메뉴 건너뛰기




Volumn 2, Issue 2, 2010, Pages 57-62

Role of heat shock proteins in immune response and immunotherapy for human cancer

Author keywords

Cancer; Chaperone; Heat Shock Factor; Immune response

Indexed keywords

CANCER VACCINE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90;

EID: 79952013014     PISSN: None     EISSN: 0976044X     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (9)

References (55)
  • 1
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in drosophila
    • Ritossa F, A new puffing pattern induced by temperature shock and DNP in drosophila, Cellular and Molecular Life Sciences (CMLS), 18(12), 1962, 571-573.
    • (1962) Cellular and Molecular Life Sciences (CMLS) , vol.18 , Issue.12 , pp. 571-573
    • Ritossa, F.1
  • 2
    • 0030154255 scopus 로고    scopus 로고
    • Discovery of the heat shock response
    • Ritossa F, Discovery of the heat shock response, Cell Stress Chaperones, 1(2), 1996, 97-8.
    • (1996) Cell Stress Chaperones , vol.1 , Issue.2 , pp. 97-98
    • Ritossa, F.1
  • 4
    • 0034957003 scopus 로고    scopus 로고
    • The Drosophila Dpit47 protein is a nuclear HSP90 cochaperone that interacts with DNA polymerase alpha
    • June
    • Crevel G, Bates H, Huikeshoven H, Cotterill S, The Drosophila Dpit47 protein is a nuclear HSP90 cochaperone that interacts with DNA polymerase alpha., J. Cell. Sci., 114, 2001, June, 2015-25.
    • (2001) J. Cell. Sci. , vol.114 , pp. 2015-2025
    • Crevel, G.1    Bates, H.2    Huikeshoven, H.3    Cotterill, S.4
  • 6
    • 0027423102 scopus 로고
    • Biological and clinical implications of heat shock protein 27,000 (Hsp27): A review
    • Ciocca DR, Oesterrich S, Chamness GC, McGuire WL, and Fuqua SA, Biological and clinical implications of heat shock protein 27,000 (Hsp27): a review, J Natl Cancer Inst, 85(19), 1993, 1570-88.
    • (1993) J Natl Cancer Inst , vol.85 , Issue.19 , pp. 1570-1588
    • Ciocca, D.R.1    Oesterrich, S.2    Chamness, G.C.3    McGuire, W.L.4    Fuqua, S.A.5
  • 7
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat shock protein
    • Kim KK, Kim R, Kim S, Crystal structure of a small heat shock protein, Nature, 394, 1998, 595-9.
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.3
  • 8
    • 0035718677 scopus 로고    scopus 로고
    • Structure and function of the small heat shock protein/alphacrystallin family of molecular chaperones
    • Van Montfort R, Slingsby C, Vierling E, Structure and function of the small heat shock protein/alphacrystallin family of molecular chaperones, Adv Protein Chem., 59, 2001, 105-56.
    • (2001) Adv Protein Chem. , vol.59 , pp. 105-156
    • van Montfort, R.1    Slingsby, C.2    Vierling, E.3
  • 9
    • 0034057881 scopus 로고    scopus 로고
    • Heat shock proteins in human cancer
    • Sarto C, Binz PA, Mocarelli P, Heat shock proteins in human cancer, Electrophoresis, 21(6), 2000, 1218-26.
    • (2000) Electrophoresis , vol.21 , Issue.6 , pp. 1218-1226
    • Sarto, C.1    Binz, P.A.2    Mocarelli, P.3
  • 10
    • 18444366777 scopus 로고    scopus 로고
    • In search of the molecular mechanism by which small stress proteins counteract apoptosis during cellular differentiation
    • Arrigo AP, In search of the molecular mechanism by which small stress proteins counteract apoptosis during cellular differentiation, J Cell Biochem, 94(2), 2005, 241-6.
