메뉴 건너뛰기




Volumn 661, Issue 1-2, 2009, Pages 41-46

Inhibition of benzopyrene-diol-epoxide (BPDE)-induced bax and caspase-9 by cadmium: Role of mitogen activated protein kinase

Author keywords

Apoptosis; Bax; Bcl2; Benzo a pyrene diol epoxide; Cadmium; ERK

Indexed keywords

BENZO[A]PYRENE 7,8 DIHYDRODIOL 9,10 OXIDE; CADMIUM; CASPASE 9; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN BAX; PROTEIN BCL 2; STRESS ACTIVATED PROTEIN KINASE;

EID: 58549098717     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2008.10.020     Document Type: Article
Times cited : (16)

References (59)
  • 1
    • 0002256633 scopus 로고
    • Advances in tobacco carcinogenesis
    • Cooper C.S., and Grover P.L. (Eds), Springer-Verlag, Heidelberg
    • Hoffmann D., and Hecht S.S. Advances in tobacco carcinogenesis. In: Cooper C.S., and Grover P.L. (Eds). Handbook of Experimental Pharmacology, vol. 94 no. 1 (1990), Springer-Verlag, Heidelberg 63-102
    • (1990) Handbook of Experimental Pharmacology, vol. 94 no. 1 , pp. 63-102
    • Hoffmann, D.1    Hecht, S.S.2
  • 2
    • 0030754664 scopus 로고    scopus 로고
    • Approaches to chemoprevention of lung cancer based on carcinogens in tobacco smoke
    • Hecht S.S. Approaches to chemoprevention of lung cancer based on carcinogens in tobacco smoke. Environ. Health Perspect. 105 (1997) 955-963
    • (1997) Environ. Health Perspect. , vol.105 , pp. 955-963
    • Hecht, S.S.1
  • 3
    • 0025144121 scopus 로고
    • Health effects of environmental exposure to cadmium: objectives, design and organization of the Cadmibel Study: a cross-sectional morbidity study carried out in Belgium from 1985 to 1989
    • Lawyers R., Amery A., Bernard A., Bruaux P., Buchet J.P., Claeys F., De Plaen P., Ducoffre G., Fagard R., and Lijnen P. Health effects of environmental exposure to cadmium: objectives, design and organization of the Cadmibel Study: a cross-sectional morbidity study carried out in Belgium from 1985 to 1989. Environ. Health Perspect. 87 (1990) 283-289
    • (1990) Environ. Health Perspect. , vol.87 , pp. 283-289
    • Lawyers, R.1    Amery, A.2    Bernard, A.3    Bruaux, P.4    Buchet, J.P.5    Claeys, F.6    De Plaen, P.7    Ducoffre, G.8    Fagard, R.9    Lijnen, P.10
  • 5
    • 0017577435 scopus 로고
    • Liver homogenate-mediated mutagenesis in chinese hamster V79 cells by polycyclic aromatic hydrocarbons and aflatoxins
    • Krahn D.F., and Heidelberger C. Liver homogenate-mediated mutagenesis in chinese hamster V79 cells by polycyclic aromatic hydrocarbons and aflatoxins. Mutat. Res. 46 (1977) 27-44
    • (1977) Mutat. Res. , vol.46 , pp. 27-44
    • Krahn, D.F.1    Heidelberger, C.2
  • 6
    • 0020609180 scopus 로고
    • Carcinogenic activity of benzo[a]pyrene and some of its synthetic derivatives by direct injection into the mouse fetus
    • Rossi L., Barbieri O., Sanguineti M., Staccione A., Santi L.F., and Santi L. Carcinogenic activity of benzo[a]pyrene and some of its synthetic derivatives by direct injection into the mouse fetus. Carcinogenesis 4 (1983) 153-156
    • (1983) Carcinogenesis , vol.4 , pp. 153-156
    • Rossi, L.1    Barbieri, O.2    Sanguineti, M.3    Staccione, A.4    Santi, L.F.5    Santi, L.6
  • 7
    • 0025893062 scopus 로고
    • Benzo-a-pyrene: environmental partitioning and human exposure
    • Hattemer-Frey H.A., and Travis C.C. Benzo-a-pyrene: environmental partitioning and human exposure. Toxicol. Ind. Health 7 (1991) 141-157
    • (1991) Toxicol. Ind. Health , vol.7 , pp. 141-157
    • Hattemer-Frey, H.A.1    Travis, C.C.2
