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Volumn 64, Issue 12, 2002, Pages 1713-1724

Emodin induces apoptosis in human promyeloleukemic HL-60 cells accompanied by activation of caspase 3 cascade but independent of reactive oxygen species production

Author keywords

Apoptosis; Caspase 3; Catalase; Emodin; ROS; SOD

Indexed keywords

ACETYLCYSTEINE; ALLOPURINOL; ANTHRAQUINONE DERIVATIVE; CASPASE 3 INHIBITOR; CATALASE; CHRYSOPHANIC ACID; DIPHENYLIODONIUM SALT; EMODIN; HYDROGEN PEROXIDE; INTERLEUKIN 1BETA CONVERTING ENZYME; INTERLEUKIN 1BETA CONVERTING ENZYME INHIBITOR; N(G) NITROARGININE METHYL ESTER; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PHYSCION; PROTEIN; PROTEIN BAD; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN D4 GDI; PROTEIN MCL 1; PYRROLIDINE DITHIOCARBAMATE; REACTIVE OXYGEN METABOLITE; SCAVENGER; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG;

EID: 0037114436     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(02)01386-2     Document Type: Article
Times cited : (213)

References (46)
  • 1
    • 0033162401 scopus 로고    scopus 로고
    • Involvement of p53 and HSP70 proteins in attenuation of UVC-induced apoptosis by thermal stress in hepatocellular carcinoma cells
    • Chen Y.C., Lin-Shiau S.Y., Lin J.K. Involvement of p53 and HSP70 proteins in attenuation of UVC-induced apoptosis by thermal stress in hepatocellular carcinoma cells. Photochem. Photobiol. 70:1996;78-86.
    • (1996) Photochem. Photobiol. , vol.70 , pp. 78-86
    • Chen, Y.C.1    Lin-Shiau, S.Y.2    Lin, J.K.3
  • 2
    • 0032007312 scopus 로고    scopus 로고
    • Chemopreventive isothiocyanates induce apoptosis and caspase-3-like protease activity
    • Yu R., Mandlekar S., Harvey K.J., Ucker D.S., Kong T.A.N. Chemopreventive isothiocyanates induce apoptosis and caspase-3-like protease activity. Cancer Res. 58:2000;402-408.
    • (2000) Cancer Res. , vol.58 , pp. 402-408
    • Yu, R.1    Mandlekar, S.2    Harvey, K.J.3    Ucker, D.S.4    Kong, T.A.N.5
  • 3
    • 0036179645 scopus 로고    scopus 로고
    • Death receptors couple to both cell proliferation and apoptosis
    • Budd R.C. Death receptors couple to both cell proliferation and apoptosis. J. Clin. Invest. 109:2002;437-441.
    • (2002) J. Clin. Invest. , vol.109 , pp. 437-441
    • Budd, R.C.1
  • 4
    • 0028927607 scopus 로고
    • The Fas death factor
    • Nagata S., Golstein P. The Fas death factor. Science. 267:1995;1449-1456.
    • (1995) Science , vol.267 , pp. 1449-1456
    • Nagata, S.1    Golstein, P.2
  • 5
    • 0025047803 scopus 로고
    • Activation of programmed cell death (apoptosis) by cisplatin, other anticancer drugs, toxins and hyperthermia
    • Barry M.A., Behnke C.A., Eastman A. Activation of programmed cell death (apoptosis) by cisplatin, other anticancer drugs, toxins and hyperthermia. Biochem. Pharmacol. 40:1990;2353-2361.
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 2353-2361
    • Barry, M.A.1    Behnke, C.A.2    Eastman, A.3
  • 6
    • 0035501249 scopus 로고    scopus 로고
    • Differential regulation of phosphatidylserine externalization and DNA fragmentation by caspases in anticancer drug-induced apoptosis of rat mammary adenocarcinoma MTLn3 cells
    • Huigsloot M., Tijdens I.B., Mulder G.J., Van de Water B. Differential regulation of phosphatidylserine externalization and DNA fragmentation by caspases in anticancer drug-induced apoptosis of rat mammary adenocarcinoma MTLn3 cells. Biochem. Pharmacol. 62:2001;1087-1097.
