메뉴 건너뛰기




Volumn 63, Issue 23, 2003, Pages 8212-8220

Differential Effect of Acute and Permanent Heat Shock Protein 70 Overexpression in Tumor Cells on Lysability by Cytotoxic T Lymphocytes

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; DOXYCYCLINE; HEAT SHOCK PROTEIN 70; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; RETROVIRUS VECTOR;

EID: 0345734274     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (26)

References (48)
  • 1
    • 0035182221 scopus 로고    scopus 로고
    • Stress management - Heat shock protein-70 and the regulation of apoptosis
    • Beere, H. M., and Green, D. R. Stress management - heat shock protein-70 and the regulation of apoptosis. Trends Cell Biol., 11: 6-10, 2001.
    • (2001) Trends Cell Biol. , vol.11 , pp. 6-10
    • Beere, H.M.1    Green, D.R.2
  • 5
    • 0038668000 scopus 로고    scopus 로고
    • Escaping cell death: Survival proteins in cancer
    • Jäättelä, M. Escaping cell death: survival proteins in cancer. Exp. Cell Res., 248: 30-43, 1999.
    • (1999) Exp. Cell Res. , vol.248 , pp. 30-43
    • Jäättelä, M.1
  • 6
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly, C., and Morimoto, R. I. Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J. Natl. Cancer Inst., 92: 1564-1572, 2000.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 10
    • 0036512171 scopus 로고    scopus 로고
    • Roles of heat-shock proteins in innate and adaptive immunity
    • Srivastava, P. Roles of heat-shock proteins in innate and adaptive immunity. Nat. Rev. Immunol., 2: 185-194, 2002.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 185-194
    • Srivastava, P.1
  • 11
    • 0037066427 scopus 로고    scopus 로고
    • The danger model: A renewed sense of self
    • Matzinger, P. The danger model: a renewed sense of self. Science (Wash. DC), 296: 301-305, 2002.
    • (2002) Science (Wash. DC) , vol.296 , pp. 301-305
    • Matzinger, P.1
  • 13
    • 0034608370 scopus 로고    scopus 로고
    • Receptor-mediated uptake of antigen/heat shock protein complexes results in major histocompatibility complex class 1 antigen presentation via two distinct processing pathways
    • Castellino, F., Boucher, P. E., Eichelberg, K., Mayhew, M., Rothman, J. E., Houghton, A. N., and Germain, R. N. Receptor-mediated uptake of antigen/ heat shock protein complexes results in major histocompatibility complex class 1 antigen presentation via two distinct processing pathways. J. Exp. Med., 191: 1957-1964, 2000.
    • (2000) J. Exp. Med. , vol.191 , pp. 1957-1964
    • Castellino, F.1    Boucher, P.E.2    Eichelberg, K.3    Mayhew, M.4    Rothman, J.E.5    Houghton, A.N.6    Germain, R.N.7
  • 14
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • Basu, S., Binder, R. J., Ramalingam, T., and Srivastava, P. K. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity, 14: 303-313, 2001.
    • (2001) Immunity , vol.14 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 15
    • 0028366212 scopus 로고
    • Heat shock proteins transfer peptides during antigen processing and CTL priming
    • Srivastava, P. K., Udono, H., Blachere, N. E., and Li, Z. Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics, 39: 93-98, 1994.
    • (1994) Immunogenetics , vol.39 , pp. 93-98
    • Srivastava, P.K.1    Udono, H.2    Blachere, N.E.3    Li, Z.4
  • 16
    • 0031906738 scopus 로고    scopus 로고
    • b-binding ovalbumin-derived peptides associated with the stress proteins HSP70 and gp96
    • b-binding ovalbumin-derived peptides associated with the stress proteins HSP70 and gp96. Eur. J. Immunol., 28: 1016-1021, 1998.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 1016-1021
    • Breloer, M.1    Marti, T.2    Fleischer, B.3    Von Bonin, A.4
  • 17
    • 0033083413 scopus 로고    scopus 로고
    • Isolation of MHC class I-restricted tumor antigen peptide and its precursors associated with heat shock proteins hsp70, hsp90, and gp96
    • Ishii, T., Udono, H., Yamano, T., Ohta, H., Uenaka, A., Ono, T., Hizuta, A., Tanaka, N., Srivastava, P. K., and Nakayama, E. Isolation of MHC class I-restricted tumor antigen peptide and its precursors associated with heat shock proteins hsp70, hsp90, and gp96. J. Immunol., 162: 1303-1309, 1999.
