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Volumn 169, Issue 10, 2002, Pages 5424-5432

Tumor-derived heat shock protein 70 peptide complexes are cross-presented by human dendritic cells

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 70; HLA A ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MONOPHENOL MONOOXYGENASE; PEPTIDE; RECEPTOR; TUMOR NECROSIS FACTOR ALPHA;

EID: 0037111218     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.169.10.5424     Document Type: Article
Times cited : (224)

References (58)
  • 1
    • 0028114348 scopus 로고
    • Heat shock protein-peptide complexes in cancer immunotherapy
    • Srivastava, P. K., and H. Udono. 1994. Heat shock protein-peptide complexes in cancer immunotherapy. Curr. Opin. Immunol. 6:728.
    • (1994) Curr. Opin. Immunol. , vol.6 , pp. 728
    • Srivastava, P.K.1    Udono, H.2
  • 2
    • 0028979675 scopus 로고
    • A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides
    • Suto, R., and P. K. Srivastava. 1995. A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 269:1585.
    • (1995) Science , vol.269 , pp. 1585
    • Suto, R.1    Srivastava, P.K.2
  • 4
    • 0030820099 scopus 로고    scopus 로고
    • Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations
    • Tamura, Y., P. Peng, K. Liu, M. Daou, and P. K. Srivastava. 1997. Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations. Science 278:117.
    • (1997) Science , vol.278 , pp. 117
    • Tamura, Y.1    Peng, P.2    Liu, K.3    Daou, M.4    Srivastava, P.K.5
  • 5
    • 0033819308 scopus 로고    scopus 로고
    • Immunization of cancer patients with autologous cancer-derived heat shock protein gp96 preparations: A pilot study
    • Janetzki, S., D. Palla, V. Rosenhauer, H. Lochs, J. J. Lewis, and P. K. Srivastava. 2000. Immunization of cancer patients with autologous cancer-derived heat shock protein gp96 preparations: A pilot study. Int. J. Cancer 88:232.
    • (2000) Int. J. Cancer , vol.88 , pp. 232
    • Janetzki, S.1    Palla, D.2    Rosenhauer, V.3    Lochs, H.4    Lewis, J.J.5    Srivastava, P.K.6
  • 6
    • 0034328883 scopus 로고    scopus 로고
    • Immunotherapy of human cancer: Lessons from mice
    • Srivastava, P. K. 2001. Immunotherapy of human cancer: Lessons from mice. Nat. Immunol. 5:363.
    • (2001) Nat. Immunol. , vol.5 , pp. 363
    • Srivastava, P.K.1
  • 7
    • 0036512171 scopus 로고    scopus 로고
    • Roles of heat-shock proteins in innate and adaptive immunity
    • Srivastava, P. K. 2002. Roles of heat-shock proteins in innate and adaptive immunity. Nat. Rev. Immunol. 2:185.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 185
    • Srivastava, P.K.1
  • 9
    • 0032849641 scopus 로고    scopus 로고
    • Dendritic cells: Expansion and differentiation with hematopoietic growth factors
    • Young, J. W. 1999. Dendritic cells: Expansion and differentiation with hematopoietic growth factors. Curr. Opin. Hematol. 6:135.
    • (1999) Curr. Opin. Hematol. , vol.6 , pp. 135
    • Young, J.W.1
  • 11
    • 0029812040 scopus 로고    scopus 로고
    • Constitutive class 1-restricted exogenous presentation of self antigens in vivo
    • Kurts, C., W. R. Heath, F. R. Carbone, J. Allison, J. F. Miller, and H. Kosaka. 1996. Constitutive class 1-restricted exogenous presentation of self antigens in vivo. J. Exp. Med. 184:923.
    • (1996) J. Exp. Med. , vol.184 , pp. 923
    • Kurts, C.1    Heath, W.R.2    Carbone, F.R.3    Allison, J.4    Miller, J.F.5    Kosaka, H.6
  • 14
  • 16
    • 0035070198 scopus 로고    scopus 로고
    • CD91: CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70 and calreticulin
    • Basu, S., R. J. Binder, T. Ramalingam, and P. K. Srivastava. 2001. CD91: CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70 and calreticulin. Immunity 14:303.
    • (2001) Immunity , vol.14 , pp. 303
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 17
    • 0034252620 scopus 로고    scopus 로고
    • CD91: A receptor for heat shock protein gp96
    • Binder, R. J., D. K. Han, and P. K. Srivastava. 2000. CD91: A receptor for heat shock protein gp96. Nat. Immunol. 1:151.
