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Volumn 19, Issue 1 A, 1999, Pages 181-187

Change in the localization of heat shock protein 27 (HSP 27) in BG-1 human ovarian cancer cells following treatment by the ether lipid ET-18-OCH3

Author keywords

Ether lipid; HSP27; Hypodiploid fraction; Ovarian cancer cell; Translocation

Indexed keywords

ETHER LIPID; HEAT SHOCK PROTEIN 27; NUCLEAR PROTEIN;

EID: 0032945845     PISSN: 02507005     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (9)

References (44)
  • 1
    • 0024560120 scopus 로고
    • Membrane damage in leukemic cells induced by ether and ester lipids: An electron microscopic study
    • Noseda A, White JG, Godwin PL, Jerome WG, and Modest EJ: Membrane damage in leukemic cells induced by ether and ester lipids: an electron microscopic study. Exp Mol Pathol 50: 69-83, 1989.
    • (1989) Exp Mol Pathol , vol.50 , pp. 69-83
    • Noseda, A.1    White, J.G.2    Godwin, P.L.3    Jerome, W.G.4    Modest, E.J.5
  • 2
    • 0028597086 scopus 로고
    • Antitumor ether lipids and alkylphosphocholines
    • Lohmeyer M and Bittman R: Antitumor ether lipids and alkylphosphocholines. Drugs of the Future 19: 10021-1027, 1994.
    • (1994) Drugs of the Future , vol.19 , pp. 10021-11027
    • Lohmeyer, M.1    Bittman, R.2
  • 3
    • 0026755717 scopus 로고
    • Daily oral miltefosine (hexadecylphophocholine) in patients with advanced non-small cell lung cancer. A phase II study
    • Berdel WE, Becher B, Eibl H, and et al: Daily oral miltefosine (hexadecylphophocholine) in patients with advanced non-small cell lung cancer. A phase II study. Onkologie 15: 238-242, 1992.
    • (1992) Onkologie , vol.15 , pp. 238-242
    • Berdel, W.E.1    Becher, B.2    Eibl, H.3
  • 4
    • 0026621940 scopus 로고
    • Hexadecylphosphocholine in the topical treatment of skin metasitases in breast cancer patients
    • Unger C, Sindermann H, Peukert M, Hilgard P, Engel J, and Eibl H: Hexadecylphosphocholine in the topical treatment of skin metasitases in breast cancer patients. Prog Exp Tumor Res 34: 1591992.
    • (1992) Prog Exp Tumor Res , vol.34 , pp. 159
    • Unger, C.1    Sindermann, H.2    Peukert, M.3    Hilgard, P.4    Engel, J.5    Eibl, H.6
  • 5
    • 0027486720 scopus 로고
    • Topical administration of hexadecylphosphocholine in patients with cutaneous lymphomas: Results of a phase I/II study
    • Dummer R, Krasovec M, Roger J, Sindermann H, and Burg G: Topical administration of hexadecylphosphocholine in patients with cutaneous lymphomas: Results of a phase I/II study. J Amer Acad Dermatol 29: 9701993.
    • (1993) J Amer Acad Dermatol , vol.29 , pp. 970
    • Dummer, R.1    Krasovec, M.2    Roger, J.3    Sindermann, H.4    Burg, G.5
  • 9
    • 0030763045 scopus 로고    scopus 로고
    • Cytokinetic and morphologic differences in ovarian cancer cells treated with ET-18-OCH3 and the DNA-interacting agent, etoposide
    • Fujiwara K, Koike H, Ohishi Y, Shirafuji H, Kohno I, Modest EJ, and Kataoka S: Cytokinetic and morphologic differences in ovarian cancer cells treated with ET-18-OCH3 and the DNA-interacting agent, etoposide. Anticancer Res 17: 2159-2167, 1997.
    • (1997) Anticancer Res , vol.17 , pp. 2159-2167
    • Fujiwara, K.1    Koike, H.2    Ohishi, Y.3    Shirafuji, H.4    Kohno, I.5    Modest, E.J.6    Kataoka, S.7
  • 11
    • 0024326432 scopus 로고
    • Cytotoxic interactions of heat and an ether lipid analogue in human ovarian carcinoma cells
    • Fujiwara K, Modest EJ, Welander CE, and Wallen CA: Cytotoxic interactions of heat and an ether lipid analogue in human ovarian carcinoma cells. Cancer Res 49: 6285-6289, 1989.
