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Volumn 1770, Issue 1, 2007, Pages 63-70

PKC inhibition is involved in trichosanthin-induced apoptosis in human chronic myeloid leukemia cell line K562

Author keywords

Apoptosis; Calcium; Caspase 3; PKC; Trichosanthin

Indexed keywords

CALPHOSTIN C; CASPASE 3; TRICHOSANTHIN;

EID: 33845528947     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2006.07.011     Document Type: Article
Times cited : (33)

References (36)
  • 1
    • 15944368960 scopus 로고    scopus 로고
    • Recent advances in trichosanthin, a ribosome-inactivating protein with multiple pharmacological properties
    • Shaw P.C., Lee K.M., and Wong K.B. Recent advances in trichosanthin, a ribosome-inactivating protein with multiple pharmacological properties. Toxicon 45 (2005) 683-689
    • (2005) Toxicon , vol.45 , pp. 683-689
    • Shaw, P.C.1    Lee, K.M.2    Wong, K.B.3
  • 2
    • 0026549787 scopus 로고
    • The mechanism of action of trichosanthin on eukaryotic ribosomes-RNA N-glycosidase activity of the cytotoxin
    • Zhang J.S., and Liu W.Y. The mechanism of action of trichosanthin on eukaryotic ribosomes-RNA N-glycosidase activity of the cytotoxin. Nucleic Acids Res. 20 (1992) 1271-1275
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1271-1275
    • Zhang, J.S.1    Liu, W.Y.2
  • 3
    • 24344458968 scopus 로고    scopus 로고
    • Ribosomal protein L10a, a bridge between trichosanthin and the ribosome
    • Xia X., Hou F., Li J., and Nie H. Ribosomal protein L10a, a bridge between trichosanthin and the ribosome. Biochem. Biophys. Res. Commun. 336 (2005) 281-286
    • (2005) Biochem. Biophys. Res. Commun. , vol.336 , pp. 281-286
    • Xia, X.1    Hou, F.2    Li, J.3    Nie, H.4
  • 4
    • 0035340832 scopus 로고    scopus 로고
    • Reactive oxygen species involved in trichosanthin-induced apoptosis of human choriocarcinoma cells
    • Zhang C., Gong Y., Ma H., An C., Chen D., and Chen Z.L. Reactive oxygen species involved in trichosanthin-induced apoptosis of human choriocarcinoma cells. Biochem. J. 355 (2001) 653-661
    • (2001) Biochem. J. , vol.355 , pp. 653-661
    • Zhang, C.1    Gong, Y.2    Ma, H.3    An, C.4    Chen, D.5    Chen, Z.L.6
  • 5
    • 4043173966 scopus 로고    scopus 로고
    • Effect of extracts of trichosanthes root tubers on HepA-H cells and HeLa cells
    • Dou C.M., and Li J.C. Effect of extracts of trichosanthes root tubers on HepA-H cells and HeLa cells. World J. Gastroenterol. 10 (2004) 2091-2094
    • (2004) World J. Gastroenterol. , vol.10 , pp. 2091-2094
    • Dou, C.M.1    Li, J.C.2
  • 6
    • 0031598069 scopus 로고    scopus 로고
    • Effect of trichosanthin of cell cycle and apoptosis of murine melanoma cells
    • Bi L., Li H., and Zhang Y. Effect of trichosanthin of cell cycle and apoptosis of murine melanoma cells. Zhongguo Zhong Xi Yi Jie He Za Zhi 18 (1998) 35-37
    • (1998) Zhongguo Zhong Xi Yi Jie He Za Zhi , vol.18 , pp. 35-37
    • Bi, L.1    Li, H.2    Zhang, Y.3
  • 7
    • 23744465712 scopus 로고    scopus 로고
    • Trichosanthin inhibits antigen-specific T cell expansion through nitric oxide-mediated apoptosis pathway
    • Li F., Mei Y., Wang Y., Chen C., Tu J., Xiao B., and Xu L. Trichosanthin inhibits antigen-specific T cell expansion through nitric oxide-mediated apoptosis pathway. Cell. Immunol. 234 (2005) 23-30