  • 8
    • 0019409895 scopus 로고
    • Metal salts as promoters of in vitro morphological transformation of hamster embryo cells initiated by benzo[a]pyrene
    • Rivedal E., and Sanner T. Metal salts as promoters of in vitro morphological transformation of hamster embryo cells initiated by benzo[a]pyrene. Cancer Res. 41 (1981) 2950-2953
    • (1981) Cancer Res. , vol.41 , pp. 2950-2953
    • Rivedal, E.1    Sanner, T.2
  • 9
    • 0038143266 scopus 로고    scopus 로고
    • The role of the Ah receptor and p38 in benzo[a]pyrene-7,8-dihydrodiol and benzo[a]pyrene-7,8 dihydrodiol-9,10-epoxide-induced apoptosis
    • Chen S., Nguyen N., Tamura K., Karin M., and Tukey R.H. The role of the Ah receptor and p38 in benzo[a]pyrene-7,8-dihydrodiol and benzo[a]pyrene-7,8 dihydrodiol-9,10-epoxide-induced apoptosis. J. Biol. Chem. 278 (2003) 19526-19533
    • (2003) J. Biol. Chem. , vol.278 , pp. 19526-19533
    • Chen, S.1    Nguyen, N.2    Tamura, K.3    Karin, M.4    Tukey, R.H.5
  • 10
    • 0032524017 scopus 로고    scopus 로고
    • Induction of apoptosis and activation of interleukin 1beta-converting enzyme/Ced-3 protease (caspase-3) and c-Jun NH2-terminal kinase 1 by benzo(a)pyrene
    • Lei W., Yu R., Mandlekar S., and Kong A.N. Induction of apoptosis and activation of interleukin 1beta-converting enzyme/Ced-3 protease (caspase-3) and c-Jun NH2-terminal kinase 1 by benzo(a)pyrene. Cancer Res. 58 (1998) 2102-2106
    • (1998) Cancer Res. , vol.58 , pp. 2102-2106
    • Lei, W.1    Yu, R.2    Mandlekar, S.3    Kong, A.N.4
  • 11
    • 0034812916 scopus 로고    scopus 로고
    • Involvement of alpha-PAK-interacting exchange factor in the PAK1-c-Jun NH(2)-terminal kinase 1 activation and apoptosis induced by benzo[a]pyrene
    • Yoshii S., Tanaka M., Otsuki Y., Fujiyama T., Kataoka H., Arai H., Hanai H., and Sugimura H. Involvement of alpha-PAK-interacting exchange factor in the PAK1-c-Jun NH(2)-terminal kinase 1 activation and apoptosis induced by benzo[a]pyrene. Mol. Cell. Biol. 21 (2001) 6796
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6796
    • Yoshii, S.1    Tanaka, M.2    Otsuki, Y.3    Fujiyama, T.4    Kataoka, H.5    Arai, H.6    Hanai, H.7    Sugimura, H.8
  • 12
    • 77957186430 scopus 로고
    • DMBA induces programmed cell death (apoptosis) in the A20.1 murine B cell lymphoma
    • Burchiel S.W., Davis D.A., Ray S.D., and Barton S.L. DMBA induces programmed cell death (apoptosis) in the A20.1 murine B cell lymphoma. Fundam. Appl. Toxicol. 21 (1993) 120-124
    • (1993) Fundam. Appl. Toxicol. , vol.21 , pp. 120-124
    • Burchiel, S.W.1    Davis, D.A.2    Ray, S.D.3    Barton, S.L.4
  • 13
    • 13444261149 scopus 로고    scopus 로고
    • Role of cell signaling in B[a]P-induced apoptosis: characterization of unspecific effects of cell signaling inhibitors and apoptotic effects of B[a]P metabolites
    • Solhaug A., Øvrebø S., Mollerup S., Låg M., Schwarze P.E., Nesnow S., and Holme J.A. Role of cell signaling in B[a]P-induced apoptosis: characterization of unspecific effects of cell signaling inhibitors and apoptotic effects of B[a]P metabolites. Chem. Biol. Interact. 151 (2005) 101-119
    • (2005) Chem. Biol. Interact. , vol.151 , pp. 101-119
    • Solhaug, A.1    Øvrebø, S.2    Mollerup, S.3    Låg, M.4    Schwarze, P.E.5    Nesnow, S.6    Holme, J.A.7
  • 14
    • 0032138169 scopus 로고    scopus 로고
    • Apoptosis in Daudi human B cells in response to benzo[a]pyrene and benzo[a]pyrene-7,8-dihydrodiol