    • (1989) Cancer Res , vol.49 , pp. 6285-6289
    • Fujiwara, K.1    Modest, E.J.2    Welander, C.E.3    Wallen, C.A.4
  • 12
    • 0023057847 scopus 로고
    • Sequence and organization of genes encoding the human 27 kDa heat shock protein
    • published erratum appears in Nucleic Acids Res 1986 Oct 24; 14(20): 8230
    • Hickey E, Brandon SE, Potter R, Stein G, Stein J, and Weber LA: Sequence and organization of genes encoding the human 27 kDa heat shock protein [published erratum appears in Nucleic Acids Res 1986 Oct 24; 14(20): 8230]. Nucleic Acids Res 14: 4127-4145, 1986.
    • (1986) Nucleic Acids Res , vol.14 , pp. 4127-4145
    • Hickey, E.1    Brandon, S.E.2    Potter, R.3    Stein, G.4    Stein, J.5    Weber, L.A.6
  • 13
    • 0025374119 scopus 로고
    • Sequence of the chinese hamster small heat shock protein HSP27
    • Lavoie J, Chretien P, and Landry J: Sequence of the Chinese hamster small heat shock protein HSP27. Nucleic Acids Res 18: 16371990.
    • (1990) Nucleic Acids Res , vol.18 , pp. 1637
    • Lavoie, J.1    Chretien, P.2    Landry, J.3
  • 15
    • 0025988318 scopus 로고
    • Increased survival after treatments with anticancer agents of chinese hamster cells expressing the human Mr 27,000 heat shock protein
    • Huot J, Roy G, Lambert H, Chretien P, and Landry J: Increased survival after treatments with anticancer agents of Chinese hamster cells expressing the human Mr 27,000 heat shock protein. Cancer Res 51: 5245-5252, 1991.
    • (1991) Cancer Res , vol.51 , pp. 5245-5252
    • Huot, J.1    Roy, G.2    Lambert, H.3    Chretien, P.4    Landry, J.5
  • 16
    • 0029882949 scopus 로고    scopus 로고
    • Effect of overexpression of the small heat shock protein HSP27 on the heat and drug sensitivities of human testis tumor cells
    • Richards EH, Hickey E, Weber L, and Master JR: Effect of overexpression of the small heat shock protein HSP27 on the heat and drug sensitivities of human testis tumor cells. Cancer Res 56: 2446-2451, 1996.
    • (1996) Cancer Res , vol.56 , pp. 2446-2451
    • Richards, E.H.1    Hickey, E.2    Weber, L.3    Master, J.R.4
  • 17
    • 0030902367 scopus 로고    scopus 로고
    • Overexpression of resistance-related proteins (metallothioneins, glutathione-s-transferase pi, heat shock protein 27, and lung resistance-related protein) in osteosarcoma. Relationship with poor prognosis
    • Uozaki H, Horiuchi H, Ishida T, Iijima T, Imamura T, and Machinami R: Overexpression of resistance-related proteins (metallothioneins, glutathione-S-transferase pi, heat shock protein 27, and lung resistance-related protein) in osteosarcoma. Relationship with poor prognosis. Cancer 79: 2336-2344, 1997.
    • (1997) Cancer , vol.79 , pp. 2336-2344
    • Uozaki, H.1    Horiuchi, H.2    Ishida, T.3    Iijima, T.4    Imamura, T.5    Machinami, R.6
  • 18
    • 0029979079 scopus 로고    scopus 로고
    • Inconstant association between 27-kDa heat-shock protein (Hsp27) content and doxorubicin resistance in human colon cancer cells. The doxorubicin-protecting effect of Hsp27
    • Garrido C, Mehlen P, Fromentin A, Hammann A, Assem M, Arrigo AP, and Chauffert B: Inconstant association between 27-kDa heat-shock protein (Hsp27) content and doxorubicin resistance in human colon cancer cells. The doxorubicin-protecting effect of Hsp27. Eur J Biochem 237: 653-659, 1996.
    • (1996) Eur J Biochem , vol.237 , pp. 653-659
    • Garrido, C.1    Mehlen, P.2    Fromentin, A.3    Hammann, A.4    Assem, M.5    Arrigo, A.P.6    Chauffert, B.7
  • 21
    • 0030048157 scopus 로고    scopus 로고
    • Markers of chemoresistance in ovarian carcinomas: An immunohistochemical study of 86 cases
    • Germain I, Tetu B, Brisson J, Mondor M, and Cherian MG: Markers of chemoresistance in ovarian carcinomas: an immunohistochemical study of 86 cases. Int J Gynecol Pathol 15: 54-62, 1996.
