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Volumn 10, Issue 3, 2003, Pages 313-322

Interferon-γ downregulates Hsp27 expression and suppresses the negative regulation of cell death in oral squamous cell carcinoma lines

Author keywords

Cisplatin; Hsp27; Interferon ; Molecular chaperone; Oral squamous cell carcinoma

Indexed keywords

ALPHA INTERFERON; ANTINEOPLASTIC AGENT; CASPASE 3; CHAPERONE; CISPLATIN; DNA; GAMMA INTERFERON; GLYCINE; HEAT SHOCK PROTEIN 27; MUTANT PROTEIN; SERINE; TUMOR NECROSIS FACTOR ALPHA;

EID: 0038297011     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401169     Document Type: Review
Times cited : (21)

References (49)
  • 1
    • 0022001780 scopus 로고
    • Fundamental studies with cisplatin
    • Rosenberg B. (1985) Fundamental studies with cisplatin. Cancer 55: 2303-2306
    • (1985) Cancer , vol.55 , pp. 2303-2306
    • Rosenberg, B.1
  • 2
    • 0028272074 scopus 로고
    • Modulation of cisplatin cytotoxicity by human recombinant interferon-γ in human ovarian cancer cell lines
    • Nehme A, Julia AM, Jozan S, Chevreau C, Bugat R and Canal P. (1994) Modulation of cisplatin cytotoxicity by human recombinant interferon-γ in human ovarian cancer cell lines. Eur. J. Cancer 4: 520-525
    • (1994) Eur. J. Cancer , vol.4 , pp. 520-525
    • Nehme, A.1    Julia, A.M.2    Jozan, S.3    Chevreau, C.4    Bugat, R.5    Canal, P.6
  • 3
    • 0028290902 scopus 로고
    • The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis
    • Lee SB and Esteban M (1994) The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis. Virology 199: 491-496
    • (1994) Virology , vol.199 , pp. 491-496
    • Lee, S.B.1    Esteban, M.2
  • 4
    • 0030794883 scopus 로고    scopus 로고
    • Activation of the IFN-inducible enzyme RNase L causes apoptosis of animal cells
    • Diaz-Guerra M, Rivas C and Esteban M (1997) Activation of the IFN-inducible enzyme RNase L causes apoptosis of animal cells. Virology 236: 354-363
    • (1997) Virology , vol.236 , pp. 354-363
    • Diaz-Guerra, M.1    Rivas, C.2    Esteban, M.3
  • 5
    • 0029981093 scopus 로고    scopus 로고
    • An essential role for the interferon-inducible, double-stranded RNA-activated protein kinase PKR in the tumor necrosis factor-induced apoptosis in U937 cells
    • Yeung MC, Liu J and Lau AS (1996) An essential role for the interferon-inducible, double-stranded RNA-activated protein kinase PKR in the tumor necrosis factor-induced apoptosis in U937 cells. Proc. Natl. Acad. Sci. USA 93: 12451-12455
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12451-12455
    • Yeung, M.C.1    Liu, J.2    Lau, A.S.3
  • 7
    • 0034456563 scopus 로고    scopus 로고
    • Interferon-alpha and interferon-gamma augment apoptosis in oral carcinoma cells treated with Shiga toxin 2 (Stx2)
    • Yonekura N, Yokosawa N, Hariya Y, Dehari H, Kohama G and Fujii N (2000) Interferon-alpha and interferon-gamma augment apoptosis in oral carcinoma cells treated with Shiga toxin 2 (Stx2). Tumor Res. 35: 25-33
    • (2000) Tumor Res. , vol.35 , pp. 25-33
    • Yonekura, N.1    Yokosawa, N.2    Hariya, Y.3    Dehari, H.4    Kohama, G.5    Fujii, N.6
  • 9
    • 0033944777 scopus 로고    scopus 로고
    • Heat shock proteins-modulators of apoptosis in tumor cells
    • Creagh EM, Sheehan D and Cotter TG (2000) Heat shock proteins-modulators of apoptosis in tumor cells. Leukemia 14: 1161-1173
    • (2000) Leukemia , vol.14 , pp. 1161-1173
    • Creagh, E.M.1    Sheehan, D.2    Cotter, T.G.3
  • 10
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly C and Morimoto RI (2000) Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J. Natl. Cancer Inst. 92: 1564-1572
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 11
    • 0032454360 scopus 로고    scopus 로고
    • Molecular chaperones in the etiology and therapy of cancer
    • Sõti C and Csermely P (1998) Molecular chaperones in the etiology and therapy of cancer. Pathol. Oncol. Res. 4: 316-321
    • (1998) Pathol. Oncol. Res. , vol.4 , pp. 316-321
    • Sõti, C.1    Csermely, P.2
  • 12
    • 0032440847 scopus 로고    scopus 로고
    • Heat shock proteins: Regulators of stress response and apoptosis