    • (2005) Cell. Immunol. , vol.234 , pp. 23-30
    • Li, F.1    Mei, Y.2    Wang, Y.3    Chen, C.4    Tu, J.5    Xiao, B.6    Xu, L.7
  • 9
    • 0035525733 scopus 로고    scopus 로고
    • Cellular stress response and apoptosis in cancer therapy
    • Herr I., and Debatin K.M. Cellular stress response and apoptosis in cancer therapy. Blood 98 (2001) 2603-2614
    • (2001) Blood , vol.98 , pp. 2603-2614
    • Herr, I.1    Debatin, K.M.2
  • 10
    • 0032742205 scopus 로고    scopus 로고
    • Cytotoxic drugs and the CD95 pathway
    • Friesen C., Fulda S., and Debatin K.M. Cytotoxic drugs and the CD95 pathway. Leukemia 13 (1999) 1854-1858
    • (1999) Leukemia , vol.13 , pp. 1854-1858
    • Friesen, C.1    Fulda, S.2    Debatin, K.M.3
  • 11
    • 0036449793 scopus 로고    scopus 로고
    • Current status of the molecular mechanisms of anticancer drug-induced apoptosis. The contribution of molecular-level analysis to cancer chemotherapy
    • Kim R., Tanabe K., Uchida Y., Emi M., Inoue H., and Toge T. Current status of the molecular mechanisms of anticancer drug-induced apoptosis. The contribution of molecular-level analysis to cancer chemotherapy. Cancer Chemother. Pharmacol. 50 (2002) 343-352
    • (2002) Cancer Chemother. Pharmacol. , vol.50 , pp. 343-352
    • Kim, R.1    Tanabe, K.2    Uchida, Y.3    Emi, M.4    Inoue, H.5    Toge, T.6
  • 13
    • 0037710311 scopus 로고    scopus 로고
    • The isoform-specific regulation of apoptosis by protein kinase C
    • Gutcher I., Webb P.R., and Anderson N.G. The isoform-specific regulation of apoptosis by protein kinase C. Cell. Mol. Life Sci. 60 (2003) 1061-1070
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1061-1070
    • Gutcher, I.1    Webb, P.R.2    Anderson, N.G.3
  • 14
    • 3843062429 scopus 로고    scopus 로고
    • Atypical protein-kinase Czeta, but neither conventional Ca2+-dependent protein-kinase C isoenzymes nor Ca2+-calmodulin, participates in regulation of telomerase activity in Burkitt's lymphoma cells
    • Bakalova R., Ohba H., Zhelev Z., Kubo T., Fujii M., Ishikawa M., Shinohara Y., and Baba Y. Atypical protein-kinase Czeta, but neither conventional Ca2+-dependent protein-kinase C isoenzymes nor Ca2+-calmodulin, participates in regulation of telomerase activity in Burkitt's lymphoma cells. Cancer Chemother. Pharmacol. 54 (2004) 161-172
    • (2004) Cancer Chemother. Pharmacol. , vol.54 , pp. 161-172
    • Bakalova, R.1    Ohba, H.2    Zhelev, Z.3    Kubo, T.4    Fujii, M.5    Ishikawa, M.6    Shinohara, Y.7    Baba, Y.8
  • 15
    • 0034666062 scopus 로고    scopus 로고
    • Involvement of protein kinase C-regulated ceramide generation in inostamycin-induced apoptosis
    • Kawatani M., Simizu S., Osada H., Takada M., Arber N., and Imoto M. Involvement of protein kinase C-regulated ceramide generation in inostamycin-induced apoptosis. Exp. Cell Res. 259 (2000) 389-397
    • (2000) Exp. Cell Res. , vol.259 , pp. 389-397
    • Kawatani, M.1    Simizu, S.2    Osada, H.3    Takada, M.4    Arber, N.5    Imoto, M.6
  • 16
    • 2642510832 scopus 로고    scopus 로고
    • Membrane receptor-mediated apoptosis and caspase activation in the differentiated EoL-1 eosinophilic cell line
    • Al-Rabia M.W., Blaylock M.G., Sexton D.W., and Walsh G.M. Membrane receptor-mediated apoptosis and caspase activation in the differentiated EoL-1 eosinophilic cell line. J. Leukocyte Biol. 75 (2004) 1045-1055