    • (1996) Int J Gynecol Pathol , vol.15 , pp. 54-62
    • Germain, I.1    Tetu, B.2    Brisson, J.3    Mondor, M.4    Cherian, M.G.5
  • 23
    • 0032054581 scopus 로고    scopus 로고
    • Heat schok protein 27: An independent prognostic indicator of survival in patients with epithelial ovarian carcinoma
    • In Press
    • Geisler JP, Geisler HE, Tammela J, Wiemann MC, Zhou Z, Miller GA, and Crabtree W: Heat Schok Protein 27: An independent prognostic Indicator of survival in patients with epithelial ovarian carcinoma. Gynecol Oncol In Press: 1998.
    • (1998) Gynecol Oncol
    • Geisler, J.P.1    Geisler, H.E.2    Tammela, J.3    Wiemann, M.C.4    Zhou, Z.5    Miller, G.A.6    Crabtree, W.7
  • 24
    • 0028832107 scopus 로고
    • Characterization of 45-kDa/54-kDa HSP27 kinase, a stress-sensitive kinase which may activate the phosphorylation-dependent protective function of mammalian 27-kDa heat-shock protein HSP27
    • Huot J, Lambert H, Lavoie JN, Guimond A, Houle F, and Landry J: Characterization of 45-kDa/54-kDa HSP27 kinase, a stress-sensitive kinase which may activate the phosphorylation-dependent protective function of mammalian 27-kDa heat-shock protein HSP27. Eur J Biochem 227: 416-427, 1995.
    • (1995) Eur J Biochem , vol.227 , pp. 416-427
    • Huot, J.1    Lambert, H.2    Lavoie, J.N.3    Guimond, A.4    Houle, F.5    Landry, J.6
  • 25
    • 0027482463 scopus 로고
    • Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27
    • Lavoie JN, Hickey E, Weber LA, and Landry J: Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27. J Biol Chem 268: 24210-24214, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 24210-24214
    • Lavoie, J.N.1    Hickey, E.2    Weber, L.A.3    Landry, J.4
  • 26
    • 0030069517 scopus 로고    scopus 로고
    • HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress
    • Huot J, Houle F, Spitz DR, and Landry J: HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress. Cancer Res 56: 273-279, 1996.
    • (1996) Cancer Res , vol.56 , pp. 273-279
    • Huot, J.1    Houle, F.2    Spitz, D.R.3    And Landry, J.4
  • 27
    • 0028564842 scopus 로고
    • Interleukin-1-induced intracellular signaling pathways converge in the activation of mitogen-activated protein kinase and mitogen-activated protein kinase-activated protein kinase 2 and the subsequent phosphorylation of the 27-kilodalton heat shock protein in monocytic cells
    • Ahlers A, Belka C, Gaestel M, Lamping N, Sott C, Herrmann F, and Brach MA: Interleukin-1-induced intracellular signaling pathways converge in the activation of mitogen-activated protein kinase and mitogen-activated protein kinase-activated protein kinase 2 and the subsequent phosphorylation of the 27-kilodalton heat shock protein in monocytic cells. Mol Pharmacol 46: 1077-1083, 1994.
    • (1994) Mol Pharmacol , vol.46 , pp. 1077-1083
    • Ahlers, A.1    Belka, C.2    Gaestel, M.3    Lamping, N.4    Sott, C.5    Herrmann, F.6    Brach, M.A.7
  • 28
    • 0028270016 scopus 로고
    • Interleukin-3 and granulocyte-macrophage colony-stimulating factor induce activation of the MAPKAP kinase 2 resulting in in vitro serine phosphorylation of the small heat shock protein (Hsp 27)
    • Ahlers A, Engel K, Sott C, Gaestel M, Herrmann F, and Brach MA: Interleukin-3 and granulocyte-macrophage colony-stimulating factor induce activation of the MAPKAP kinase 2 resulting in in vitro serine phosphorylation of the small heat shock protein (Hsp 27). Blood 83: 1791-1798, 1994.