    • (2000) Nat. Immunol. , vol.1 , pp. 151
    • Binder, R.J.1    Han, D.K.2    Srivastava, P.K.3
  • 18
    • 0022534393 scopus 로고
    • Tumor rejection antigens of chemically induced sarcomas in inbred mice
    • Srivastava, P. K., A. B. DeLeo, and L. J. Old. 1986. Tumor rejection antigens of chemically induced sarcomas in inbred mice. Proc. Natl. Acad. Sci. USA 83:3407.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3407
    • Srivastava, P.K.1    DeLeo, A.B.2    Old, L.J.3
  • 19
    • 0027260585 scopus 로고
    • Heat shock protein 70-associated peptides elicit specific cancer immunity
    • Udono, H., and P. K. Srivastava. 1993. Heat shock protein 70-associated peptides elicit specific cancer immunity. J. Exp. Med. 178:1391.
    • (1993) J. Exp. Med. , vol.178 , pp. 1391
    • Udono, H.1    Srivastava, P.K.2
  • 20
    • 0028301079 scopus 로고
    • Comparison of tumor-specific immuno-genicities of stress-induced proteins gp96, HSP90 and HSP70
    • Udono, H., and P. K. Srivastava. 1994. Comparison of tumor-specific immuno-genicities of stress-induced proteins gp96, HSP90 and HSP70. J. Immunol. 152:5398.
    • (1994) J. Immunol. , vol.152 , pp. 5398
    • Udono, H.1    Srivastava, P.K.2
  • 22
    • 0030775140 scopus 로고    scopus 로고
    • Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity
    • Blachere, N. E., Z. Li, R. Y. Chandawarkar, R. Suto, N. S. Jaikaria, S. Basu, H. Udono, and P. K. Srivastava. 1997. Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity. J. Exp. Med. 186:1315.
    • (1997) J. Exp. Med. , vol.186 , pp. 1315
    • Blachere, N.E.1    Li, Z.2    Chandawarkar, R.Y.3    Suto, R.4    Jaikaria, N.S.5    Basu, S.6    Udono, H.7    Srivastava, P.K.8
  • 23
    • 0032473485 scopus 로고    scopus 로고
    • Immunization with a lymphocytic choriomeningitis virus peptide mixed with heat shock protein 70 results in protective antiviral immunity and specific cytotoxic T lymphocytes
    • Ciupitu, A. M., M. Petersson, C. L. O'Donnell, K. Williams, S. Jindal, R. Kiessling, and R. M. Welsh. 1998. Immunization with a lymphocytic choriomeningitis virus peptide mixed with heat shock protein 70 results in protective antiviral immunity and specific cytotoxic T lymphocytes. J. Exp. Med. 187:685.
    • (1998) J. Exp. Med. , vol.187 , pp. 685
    • Ciupitu, A.M.1    Petersson, M.2    O'Donnell, C.L.3    Williams, K.4    Jindal, S.5    Kiessling, R.6    Welsh, R.M.7
  • 25
    • 0031700780 scopus 로고    scopus 로고
    • Heat-shock protein-based anticancer immunotherapy: An idea whose time has come
    • Menoret, A., and R. Chandawarkar. 1998. Heat-shock protein-based anticancer immunotherapy: An idea whose time has come. Semin. Oncol. 25:654.
    • (1998) Semin. Oncol. , vol.25 , pp. 654
    • Menoret, A.1    Chandawarkar, R.2
  • 29
    • 0019285686 scopus 로고
    • A monoclonal antibody that recognizes an antigenic determinant shared by HLA A2 and B17
    • McMichael, A. J., P. Parham, N. Rust, and F. Brodsky. 1980. A monoclonal antibody that recognizes an antigenic determinant shared by HLA A2 and B17. Hum. Immunol. 1:121.
    • (1980) Hum. Immunol. , vol.1 , pp. 121
    • McMichael, A.J.1    Parham, P.2    Rust, N.3    Brodsky, F.4
  • 31
    • 0342547302 scopus 로고    scopus 로고
    • Purification of immunogenic heat shock protein-peptide complexes by ADP-affinity chromatography
    • Peng, P., A. Menoret, and P. K. Srivastava. 1997. Purification of immunogenic heat shock protein-peptide complexes by ADP-affinity chromatography. J. Immunol. Methods 204:3.
    • (1997) J. Immunol. Methods , vol.204 , pp. 3
    • Peng, P.1    Menoret, A.2    Srivastava, P.K.3
  • 33
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine
    • Asea, A., S.-K. Kraeft, E. A. Kurt-Jones, M. A. Stevenson, L. B. Chen, R. W. Finberg, G. C. Koo, and S. K. Calderwood. 2000. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat. Med. 6:435.