    • (2005) J Cell Biochem , vol.94 , Issue.2 , pp. 241-246
    • Arrigo, A.P.1
  • 11
    • 0028960169 scopus 로고
    • Evolution of the chaperonin families (HSP60, HSP10 and Tcp-1) of proteins and the origin of eukaryotic cells
    • Gupta RS, Evolution of the chaperonin families (HSP60, HSP10 and Tcp-1) of proteins and the origin of eukaryotic cells, Mol. Microbiol, 15(1), 1995, 1-11.
    • (1995) Mol. Microbiol , vol.15 , Issue.1 , pp. 1-11
    • Gupta, R.S.1
  • 12
    • 56149106877 scopus 로고    scopus 로고
    • H.S.P 60 expression, new locations, functions and perspectives for cancer diagnosis and therapy
    • Cappello F, de Macario EC, Marasa L, Zummo G, Macario AJ, HSP 60 expression, new locations, functions and perspectives for cancer diagnosis and therapy, Cancer Biol Ther, 7(6), 2008, 801-9.
    • (2008) Cancer Biol Ther , vol.7 , Issue.6 , pp. 801-809
    • Cappello, F.1    de Macario, E.C.2    Marasa, L.3    Zummo, G.4    Macario, A.J.5
  • 13
    • 18744402993 scopus 로고    scopus 로고
    • Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration
    • Itoh H, Komatsuda A, Ohtani H, et al., Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration, Eur. J. Biochem, 269(23), 2002, 5931-8.
    • (2002) Eur. J. Biochem , vol.269 , Issue.23 , pp. 5931-5938
    • Itoh, H.1    Komatsuda, A.2    Ohtani, H.3
  • 14
    • 85012505857 scopus 로고    scopus 로고
    • Chaperonins are cell-signalling proteins: The unfolding biology of molecular chaperones
    • Ranford JC, Coates AR, Henderson B, Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones, Expert Rev Mol Med, 2(8), 2000, 1-17.
    • (2000) Expert Rev Mol Med , vol.2 , Issue.8 , pp. 1-17
    • Ranford, J.C.1    Coates, A.R.2    Henderson, B.3
  • 15
    • 0037208893 scopus 로고    scopus 로고
    • Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter
    • Hansen JJ, Bross P, Westergaard M, et al., Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter, Hum. Genet, 112 (1), 2003, 71-7.
    • (2003) Hum. Genet , vol.112 , Issue.1 , pp. 71-77
    • Hansen, J.J.1    Bross, P.2    Westergaard, M.3
  • 16
    • 34447624723 scopus 로고    scopus 로고
    • HSP60 may predict good pathological response to neoadjuvant chemoradiotherapy in bladder cancer
    • Urushibara M, Kageyama Y, Akashi T, et al., HSP60 may predict good pathological response to neoadjuvant chemoradiotherapy in bladder cancer, Jpn. J. Clin. Oncol., 37(1), 2007, 56-61.
    • (2007) Jpn. J. Clin. Oncol. , vol.37 , Issue.1 , pp. 56-61
    • Urushibara, M.1    Kageyama, Y.2    Akashi, T.3
  • 17
    • 0025258481 scopus 로고
    • The mitochondrial chaperonin HSP60 is required for its own assembly
    • Cheng MY, Hartl FU, Horwich AL, The mitochondrial chaperonin HSP60 is required for its own assembly, Nature, 348, 1990, 455-8.
    • (1990) Nature , vol.348 , pp. 455-458
    • Cheng, M.Y.1    Hartl, F.U.2    Horwich, A.L.3
  • 18
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton WA, Kashi Y, Furtak K, Horwich AL, Residues in chaperonin GroEL required for polypeptide binding and release, Nature, 371, 1994, 614-9.
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 19
    • 33947540266 scopus 로고    scopus 로고
    • Heat shock protein 60: Regulatory role on innate immune cells
    • Habich C, Burkart V, Heat shock protein 60: regulatory role on innate immune cells, Cell. Mol. Life Sci., 64(6), 2007, 742-51.