    • (2001) Biochem. Pharmacol. , vol.62 , pp. 1087-1097
    • Huigsloot, M.1    Tijdens, I.B.2    Mulder, G.J.3    Van de Water, B.4
  • 7
    • 0033573020 scopus 로고    scopus 로고
    • Caspase 8 and apaf-1 form an active holoenzyme
    • Rodriguez J., Lazebnik Y. Caspase 8 and apaf-1 form an active holoenzyme. Gene Dev. 13:1999;3179-3184.
    • (1999) Gene Dev. , vol.13 , pp. 3179-3184
    • Rodriguez, J.1    Lazebnik, Y.2
  • 8
    • 0033231614 scopus 로고    scopus 로고
    • Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-1/CED-4-related caspase activator
    • Kanuka H., Sawamoto K., Inohara W., Matsuno K., Okano H., Miura M. Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-1/CED-4-related caspase activator. Mol. Cell. 4:1999;757-769.
    • (1999) Mol. Cell , vol.4 , pp. 757-769
    • Kanuka, H.1    Sawamoto, K.2    Inohara, W.3    Matsuno, K.4    Okano, H.5    Miura, M.6
  • 10
    • 0034194258 scopus 로고    scopus 로고
    • Serine protease inhibitors suppress cytochrome c-mediated caspase-9 activation and apoptosis during hypoxia-reoxygenation
    • Dong Z., Saikumar P., Patel Y., Weinberg J.M., Venkatachalam M.A. Serine protease inhibitors suppress cytochrome c-mediated caspase-9 activation and apoptosis during hypoxia-reoxygenation. Biochem. J. 347:1999;669-677.
    • (1999) Biochem. J. , vol.347 , pp. 669-677
    • Dong, Z.1    Saikumar, P.2    Patel, Y.3    Weinberg, J.M.4    Venkatachalam, M.A.5
  • 12
    • 0035426195 scopus 로고    scopus 로고
    • Ca(2+)-calmodulin antagonist chlorpromazine and poly(ADP-ribose) polymerase modulators 4-aminobenzamide and nicotinamide influence hepatic expression of BCL-XL and P53 and protect against acetaminophen-induced programmed and unprogrammed cell death in mice
    • Ray S.D., Balasubramanian G., Bagchi D., Reddy C.S. Ca(2+)-calmodulin antagonist chlorpromazine and poly(ADP-ribose) polymerase modulators 4-aminobenzamide and nicotinamide influence hepatic expression of BCL-XL and P53 and protect against acetaminophen-induced programmed and unprogrammed cell death in mice. Free Radic. Biol. Med. 31:2001;277-291.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 277-291
    • Ray, S.D.1    Balasubramanian, G.2    Bagchi, D.3    Reddy, C.S.4
  • 13
    • 0032991861 scopus 로고    scopus 로고
    • Cleavage and nuclear translocation of the caspase 3 substrate Rho GDP-dissociation inhibitor, D4-GDI, during apoptosis
    • Krieser R.J., Eastman A. Cleavage and nuclear translocation of the caspase 3 substrate Rho GDP-dissociation inhibitor, D4-GDI, during apoptosis. Cell Death Differ. 6:1999;412-419.
    • (1999) Cell Death Differ. , vol.6 , pp. 412-419
    • Krieser, R.J.1    Eastman, A.2
  • 14
    • 0029951250 scopus 로고    scopus 로고
    • Defective Rho-GTPase regulation by IL-1 beta-converting enzyme-mediated cleavage of D4-GDP dissociation inhibitor
    • Danley D.E., Chuang T.H., Bokoch G.M. Defective Rho-GTPase regulation by IL-1 beta-converting enzyme-mediated cleavage of D4-GDP dissociation inhibitor. J. Immunol. 157:1996;500-503.
    • (1996) J. Immunol. , vol.157 , pp. 500-503
    • Danley, D.E.1    Chuang, T.H.2    Bokoch, G.M.3
  • 16
    • 0035501242 scopus 로고    scopus 로고
    • Cisplatin-induced apoptosis by translocation of endogenous Bax in mouse collecting duct cells
    • Lee R.H., Song J.M., Park M.Y., Kang S.K., Kim Y.K., Jung J.S. Cisplatin-induced apoptosis by translocation of endogenous Bax in mouse collecting duct cells. Biochem. Pharmacol. 62:2001;1013-1023.
