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Volumn 7, Issue 2, 2005, Pages 104-108

Immunotherapy for human cancer using heat shock protein-peptide complexes

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN GP 96; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; TUMOR VACCINE;

EID: 16844371156     PISSN: 15233790     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11912-005-0035-8     Document Type: Review
Times cited : (90)

References (37)
  • 1
    • 0036214288 scopus 로고    scopus 로고
    • Interaction of heat shock proteins with peptides and antigen presenting cells: Chaperoning of the innate and adaptive immune responses
    • Srivastava P: Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses. Annu Rev Immunol 2002, 20: 95-425.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 395-425
    • Srivastava, P.1
  • 2
    • 0028366212 scopus 로고
    • Heat shock proteins transfer peptides during antigen processing and CTL priming
    • Srivastava PK, Udono H, Blachere NE, Li Z: Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics 1994, 39:93-98.
    • (1994) Immunogenetics , vol.39 , pp. 93-98
    • Srivastava, P.K.1    Udono, H.2    Blachere, N.E.3    Li, Z.4
  • 3
    • 0029937037 scopus 로고    scopus 로고
    • Structural analysis of substrate binding by the molecular chaperone DnaK
    • Zhu X, Zhao Y, Burkholder WF, et al.: Structural analysis of substrate binding by the molecular chaperone DnaK. Science 1996, 272:1606-1614.
    • (1996) Science , vol.272 , pp. 1606-1614
    • Zhu, X.1    Zhao, Y.2    Burkholder, W.F.3
  • 4
    • 1642456660 scopus 로고    scopus 로고
    • HSP70 peptide binding mutants separate antigen delivery from dendritic cell stimulation
    • MacAry PA, Javid B, Floto RA, et al.: HSP70 peptide binding mutants separate antigen delivery from dendritic cell stimulation. Immunity 2004, 20:95-106.
    • (2004) Immunity , vol.20 , pp. 95-106
    • MacAry, P.A.1    Javid, B.2    Floto, R.A.3
  • 5
    • 1942469336 scopus 로고    scopus 로고
    • Identification of the N-terminal peptide binding site of glucose-regulated protein 94
    • Gidalevitz T, Biswas C, Ding H, et al.: Identification of the N-terminal peptide binding site of glucose-regulated protein 94. J Biol Chem 2004, 279: 6543-16552.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16543-16552
    • Gidalevitz, T.1    Biswas, C.2    Ding, H.3
  • 6
    • 0037011072 scopus 로고    scopus 로고
    • GRP94 (gp96) and GRP94 N-terminal geldanamycin binding domain elicit tissue nonrestricted tumor suppression
    • Baker-LePain JC, Sarzotti M, Fields TA, et al.: GRP94 (gp96) and GRP94 N-terminal geldanamycin binding domain elicit tissue nonrestricted tumor suppression. J Exp Med 2002, 196: 447-1459.
    • (2002) J. Exp. Med. , vol.196 , pp. 1447-1459
    • Baker-LePain, J.C.1    Sarzotti, M.2    Fields, T.A.3
  • 7
    • 2942518348 scopus 로고    scopus 로고
    • Proteomics shows Hsp70 does not bind peptide sequences indiscriminately in vivo
    • Grossmann ME, Madden BJ, Gao F, et al.: Proteomics shows Hsp70 does not bind peptide sequences indiscriminately in vivo. Exp Cell Res 2004, 297:108-117.
    • (2004) Exp. Cell Res. , vol.297 , pp. 108-117
    • Grossmann, M.E.1    Madden, B.J.2    Gao, F.3
  • 8
    • 0027484417 scopus 로고
    • Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
    • Blond-Elguindi S, Cwirla SE, Dower WJ, et al.: Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 1993, 75: 17-728.
    • (1993) Cell , vol.75 , pp. 717-728
    • Blond-Elguindi, S.1    Cwirla, S.E.2    Dower, W.J.3
  • 9
    • 0033571087 scopus 로고    scopus 로고
    • Cutting edge: Tumor secreted heat shock-fusion protein elicits CD8 cells for rejection
    • Podack Yamazaki K, Nguyen T, Podack ER: Cutting edge: Tumor secreted heat shock-fusion protein elicits CD8 cells for rejection. J Immunol 1999, 163:5178-5182.
    • (1999) J. Immunol. , vol.163 , pp. 5178-5182
    • Podack Yamazaki, K.1    Nguyen, T.2    Podack, E.R.3
  • 10
    • 1242316148 scopus 로고    scopus 로고
    • Enhanced efficacy of tumor cell vaccines transfected with secretable hsp70
    • Massa C, Guiducci C, Arioli I, et al.: Enhanced efficacy of tumor cell vaccines transfected with secretable hsp70. Cancer Res 2004, 64:1502-1508.