    • Salas V.M., and Burchiel S.W. Apoptosis in Daudi human B cells in response to benzo[a]pyrene and benzo[a]pyrene-7,8-dihydrodiol. Toxicol. Appl. Pharmacol. 151 (1998) 367-376
    • (1998) Toxicol. Appl. Pharmacol. , vol.151 , pp. 367-376
    • Salas, V.M.1    Burchiel, S.W.2
  • 15
    • 0036130889 scopus 로고    scopus 로고
    • Apoptosis and cancer: when BAX is TRAILing away
    • Roth W., and Reed J.C. Apoptosis and cancer: when BAX is TRAILing away. Nat. Med. 8 (2002) 216-218
    • (2002) Nat. Med. , vol.8 , pp. 216-218
    • Roth, W.1    Reed, J.C.2
  • 16
    • 0027729378 scopus 로고
    • Rapid activation of apoptosis in human promyelocytic leukemic cells by (+/-)-anti-benzo[a]pyrene diol epoxide induced DNA damage
    • Venkatachalam S., Denissenko M.F., Alvi N., and Wani A.A. Rapid activation of apoptosis in human promyelocytic leukemic cells by (+/-)-anti-benzo[a]pyrene diol epoxide induced DNA damage. Biochem. Biophys. Res. Commun. 1972 (1993) 722-729
    • (1993) Biochem. Biophys. Res. Commun. , vol.1972 , pp. 722-729
    • Venkatachalam, S.1    Denissenko, M.F.2    Alvi, N.3    Wani, A.A.4
  • 17
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: from caspases to alternative mechanisms
    • Leist M., and Jaattela M. Four deaths and a funeral: from caspases to alternative mechanisms. Nat. Rev. Mol. Cell. Biol. 2 (2001) 589
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 589
    • Leist, M.1    Jaattela, M.2
  • 18
    • 0035368563 scopus 로고    scopus 로고
    • Apoptotic death sensor: an organelle's alter ego?
    • Bratton S.B., and Cohen G.M. Apoptotic death sensor: an organelle's alter ego?. Trends Pharmacol. Sci. 22 (2001) 306
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 306
    • Bratton, S.B.1    Cohen, G.M.2
  • 19
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., and Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91 (1997) 479
    • (1997) Cell , vol.91 , pp. 479
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 20
    • 0035369143 scopus 로고    scopus 로고
    • The mitochondrial apoptosome: a killer unleashed by the cytochrome seas
    • Adrain C., and Martin S.J. The mitochondrial apoptosome: a killer unleashed by the cytochrome seas. Trends Biochem. Sci. 26 (2001) 390
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 390
    • Adrain, C.1    Martin, S.J.2
  • 23
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells
    • Antonsson B., Montessuit S., Sanchez B., and Martinou J.C. Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. J. Biol. Chem. 276 (2001) 11615
    • (2001) J. Biol. Chem. , vol.276 , pp. 11615
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 24
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes R., Desagher S., Antonsson B., and Martinou J.C. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol. Cell. Biol. 20 (2000) 929
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 929
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 25
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • Zong W., Lindsten X.T., Ross A.J., MacGregor G.R., and Thompson C.B. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev. 15 (2001) 1481
    • (2001) Genes Dev. , vol.15 , pp. 1481
    • Zong, W.1    Lindsten, X.T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5
  • 26
    • 0035512186 scopus 로고    scopus 로고
    • Transcription activator protein 1 (AP-1) mediates NO-induced apoptosis of adult cardiomyocytes
    • Taimor G., Rakow A., and Piper H.M. Transcription activator protein 1 (AP-1) mediates NO-induced apoptosis of adult cardiomyocytes. FASEB J. 15 (2001) 2518-2520