    • (2007) Cell. Mol. Life Sci. , vol.64 , Issue.6 , pp. 742-751
    • Habich, C.1    Burkart, V.2
  • 20
    • 0026520064 scopus 로고
    • Antifolding activity of HSP60 couples protein import into the mitochondrial matrix with export to the intermembrane space
    • Koll H, Guiard B, Rassow J, et al., Antifolding activity of HSP60 couples protein import into the mitochondrial matrix with export to the intermembrane space, Cell, 68(6), 1992, 1163-75.
    • (1992) Cell , vol.68 , Issue.6 , pp. 1163-1175
    • Koll, H.1    Guiard, B.2    Rassow, J.3
  • 23
    • 0035091046 scopus 로고    scopus 로고
    • Long-term prognostic significance of HSP-70, c-myc and HLA-DR expression in patients with malignant melanoma
    • Ricaniadis N, Kataki A, Agnantis N, Androulakis G, Karakousis CP, Long-term prognostic significance of HSP-70, c-myc and HLA-DR expression in patients with malignant melanoma, Eur J Surg Oncol, 27 (1), 2001, 88-93.
    • (2001) Eur J Surg Oncol , vol.27 , Issue.1 , pp. 88-93
    • Ricaniadis, N.1    Kataki, A.2    Agnantis, N.3    Androulakis, G.4    Karakousis, C.P.5
  • 24
    • 34547560174 scopus 로고    scopus 로고
    • Expression of heat shock protein 70 in renal cell carcinoma and its relation to tumor progression and prognosis
    • Ramp U, Mahotka C, Heikaus S, Shibata T, Grimm MO, Willers R, Gabbert HE, Expression of heat shock protein 70 in renal cell carcinoma and its relation to tumor progression and prognosis, Histol. Histopathol. 22(10), 2007, 1099-107.
    • (2007) Histol. Histopathol , vol.22 , Issue.10 , pp. 1099-1107
    • Ramp, U.1    Mahotka, C.2    Heikaus, S.3    Shibata, T.4    Grimm, M.O.5    Willers, R.6    Gabbert, H.E.7
  • 25
    • 79952026395 scopus 로고    scopus 로고
    • Available from:, Retrieved, 2009-05-26
    • Heat shock proteins and cancer (Internet), Available from: http://www.healthvalue.net/HSP.html, Retrieved, 2009-05-26.
    • Heat shock proteins and cancer (Internet)
  • 26
    • 0033566936 scopus 로고    scopus 로고
    • The HSC73 molecular chaperone: Involvement in MHC class II antigen presentation
    • Panjwani N, Akbari O, Garcia S, Brazil M, Stockinger B, The HSC73 molecular chaperone: involvement in MHC class II antigen presentation, J Immunol, 163, 1999, 1936-1942.
    • (1999) J Immunol , vol.163 , pp. 1936-1942
    • Panjwani, N.1    Akbari, O.2    Garcia, S.3    Brazil, M.4    Stockinger, B.5
  • 28
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review
    • Csermely P, Schnaider T, Soti C, Prohászka Z, Nardai G, The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review, Pharmacol. Ther., 79(2), 1998, 129-68.
    • (1998) Pharmacol. Ther. , vol.79 , Issue.2 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohászka, Z.4    Nardai, G.5
  • 29
    • 33746660802 scopus 로고    scopus 로고
    • Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms
    • Chen B, Zhong D, Monteiro A, Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms, BMC Genomics, 7, 2006, 156.
    • (2006) BMC Genomics , vol.7 , pp. 156
    • Chen, B.1    Zhong, D.2    Monteiro, A.3
  • 30
    • 33646575879 scopus 로고    scopus 로고
    • HSP90alpha chaperones large C-terminally extended proteolytic intermediates in the MHC class I antigen processing pathway
    • Kunisawa J, Shastri N, HSP90alpha chaperones large C-terminally extended proteolytic intermediates in the MHC class I antigen processing pathway, Immunity, 24, 2006, 523-534.