    • (2004) Cancer Res. , vol.64 , pp. 1502-1508
    • Massa, C.1    Guiducci, C.2    Arioli, I.3
  • 11
    • 2142750909 scopus 로고    scopus 로고
    • Bacterial heat shock proteins promote CD91-dependent class I MHC cross-presentation of chaperoned peptide to CD8+ T cells by cytosolic mechanisms in dendritic cells versus vacuolar mechanisms in macrophages
    • Tobian AA, Canaday DH, Boom WH, Harding CV: Bacterial heat shock proteins promote CD91-dependent class I MHC cross-presentation of chaperoned peptide to CD8+ T cells by cytosolic mechanisms in dendritic cells versus vacuolar mechanisms in macrophages. J Immunol 2004, 172:5277-5286.
    • (2004) J. Immunol. , vol.172 , pp. 5277-5286
    • Tobian, A.A.1    Canaday, D.H.2    Boom, W.H.3    Harding, C.V.4
  • 12
    • 6344276691 scopus 로고    scopus 로고
    • Bacterial heat shock proteins enhance class II MHC antigen processing and presentation of chaperoned peptides to CD4+ T cells
    • Tobian AA, Canaday DH, Harding CV: Bacterial heat shock proteins enhance class II MHC antigen processing and presentation of chaperoned peptides to CD4+ T cells. J Immunol, 2004, 173: 130-5137.
    • (2004) J. Immunol. , vol.173 , pp. 5130-5137
    • Tobian, A.A.1    Canaday, D.H.2    Harding, C.V.3
  • 13
    • 3242811091 scopus 로고    scopus 로고
    • Heat shock protein-mediated cross-presentation of exogenous HIV antigen on HLA class I and class II
    • SenGupta D, Norris PJ, Suscovich TJ, et al.: Heat shock protein-mediated cross-presentation of exogenous HIV antigen on HLA class I and class II. J Immunol 2004, 173:1987-1993.
    • (2004) J. Immunol. , vol.173 , pp. 1987-1993
    • SenGupta, D.1    Norris, P.J.2    Suscovich, T.J.3
  • 14
    • 0036133062 scopus 로고    scopus 로고
    • Immunization with chaperone-peptide complex induces low-avidity cytotoxic T lymphocytes providing transient protection against herpes simplex virus infection
    • Kumaraguru U, Gierynska M, Norman S, et al.: Immunization with chaperone-peptide complex induces low-avidity cytotoxic T lymphocytes providing transient protection against herpes simplex virus infection. J Virol 2002, 76:136-141.
    • (2002) J. Virol. , vol.76 , pp. 136-141
    • Kumaraguru, U.1    Gierynska, M.2    Norman, S.3
  • 15
    • 1542514719 scopus 로고    scopus 로고
    • Concomitant helper response rescues otherwise low avidity CD8+ memory CTLs to become efficient effectors in vivo
    • Kumaraguru U, Suvas S, Biswas PS, et al.: Concomitant helper response rescues otherwise low avidity CD8+ memory CTLs to become efficient effectors in vivo. J Immunol 2004, 172:3719-3124.
    • (2004) J. Immunol. , vol.172 , pp. 3124-3719
    • Kumaraguru, U.1    Suvas, S.2    Biswas, P.S.3
  • 16
    • 2442517310 scopus 로고    scopus 로고
    • Glycoprotein 96 can chaperone both MHC class I- and class II-restricted epitopes for in vivo presentation, but selectively primes CD8(+) T cell effector function
    • Doody AD, Kovalchin JT, Mihalyo MA, et al.: Glycoprotein 96 can chaperone both MHC class I- and class II-restricted epitopes for in vivo presentation, but selectively primes CD8(+) T cell effector function. J Immunol 2004, 172:6087-6092.
    • (2004) J. Immunol. , vol.172 , pp. 6087-6092
    • Doody, A.D.1    Kovalchin, J.T.2    Mihalyo, M.A.3
  • 17
    • 1842865717 scopus 로고    scopus 로고
    • DNA vaccination with gp96-peptide fusion proteins induces protection against an intracellular bacterial pathogen
    • Rapp UK, Kaufmann SH: DNA vaccination with gp96-peptide fusion proteins induces protection against an intracellular bacterial pathogen. Int Immunol 2004, 16:597-605.
    • (2004) Int. Immunol. , vol.16 , pp. 597-605
    • Rapp, U.K.1    Kaufmann, S.H.2
  • 18
    • 0037431540 scopus 로고    scopus 로고
    • Immunization with tumor-derived ER chaperone grp170 elicits tumor-specific CD8+ T-cell responses and reduces pulmonary metastatic disease
    • Wang XY, Kazim L, Repasky EA, Subjeck JR: Immunization with tumor-derived ER chaperone grp170 elicits tumor-specific CD8+ T-cell responses and reduces pulmonary metastatic disease. Int J Cancer 2003, 105:226-231.