    • Samali A and Orrenius S (1998) Heat shock proteins: regulators of stress response and apoptosis. Cell Stress Chaperones 3: 228-236
    • (1998) Cell Stress Chaperones , vol.3 , pp. 228-236
    • Samali, A.1    Orrenius, S.2
  • 14
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • Leist M and Jäättelä M (2001) Four deaths and a funeral: from caspases to alternative mechanisms. Nat. Rev. Mol. Cell Biol. 2: 589-598
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 589-598
    • Leist, M.1    Jäättelä, M.2
  • 15
    • 0024155498 scopus 로고
    • Establishment and characterization of a human cell line derived from a oral sqamous carcinoma of the tongue
    • Yokoi T, Yamaguchi A, Odajima T and Furukawa K (1988) Establishment and characterization of a human cell line derived from a oral sqamous carcinoma of the tongue. Tumor Res. 23: 46-57
    • (1988) Tumor Res. , vol.23 , pp. 46-57
    • Yokoi, T.1    Yamaguchi, A.2    Odajima, T.3    Furukawa, K.4
  • 17
    • 0030937570 scopus 로고    scopus 로고
    • Cytotoxicity of histocompatibility leukocyte antigen-DR8-restricted CD4 killer T cells against human autologous squamous cell carcinoma
    • Miyazaki A, Sato N, Takahashi S, Sasaki A, Kohama G, Yamaguchi A, Yagihashi A and Kikuchi K (1997) Cytotoxicity of histocompatibility leukocyte antigen-DR8-restricted CD4 killer T cells against human autologous squamous cell carcinoma. Jpn. J. Cancer Res. 88: 191-197
    • (1997) Jpn. J. Cancer Res. , vol.88 , pp. 191-197
    • Miyazaki, A.1    Sato, N.2    Takahashi, S.3    Sasaki, A.4    Kohama, G.5    Yamaguchi, A.6    Yagihashi, A.7    Kikuchi, K.8
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0031731861 scopus 로고    scopus 로고
    • Poor induction of interferon-induced 2′,5′-oligoadenylate synthetase (2-5 AS) in cells persistently infected with mumps virus is caused by decrease of STAT-1α
    • Yokosawa N, Kubota T and Fujii N (1998) Poor induction of interferon-induced 2′,5′-oligoadenylate synthetase (2-5 AS) in cells persistently infected with mumps virus is caused by decrease of STAT-1α. Arch. Virol. 143: 1985-1992
    • (1998) Arch. Virol. , vol.143 , pp. 1985-1992
    • Yokosawa, N.1    Kubota, T.2    Fujii, N.3
  • 20
    • 0008107233 scopus 로고    scopus 로고
    • Upregulation of cytosolic chaperonin CCT subunits during recovery from chemical stress that causes accumulation of unfolded proteins
    • Yokota S, Yanagi H, Yura T and Kubota H (2000) Upregulation of cytosolic chaperonin CCT subunits during recovery from chemical stress that causes accumulation of unfolded proteins. Eur. J. Biochem. 267: 1658-1664
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1658-1664
    • Yokota, S.1    Yanagi, H.2    Yura, T.3    Kubota, H.4
  • 21
    • 0029043135 scopus 로고
    • Effects of the overexpression of the small heat shock protein, HSP27, on the sensitivity of human fibroblast cells exposed to oxidative stress
    • Arata S, Hamaguchi S and Nose K (1995) Effects of the overexpression of the small heat shock protein, HSP27, on the sensitivity of human fibroblast cells exposed to oxidative stress. J. Cell Physiol. 163: 458-465
    • (1995) J. Cell Physiol. , vol.163 , pp. 458-465
    • Arata, S.1    Hamaguchi, S.2    Nose, K.3
  • 22
    • 0031013644 scopus 로고    scopus 로고
    • Inhibition of colony formation of NIH 3T3 cells by the expression of the small molecular weight heat shock protein HSP27: Involvement of its phosphorylation and aggregation at the C-terminal region
    • Arata S, Hamaguchi S and Nose K (1997) Inhibition of colony formation of NIH 3T3 cells by the expression of the small molecular weight heat shock protein HSP27: involvement of its phosphorylation and aggregation at the C-terminal region. J. Cell Physiol. 170: 19-26
    • (1997) J. Cell Physiol. , vol.170 , pp. 19-26
    • Arata, S.1    Hamaguchi, S.2    Nose, K.3
  • 23
    • 0026570931 scopus 로고
    • Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II
    • Landry J, Lambert H, Zhou M, Lavoie JN, Hickey E, Weber LA and Anderson CW (1992) Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II. J. Biol. Chem. 267: 794-803
