: 1647-1655, 1990.
    • (1990) Involvement of Free Radicals. Biochem Pharmacol , vol.39 , pp. 1647-1655
    • Morel, I.1    Lescoat, G.2    Cillard, J.3
  • 5
    • 0030069695 scopus 로고    scopus 로고
    • Structural origins of bulky oxidative DNA adducts (type II I-compounds) as deduced by oxidation of oligonucleotides of known sequence
    • Randerath K, Randerath E, Smith CV and Chang J: Structural origins of bulky oxidative DNA adducts (type II I-compounds) as deduced by oxidation of oligonucleotides of known sequence. Chem Res Toxicol 9: 247-254, 1996.
    • (1996) Chem Res Toxicol , vol.9 , pp. 247-254
    • Randerath, K.1    Randerath, E.2    Smith, C.V.3    Chang, J.4
  • 6
    • 0024462967 scopus 로고
    • Endogenous DNA damage as related to cancer and aging
    • Ames BN: Endogenous DNA damage as related to cancer and aging. Mutat Res 214: 41-46, 1989.
    • (1989) Mutat Res , vol.214 , pp. 41-46
    • Ames, B.N.1
  • 7
    • 0026021362 scopus 로고
    • Production of large amounts of hydrogen peroxide by human tumor cells
    • Szatrowski TP and Nathan CF: Production of large amounts of hydrogen peroxide by human tumor cells. Cancer Res 51: 794-798, 1991.
    • (1991) Cancer Res , vol.51 , pp. 794-798
    • Szatrowski, T.P.1    Nathan, C.F.2
  • 8
    • 0141529729 scopus 로고    scopus 로고
    • Curcumin inhibits UV irradiation-induced oxidative stress and apoptotic biochemical changes in human epidermoid carcinoma A431 cells
    • Chan WH, Wu CC and Yu JS: Curcumin inhibits UV irradiation-induced oxidative stress and apoptotic biochemical changes in human epidermoid carcinoma A431 cells. J Cell Biochem 90: 327-338, 2003.
    • (2003) J Cell Biochem , vol.90 , pp. 327-338
    • Chan, W.H.1    Wu, C.C.2    Yu, J.S.3
  • 9
    • 0029042718 scopus 로고
    • Nuclear changes in apoptosis
    • Earnshaw WC: Nuclear changes in apoptosis. Curr Opin Cell Biol 7: 337-343, 1995.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 337-343
    • Earnshaw, W.C.1
  • 10
    • 59049091828 scopus 로고    scopus 로고
    • Apoptotic activity of fatty acid derivatives may correlate with their inhibition of DNA replication
    • Miao C, Du J, Dang HT, et al: Apoptotic activity of fatty acid derivatives may correlate with their inhibition of DNA replication. Int J Oncol 33: 1291-1298, 2008.
    • (2008) Int J Oncol , vol.33 , pp. 1291-1298
    • Miao, C.1    Du, J.2    Dang, H.T.3
  • 11
    • 80054826722 scopus 로고    scopus 로고
    • A novel cromakalim analogue induces cell cycle arrest and apoptosis in human cervical carcinoma HeLa cells through the caspase- and mitochondria-dependent pathway
    • Zhang X, Zhao J, Kang S, et al: A novel cromakalim analogue induces cell cycle arrest and apoptosis in human cervical carcinoma HeLa cells through the caspase- and mitochondria-dependent pathway. Int J Oncol 39: 1609-1617, 2011.
    • (2011) Int J Oncol , vol.39 , pp. 1609-1617
    • Zhang, X.1    Zhao, J.2    Kang, S.3
  • 12
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner MO: The biochemistry of apoptosis. Nature 407: 770-776, 2000.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 13
    • 0033118475 scopus 로고    scopus 로고
    • Apoptosis, p53, and tumor cell sensitivity to anticancer agents
    • Brown JM and Wouters BG: Apoptosis, p53, and tumor cell sensitivity to anticancer agents. Cancer Res 59: 1391-1399, 1999.
    • (1999) Cancer Res , vol.59 , pp. 1391-1399
    • Brown, J.M.1    Wouters, B.G.2
  • 14
    • 0036159031 scopus 로고    scopus 로고
    • Remodeling for demolition: Changes in mitochondrial ultrastructure during apoptosis
    • Reed JC and Green DR: Remodeling for demolition: changes in mitochondrial ultrastructure during apoptosis. Mol Cell 9: 1-3, 2002.
    • (2002) Mol Cell , vol.9 , pp. 1-3
    • Reed, J.C.1    Green, D.R.2
  • 15
    • 73349091842 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis
    • Wang C and Youle RJ: The role of mitochondria in apoptosis. Ann Rev Genet 43: 95-118, 2009.
