메뉴 건너뛰기




Volumn 11, Issue SUPPL.1, 2011, Pages

HSP90 inhibitors as therapy for multiple myeloma

Author keywords

Cancer; Clinical trial; Heat shock protein 90; Multiple myeloma; Unfolded protein response

Indexed keywords

17AAG; 17DMAG; 5 (2,4 DIHYDROXY 5 ISOPROPYLPHENYL) 4 (4 MORPHOLINOMETHYLPHENYL) 3 ISOXAZOLECARBOXYLIC ACID ETHYLAMIDE; ALVESPIMYCIN; AT113387; AUY992; BEP800; BIIB021; BORTEZOMIB; CHAPERONE; DEXAMETHASONE; GANETESPIB; GELDANAMYCIN; HEAT SHOCK PROTEIN 90 INHIBITOR; HSP90I; IPI 493; KW 2478; MPC 3100; PU H71; RAPAMYCIN; RETASPIMYCIN; SNX 2112; SNX 542; SNX 5422; TANESPIMYCIN; UNCLASSIFIED DRUG;

EID: 84860557226     PISSN: 21522650     EISSN: 21522669     Source Type: Journal    
DOI: 10.1016/j.clml.2011.03.027     Document Type: Conference Paper
Times cited : (20)

References (37)
  • 1
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in dro-sophila
    • Ritossa F. A new puffing pattern induced by temperature shock and DNP in dro-sophila. Experentia 1962; 18:571-3.
    • (1962) Experentia , vol.18 , pp. 571-573
    • Ritossa, F.1
  • 2
    • 0016373748 scopus 로고
    • Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs
    • Tissires A, Mitchell HK, Tracy U. Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs. J Mol Biol 1974; 84:389-98.
    • (1974) J Mol Biol , vol.84 , pp. 389-398
    • Tissires, A.1    Mitchell, H.K.2    Tracy, U.3
  • 3
    • 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, et al. The 90-kDa molecular chaperone family: structure, function, and clinical applications-a comprehensive review. Pharmacol Ther 1998; 79:129-168.
    • (1998) Pharmacol Ther , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3
  • 4
    • 20044382800 scopus 로고    scopus 로고
    • Navigating the chaperone network: An integrative map of physical and genetic interactions mediated by the Hsp90 chaperone
    • Zhao R, Davey M, Hsu YC, et al. Navigating the chaperone network: An integrative map of physical and genetic interactions mediated by the Hsp90 chaperone. Cell 2005; 120:715-27.
    • (2005) Cell , vol.120 , pp. 715-727
    • Zhao, R.1    Davey, M.2    Hsu, Y.C.3
  • 5
    • 0023224123 scopus 로고
    • Nucleotide sequence of acDNA for a member of the human 90kDa heat shock protein family
    • Rebbe NF, Ware J, Bertina RM, et al. Nucleotide sequence of acDNA for a member of the human 90kDa heat shock protein family. Gene 1987; 53:235-45.
    • (1987) Gene , vol.53 , pp. 235-245
    • Rebbe, N.F.1    Ware, J.2    Bertina, R.M.3
  • 6
    • 0024214254 scopus 로고
    • Heat-shock proteins, Hsp84 and Hsp86, of mice and men: Two related genes encode formerly identified tumour-specific transplantation antigens
    • Hoffmann T, Hovemann B. Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens. Gene 1988; 74:491-501.
    • (1988) Gene , vol.74 , pp. 491-501
    • Hoffmann, T.1    Hovemann, B.2
  • 7
    • 0037040975 scopus 로고    scopus 로고
    • The Role of Hsp90N, a new member of the Hsp90 family, in signal transduction and neoplastic transformation
    • Grammatikakis N, Vultur A, Ramana CV, et al. The Role of Hsp90N, a new member of the Hsp90 family, in signal transduction and neoplastic transformation. J Biol Chem 2002; 277:8312-20.
    • (2002) J Biol Chem , vol.277 , pp. 8312-8320
    • Grammatikakis, N.1    Vultur, A.2    Ramana, C.V.3
  • 8
    • 4143095430 scopus 로고    scopus 로고
    • Altered Hsp90 function in cancer: A unique therapeutic opportunity
    • Bagatell R, Whitesell L. Altered Hsp90 function in cancer: a unique therapeutic opportunity. Mol Cancer Ther 2004; 3:1021-30.
    • (2004) Mol Cancer Ther , vol.3 , pp. 1021-1030
    • Bagatell, R.1    Whitesell, L.2
  • 9
    • 70350548428 scopus 로고    scopus 로고
    • 17-AAG for HSP90 inhibition in cancer-from bench to bedside
    • Usmani SZ, Bona RD, Li Z. 17-AAG for HSP90 inhibition in cancer-from bench to bedside. Curr Mol Med 2009; 9:654-64.
    • (2009) Curr Mol Med , vol.9 , pp. 654-664
    • Usmani, S.Z.1    Bona, R.D.2    Li, Z.3
  • 11