    • (1999) J. Immunol. , vol.162 , pp. 1303-1309
    • Ishii, T.1    Udono, H.2    Yamano, T.3    Ohta, H.4    Uenaka, A.5    Ono, T.6    Hizuta, A.7    Tanaka, N.8    Srivastava, P.K.9    Nakayama, E.10
  • 18
    • 0031947942 scopus 로고    scopus 로고
    • Hsp72-mediated augmentation of MHC class I surface expression and endogenous antigen presentation
    • Wells, A. D., Rai, S. K., Salvato, M. S., Band, H., and Malkovsky, M. Hsp72-mediated augmentation of MHC class I surface expression and endogenous antigen presentation. Int. Immunol., 10: 609-617, 1998.
    • (1998) Int. Immunol. , vol.10 , pp. 609-617
    • Wells, A.D.1    Rai, S.K.2    Salvato, M.S.3    Band, H.4    Malkovsky, M.5
  • 20
    • 0033179274 scopus 로고    scopus 로고
    • Heat shock protein 70 induced during tumor cell killing induces Th1 cytokines and targets immature dendritic cell precursors to enhance antigen uptake
    • Todryk, S., Melcher, A. A., Hardwick, N., Linardakis, E., Bateman, A., Colombo, M. P., Stoppacciaro, A., and Vile, R. G. Heat shock protein 70 induced during tumor cell killing induces Th1 cytokines and targets immature dendritic cell precursors to enhance antigen uptake. J. Immunolt., 163: 1398-1408, 1999.
    • (1999) J. Immunolt. , vol.163 , pp. 1398-1408
    • Todryk, S.1    Melcher, A.A.2    Hardwick, N.3    Linardakis, E.4    Bateman, A.5    Colombo, M.P.6    Stoppacciaro, A.7    Vile, R.G.8
  • 21
    • 0344129020 scopus 로고    scopus 로고
    • Enhanced susceptibility to cytotoxic T lymphocytes without increase of MHC class I antigen expression after conditional overexpression of heat shock protein 70 in target cells
    • Dressel, R., Lübbers, M., Walter, L., Herr, W., and Günther, E. Enhanced susceptibility to cytotoxic T lymphocytes without increase of MHC class I antigen expression after conditional overexpression of heat shock protein 70 in target cells. Eur. J. Immunol., 29: 3925-3935, 1999.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 3925-3935
    • Dressel, R.1    Lübbers, M.2    Walter, L.3    Herr, W.4    Günther, E.5
  • 22
    • 0032446378 scopus 로고    scopus 로고
    • Heterogeneous patterns of constitutive and heat shock induced expression of HLA-linked HSP70-1 and HSP70-2 heat shock genes in human melanoma cell lines
    • Dressel, R., Johnson, J. P., and Günther, E. Heterogeneous patterns of constitutive and heat shock induced expression of HLA-linked HSP70-1 and HSP70-2 heat shock genes in human melanoma cell lines. Melanoma Res., 8: 482-492, 1998.
    • (1998) Melanoma Res. , vol.8 , pp. 482-492
    • Dressel, R.1    Johnson, J.P.2    Günther, E.3
  • 23
    • 0030912893 scopus 로고    scopus 로고
    • Efficient pseudotyping of murine leukemia virus particles with chimeric human foamy virus envelope proteins
    • Lindemann, D., Bock, M., Schweizer, M., and Rethwilm, A. Efficient pseudotyping of murine leukemia virus particles with chimeric human foamy virus envelope proteins. J. Virol., 71: 4815-4820, 1997.
    • (1997) J. Virol. , vol.71 , pp. 4815-4820
    • Lindemann, D.1    Bock, M.2    Schweizer, M.3    Rethwilm, A.4
  • 25
    • 0032976195 scopus 로고    scopus 로고
    • Foamy virus capsids require the cognate envelope protein for particle export
    • Pietschmann, T., Heinkelein, M., Zentgraf, H-W., Rethwilm, A., and Lindemann, D. Foamy virus capsids require the cognate envelope protein for particle export. J. Virol., 73: 2613-2621, 1999.
    • (1999) J. Virol. , vol.73 , pp. 2613-2621
    • Pietschmann, T.1    Heinkelein, M.2    Zentgraf, H.-W.3    Rethwilm, A.4    Lindemann, D.5
  • 26
    • 0028705684 scopus 로고
    • Generation of high-titer pseudotyped retroviral vectors with very broad host range
    • Yee, J. K., Friedmann, T., and Burns, J. C. Generation of high-titer pseudotyped retroviral vectors with very broad host range. Methods Cell Biol., 43: 99-112, 1994.
    • (1994) Methods Cell Biol. , vol.43 , pp. 99-112
    • Yee, J.K.1    Friedmann, T.2    Burns, J.C.3
  • 27
    • 0034163280 scopus 로고    scopus 로고
    • Heat shock protein 70 is able to prevent heat shock-induced resistance of target cells to CTL
    • Dressel, R., Elsner, L., Quentin, T., Walter, L., and Günther, E. Heat shock protein 70 is able to prevent heat shock-induced resistance of target cells to CTL. J. Immunol., 164: 2362-2371, 2000.