    • (2004) J. Leukocyte Biol. , vol.75 , pp. 1045-1055
    • Al-Rabia, M.W.1    Blaylock, M.G.2    Sexton, D.W.3    Walsh, G.M.4
  • 17
    • 0037081782 scopus 로고    scopus 로고
    • Wogonin and fisetin induce apoptosis in human promyeloleukemic cells, accompanied by a decrease of reactive oxygen species, and activation of caspase 3 and Ca(2+)-dependent endonuclease
    • Lee W.R., Shen S.C., Lin H.Y., Hou W.C., Yang L.L., and Chen Y.C. Wogonin and fisetin induce apoptosis in human promyeloleukemic cells, accompanied by a decrease of reactive oxygen species, and activation of caspase 3 and Ca(2+)-dependent endonuclease. Biochem. Pharmacol. 63 (2002) 225-236
    • (2002) Biochem. Pharmacol. , vol.63 , pp. 225-236
    • Lee, W.R.1    Shen, S.C.2    Lin, H.Y.3    Hou, W.C.4    Yang, L.L.5    Chen, Y.C.6
  • 18
    • 0037455822 scopus 로고    scopus 로고
    • Direct interaction with and activation of p53 by SMAR1 retards cell-cycle progression at G2/M phase and delays tumor growth in mice
    • Kaul R., Mukherjee S., Ahmed F., Bhat M.K., Chhipa R., Galande S., and Chattopadhyay S. Direct interaction with and activation of p53 by SMAR1 retards cell-cycle progression at G2/M phase and delays tumor growth in mice. Int. J. Cancer 103 (2003) 606-615
    • (2003) Int. J. Cancer , vol.103 , pp. 606-615
    • Kaul, R.1    Mukherjee, S.2    Ahmed, F.3    Bhat, M.K.4    Chhipa, R.5    Galande, S.6    Chattopadhyay, S.7
  • 19
    • 0032479284 scopus 로고    scopus 로고
    • Differential regulation of discrete apoptotic pathways by Ras
    • Chen C.Y., Liou J., Forman L.W., and Faller D.V. Differential regulation of discrete apoptotic pathways by Ras. J. Biol. Chem. 273 (1998) 16700-16709
    • (1998) J. Biol. Chem. , vol.273 , pp. 16700-16709
    • Chen, C.Y.1    Liou, J.2    Forman, L.W.3    Faller, D.V.4
  • 20
    • 0030760711 scopus 로고    scopus 로고
    • Diacylglycerol and phosphatidate generated by phospholipases C and D, respectively, have distinct fatty acid compositions and functions. Phospholipase D-derived diacylglycerol does not activate protein kinase C in porcine aortic endothelial cells
    • Pettitt T.R., Martin A., Horton T., Liossis C., Lord J.M., and Wakelam M.J. Diacylglycerol and phosphatidate generated by phospholipases C and D, respectively, have distinct fatty acid compositions and functions. Phospholipase D-derived diacylglycerol does not activate protein kinase C in porcine aortic endothelial cells. J. Biol. Chem. 272 (1997) 17354-17359
    • (1997) J. Biol. Chem. , vol.272 , pp. 17354-17359
    • Pettitt, T.R.1    Martin, A.2    Horton, T.3    Liossis, C.4    Lord, J.M.5    Wakelam, M.J.6
  • 22
    • 0033800914 scopus 로고    scopus 로고
    • Trichosanthin induced calcium-dependent generation of reactive oxygen species in human choriocarcinoma cells
    • Zhang C.Y., Gong Y.X., Ma H., An C.C., and Chen D.Y. Trichosanthin induced calcium-dependent generation of reactive oxygen species in human choriocarcinoma cells. Analyst 125 (2000) 1539-1542
    • (2000) Analyst , vol.125 , pp. 1539-1542
    • Zhang, C.Y.1    Gong, Y.X.2    Ma, H.3    An, C.C.4    Chen, D.Y.5
  • 23
  • 24
    • 0027537711 scopus 로고
    • Localization and functional analysis of DNase-I-hypersensitive sites in the human c-sis/PDGF-B gene transcription unit and its flanking regions