    • (1992) J. Biol. Chem. , vol.267 , pp. 794-803
    • Landry, J.1    Lambert, H.2    Zhou, M.3    Lavoie, J.N.4    Hickey, E.5    Weber, L.A.6    Anderson, C.W.7
  • 24
    • 0033012421 scopus 로고    scopus 로고
    • Augmentation of verotoxin-induced cytotoxicity/apoptosis by interferon is repressed in cells persistently infected with mumps virus
    • Hariya Y, Shirakawa S, Yonekura N, Yokosawa N, Kohama G and Fujii N (1999) Augmentation of verotoxin-induced cytotoxicity/apoptosis by interferon is repressed in cells persistently infected with mumps virus. J. Interferon Cytokine Res. 19: 479-485
    • (1999) J. Interferon Cytokine Res. , vol.19 , pp. 479-485
    • Hariya, Y.1    Shirakawa, S.2    Yonekura, N.3    Yokosawa, N.4    Kohama, G.5    Fujii, N.6
  • 25
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry NA and Lazebnik Y (1998) Caspases: enemies within. Science 281: 1312-1316
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 26
    • 0035182221 scopus 로고    scopus 로고
    • Stress management - Heat shock protein-70 and the regulation of apoptosis
    • Beere HM and Green DR (2001) Stress management - heat shock protein-70 and the regulation of apoptosis. Trends Cell Biol. 11: 6-10
    • (2001) Trends Cell Biol. , vol.11 , pp. 6-10
    • Beere, H.M.1    Green, D.R.2
  • 27
    • 0032516917 scopus 로고    scopus 로고
    • Cytotoxic T lymphocyte-assisted suicide. Caspase 3 activation is primarily the result of the direct action of granzyme B
    • Atkinson EA, Barry M, Darmon AJ, Shostak I, Turner PC, Moyer RW and Bleackley RC (1998) Cytotoxic T lymphocyte-assisted suicide. Caspase 3 activation is primarily the result of the direct action of granzyme B. J. Biol. Chem. 273: 21261-21266
    • (1998) J. Biol. Chem. , vol.273 , pp. 21261-21266
    • Atkinson, E.A.1    Barry, M.2    Darmon, A.J.3    Shostak, I.4    Turner, P.C.5    Moyer, R.W.6    Bleackley, R.C.7
  • 29
    • 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 (1991) 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) Cancer Res. , vol.51 , pp. 5245-5252
    • Huot, J.1    Roy, G.2    Lambert, H.3    Chretien, P.4    Landry, J.5
  • 30
    • 0027366354 scopus 로고
    • The small heat shock protein hsp27 is correlated with growth and drug resistance in human breast cancer cell lines
    • Oesterreich S, Weng CN, Qiu M, Hilsenbeck SG, Osborne CK and Fuqua SA (1993) The small heat shock protein hsp27 is correlated with growth and drug resistance in human breast cancer cell lines. Cancer Res. 53: 4443-4448
    • (1993) Cancer Res. , vol.53 , pp. 4443-4448
    • Oesterreich, S.1    Weng, C.N.2    Qiu, M.3    Hilsenbeck, S.G.4    Osborne, C.K.5    Fuqua, S.A.6
  • 33
    • 0007404243 scopus 로고    scopus 로고
    • Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFα in NIH-3T3-ras cells
    • Mehlen P, Hickey E, Weber LA and Arrigo AP (1997) Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFα in NIH-3T3-ras cells. Biochem. Biophys. Res. Commun. 241: 187-192
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 187-192
    • Mehlen, P.1    Hickey, E.2    Weber, L.A.3    Arrigo, A.P.4
  • 34
    • 0033991539 scopus 로고    scopus 로고
    • Induction of apoptosis by abrogation of HSP70 expression in human oral cancer cells
    • Kaur J, Kaur J and Ralhan R (2000) Induction of apoptosis by abrogation of HSP70 expression in human oral cancer cells. Int. J. Cancer 85: 1-5
    • (2000) Int. J. Cancer , vol.85 , pp. 1-5
    • Kaur, J.1    Kaur, J.2    Ralhan, R.3
  • 35
    • 0034608892 scopus 로고    scopus 로고
    • Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2
    • Nylandsted J, Rohde M, Brand K, Bastholm L, Elling F and Jäättelä M (2000) Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2. Proc. Natl. Acad. Sci. USA 97: 7871-7876
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7871-7876
    • Nylandsted, J.1    Rohde, M.2    Brand, K.3    Bastholm, L.4    Elling, F.5    Jäättelä, M.6
  • 36
    • 0026457201 scopus 로고
    • Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins
    • Stokoe D, Engel K, Campbell DG, Cohen P and Gaestel M (1992) Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins. FEBS Lett. 313: 307-313