    • (2003) Int. J. Cancer , vol.105 , pp. 226-231
    • Wang, X.Y.1    Kazim, L.2    Repasky, E.A.3    Subjeck, J.R.4
  • 19
    • 0141992909 scopus 로고    scopus 로고
    • HSP110-HER2/neu chaperone complex vaccine induces protective immunity against spontaneous mammary tumors in HER-2/neu transgenic mice
    • Manjili MH, Wang XY, Chen X, et al.: HSP110-HER2/neu chaperone complex vaccine induces protective immunity against spontaneous mammary tumors in HER-2/neu transgenic mice. J Immunol 2003, 171:4054-4061.
    • (2003) J. Immunol. , vol.171 , pp. 4054-4061
    • Manjili, M.H.1    Wang, X.Y.2    Chen, X.3
  • 20
    • 0037298180 scopus 로고    scopus 로고
    • Heat shock protein 70 expression induces antitumor immunity during intracellular hyperthermia using magnetite nanoparticles
    • Ito A, Shinkai M, Honda H, et al.: Heat shock protein 70 expression induces antitumor immunity during intracellular hyperthermia using magnetite nanoparticles. Cancer Immunol Immunother 2003, 52:80-88.
    • (2003) Cancer Immunol. Immunother. , vol.52 , pp. 80-88
    • Ito, A.1    Shinkai, M.2    Honda, H.3
  • 21
    • 0038408927 scopus 로고    scopus 로고
    • Tumor-derived chaperone-rich cell lysates are effective therapeutic vaccines against a variety of cancers
    • Graner MW, Zeng Y, Feng H, Katsanis E: Tumor-derived chaperone-rich cell lysates are effective therapeutic vaccines against a variety of cancers. Cancer Immunol Immunother 2003, 52: 26-234.
    • (2003) Cancer Immunol. Immunother. , vol.52 , pp. 226-234
    • Graner, M.W.1    Zeng, Y.2    Feng, H.3    Katsanis, E.4
  • 23
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • Basu S, Binder RJ, Ramalingam T, Srivastava PK: CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 2001, 14:303-313.
    • (2001) Immunity , vol.14 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 24
    • 4744371115 scopus 로고    scopus 로고
    • The heat-shock protein receptors: Some answers and more questions
    • Binder RJ, Vatner R, Srivastava P: The heat-shock protein receptors: some answers and more questions. Tissue Antigens 2004, 64:442-445.
    • (2004) Tissue Antigens , vol.64 , pp. 442-445
    • Binder, R.J.1    Vatner, R.2    Srivastava, P.3
  • 25
    • 1942501656 scopus 로고    scopus 로고
    • Essential role of CD91 in re-presentation of gp96-chaperoned peptides
    • Binder RJ, Srivastava PK: Essential role of CD91 in re-presentation of gp96-chaperoned peptides. Proc Natl Acad Sci U S A 2004, 101:6128-6133.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 6128-6133
    • Binder, R.J.1    Srivastava, P.K.2
  • 26
    • 0037477628 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein is a calreticulin coreceptor that signals focal adhesion disassembly
    • Orr AW, Pedraza CE, Pallero MA, et al.: Low density lipoprotein receptor-related protein is a calreticulin coreceptor that signals focal adhesion disassembly. J Cell Biol 2003, 161: 179-1189.
    • (2003) J. Cell Biol. , vol.161 , pp. 1179-1189
    • Orr, A.W.1    Pedraza, C.E.2    Pallero, M.A.3
  • 27
    • 0038603179 scopus 로고    scopus 로고
    • The heat-shock protein receptor CD91 is up-regulated in monocytes of HIV-1-infected 'true' long-term nonprogressors
    • Stebbing J, Gazzard B, Kim L, et al.: The heat-shock protein receptor CD91 is up-regulated in monocytes of HIV-1-infected 'true' long-term nonprogressors. Blood 2003, 101: 000-4004.
    • (2003) Blood , vol.101 , pp. 4000-4004
    • Stebbing, J.1    Gazzard, B.2    Kim, L.3
  • 28
    • 0042442014 scopus 로고    scopus 로고
    • Disease associated dendritic cells respond to disease-specific antigens through the common heat shock protein receptor
    • Stebbing J, Gazzard B, Portsmouth S, et al.: Disease associated dendritic cells respond to disease-specific antigens through the common heat shock protein receptor. Blood 2003, 102: 806-1814.