    • (2009) Ann Rev Genet , vol.43 , pp. 95-118
    • Wang, C.1    Youle, R.J.2
  • 16
  • 17
    • 0032550363 scopus 로고    scopus 로고
    • The permeability transition pore complex: A target for apoptosis regulation by caspases and Bcl-2 related proteins
    • Marzo I, Brenner C, Zamzami N, et al: The permeability transition pore complex: a target for apoptosis regulation by caspases and Bcl-2 related proteins. J Exp Med 187: 1261-1271, 1998.
    • (1998) J Exp Med , vol.187 , pp. 1261-1271
    • Marzo, I.1    Brenner, C.2    Zamzami, N.3
  • 18
    • 0345276414 scopus 로고    scopus 로고
    • Bcl-2-family proteins and the role of mitochondria in apoptosis
    • Kuwana T and Newmeyer DD: Bcl-2-family proteins and the role of mitochondria in apoptosis. Curr Opin Cell Biol 15: 691-699, 2003.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 691-699
    • Kuwana, T.1    Newmeyer, D.D.2
  • 19
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain
    • Boldin MP, Varfolomeev EE, Pancer Z, et al: A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. J Biol Chem 270: 7796-7798, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 7796-7798
    • Boldin, M.P.1    Varfolomeev, E.E.2    Pancer, Z.3
  • 20
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with death domain of Fas and initiates apoptosis
    • Chinnaiyan AM, O'Rourke KO, Tewari M and Dixit VM: FADD, a novel death domain-containing protein, interacts with death domain of Fas and initiates apoptosis. Cell 81: 505-512, 1995.
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.O.2    Tewari, M.3    Dixit, V.M.4
  • 21
    • 0000321259 scopus 로고
    • Symbiotic interactions between marine sponges and algae
    • Reisser W (ed). Biopress, Bristol
    • Wilkinson CR: Symbiotic interactions between marine sponges and algae. In: Algae and Symbioses. Reisser W (ed). Biopress, Bristol, pp112-151, 1992.
    • (1992) Algae and Symbioses , pp. 112-151
    • Wilkinson, C.R.1
  • 23
    • 84882735460 scopus 로고
    • Cytochalasins as probes in selected morphogenetic processes
    • Tanenbaum SW (ed). Elsevier/North Holland Biomedical Press, Amsterdam
    • Spooner BS: Cytochalasins as probes in selected morphogenetic processes. In: Cytochalasins. Biochemical and Cell Biological Aspects. Tanenbaum SW (ed). Elsevier/North Holland Biomedical Press, Amsterdam, pp161-189, 1978.
    • (1978) Cytochalasins. Biochemical and Cell Biological Aspects , pp. 161-189
    • Spooner, B.S.1
  • 24
    • 0022646342 scopus 로고
    • Cytochalasin B slows but does not prevent monomer addition at the barbed end of the actin filament
    • Bonder EM and Mooseker MS: Cytochalasin B slows but does not prevent monomer addition at the barbed end of the actin filament. J Cell Biol 102: 282-288, 1986.
    • (1986) J Cell Biol , vol.102 , pp. 282-288
    • Bonder, E.M.1    Mooseker, M.S.2
  • 25
    • 34250366632 scopus 로고    scopus 로고
    • Wide-ranging effects of eight cytochalasins and latrunculin A and B on intracellular motility and actin filament reorganization in characean internodal cells
    • Foissner I and Wasteneys GO: Wide-ranging effects of eight cytochalasins and latrunculin A and B on intracellular motility and actin filament reorganization in characean internodal cells. Plant Cell Physiol 48: 585-587, 2007.
    • (2007) Plant Cell Physiol , vol.48 , pp. 585-587
    • Foissner, I.1    Wasteneys, G.O.2
  • 26
    • 0026532680 scopus 로고
    • Direct proof that the primary site of action of cytochalasin on cell motility processes is actin
    • Ohmori H, Toyama S and Toyama S: Direct proof that the primary site of action of cytochalasin on cell motility processes is actin. J Cell Biol 116: 933-941, 1992.
    • (1992) J Cell Biol , vol.116 , pp. 933-941
    • Ohmori, H.1    Toyama, S.2    Toyama, S.3
  • 27
    • 85047683345 scopus 로고    scopus 로고
    • Apoptosis induced by disruption of the actin cytoskeleton is mediated via activation of CD95 (Fas/APO-1)
    • Kulms D, Düssmann H, Pöppelmann B, et al: Apoptosis induced by disruption of the actin cytoskeleton is mediated via activation of CD95 (Fas/APO-1). Cell Death Differ 9: 598-608, 2002.
    • (2002) Cell Death Differ , vol.9 , pp. 598-608
    • Kulms, D.1    Düssmann, H.2    Pöppelmann, B.3
  • 28
    • 0002494823 scopus 로고    scopus 로고
    • A water-soluble tetrazolium salt useful for colorimetric cell viability assay
    • Tominaga H, Ishiyama M, Ohseto F, et al: A water-soluble tetrazolium salt useful for colorimetric cell viability assay. Anal Commun 36: 47-50, 1999.