    • Dirks R.P., Jansen H.J., Gerritsma J., Onnekink C., and Bloemers H.P. Localization and functional analysis of DNase-I-hypersensitive sites in the human c-sis/PDGF-B gene transcription unit and its flanking regions. Eur. J. Biochem. 211 (1993) 509-519
    • (1993) Eur. J. Biochem. , vol.211 , pp. 509-519
    • Dirks, R.P.1    Jansen, H.J.2    Gerritsma, J.3    Onnekink, C.4    Bloemers, H.P.5
  • 25
    • 1842523082 scopus 로고    scopus 로고
    • Cytoprotection following endoplasmic reticulum stress protein induction in continuous cell lines
    • Bedard K., MacDonald N., Collins J., and Cribb A. Cytoprotection following endoplasmic reticulum stress protein induction in continuous cell lines. Basic Clin. Pharmacol. Toxicol. 94 (2004) 124-131
    • (2004) Basic Clin. Pharmacol. Toxicol. , vol.94 , pp. 124-131
    • Bedard, K.1    MacDonald, N.2    Collins, J.3    Cribb, A.4
  • 26
    • 0031813604 scopus 로고    scopus 로고
    • Inhibition of the protein kinase C pathway promotes anti-CD95-induced apoptosis in Jurkat T cells
    • Drew L., Kumar R., Bandyopadhyay D., and Gupta S. Inhibition of the protein kinase C pathway promotes anti-CD95-induced apoptosis in Jurkat T cells. Int. Immunol. 10 (1998) 877-889
    • (1998) Int. Immunol. , vol.10 , pp. 877-889
    • Drew, L.1    Kumar, R.2    Bandyopadhyay, D.3    Gupta, S.4
  • 27
    • 0028316195 scopus 로고
    • Induction of apoptotic DNA fragmentation and cell death in HL-60 human promyelocytic leukemia cells by pharmacological inhibitors of protein kinase C
    • Jarvis W.D., Turner A.J., Povirk L.F., Traylor R.S., and Grant S. Induction of apoptotic DNA fragmentation and cell death in HL-60 human promyelocytic leukemia cells by pharmacological inhibitors of protein kinase C. Cancer Res. 54 (1994) 1707-1714
    • (1994) Cancer Res. , vol.54 , pp. 1707-1714
    • Jarvis, W.D.1    Turner, A.J.2    Povirk, L.F.3    Traylor, R.S.4    Grant, S.5
  • 28
    • 0032528337 scopus 로고    scopus 로고
    • Granulocyte-macrophage colony-stimulating factor rescues TF-1 leukemia cells from ionizing radiation-induced apoptosis through a pathway mediated by protein kinase Calpha
    • Kelly M.L., Tang Y., Rosensweig N., Clejan S., and Beckman B.S. Granulocyte-macrophage colony-stimulating factor rescues TF-1 leukemia cells from ionizing radiation-induced apoptosis through a pathway mediated by protein kinase Calpha. Blood 92 (1998) 416-424
    • (1998) Blood , vol.92 , pp. 416-424
    • Kelly, M.L.1    Tang, Y.2    Rosensweig, N.3    Clejan, S.4    Beckman, B.S.5
  • 29
    • 0030836301 scopus 로고    scopus 로고
    • Atypical protein kinase C iota protects human leukemia cells against drug-induced apoptosis
    • Murray N.R., and Fields A.P. Atypical protein kinase C iota protects human leukemia cells against drug-induced apoptosis. J. Biol. Chem. 272 (1997) 27521-27524
    • (1997) J. Biol. Chem. , vol.272 , pp. 27521-27524
    • Murray, N.R.1    Fields, A.P.2
  • 30
    • 0035833317 scopus 로고    scopus 로고
    • NF-kappaB/RelA transactivation is required for atypical protein kinase C iota-mediated cell survival
    • Lu Y., Jamieson L., Brasier A.R., and Fields A.P. NF-kappaB/RelA transactivation is required for atypical protein kinase C iota-mediated cell survival. Oncogene 20 (2001) 4777-4792
    • (2001) Oncogene , vol.20 , pp. 4777-4792