    • (2001) FASEB J. , vol.15 , pp. 2518-2520
    • Taimor, G.1    Rakow, A.2    Piper, H.M.3
  • 27
    • 0142184964 scopus 로고    scopus 로고
    • Norcantharidin-induced apoptosis is via the extracellular signal-regulated kinase and c-Jun-NH2-terminal kinase signaling pathways in human hepatoma HepG2 cells
    • Chen Y.N., Cheng C.C., Chen J.C., Tsauer W., and Hsu S.L. Norcantharidin-induced apoptosis is via the extracellular signal-regulated kinase and c-Jun-NH2-terminal kinase signaling pathways in human hepatoma HepG2 cells. Br. J. Pharmacol. 140 (2003) 461-470
    • (2003) Br. J. Pharmacol. , vol.140 , pp. 461-470
    • Chen, Y.N.1    Cheng, C.C.2    Chen, J.C.3    Tsauer, W.4    Hsu, S.L.5
  • 28
    • 0031806003 scopus 로고    scopus 로고
    • AP1 regulation of proliferation and initiation of apoptosis in erythropoietin-dependent erythroid cells
    • Jacobs-Helber S.M., Wickrema A., Birrer M.J., and Sawyer S.T. AP1 regulation of proliferation and initiation of apoptosis in erythropoietin-dependent erythroid cells. Mol. Cell. Biol. 18 (1998) 3699-3707
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3699-3707
    • Jacobs-Helber, S.M.1    Wickrema, A.2    Birrer, M.J.3    Sawyer, S.T.4
  • 29
    • 33644865443 scopus 로고    scopus 로고
    • ERK and JNK signaling pathways are involved in the regulation of activator protein 1 and cell death elicited by three isothiocyanates in human prostate cancer PC-3 cells
    • Xu C., Shen G., Yuan X., Kim J.H., Gopalkrishnan A., Keum Y.S., Nair S., and Kong A.N. ERK and JNK signaling pathways are involved in the regulation of activator protein 1 and cell death elicited by three isothiocyanates in human prostate cancer PC-3 cells. Carcinogenesis 27 (2006) 437-445
    • (2006) Carcinogenesis , vol.27 , pp. 437-445
    • Xu, C.1    Shen, G.2    Yuan, X.3    Kim, J.H.4    Gopalkrishnan, A.5    Keum, Y.S.6    Nair, S.7    Kong, A.N.8
  • 30
    • 0030605403 scopus 로고    scopus 로고
    • The regulation of AP-1 activity by mitogen-activated protein kinases
    • Karin M. The regulation of AP-1 activity by mitogen-activated protein kinases. Philos. Trans. R. Soc. Lond. Biol. 351 (1996) 127-134
    • (1996) Philos. Trans. R. Soc. Lond. Biol. , vol.351 , pp. 127-134
    • Karin, M.1
  • 32
    • 13444287101 scopus 로고    scopus 로고
    • Role of cell signalling involved in induction of apoptosis by benzo[a]pyrene and cyclopenta[c,d]pyrene in Hepa1c1c7 cells
    • Solhaug A., Refsnes M., and Holme J.A. Role of cell signalling involved in induction of apoptosis by benzo[a]pyrene and cyclopenta[c,d]pyrene in Hepa1c1c7 cells. J. Cell. Biochem. 93 (2004) 1143-1154
    • (2004) J. Cell. Biochem. , vol.93 , pp. 1143-1154
    • Solhaug, A.1    Refsnes, M.2    Holme, J.A.3
  • 34
    • 0034812916 scopus 로고    scopus 로고
    • Involvement of alpha-PAK-interacting exchange factor in the PAK1-c-Jun NH(2)-terminal kinase 1 activation and apoptosis induced by benzo[a]pyrene
    • Yoshii S., Tanaka M., Otsuki Y., Fujiyama T., Kataoka H., Arai H., Hanai H., and Sugimura H. Involvement of alpha-PAK-interacting exchange factor in the PAK1-c-Jun NH(2)-terminal kinase 1 activation and apoptosis induced by benzo[a]pyrene. Mol. Cell. Biol. 21 (2001) 6796-6807
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6796-6807
    • Yoshii, S.1    Tanaka, M.2    Otsuki, Y.3    Fujiyama, T.4    Kataoka, H.5    Arai, H.6    Hanai, H.7    Sugimura, H.8
  • 36
    • 0033258120 scopus 로고    scopus 로고
    • Bcl-2 proteins: regulators of apoptosis or mitochondrial apoptosis?