    • (2006) Immunity , vol.24 , pp. 523-534
    • Kunisawa, J.1    Shastri, N.2
  • 32
    • 0033951278 scopus 로고    scopus 로고
    • Structure and in vivo function of HSP90
    • Pearl LH, Prodromou C, Structure and in vivo function of HSP90, Curr. Opin. Struct. Biol. 10 (1), 2000, 46-51
    • (2000) Curr. Opin. Struct. Biol , vol.10 , Issue.1 , pp. 46-51
    • Pearl, L.H.1    Prodromou, C.2
  • 33
    • 0141596939 scopus 로고    scopus 로고
    • Structure and functional relationships of HSP90
    • Prodromou C, Pearl LH, Structure and functional relationships of HSP90, Curr Cancer Drug Targets 3(5), 2003, 301-23.
    • (2003) Curr Cancer Drug Targets , vol.3 , Issue.5 , pp. 301-323
    • Prodromou, C.1    Pearl, L.H.2
  • 34
    • 0035718899 scopus 로고    scopus 로고
    • Structure, function and mechanism of the HSP90 molecular chaperone
    • Pearl LH, Prodromou C, Structure, function, and mechanism of the HSP90 molecular chaperone, Adv. Protein Chem., 59, 2001, 157-86.
    • (2001) Adv. Protein Chem. , vol.59 , pp. 157-186
    • Pearl, L.H.1    Prodromou, C.2
  • 35
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an HSP90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP, Crystal structure of an HSP90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent, Cell, 89 (2), 1997, 239-50.
    • (1997) Cell , vol.89 , Issue.2 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 36
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the HSP90 molecular chaperone
    • Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH, Identification and structural characterization of the ATP/ADP-binding site in the HSP90 molecular chaperone, Cell, 90 (1), 1997, 65-75.
    • (1997) Cell , vol.90 , Issue.1 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 37
    • 0030901877 scopus 로고    scopus 로고
    • Molecular clamp in the crystal structure of the Nterminal domain of the yeast HSP90 chaperone
    • Prodromou C, Roe SM, Piper PW, Pearl, A molecular clamp in the crystal structure of the Nterminal domain of the yeast HSP90 chaperone, Nat. Struct. Biol, 4 (6), 1997, 477-82.
    • (1997) Nat. Struct. Biol , vol.4 , Issue.6 , pp. 477-482
    • Prodromou, C.1    Roe, S.M.2    Piper, P.W.3    Pearl, A.4
  • 38
    • 0037352446 scopus 로고    scopus 로고
    • Structural and functional analysis of the middle segment of HSP90: Implications for ATP hydrolysis and client protein and cochaperone interactions
    • Meyer P, Prodromou C, Hu B, Vaughan C, Roe SM, Panaretou B, Piper PW, Pearl LH, Structural and functional analysis of the middle segment of HSP90: implications for ATP hydrolysis and client protein and cochaperone interactions, Mol. Cell, 11 (3), 2003, 647-58.
    • (2003) Mol. Cell , vol.11 , Issue.3 , pp. 647-658
    • Meyer, P.1    Prodromou, C.2    Hu, B.3    Vaughan, C.4    Roe, S.M.5    Panaretou, B.6    Piper, P.W.7    Pearl, L.H.8
  • 40
    • 0032924953 scopus 로고    scopus 로고
    • HSP90 & Co. - a holding for folding
    • Buchner J, HSP90 & Co. - a holding for folding, Trends Biochem. Sci., 24 (4), 1999, 136-41.
    • (1999) Trends Biochem. Sci. , vol.24 , Issue.4 , pp. 136-141
    • Buchner, J.1
  • 41
    • 0026669310 scopus 로고
    • The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity
    • Miyata Y, Yahara I, The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity, J. Biol. Chem., 267 (10), 1992, 7042-7.