    • (2000) Nat. Med. , vol.6 , pp. 435
    • Asea, A.1    Kraeft, S.-K.2    Kurt-Jones, E.A.3    Stevenson, M.A.4    Chen, L.B.5    Finberg, R.W.6    Koo, G.C.7    Calderwood, S.K.8
  • 34
    • 0035007710 scopus 로고    scopus 로고
    • The role of heat shock protein (HSP70) in dendritic cell maturation: HSP70 induces the maturation of immature dendritic cells but reduces DC differentiation from monocyte precursors
    • Kuppner, M. C., R. Gastpar, S. Gelwer, E. Noessner, O. Ochmann, A. Scharner, and R. D. Issels. 2001. The role of heat shock protein (HSP70) in dendritic cell maturation: HSP70 induces the maturation of immature dendritic cells but reduces DC differentiation from monocyte precursors. Eur. J. Immunol. 31:1602.
    • (2001) Eur. J. Immunol. , vol.31 , pp. 1602
    • Kuppner, M.C.1    Gastpar, R.2    Gelwer, S.3    Noessner, E.4    Ochmann, O.5    Scharner, A.6    Issels, R.D.7
  • 37
    • 0035500779 scopus 로고    scopus 로고
    • Primary tumor tissue lysates are enriched in heat shock proteins and induce the maturation of human dendritic cells
    • Somersan, S., M. Larsson, J. Fonteneau, S. Basu, P. Srivastava, and N. Bhardway. 2001. Primary tumor tissue lysates are enriched in heat shock proteins and induce the maturation of human dendritic cells. J. Immunol. 167:4844.
    • (2001) J. Immunol. , vol.167 , pp. 4844
    • Somersan, S.1    Larsson, M.2    Fonteneau, J.3    Basu, S.4    Srivastava, P.5    Bhardway, N.6
  • 38
    • 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., A. A. Melcher, N. Hardwick, E. Linardakis, A. Bateman, M. P. Colombo, A. Stoppacciaro, and R. G. Vile. 1999. Heat shock protein 70 induced during tumor cell killing induces Th1 cytokines and targets immature dendritic cell precursors to enhance antigen uptake. J. Immunol. 163:1398.
    • (1999) J. Immunol. , vol.163 , pp. 1398
    • 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
  • 39
    • 0031132876 scopus 로고    scopus 로고
    • Heat shock protein 72 on tumor cells: A recognition structure for natural killer cells
    • Multhoff, G., C. Botzler, L. Jennen, J. Schmidt, J. Ellwart, and R. D. Issels. 1997. Heat shock protein 72 on tumor cells: A recognition structure for natural killer cells. J. Immunol. 158:4341.
    • (1997) J. Immunol. , vol.158 , pp. 4341
    • Multhoff, G.1    Botzler, C.2    Jennen, L.3    Schmidt, J.4    Ellwart, J.5    Issels, R.D.6
  • 41
    • 3543053363 scopus 로고    scopus 로고
    • Immature dendritic cells phagocytose apoptotic cells via α,β and CD36, and cross-present antigens to cytotoxic T lymphocytes
    • Albert, M. L., S. F. Pearce, L. M. Francisco, B. Sauter, P. Roy, R. L. Silverstein, and N. Bhardwaj. 1998. Immature dendritic cells phagocytose apoptotic cells via α,β and CD36, and cross-present antigens to cytotoxic T lymphocytes. J. Exp. Med. 188:1359.
    • (1998) J. Exp. Med. , vol.188 , pp. 1359
    • Albert, M.L.1    Pearce, S.F.2    Francisco, L.M.3    Sauter, B.4    Roy, P.5    Silverstein, R.L.6    Bhardwaj, N.7
  • 42
    • 0032101221 scopus 로고    scopus 로고
    • Heat shock proteins come of age: Primitive functions acquire new roles in an adaptive world
    • Srivastava, P. K., A. Menoret, S. Basu, R. J. Binder, and K. L. McQuade. 1998. Heat shock proteins come of age: Primitive functions acquire new roles in an adaptive world. Immunity 8:657.
    • (1998) Immunity , vol.8 , pp. 657
    • Srivastava, P.K.1    Menoret, A.2    Basu, S.3    Binder, R.J.4    McQuade, K.L.5
  • 43
    • 0033559496 scopus 로고    scopus 로고
    • Human 60-kDa heat-shock protein: A danger signal to the innate immune system
    • Chen, W., U. Syldath, K. Bellmann, V. Burkart, and H. Kolb. 1999. Human 60-kDa heat-shock protein: A danger signal to the innate immune system. J. Immunol. 162:3212.