    • Vander Heiden M.G., and Thompson C.B. Bcl-2 proteins: regulators of apoptosis or mitochondrial apoptosis?. Nat. Cell. Biol. 1 (1999) E209-E216
    • (1999) Nat. Cell. Biol. , vol.1
    • Vander Heiden, M.G.1    Thompson, C.B.2
  • 38
    • 0032900855 scopus 로고    scopus 로고
    • Characterization of cadmium-induced apoptosis in rat lung epithelial cells: evidence for the participation of oxidant stress
    • Hart B.A., Lee C.H., Shukla G.S., Shukla A., Osier M., Eneman J.D., and Chiu J.F. Characterization of cadmium-induced apoptosis in rat lung epithelial cells: evidence for the participation of oxidant stress. Toxicology 133 (1999) 43-58
    • (1999) Toxicology , vol.133 , pp. 43-58
    • Hart, B.A.1    Lee, C.H.2    Shukla, G.S.3    Shukla, A.4    Osier, M.5    Eneman, J.D.6    Chiu, J.F.7
  • 39
    • 0036151310 scopus 로고    scopus 로고
    • Attenuation of both apoptotic and necrotic actions of cadmium by Bcl-2
    • Ishido M., Ohtsubo R., Adachi T., and Kunimoto M. Attenuation of both apoptotic and necrotic actions of cadmium by Bcl-2. Environ. Health Perspect. 110 (2002) 37-42
    • (2002) Environ. Health Perspect. , vol.110 , pp. 37-42
    • Ishido, M.1    Ohtsubo, R.2    Adachi, T.3    Kunimoto, M.4
  • 41
  • 42
    • 0032479565 scopus 로고    scopus 로고
    • Cadmium induces apoptosis differentially on immune system cell lines
    • Tsangaris G.T., and Tzortzatou-Stathopoulou F. Cadmium induces apoptosis differentially on immune system cell lines. Toxicology 128 (1998) 143-150
    • (1998) Toxicology , vol.128 , pp. 143-150
    • Tsangaris, G.T.1    Tzortzatou-Stathopoulou, F.2
  • 43
    • 0036159106 scopus 로고    scopus 로고
    • Induction of apoptosis in mammalian cells by cadmium and zinc
    • Watjen W., Cox M., Biagioli M., and Beyersmann D. Induction of apoptosis in mammalian cells by cadmium and zinc. Bio Met. 15 (2002) 15-25
    • (2002) Bio Met. , vol.15 , pp. 15-25
    • Watjen, W.1    Cox, M.2    Biagioli, M.3    Beyersmann, D.4
  • 48
    • 0029960812 scopus 로고    scopus 로고
    • Eukaryotic DNA topoisomerase I: genome gatekeeper and its intruders, camptothecins
    • Pommier Y. Eukaryotic DNA topoisomerase I: genome gatekeeper and its intruders, camptothecins. Semin. Oncol. 23 (1996) 1-10
    • (1996) Semin. Oncol. , vol.23 , pp. 1-10
    • Pommier, Y.1
  • 49
    • 0030886788 scopus 로고    scopus 로고
    • Camptothecin-induced apoptosis in p53-null human leukemia HL60 cells and their isolated nuclei: effects of the protease inhibitors Z-VAD-fmk and dichloroisocoumarin suggest an involvement of both caspases and serine proteases
    • Shimizu T., and Pommier Y. Camptothecin-induced apoptosis in p53-null human leukemia HL60 cells and their isolated nuclei: effects of the protease inhibitors Z-VAD-fmk and dichloroisocoumarin suggest an involvement of both caspases and serine proteases. Leukemia 11 (1997) 1238-1244
    • (1997) Leukemia , vol.11 , pp. 1238-1244
    • Shimizu, T.1    Pommier, Y.2
  • 50
    • 5744253112 scopus 로고    scopus 로고
    • 2-terminal kinase (JNK) and apoptosis in response to cadmium in murine macrophages
    • 2-terminal kinase (JNK) and apoptosis in response to cadmium in murine macrophages. Toxicol. Sci. 81 (2004) 518-527
    • (2004) Toxicol. Sci. , vol.81 , pp. 518-527
    • Kim, J.1    Sharma, R.P.2
  • 51
    • 12844251358 scopus 로고    scopus 로고
    • Identification of ASK1, MKK4, JNK, c-Jun, and caspase-3 as a signaling cascade involved in cadmium-induced neuronal cell apoptosis
    • Kim S.D., Moon C.K., Eun S.Y., Ryu P.D., and Jo S.A. Identification of ASK1, MKK4, JNK, c-Jun, and caspase-3 as a signaling cascade involved in cadmium-induced neuronal cell apoptosis. Biochem. Biophys. Res. Commun. 328 (2005) 326-334
    • (2005) Biochem. Biophys. Res. Commun. , vol.328 , pp. 326-334