    • (1992) FEBS Lett. , vol.313 , pp. 307-313
    • Stokoe, D.1    Engel, K.2    Campbell, D.G.3    Cohen, P.4    Gaestel, M.5
  • 37
    • 0029912650 scopus 로고    scopus 로고
    • 3pK, a novel mitogen-activated protein (MAP) kinase-activated protein kinase, is targeted by three MAP kinase pathways
    • Ludwig S, Engel K, Hoffmeyer A, Sithanandam G, Neufeld B, Palm D, Gaestel M and Rapp UR (1996) 3pK, a novel mitogen-activated protein (MAP) kinase-activated protein kinase, is targeted by three MAP kinase pathways. Mol. Cell. Biol. 16: 6687-6697
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6687-6697
    • Ludwig, S.1    Engel, K.2    Hoffmeyer, A.3    Sithanandam, G.4    Neufeld, B.5    Palm, D.6    Gaestel, M.7    Rapp, U.R.8
  • 39
    • 0028071812 scopus 로고
    • Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity
    • Benndorf R, Hayess K, Ryazantsev S, Wieske M, Behlke J and Lutsch G (1994) Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity. J. Biol. Chem. 269: 20780-20784
    • (1994) J. Biol. Chem. , vol.269 , pp. 20780-20784
    • Benndorf, R.1    Hayess, K.2    Ryazantsev, S.3    Wieske, M.4    Behlke, J.5    Lutsch, G.6
  • 40
    • 0027417852 scopus 로고
    • Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock* HSP27 stabilization of the microfilament organization
    • Lavoie JN, Gingras-Breton G, Tanguay RM and Landry J (1993) Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock* HSP27 stabilization of the microfilament organization. J. Biol. Chem. 268: 3420-3429
    • (1993) J. Biol. Chem. , vol.268 , pp. 3420-3429
    • Lavoie, J.N.1    Gingras-Breton, G.2    Tanguay, R.M.3    Landry, J.4
  • 41
    • 0030014643 scopus 로고    scopus 로고
    • Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death
    • Mehlen P, Schulze-Osthoff K and Arrigo AP (1996) Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death. J. Biol. Chem. 271: 16510-16514
    • (1996) J. Biol. Chem. , vol.271 , pp. 16510-16514
    • Mehlen, P.1    Schulze-Osthoff, K.2    Arrigo, A.P.3
  • 42
    • 0345410965 scopus 로고    scopus 로고
    • Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery
    • Previllé X, Salvemini F, Giraud S, Chaufour S, Paul C, Stepien G, Ursini MV and Arrigo AP (1999) Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery. Exp. Cell Res. 247: 61-78
    • (1999) Exp. Cell Res. , vol.247 , pp. 61-78
    • Previllé, X.1    Salvemini, F.2    Giraud, S.3    Chaufour, S.4    Paul, C.5    Stepien, G.6    Ursini, M.V.7    Arrigo, A.P.8
  • 45
    • 0033796051 scopus 로고    scopus 로고
    • Inhibition of Daxx-mediated apoptosis by heat shock protein 27
    • Charette SJ, Lavoie JN, Lambert H and Landry J (2000) Inhibition of Daxx-mediated apoptosis by heat shock protein 27. Mol. Cell. Biol. 20: 7602-7612
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7602-7612
    • Charette, S.J.1    Lavoie, J.N.2    Lambert, H.3    Landry, J.4
  • 46
    • 0027158545 scopus 로고
    • Structure and organisation of a murine gene encoding small heat-shock protein Hsp25
    • Gaestel M, Gotthardt R and Muller T (1993) Structure and organisation of a murine gene encoding small heat-shock protein Hsp25. Gene 128: 279-283
    • (1993) Gene , vol.128 , pp. 279-283
    • Gaestel, M.1    Gotthardt, R.2    Muller, T.3
  • 47
    • 0038668000 scopus 로고    scopus 로고
    • Escaping cell death: Survival proteins in cancer
    • Jäättelä M (1999) Escaping cell death: survival proteins in cancer. Exp. Cell Res. 248: 30-43
    • (1999) Exp. Cell Res. , vol.248 , pp. 30-43
    • Jäättelä, M.1
  • 48
    • 0032768772 scopus 로고    scopus 로고
    • Heat shock proteins as cellular lifeguards
    • Jäättelä M (1999) Heat shock proteins as cellular lifeguards, Ann. Med. 31: 261-271
    • (1999) Ann. Med. , vol.31 , pp. 261-271
    • Jäättelä, M.1
  • 49
    • 0034081704 scopus 로고    scopus 로고
    • sHsp as novel regulators of programmed cell death and tumorigenicity
    • Arrigo AP (2000) sHsp as novel regulators of programmed cell death and tumorigenicity. Pathol. Biol. 48: 280-288
    • (2000) Pathol. Biol. , vol.48 , pp. 280-288
    • Arrigo, A.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.