    • (1994) Blood , vol.83 , pp. 1791-1798
    • Ahlers, A.1    Engel, K.2    Sott, C.3    Gaestel, M.4    Herrmann, F.5    Brach, M.A.6
  • 29
    • 0028906774 scopus 로고
    • Interleukin (IL)-6 signaling leads to phosphorylation of the small heat shock protein (Hsp)27 through activation of the MAP kinase and MAPKAP kinase 2 pathway in monocytes and monocytic leukemia cells
    • Belka C, Ahlers A, Sott C, Gaestel M, Herrmann F, and Brach MA: Interleukin (IL)-6 signaling leads to phosphorylation of the small heat shock protein (Hsp)27 through activation of the MAP kinase and MAPKAP kinase 2 pathway in monocytes and monocytic leukemia cells. Leukemia 9: 288-294, 1995.
    • (1995) Leukemia , vol.9 , pp. 288-294
    • Belka, C.1    Ahlers, A.2    Sott, C.3    Gaestel, M.4    Herrmann, F.5    Brach, M.A.6
  • 30
    • 0028815952 scopus 로고
    • MAPKAP kinase 2 is activated by heat shock and TNF-alpha: In vivo phosphorylation of small heat shock protein results from stimulation of the MAP kinase cascade
    • Engel K, Ahlers A, Brach MA, Herrmann F, and Gaestel M: MAPKAP kinase 2 is activated by heat shock and TNF-alpha: in vivo phosphorylation of small heat shock protein results from stimulation of the MAP kinase cascade. J Cell Biochem 57: 321-330, 1995.
    • (1995) J Cell Biochem , vol.57 , pp. 321-330
    • Engel, K.1    Ahlers, A.2    Brach, M.A.3    Herrmann, F.4    Gaestel, M.5
  • 31
    • 0028022750 scopus 로고
    • A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins
    • Rouse J, Cohen P, Trigon S, Morange M, Alonso LA, Zamanillo D, Hunt T, and Nebreda AR: A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. Cell 78: 1027-1037, 1994.
    • (1994) Cell , vol.78 , pp. 1027-1037
    • Rouse, J.1    Cohen, P.2    Trigon, S.3    Morange, M.4    Alonso, L.A.5    Zamanillo, D.6    Hunt, T.7    Nebreda, A.R.8
  • 32
    • 0028924759 scopus 로고
    • Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27
    • Lavoie JN, Lambert H, Hickey E, Weber LA, and Landry J: Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. Mol Cell Biol 15: 505-516, 1995.
    • (1995) Mol Cell Biol , vol.15 , pp. 505-516
    • Lavoie, J.N.1    Lambert, H.2    Hickey, E.3    Weber, L.A.4    Landry, J.5
  • 34
    • 0030839309 scopus 로고    scopus 로고
    • 1-O-Octadecyl-2-O-methylglycerophosphocholine inhibits protein kinase C-dependent phosphorylation of endogenous proteins in MCF-7 cells
    • Zhou X and Arthur G: 1-O-Octadecyl-2-O-methylglycerophosphocholine inhibits protein kinase C-dependent phosphorylation of endogenous proteins in MCF-7 cells. Biochem J, 324: 897-902, 1997.
    • (1997) Biochem J , vol.324 , pp. 897-902
    • Zhou, X.1    Arthur, G.2
  • 35
    • 0027014526 scopus 로고
    • Drugs active against growth factor and oncogene phosphatidylinositol signalling pathways
    • Powis G: Drugs active against growth factor and oncogene phosphatidylinositol signalling pathways. Semin Cancer Biol 3: 343-350, 1992.
    • (1992) Semin Cancer Biol , vol.3 , pp. 343-350
    • Powis, G.1
  • 36
    • 0029787879 scopus 로고    scopus 로고
    • 1-O-octadecyl-2-o-methyl-glycerophosphocholine inhibits the transduction of growth signals via the MAPK cascade in cultured MCF-7 cells
    • Zhou X, Lu X, Richard C, Xiong W, Litchfield DW, Bittman R, and Arthur G: 1-O-octadecyl-2-O-methyl-glycerophosphocholine inhibits the transduction of growth signals via the MAPK cascade in cultured MCF-7 cells. J Clin Invest 98: 937-944, 1996.
    • (1996) J Clin Invest , vol.98 , pp. 937-944
    • Zhou, X.1    Lu, X.2    Richard, C.3    Xiong, W.4    Litchfield, D.W.5    Bittman, R.6    Arthur, G.7
  • 37
    • 0023894145 scopus 로고
    • Characterization of HSP27 and three immunologically related polypeptides during drosophila development
    • Arrigo AP and Pauli D: Characterization of HSP27 and three immunologically related polypeptides during Drosophila development. Exp Cell Res 175: 169-183, 1988.