    • Kim, S.D.1    Moon, C.K.2    Eun, S.Y.3    Ryu, P.D.4    Jo, S.A.5
  • 52
    • 0033923816 scopus 로고    scopus 로고
    • Roles of JNK, p38 and ERK mitogen-activated protein kinases in the growth inhibition and apoptosis induced by cadmium
    • Chuang S.M., Wang I.C., and Yang J.L. Roles of JNK, p38 and ERK mitogen-activated protein kinases in the growth inhibition and apoptosis induced by cadmium. Carcinogenesis 21 (2000) 1423-1432
    • (2000) Carcinogenesis , vol.21 , pp. 1423-1432
    • Chuang, S.M.1    Wang, I.C.2    Yang, J.L.3
  • 53
    • 0034807554 scopus 로고    scopus 로고
    • Comparison of roles of three mitogen-activated protein kinases induced by chromium(VI) and cadmium in non-small-cell lung carcinoma cells
    • Chuang S.M., and Yang J.L. Comparison of roles of three mitogen-activated protein kinases induced by chromium(VI) and cadmium in non-small-cell lung carcinoma cells. Mol. Cell. Biochem. 222 (2001) 85-95
    • (2001) Mol. Cell. Biochem. , vol.222 , pp. 85-95
    • Chuang, S.M.1    Yang, J.L.2
  • 54
    • 0034808509 scopus 로고    scopus 로고
    • Opposite roles of ERK and p38 mitogen-activated protein kinases in cadmium-induced genotoxicity and mitotic arrest
    • Chao J.I., and Yang J.L. Opposite roles of ERK and p38 mitogen-activated protein kinases in cadmium-induced genotoxicity and mitotic arrest. Chem. Res. Toxicol. 14 (2001) 1193-1202
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 1193-1202
    • Chao, J.I.1    Yang, J.L.2
  • 55
    • 18344399012 scopus 로고    scopus 로고
    • Stimulation of p38 mitogen-activated protein kinase is an early regulatory event for the cadmium-induced apoptosis in human promonocytic cells
    • Galan A., Garcia-Bermejo M.L., Troyano A., Vilaboa N.E., de Blas E., Kazanietz M.G., and Aller P. Stimulation of p38 mitogen-activated protein kinase is an early regulatory event for the cadmium-induced apoptosis in human promonocytic cells. J. Biol. Chem. 275 (2000) 11418-11424
    • (2000) J. Biol. Chem. , vol.275 , pp. 11418-11424
    • Galan, A.1    Garcia-Bermejo, M.L.2    Troyano, A.3    Vilaboa, N.E.4    de Blas, E.5    Kazanietz, M.G.6    Aller, P.7
  • 56
    • 0034672641 scopus 로고    scopus 로고
    • Involvement of the extracellular signal-regulated protein kinase (ERK) pathway in the induction of apoptosis by cadmium chloride in CCRF-CEM cells
    • Iryo Y., Matsuoka M., Wispriyono B., Sugiura T., and Igisu H. Involvement of the extracellular signal-regulated protein kinase (ERK) pathway in the induction of apoptosis by cadmium chloride in CCRF-CEM cells. Biochem. Pharmacol. 60 (2000) 1875-1882
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 1875-1882
    • Iryo, Y.1    Matsuoka, M.2    Wispriyono, B.3    Sugiura, T.4    Igisu, H.5
  • 58
    • 0032489323 scopus 로고    scopus 로고
    • Cadmium inhibits BPDE alkylation of DNA in the major groove but not in the minor groove
    • Prakash A.S., Rao K.S., and Dameron C.T. Cadmium inhibits BPDE alkylation of DNA in the major groove but not in the minor groove. Biochem. Biophys. Res. Commun. 244 (1998) 198-203
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 198-203
    • Prakash, A.S.1    Rao, K.S.2    Dameron, C.T.3
  • 59
    • 0033982782 scopus 로고    scopus 로고
    • Kinetics of DNA alkylation, depurination and hydrolysis of anti diol epoxide of benzo(a)pyrene and the effect of cadmium on DNA alkylation
    • Prakash A.S., Tran H.P., Peng C., Koyalamudi S.R., and Dameron C.T. Kinetics of DNA alkylation, depurination and hydrolysis of anti diol epoxide of benzo(a)pyrene and the effect of cadmium on DNA alkylation. Chem. Biol. Interact. 125 (2000) 133-150
    • (2000) Chem. Biol. Interact. , vol.125 , pp. 133-150
    • Prakash, A.S.1    Tran, H.P.2    Peng, C.3    Koyalamudi, S.R.4    Dameron, C.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.