    • (1999) Anal Commun , vol.36 , pp. 47-50
    • Tominaga, H.1    Ishiyama, M.2    Ohseto, F.3
  • 29
    • 0035702912 scopus 로고    scopus 로고
    • Magnolol suppresses proliferation of cultured human colon and liver cancer cells by inhibiting DNA synthesis and activating apoptosis
    • Lin SY, Liu JD, Chang HC, et al: Magnolol suppresses proliferation of cultured human colon and liver cancer cells by inhibiting DNA synthesis and activating apoptosis. J Cell Biochem 84: 532-544, 2002.
    • (2002) J Cell Biochem , vol.84 , pp. 532-544
    • Lin, S.Y.1    Liu, J.D.2    Chang, H.C.3
  • 30
    • 0032479465 scopus 로고    scopus 로고
    • Decrease in mitochondrial energy coupling by thyroid hormones: A physiological effect rather than a pathological hyperthyroidism consequence
    • Bobyleva V, Pazienza TL, Maseroli R, et al: Decrease in mitochondrial energy coupling by thyroid hormones: a physiological effect rather than a pathological hyperthyroidism consequence. FEBS Lett 430: 409-413, 1998.
    • (1998) FEBS Lett , vol.430 , pp. 409-413
    • Bobyleva, V.1    Pazienza, T.L.2    Maseroli, R.3
  • 31
    • 77951181570 scopus 로고    scopus 로고
    • Cinobufacini, an aqueous extract from Bufo bufo gargarizans Cantor, induces apoptosis through a mitochondria-mediated pathway in human hepatocellular carcinoma cells
    • Qi F, Li A, Zhao L, et al: Cinobufacini, an aqueous extract from Bufo bufo gargarizans Cantor, induces apoptosis through a mitochondria-mediated pathway in human hepatocellular carcinoma cells. J Ethnopharmacol 128: 654-661, 2010.
    • (2010) J Ethnopharmacol , vol.128 , pp. 654-661
    • Qi, F.1    Li, A.2    Zhao, L.3
  • 32
    • 17044414424 scopus 로고    scopus 로고
    • New insights into cyclins, CDKs, and cell cycle control
    • Sánchez I and Dynlacht BD: New insights into cyclins, CDKs, and cell cycle control. Semin Cell Dev Biol 16: 311-321, 2005.
    • (2005) Semin Cell Dev Biol , vol.16 , pp. 311-321
    • Sánchez, I.1    Dynlacht, B.D.2
  • 33
    • 0027582265 scopus 로고
    • Apoptosis and signal transduction: Clues to a molecular mechanism
    • Lee S, Christakos S and Small MB: Apoptosis and signal transduction: clues to a molecular mechanism. Curr Opin Cell Biol 5: 286-291, 1993.
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 286-291
    • Lee, S.1    Christakos, S.2    Small, M.B.3
  • 34
    • 0034323582 scopus 로고    scopus 로고
    • Regulation of tumor cell apoptotic sensitivity during the cell cycle (Review)
    • Smith DM, Gao G, Zhang X, et al: Regulation of tumor cell apoptotic sensitivity during the cell cycle (Review). Int J Mol Med 6: 503-507, 2000.
    • (2000) Int J Mol Med , vol.6 , pp. 503-507
    • Smith, D.M.1    Gao, G.2    Zhang, X.3
  • 35
    • 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, et al: 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.
    • (2005) Blood , vol.105 , pp. 1724-1733
    • Park, M.T.1    Kim, M.J.2    Kang, Y.H.3
  • 36
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross A, McDonnell JM and Korsmeyer SJ: BCL-2 family members and the mitochondria in apoptosis. Genes Dev 13: 1899-1911, 1999.
    • (1999) Genes Dev , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 37
    • 13144291648 scopus 로고    scopus 로고
    • Cytotoxicity of psammaplin A from a two-sponge association may correlate with the inhibition of DNA replication
    • Jiang YH, Ahn EY, Ryu SH, et al: Cytotoxicity of psammaplin A from a two-sponge association may correlate with the inhibition of DNA replication. BMC Cancer 4: 70, 2004.
    • (2004) BMC Cancer , vol.4 , pp. 70
    • Jiang, Y.H.1    Ahn, E.Y.2    Ryu, S.H.3
  • 38
    • 79954672344 scopus 로고    scopus 로고
    • Bufalin and cinobufagin induce apoptosis of human hepatocellular carcinoma cells via Fas- and mitochondria-mediated pathways
    • Qi F, Inagaki Y, Gao B, et al: Bufalin and cinobufagin induce apoptosis of human hepatocellular carcinoma cells via Fas- and mitochondria-mediated pathways. Cancer Sci 102: 951-958, 2011.
    • (2011) Cancer Sci , vol.102 , pp. 951-958
    • Qi, F.1    Inagaki, Y.2    Gao, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.