    • (2003) Blood , vol.102 , pp. 1806-1814
    • Stebbing, J.1    Gazzard, B.2    Portsmouth, S.3
  • 29
    • 0345305789 scopus 로고    scopus 로고
    • Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells
    • Berwin B, Hart JP, Rice S, et al.: Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells. EMBO J 2003, 22:6127-6136.
    • (2003) EMBO J. , vol.22 , pp. 6127-6136
    • Berwin, B.1    Hart, J.P.2    Rice, S.3
  • 30
    • 10944228434 scopus 로고    scopus 로고
    • SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin
    • Berwin B, Delneste Y, Lovingood RV, et al.: SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin. J Biol Chem 2004, 279:51250-51257.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51250-51257
    • Berwin, B.1    Delneste, Y.2    Lovingood, R.V.3
  • 31
    • 0038107402 scopus 로고    scopus 로고
    • The heat shock protein gp96 binds to human neutrophils and monocytes and stimulates effector functions
    • Radsak MP, Hilf N, Singh-Jasuja H, et al.: The heat shock protein gp96 binds to human neutrophils and monocytes and stimulates effector functions. Blood 2003, 101:2810-2815.
    • (2003) Blood , vol.101 , pp. 2810-2815
    • Radsak, M.P.1    Hilf, N.2    Singh-Jasuja, H.3
  • 32
    • 0035132104 scopus 로고    scopus 로고
    • Human heat shock protein 70 peptide complexes specifically activate antimelanoma T cells
    • Castelli C, Ciupitu AM, Rini F, et al.: Human heat shock protein 70 peptide complexes specifically activate antimelanoma T cells. Cancer Res 2001, 61:222-227.
    • (2001) Cancer Res. , vol.61 , pp. 222-227
    • Castelli, C.1    Ciupitu, A.M.2    Rini, F.3
  • 33
    • 0037111218 scopus 로고    scopus 로고
    • Tumor-derived heat shock protein 70 peptide complexes are cross-presented by human dendritic cells
    • Noessner E, Gastpar R, Milani V, et al.: Tumor-derived heat shock protein 70 peptide complexes are cross-presented by human dendritic cells. J Immunol 2002, 169:5424-5432.
    • (2002) J. Immunol. , vol.169 , pp. 5424-5432
    • Noessner, E.1    Gastpar, R.2    Milani, V.3
  • 34
    • 2942696134 scopus 로고    scopus 로고
    • Cross-presentation of human melanoma peptide antigen MART-1 to CTLs from in vitro reconstituted gp96/MART-1 complexes
    • Staib F, Distler M, Bethke K, et al.: Cross-presentation of human melanoma peptide antigen MART-1 to CTLs from in vitro reconstituted gp96/MART-1 complexes. Cancer Immun 2004, 4:3.
    • (2004) Cancer Immun. , vol.4 , pp. 3
    • Staib, F.1    Distler, M.2    Bethke, K.3
  • 35
    • 0037108696 scopus 로고    scopus 로고
    • Vaccination of metastatic melanoma patients with autologous tumor-derived heat shock protein gp96-peptide complexes: Clinical and immunologic findings
    • Belli F, Testori A, Rivoltini L, et al.: Vaccination of metastatic melanoma patients with autologous tumor-derived heat shock protein gp96-peptide complexes: clinical and immunologic findings. J Clin Oncol 2002, 20:4169-4180.
    • (2002) J. Clin. Oncol. , vol.20 , pp. 4169-4180
    • Belli, F.1    Testori, A.2    Rivoltini, L.3
  • 36
    • 10744233222 scopus 로고    scopus 로고
    • Vaccination with autologous tumor-derived heat-shock protein gp96 after liver resection for metastatic colorectal cancer
    • Mazzaferro V, Coppa J, Carrabba MG, et al.: Vaccination with autologous tumor-derived heat-shock protein gp96 after liver resection for metastatic colorectal cancer. Clin Cancer Res 2003, 9:3235-3245.
    • (2003) Clin. Cancer Res. , vol.9 , pp. 3235-3245
    • Mazzaferro, V.1    Coppa, J.2    Carrabba, M.G.3
  • 37
    • 0141955112 scopus 로고    scopus 로고
    • Human tumor-derived heat shock protein 96 mediates in vitro activation and in vivo expansion of melanoma- and colon carcinoma-specific T cells
    • Rivoltini L, Castelli C, Carrabba M, et al.: Human tumor-derived heat shock protein 96 mediates in vitro activation and in vivo expansion of melanoma- and colon carcinoma-specific T cells. J Immunol 2003, 171:3467-3474.
    • (2003) J. Immunol. , vol.171 , pp. 3467-3474
    • Rivoltini, L.1    Castelli, C.2    Carrabba, M.3


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