    • Lu, Y.1    Jamieson, L.2    Brasier, A.R.3    Fields, A.P.4
  • 31
    • 0035889243 scopus 로고    scopus 로고
    • The phosphatidylinositide 3′-kinase/Akt survival pathway is a target for the anticancer and radiosensitizing agent PKC412, an inhibitor of protein kinase C
    • Tenzer A., Zingg D., Rocha S., Hemmings B., Fabbro D., Glanzmann C., Schubiger P.A., Bodis S., and Pruschy M. The phosphatidylinositide 3′-kinase/Akt survival pathway is a target for the anticancer and radiosensitizing agent PKC412, an inhibitor of protein kinase C. Cancer Res. 61 (2001) 8203-8210
    • (2001) Cancer Res. , vol.61 , pp. 8203-8210
    • Tenzer, A.1    Zingg, D.2    Rocha, S.3    Hemmings, B.4    Fabbro, D.5    Glanzmann, C.6    Schubiger, P.A.7    Bodis, S.8    Pruschy, M.9
  • 32
    • 0141682436 scopus 로고    scopus 로고
    • Inhibition of protein kinase Calpha enhances anticancer agent-induced loss of anchorage-independent growth regardless of protection against apoptosis by Bcl-2
    • Huigsloot M., Tijdens R.B., and van de Water B. Inhibition of protein kinase Calpha enhances anticancer agent-induced loss of anchorage-independent growth regardless of protection against apoptosis by Bcl-2. Mol. Pharmacol. 64 (2003) 965-973
    • (2003) Mol. Pharmacol. , vol.64 , pp. 965-973
    • Huigsloot, M.1    Tijdens, R.B.2    van de Water, B.3
  • 33
    • 2442543262 scopus 로고    scopus 로고
    • The role of protein kinase C-alpha (PKC-alpha) in cancer and its modulation by the novel PKC-alpha-specific inhibitor aprinocarsen
    • Hanauske A.R., Sundell K., and Lahn M. The role of protein kinase C-alpha (PKC-alpha) in cancer and its modulation by the novel PKC-alpha-specific inhibitor aprinocarsen. Curr. Pharm. Des. 10 (2004) 1923-1936
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 1923-1936
    • Hanauske, A.R.1    Sundell, K.2    Lahn, M.3
  • 34
    • 0034280331 scopus 로고    scopus 로고
    • Protein kinase C as a drug target: implications for drug or diet prevention and treatment of cancer
    • Carter C.A. Protein kinase C as a drug target: implications for drug or diet prevention and treatment of cancer. Curr. Drug Targets 1 (2000) 163-183
    • (2000) Curr. Drug Targets , vol.1 , pp. 163-183
    • Carter, C.A.1
  • 35
    • 0024550448 scopus 로고
    • Calphostin C (UCN-1028C), a novel microbial compound, is a highly potent and specific inhibitor of protein kinase C
    • Kobayashi E., Nakano H., Morimoto M., and Tamaoki T. Calphostin C (UCN-1028C), a novel microbial compound, is a highly potent and specific inhibitor of protein kinase C. Biochem. Biophys. Res. Commun. 159 (1989) 548-553
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 548-553
    • Kobayashi, E.1    Nakano, H.2    Morimoto, M.3    Tamaoki, T.4
  • 36
    • 0041767513 scopus 로고    scopus 로고
    • NF-kappaB activation plays an antiapoptotic role in human leukemic K562 cells exposed to ionizing radiation
    • Cataldi A., Rapino M., Centurione L., Sabatini N., Grifone G., Garaci F., and Rana R. NF-kappaB activation plays an antiapoptotic role in human leukemic K562 cells exposed to ionizing radiation. J. Cell. Biochem. 89 (2003) 956-963
    • (2003) J. Cell. Biochem. , vol.89 , pp. 956-963
    • Cataldi, A.1    Rapino, M.2    Centurione, L.3    Sabatini, N.4    Grifone, G.5    Garaci, F.6    Rana, R.7


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