    • (1999) J. Immunol. , vol.162 , pp. 3212
    • Chen, W.1    Syldath, U.2    Bellmann, K.3    Burkart, V.4    Kolb, H.5
  • 44
    • 0033975855 scopus 로고    scopus 로고
    • Cutting edge: Heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells
    • Kol, A., A. H. Lichtman, R. W. Finberg, P. Libby, and E. A. Kurt-Jones. 2000. Cutting edge: Heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells. J. Immunol. 164:13.
    • (2000) J. Immunol. , vol.164 , pp. 13
    • Kol, A.1    Lichtman, A.H.2    Finberg, R.W.3    Libby, P.4    Kurt-Jones, E.A.5
  • 47
    • 0035893009 scopus 로고    scopus 로고
    • Cell surface targeting of heat shock protein gp96 induces dendritic cell maturation and antitumor immunity
    • Zheng, H., J. Dai, D. Stoilova, and Z. Li. 2001. Cell surface targeting of heat shock protein gp96 induces dendritic cell maturation and antitumor immunity. J. Immunol. 167:6731.
    • (2001) J. Immunol. , vol.167 , pp. 6731
    • Zheng, H.1    Dai, J.2    Stoilova, D.3    Li, Z.4
  • 50
    • 0033061017 scopus 로고    scopus 로고
    • Cytotoxic T lymphocyte activation by cross-priming
    • Heath, W. R., and F. R. Carbone. 1999. Cytotoxic T lymphocyte activation by cross-priming. Curr. Opin. Immunol. 11:314.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 314
    • Heath, W.R.1    Carbone, F.R.2
  • 51
    • 0035907379 scopus 로고    scopus 로고
    • Heat shock protein-chaperoned peptides but not free peptides introduced in the cytosol are presented efficiently by major histocompatibility complex I molecules
    • Binder, R. J., N. E. Blachere, and P. K. Srivastava. 2001. Heat shock protein-chaperoned peptides but not free peptides introduced in the cytosol are presented efficiently by major histocompatibility complex I molecules. J. Biol. Chem. 276:17163.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17163
    • Binder, R.J.1    Blachere, N.E.2    Srivastava, P.K.3
  • 54
    • 0028934336 scopus 로고
    • Randomized trials of hyperthermia as adjuvant to radio-therapy for recurrent or metastatic malignant melanoma
    • Overgaard, J., D. Gonzales, M. C. C. M. Hulshof, G. Arcangeli, O. Dahl, and S. M. Bentzen. 1995. Randomized trials of hyperthermia as adjuvant to radio-therapy for recurrent or metastatic malignant melanoma. Lancet 345:540.
    • (1995) Lancet , vol.345 , pp. 540
    • Overgaard, J.1    Gonzales, D.2    Hulshof, M.C.C.M.3    Arcangeli, G.4    Dahl, O.5    Bentzen, S.M.6
  • 56
    • 0033747044 scopus 로고    scopus 로고
    • Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the KF-κB pathway
    • Basu, S., R. J. Binder, R. Suto, K. M. Anderson, and P. K. Srivastava. 2000. Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the KF-κB pathway. Int. Immunol. 12:1539.
    • (2000) Int. Immunol. , vol.12 , pp. 1539
    • Basu, S.1    Binder, R.J.2    Suto, R.3    Anderson, K.M.4    Srivastava, P.K.5
  • 57
    • 0031836938 scopus 로고    scopus 로고
    • Tumor immunogenicity is determined by the mechanism of cell death via induction of heat shock protein expression
    • Melcher, A. A., S. Todryk, N. Hardwick, M. Ford, M. Jackobson, and R. G. Vile. 1998. Tumor immunogenicity is determined by the mechanism of cell death via induction of heat shock protein expression. Nat. Med. 4:581.
    • (1998) Nat. Med. , vol.4 , pp. 581
    • Melcher, A.A.1    Todryk, S.2    Hardwick, N.3    Ford, M.4    Jackobson, M.5    Vile, R.G.6
  • 58
    • 0035167866 scopus 로고    scopus 로고
    • Characterization of heat shock protein 110 and glucose-regulated protein 170 as cancer vaccines and the effect of fever-range hyperthermia on vaccine activity
    • Wang, X.-Y., L. Kazim, E. A. Repasky, and J. R. Subjeck. 2001. Characterization of heat shock protein 110 and glucose-regulated protein 170 as cancer vaccines and the effect of fever-range hyperthermia on vaccine activity. J. Immunol. 165:490.
    • (2001) J. Immunol. , vol.165 , pp. 490
    • Wang, X.-Y.1    Kazim, L.2    Repasky, E.A.3    Subjeck, J.R.4


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