    • (2001) Biochem. Pharmacol. , vol.62 , pp. 1013-1023
    • Lee, R.H.1    Song, J.M.2    Park, M.Y.3    Kang, S.K.4    Kim, Y.K.5    Jung, J.S.6
  • 17
    • 0036016874 scopus 로고    scopus 로고
    • Wogonin and fisetin induction of apoptosis through activation of caspase 3 cascade and alternative expression of p21 protein in hepatocellular carcinoma cells SK-HEP-1
    • Chen Y.C., Shen S.C., Lee W.R., Lin H.Y., Ko C.H., Chih C.M., Yang L.L. Wogonin and fisetin induction of apoptosis through activation of caspase 3 cascade and alternative expression of p21 protein in hepatocellular carcinoma cells SK-HEP-1. Arch. Toxicol. 76:2002;351-359.
    • (2002) Arch. Toxicol. , vol.76 , pp. 351-359
    • Chen, Y.C.1    Shen, S.C.2    Lee, W.R.3    Lin, H.Y.4    Ko, C.H.5    Chih, C.M.6    Yang, L.L.7
  • 18
    • 0034096640 scopus 로고    scopus 로고
    • Stimulatory effect of curcumin on osteoclast apoptosis
    • Ozaki K., Kawata Y., Amano S., Hanazawa S. Stimulatory effect of curcumin on osteoclast apoptosis. Biochem. Pharmacol. 59:2000;1577-1581.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 1577-1581
    • Ozaki, K.1    Kawata, Y.2    Amano, S.3    Hanazawa, S.4
  • 19
    • 0035793238 scopus 로고    scopus 로고
    • Immune responses in human mesangial cells regulated by emodin from Polygonum hypoleucum Ohwi
    • Kuo Y.C., Tsai W.J., Meng H.C., Chen W.P., Yang L.Y., Lin C.Y. Immune responses in human mesangial cells regulated by emodin from Polygonum hypoleucum Ohwi. Life Sci. 68:2001;1271-1286.
    • (2001) Life Sci. , vol.68 , pp. 1271-1286
    • Kuo, Y.C.1    Tsai, W.J.2    Meng, H.C.3    Chen, W.P.4    Yang, L.Y.5    Lin, C.Y.6
  • 20
    • 0033979253 scopus 로고    scopus 로고
    • Myocardial protection by protykin, a novel extract of trans-resveratrol and emodin
    • Sato M., Maulik G., Bagchi D., Das D.K. Myocardial protection by protykin, a novel extract of trans-resveratrol and emodin. Free Radic. Res. 32:2000;135-144.
    • (2000) Free Radic. Res. , vol.32 , pp. 135-144
    • Sato, M.1    Maulik, G.2    Bagchi, D.3    Das, D.K.4
  • 21
    • 0034846756 scopus 로고    scopus 로고
    • Effects and mechanisms of emodin on cell death in human lung squamous cell carcinoma
    • Lee H.Z. Effects and mechanisms of emodin on cell death in human lung squamous cell carcinoma. Br. J. Pharmacol. 134:2001;11-20.
    • (2001) Br. J. Pharmacol. , vol.134 , pp. 11-20
    • Lee, H.Z.1
  • 22
    • 0035097571 scopus 로고    scopus 로고
    • Regulation of cell proliferation, inflammatory cytokine production and calcium mobilization in primary human T lymphocytes by emodin from Polygonum hypoleucum Ohwi
    • Kuo Y.C., Meng H.C., Tasi W.J. Regulation of cell proliferation, inflammatory cytokine production and calcium mobilization in primary human T lymphocytes by emodin from Polygonum hypoleucum Ohwi. Inflamm. Res. 50:2001;73-82.
    • (2001) Inflamm. Res. , vol.50 , pp. 73-82
    • Kuo, Y.C.1    Meng, H.C.2    Tasi, W.J.3
  • 23
    • 0026576710 scopus 로고
    • Mutagenicity of substituted anthraquinones in the Ames/Salmonella microsome system
    • Krivobok S., Seigle-Murandi F., Steiman R., Marzin D.R., Betina V. Mutagenicity of substituted anthraquinones in the Ames/Salmonella microsome system. Mutat. Res. 279:1992;1-8.
    • (1992) Mutat. Res. , vol.279 , pp. 1-8
    • Krivobok, S.1    Seigle-Murandi, F.2    Steiman, R.3    Marzin, D.R.4    Betina, V.5
  • 24
    • 0032507619 scopus 로고    scopus 로고
    • Factors affecting the genotoxic potency ranking of natural anthraquinones in mammalian cell culture systems
    • Mueller S.O., Lutz W.K., Stopper H. Factors affecting the genotoxic potency ranking of natural anthraquinones in mammalian cell culture systems. Mutat. Res. 414:1998;125-129.