    • (1992) J. Biol. Chem. , vol.267 , Issue.10 , pp. 7042-7047
    • Miyata, Y.1    Yahara, I.2
  • 42
    • 0026778032 scopus 로고
    • HSP90 chaperones protein folding in vitro
    • Wiech H, Buchner J, Zimmermann R, Jakob U, HSP90 chaperones protein folding in vitro, Nature, 358 (6382), 1992, 169-70.
    • (1992) Nature , vol.358 , Issue.6382 , pp. 169-170
    • Wiech, H.1    Buchner, J.2    Zimmermann, R.3    Jakob, U.4
  • 43
    • 0028940309 scopus 로고
    • Transient interaction of HSP90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo
    • Jakob U, Lilie H, Meyer I, Buchner J, Transient interaction of HSP90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo, J. Biol. Chem., 270 (13), 1995, 7288-94.
    • (1995) J. Biol. Chem. , vol.270 , Issue.13 , pp. 7288-7294
    • Jakob, U.1    Lilie, H.2    Meyer, I.3    Buchner, J.4
  • 44
    • 0037013152 scopus 로고    scopus 로고
    • Domain mapping studies reveal that the M domain of HSP90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release
    • Fontana J, Fulton D, Chen Y, Fairchild TA, McCabe TJ, Fujita N, Tsuruo T, Sessa WC, Domain mapping studies reveal that the M domain of HSP90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release, Circ. Res. 90 (8), 2002, 866-73.
    • (2002) Circ. Res , vol.90 , Issue.8 , pp. 866-873
    • Fontana, J.1    Fulton, D.2    Chen, Y.3    Fairchild, T.A.4    McCabe, T.J.5    Fujita, N.6    Tsuruo, T.7    Sessa, W.C.8
  • 47
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L, Lindquist SL, HSP90 and the chaperoning of cancer, Nat. Rev. Cancer, 5(10), 2005, 761-72.
    • (2005) Nat. Rev. Cancer , vol.5 , Issue.10 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 48
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to HSP90
    • Sato S, Fujita N, Tsuruo T, Modulation of Akt kinase activity by binding to HSP90, Proc. Natl. Acad. Sci. U.S.A., 97 (20), 2000, 10832-7.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , Issue.20 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 50
    • 0035964907 scopus 로고    scopus 로고
    • In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance
    • Guzhova I, Kislyakova K, Moskaliova O, Fridlanskaya I, Tytell M, Cheetham M, Margulis B, In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance, Brain Res 914, 2001, 66-73.
    • (2001) Brain Res , vol.914 , pp. 66-73
    • Guzhova, I.1    Kislyakova, K.2    Moskaliova, O.3    Fridlanskaya, I.4    Tytell, M.5    Cheetham, M.6    Margulis, B.7
  • 52
    • 0024541931 scopus 로고
    • Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins
    • Hightower LE and Guidon PT, Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins, J Cell Physiol, 138, 1989, 257-266.
    • (1989) J Cell Physiol , vol.138 , pp. 257-266
    • Hightower, L.E.1    Guidon, P.T.2
  • 54
    • 0028366212 scopus 로고
    • Heat shock proteins transfer peptides during antigen processing and C.T.L priming
    • Srivastava PK, Udono H, Blachere NE, Li Z, Heat shock proteins transfer peptides during antigen processing and CTL priming, Immunogenetics, 39, 1994, 93-98.
    • (1994) Immunogenetics , vol.39 , pp. 93-98
    • Srivastava, P.K.1    Udono, H.2    Blachere, N.E.3    Li, Z.4
  • 55
    • 0041351872 scopus 로고    scopus 로고
    • Fever-like temperature induces maturation of dendritic cells through induction of HSP90
    • Basu S, Srivastava PK, Fever-like temperature induces maturation of dendritic cells through induction of HSP90, Int Immunol, 15, 2003, 1053-1061.
    • (2003) Int Immunol , vol.15 , pp. 1053-1061
    • Basu, S.1    Srivastava, P.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.