    • (1988) Exp Cell Res , vol.175 , pp. 169-183
    • Arrigo, A.P.1    Pauli, D.2
  • 38
    • 0025294687 scopus 로고
    • The monovalent ionophore monensin maintains the nuclear localization of the human stress protein hsp28 during heat shock recovery
    • Arrigo AP: The monovalent ionophore monensin maintains the nuclear localization of the human stress protein hsp28 during heat shock recovery. J Cell Sci 96: 419-427, 1990.
    • (1990) J Cell Sci , vol.96 , pp. 419-427
    • Arrigo, A.P.1
  • 39
    • 0027293201 scopus 로고
    • Analysis of the resistance to heat and hydrogen peroxide stresses in COS cells transiently expressing wild type or deletion mutants of the drosophila 27-kDa heat-shock protein
    • Mehlen P, Briolay J, Smith L, Diaz IC, Fabre N, Pauli D, and Arrigo AP: Analysis of the resistance to heat and hydrogen peroxide stresses in COS cells transiently expressing wild type or deletion mutants of the Drosophila 27-kDa heat-shock protein. Eur J Biochem 215: 277-284, 1993.
    • (1993) Eur J Biochem , vol.215 , pp. 277-284
    • Mehlen, P.1    Briolay, J.2    Smith, L.3    Diaz, I.C.4    Fabre, N.5    Pauli, D.6    Arrigo, A.P.7
  • 40
    • 0031708908 scopus 로고    scopus 로고
    • Heat shock protein expression and drug resistance in breast cancer patients treated with induction chemotherapy
    • In Press
    • Vargas RL, Gago FE, Tello O, Aznar JC, and Ciocca DR: Heat shock protein expression and drug resistance in breast cancer patients treated with induction chemotherapy. Int J Cancer In Press: 1998.
    • (1998) Int J Cancer
    • Vargas, R.L.1    Gago, F.E.2    Tello, O.3    Aznar, J.C.4    Ciocca, D.R.5
  • 41
    • 0031149633 scopus 로고    scopus 로고
    • UVB irradiation induces changes in cellular localization and phosphorylation of mouse HSP27
    • Nozaki J, Takehana M, and Kobayashi S: UVB irradiation induces changes in cellular localization and phosphorylation of mouse HSP27. Photochem Photobiol 65: 843-848, 1997.
    • (1997) Photochem Photobiol , vol.65 , pp. 843-848
    • Nozaki, J.1    Takehana, M.2    Kobayashi, S.3
  • 42
    • 0030785821 scopus 로고    scopus 로고
    • HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs
    • Garrido C, Ottavi P, Fromentin A, Hammann A, Arrigo AP, Chauffert B, and Mehlen P: HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs. Cancer Res 57: 2661-2667, 1997.
    • (1997) Cancer Res , vol.57 , pp. 2661-2667
    • Garrido, C.1    Ottavi, P.2    Fromentin, A.3    Hammann, A.4    Arrigo, A.P.5    Chauffert, B.6    Mehlen, P.7
  • 43
    • 0030601988 scopus 로고    scopus 로고
    • Localization of heat shock proteins in mouse male germ cells: An immunoelectron microscopical study
    • Biggiogera M, Tanguay RM, Marin R, Wu Y, Martin TE, and Fakan S: Localization of heat shock proteins in mouse male germ cells: an immunoelectron microscopical study. Exp Cell Res 229: 77-85, 1996.
    • (1996) Exp Cell Res , vol.229 , pp. 77-85
    • Biggiogera, M.1    Tanguay, R.M.2    Marin, R.3    Wu, Y.4    Martin, T.E.5    Fakan, S.6
  • 44
    • 0002241311 scopus 로고
    • Expression and function of the low-molecular-weight heat shock proteins
    • R.I. Morimoto A. Tissieres and C. Georgopoulos (eds.), Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Arrigo AP and Landry J: Expression and Function of the Low-molecular-weight Heat Shock Proteins. In: R.I. Morimoto A. Tissieres and C. Georgopoulos (eds.), The Biology of Heat Shock Proteins and Molecular Chaperones, pp. 335-373, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press. 1994.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 335-373
    • Arrigo, A.P.1    Landry, J.2


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