    • (1998) Mutat. Res. , vol.414 , pp. 125-129
    • Mueller, S.O.1    Lutz, W.K.2    Stopper, H.3
  • 25
    • 0033049036 scopus 로고    scopus 로고
    • Tyrosine kinase inhibitor emodin suppresses growth of HER-2/neu-overexpressing breast cancer cells in athymic mice and sensitizes these cells to the inhibitory effect of paclitaxel
    • Zhang L., Lau Y.K., Xia W., Hortobagyi G.N., Hung M.C. Tyrosine kinase inhibitor emodin suppresses growth of HER-2/neu-overexpressing breast cancer cells in athymic mice and sensitizes these cells to the inhibitory effect of paclitaxel. Clin. Cancer Res. 5:1999;343-353.
    • (1999) Clin. Cancer Res. , vol.5 , pp. 343-353
    • Zhang, L.1    Lau, Y.K.2    Xia, W.3    Hortobagyi, G.N.4    Hung, M.C.5
  • 26
    • 0030067015 scopus 로고    scopus 로고
    • Sensitization of HER-2/neu-overexpressing non-small cell lung cancer cells to chemotherapeutic drugs by tyrosine kinase inhibitor emodin
    • Zhang L., Hung M.C. Sensitization of HER-2/neu-overexpressing non-small cell lung cancer cells to chemotherapeutic drugs by tyrosine kinase inhibitor emodin. Oncogene. 12:1996;571-576.
    • (1996) Oncogene , vol.12 , pp. 571-576
    • Zhang, L.1    Hung, M.C.2
  • 27
    • 0034213030 scopus 로고    scopus 로고
    • Oroxylin A inhibition of lipopolysaccharide-induced iNOS and COX-2 gene expression via suppression of nuclear factor-kappaB activation
    • Chen Y.C., Yang L.L., Lee T.J. Oroxylin A inhibition of lipopolysaccharide-induced iNOS and COX-2 gene expression via suppression of nuclear factor-kappaB activation. Biochem. Pharmacol. 59:2000;1445-1457.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 1445-1457
    • Chen, Y.C.1    Yang, L.L.2    Lee, T.J.3
  • 28
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods. 65:1983;55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 29
    • 0031657760 scopus 로고    scopus 로고
    • Involvement of reactive oxygen species and caspase 3 activation in arsenite-induced apoptosis
    • Chen Y.C., Lin-Shiau S.Y., Lin J.K. Involvement of reactive oxygen species and caspase 3 activation in arsenite-induced apoptosis. J. Cell Physiol. 177:1998;324-333.
    • (1998) J. Cell Physiol. , vol.177 , pp. 324-333
    • Chen, Y.C.1    Lin-Shiau, S.Y.2    Lin, J.K.3
  • 31
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp C., Fridovich E. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44:1971;276-287.
    • (1971) Anal. Biochem. , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, E.2
  • 32
    • 0023050076 scopus 로고
    • A double staining method for differentiating between two classes of Mycobacterial catalase in polyacrylamide electrophoresis gels
    • Wayne L.G., Diaz G.A. A double staining method for differentiating between two classes of Mycobacterial catalase in polyacrylamide electrophoresis gels. Anal. Biochem. 157:1986;89-92.
    • (1986) Anal. Biochem. , vol.157 , pp. 89-92
    • Wayne, L.G.1    Diaz, G.A.2
  • 33
    • 0035860419 scopus 로고    scopus 로고
    • Apaf-1 overexpression partially overcomes apoptotic resistance in a cisplatin-selected HeLa cell line
    • Kamarajan P., Sun N.K., Sun C.L., Chao C.C. Apaf-1 overexpression partially overcomes apoptotic resistance in a cisplatin-selected HeLa cell line. FEBS Lett. 505:2001;206-212.
    • (2001) FEBS Lett. , vol.505 , pp. 206-212
    • Kamarajan, P.1    Sun, N.K.2    Sun, C.L.3    Chao, C.C.4
  • 35
    • 0034923780 scopus 로고    scopus 로고
    • Molecular mechanisms of the decision between life and death: Regulation of apoptosis by apoptosis signal-regulating kinase 1
    • Matsuzawa A., Ichijo H. Molecular mechanisms of the decision between life and death: regulation of apoptosis by apoptosis signal-regulating kinase 1. J. Biochem. 130:2001;1-8.