    • (2000) J. Immunol. , vol.164 , pp. 2362-2371
    • Dressel, R.1    Elsner, L.2    Quentin, T.3    Walter, L.4    Günther, E.5
  • 28
    • 0031945664 scopus 로고    scopus 로고
    • Definition of extracellular localized epitopes of Hsp70 involved in an NK immune response
    • Botzler, C., Li, G., Issels, R. D., and Multhoff, G. Definition of extracellular localized epitopes of Hsp70 involved in an NK immune response. Cell Stress Chaperon., 3: 6-11, 1998.
    • (1998) Cell Stress Chaperon. , vol.3 , pp. 6-11
    • Botzler, C.1    Li, G.2    Issels, R.D.3    Multhoff, G.4
  • 29
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem., 68: 850-855, 1996.
    • (1996) Anal. Chem. , vol.68 , pp. 850-855
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 30
    • 0027981459 scopus 로고
    • Comparative analysis of the three major histocompatibility complex-linked heat shock protein 70 (Hsp70) genes of the rat
    • Walter, L., Rauh, F., and Günther, E. Comparative analysis of the three major histocompatibility complex-linked heat shock protein 70 (Hsp70) genes of the rat. Immunogenetics, 40: 325-330, 1994.
    • (1994) Immunogenetics , vol.40 , pp. 325-330
    • Walter, L.1    Rauh, F.2    Günther, E.3
  • 31
    • 0025314313 scopus 로고
    • The regulation and expression of MHC class I genes
    • David-Watine, B., Israël, A., and Kourilsky, P. The regulation and expression of MHC class I genes. Immunol. Today, 11: 286-292, 1990.
    • (1990) Immunol. Today , vol.11 , pp. 286-292
    • David-Watine, B.1    Israël, A.2    Kourilsky, P.3
  • 32
    • 0034659727 scopus 로고    scopus 로고
    • Synergistic induction of HLA class 1 expression by RelA and CIITA
    • Girdlestone, J. Synergistic induction of HLA class 1 expression by RelA and CIITA. Blood, 95: 3804-3808, 2000.
    • (2000) Blood , vol.95 , pp. 3804-3808
    • Girdlestone, J.1
  • 33
    • 0021259444 scopus 로고
    • Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells
    • Welch, W. J., and Feramisco, J. R. Nuclear and nucleolar localization of the 72, 000-dalton heat shock protein in heat-shocked mammalian cells. J. Biol. Chem., 259: 4501-4513, 1984.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4501-4513
    • Welch, W.J.1    Feramisco, J.R.2
  • 34
    • 0035834122 scopus 로고    scopus 로고
    • Dynamic changes in the localization of thermally unfolded nuclear proteins associated with chaperone-dependent protection
    • Nollen, E. A., Salomons, F. A., Brunsting, J. F., Want, J. J., Sibon, O. C., and Kampinga, H. H. Dynamic changes in the localization of thermally unfolded nuclear proteins associated with chaperone-dependent protection. Proc. Natl. Acad. Sci. USA, 98: 12038-12043, 2001.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12038-12043
    • Nollen, E.A.1    Salomons, F.A.2    Brunsting, J.F.3    Want, J.J.4    Sibon, O.C.5    Kampinga, H.H.6
  • 35
    • 0031132876 scopus 로고    scopus 로고
    • Heat shock protein 72 on tumor cells: A recognition structure for natural killer cells
    • Multhoff, G., Botzler, C., Jennen, L., Schmidt, J., Ellwart, J., and Issels, R. Heat shock protein 72 on tumor cells: a recognition structure for natural killer cells. J. Immunol., 158: 4341-4350, 1997.
    • (1997) J. Immunol. , vol.158 , pp. 4341-4350
    • Multhoff, G.1    Botzler, C.2    Jennen, L.3    Schmidt, J.4    Ellwart, J.5    Issels, R.6
  • 36
    • 0028099856 scopus 로고
    • Genetic aspects of the hsp70 multigene family in vertebrates
    • Günther, E., and Walter, L. Genetic aspects of the hsp70 multigene family in vertebrates. Experientia, 50: 987-1001, 1994.
    • (1994) Experientia , vol.50 , pp. 987-1001
    • Günther, E.1    Walter, L.2
  • 37
    • 0022427782 scopus 로고
    • The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles
    • Ungewickell, E. The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles. EMBO J., 4: 3385-3391, 1985.