    • (2001) J. Biochem. , vol.130 , pp. 1-8
    • Matsuzawa, A.1    Ichijo, H.2
  • 37
    • 0032761224 scopus 로고    scopus 로고
    • Apaf 1 and apoptotic machinery
    • Cecconi F. Apaf 1 and apoptotic machinery. Cell Death Differ. 6:1999;1087-1098.
    • (1999) Cell Death Differ. , vol.6 , pp. 1087-1098
    • Cecconi, F.1
  • 38
    • 0035882351 scopus 로고    scopus 로고
    • Direct effect of taxol on free radical formation and mitochondrial permeability transition
    • Varbiro G., Veres B., Gallyas F. Jr., Sumegi B. Direct effect of taxol on free radical formation and mitochondrial permeability transition. Free Radic. Biol. Med. 31:2001;548-558.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 548-558
    • Varbiro, G.1    Veres, B.2    Gallyas F., Jr.3    Sumegi, B.4
  • 39
    • 0034927296 scopus 로고    scopus 로고
    • Vitamin E analogues as inducers of apoptosis: Implications for their potential antineoplastic role
    • Neuzil J., Weber T., Terman A., Weber C., Brunk T. Vitamin E analogues as inducers of apoptosis: implications for their potential antineoplastic role. Redox Report. 6:2001;143-151.
    • (2001) Redox Report , vol.6 , pp. 143-151
    • Neuzil, J.1    Weber, T.2    Terman, A.3    Weber, C.4    Brunk, T.5
  • 40
    • 0037082122 scopus 로고    scopus 로고
    • Induction of apoptosis by chemotherapeutic drugs without generation of reactive oxygen species
    • Senturker S., Tschirret-Guth R., Morrow J., Levine R., Shacter E. Induction of apoptosis by chemotherapeutic drugs without generation of reactive oxygen species. Arch. Biochem. Biophys. 397:2002;262-272.
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 262-272
    • Senturker, S.1    Tschirret-Guth, R.2    Morrow, J.3    Levine, R.4    Shacter, E.5
  • 41
    • 0037141773 scopus 로고    scopus 로고
    • In vitro and in vivo inhibitory activities of rutin, wogonin, and quercetin on lipopolysaccharide-induced nitric oxide and prostaglandin E2 production
    • Shen S.C., Lee W.R., Lin H.Y., Huang H.C., Ko C.H., Yang L.L., Chen Y.C. In vitro and in vivo inhibitory activities of rutin, wogonin, and quercetin on lipopolysaccharide-induced nitric oxide and prostaglandin E2 production. Eur. J. Pharmacol. 446:2002;187-194.
    • (2002) Eur. J. Pharmacol. , vol.446 , pp. 187-194
    • Shen, S.C.1    Lee, W.R.2    Lin, H.Y.3    Huang, H.C.4    Ko, C.H.5    Yang, L.L.6    Chen, Y.C.7
  • 42
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck R.M., Bossy-Wetzel E., Green D.R., Newmeyer D.D. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science. 275:1997;1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 44
    • 0035901954 scopus 로고    scopus 로고
    • Bcl-2 oncoprotein protects the human prostatic carcinoma cell line PC3 from TRAIL-mediated apoptosis
    • Rokhlin O.W., Guseva N., Tagiyev A., Knudson C.M., Cohen M.B. Bcl-2 oncoprotein protects the human prostatic carcinoma cell line PC3 from TRAIL-mediated apoptosis. Oncogene. 20:2001;2836-2843.
    • (2001) Oncogene , vol.20 , pp. 2836-2843
    • Rokhlin, O.W.1    Guseva, N.2    Tagiyev, A.3    Knudson, C.M.4    Cohen, M.B.5
  • 46
    • 0033168167 scopus 로고    scopus 로고
    • A novel function of emodin: Enhancement of the nucleotide excision repair of UV- and cisplatin-induced DNA damage in human cells
    • Chang L.C., Sheu H.M., Huang Y.S., Tsai T.R., Kuo K.W. A novel function of emodin: enhancement of the nucleotide excision repair of UV- and cisplatin-induced DNA damage in human cells. Biochem. Pharmacol. 58:1999;49-57.
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 49-57
    • Chang, L.C.1    Sheu, H.M.2    Huang, Y.S.3    Tsai, T.R.4    Kuo, K.W.5


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