    • (1985) EMBO J. , vol.4 , pp. 3385-3391
    • Ungewickell, E.1
  • 38
    • 0035661309 scopus 로고    scopus 로고
    • Augmentation of MHC class I antigen presentation via heat shock protein expression by hyperthermia
    • Ito, A., Shinkai, M., Honda, H., Wakabayashi, T., Yoshida, J., and Kobayashi, T. Augmentation of MHC class I antigen presentation via heat shock protein expression by hyperthermia. Cancer Immunol. Immunother., 50: 515-522, 2001.
    • (2001) Cancer Immunol. Immunother. , vol.50 , pp. 515-522
    • Ito, A.1    Shinkai, M.2    Honda, H.3    Wakabayashi, T.4    Yoshida, J.5    Kobayashi, T.6
  • 39
    • 0034004805 scopus 로고    scopus 로고
    • Heat shock proteins, tumor immunogenicity and antigen presentation: An integrated view
    • Wells, A. D., and Malkovsky, M. Heat shock proteins, tumor immunogenicity and antigen presentation: an integrated view. Immunol. Today, 21: 129-132, 2000.
    • (2000) Immunol. Today , vol.21 , pp. 129-132
    • Wells, A.D.1    Malkovsky, M.2
  • 40
    • 0026665975 scopus 로고
    • The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression
    • Abravaya, K., Myers, M. P., Murphy, S. P., and Morimoto, R. I. The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev., 6: 1153-1164, 1992.
    • (1992) Genes Dev. , vol.6 , pp. 1153-1164
    • Abravaya, K.1    Myers, M.P.2    Murphy, S.P.3    Morimoto, R.I.4
  • 41
    • 0036591973 scopus 로고    scopus 로고
    • BiP is feed-back regulated by control of protein translation efficiency
    • Gülow, K., Bienert, D., and Haas, I. G. BiP is feed-back regulated by control of protein translation efficiency. J. Cell Sci., 115: 2443-2452, 2002.
    • (2002) J. Cell Sci. , vol.115 , pp. 2443-2452
    • Gülow, K.1    Bienert, D.2    Haas, I.G.3
  • 42
    • 0038725690 scopus 로고    scopus 로고
    • The ABCs of granule-mediated cytotoxicity: New weapons in the arsenal
    • Lieberman, J. The ABCs of granule-mediated cytotoxicity: new weapons in the arsenal. Nat. Rev. Immunol., 3: 361-370, 2003.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 361-370
    • Lieberman, J.1
  • 44
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • Jäättelä, M., Wissing, D., Kokholm, K., Kallunki, T., and Egeblad, M. Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J., 17: 6124-6134, 1998.
    • (1998) EMBO J. , vol.17 , pp. 6124-6134
    • Jäättelä, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 45
    • 0041439707 scopus 로고    scopus 로고
    • Heat-shock protein 70 binds caspase-activated DNase and enhances its activity in TCR-stimulated T cells
    • DOI 10.1182/blood-2002-11-3499
    • Liu, Q. L., Kishi, H., Ohtsuka, K., and Muraguchi, A. Heat-shock protein 70 binds caspase-activated DNase and enhances its activity in TCR-stimulated T cells. Blood, DOI 10.1182/blood-2002-11-3499, 2003.
    • (2003) Blood
    • Liu, Q.L.1    Kishi, H.2    Ohtsuka, K.3    Muraguchi, A.4
  • 47
    • 0031708908 scopus 로고    scopus 로고
    • Heat shock protein expression and drug resistance in breast cancer patients treated with induction chemotherapy
    • Vargas-Roig, L. M., Gago, F. E., Tello, O., Aznar, J. C., and Ciocca, D. R. Heat shock protein expression and drug resistance in breast cancer patients treated with induction chemotherapy. Int. J. Cancer, 79: 468-475, 1998.
    • (1998) Int. J. Cancer , vol.79 , pp. 468-475
    • Vargas-Roig, L.M.1    Gago, F.E.2    Tello, O.3    Aznar, J.C.4    Ciocca, D.R.5
  • 48
    • 0034042857 scopus 로고    scopus 로고
    • The combined effect against colon-26 cells of heat treatment and immunization with heat treated colon-26 tumour cell extract
    • Okamoto, M., Tazawa, K., Kawagoshi, T., Maeda, M., Honda, T., Sakamoto, T., and Tsukada, K. The combined effect against colon-26 cells of heat treatment and immunization with heat treated colon-26 tumour cell extract. Int. J. Hyperthermia, 16: 263-273, 2000.
    • (2000) Int. J. Hyperthermia , vol.16 , pp. 263-273
    • Okamoto, M.1    Tazawa, K.2    Kawagoshi, T.3    Maeda, M.4    Honda, T.5    Sakamoto, T.6    Tsukada, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.