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein Hsp90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell L, Mimnaugh EG, De Costa B, et al. Inhibition of heat shock protein Hsp90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 1994; 91:8324-8.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3
  • 12
    • 0029056501 scopus 로고
    • Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent
    • Supko JG, Hickman RL, Grever MR, et al. Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent. Cancer Chemother Pharmacol 1995; 36:305-15.
    • (1995) Cancer Chemother Pharmacol , vol.36 , pp. 305-315
    • Supko, J.G.1    Hickman, R.L.2    Grever, M.R.3
  • 13
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-deme-thoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • Schulte TW, Neckers LM. The benzoquinone ansamycin 17-allylamino-17-deme- thoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol 1998; 42:273-9.
    • (1998) Cancer Chemother Pharmacol , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 14
    • 77952551024 scopus 로고    scopus 로고
    • Discovery and development of Hsp90 inhibitors: A promising pathway for cancer therapy
    • Porter JR, Fritz CC, Depew KM. Discovery and development of Hsp90 inhibitors: a promising pathway for cancer therapy. Curr Opin Chem Biol 2010; 14:412-20.
    • (2010) Curr Opin Chem Biol , vol.14 , pp. 412-420
    • Porter, J.R.1    Fritz, C.C.2    Depew, K.M.3
  • 15
    • 74249105371 scopus 로고    scopus 로고
    • Purine-scaffold Hsp90 inhibitors
    • Taldone T, Chiosis G. Purine-scaffold Hsp90 inhibitors. Curr Top Med Chem 2009; 9:1436-46.
    • (2009) Curr Top Med Chem , vol.9 , pp. 1436-1446
    • Taldone, T.1    Chiosis, G.2
  • 16
    • 66249138886 scopus 로고    scopus 로고
    • Hsp90 inhibitor PU-H71, a multi-modal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models
    • Caldas-Lopes E, Cerchietti L, Ahn JH, et al. Hsp90 inhibitor PU-H71, a multi-modal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models. Proc Natl Acad Sci USA 2009; 106:8368-73.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 8368-8373
    • Caldas-Lopes, E.1    Cerchietti, L.2    Ahn, J.H.3
  • 17
    • 71549121697 scopus 로고    scopus 로고
    • A purine scaffold Hsp90 inhibitor destabilizes BCL-6 and has specific antitumor activity in BCL-6-dependent B cell lym-phomas
    • Cerchietti LC, Lopes EC, Yang SN, et al. A purine scaffold Hsp90 inhibitor destabilizes BCL-6 and has specific antitumor activity in BCL-6-dependent B cell lym-phomas. Nat Med 2009; 15:1369-76.
    • (2009) Nat Med , vol.15 , pp. 1369-1376
    • Cerchietti, L.C.1    Lopes, E.C.2    Yang, S.N.3
  • 18
    • 67651160909 scopus 로고    scopus 로고
    • Targeting heat shock protein 90 with non-quinone inhibitors: A novel chemotherapeutic approach in human hepatocel-lular carcinoma
    • Breinig M, Caldas-Lopes E, Goeppert B, et al. Targeting heat shock protein 90 with non-quinone inhibitors: a novel chemotherapeutic approach in human hepatocel-lular carcinoma. Hepatology 2009, 50:102-12.
    • (2009) Hepatology , vol.50 , pp. 102-112
    • Breinig, M.1    Caldas-Lopes, E.2    Goeppert, B.3
  • 19
    • 77957854088 scopus 로고    scopus 로고
    • HSP90 is a therapeutic target in JAK2-dependent myeloproliferative neoplasms in mice and humans
    • Marubayashi S, Koppikar P, Taldone T, et al. HSP90 is a therapeutic target in JAK2-dependent myeloproliferative neoplasms in mice and humans. J Clin Invest 2010; 120:3578-93.
    • (2010) J Clin Invest , vol.120 , pp. 3578-3593
    • Marubayashi, S.1    Koppikar, P.2    Taldone, T.3
  • 20
    • 77958124439 scopus 로고    scopus 로고
    • The anti-myeloma activity of a novel purine scaffold HSP90 inhibitor PU-H71 is via inhibition of both HSP90A and HSP90B1
    • Usmani SZ, Chiosis G, Bona RD, et al. The anti-myeloma activity of a novel purine scaffold HSP90 inhibitor PU-H71 is via inhibition of both HSP90A and HSP90B1. J Hematol Oncol 2010; 3:40.
    • (2010) J Hematol Oncol , vol.3 , pp. 40
    • Usmani, S.Z.1    Chiosis, G.2    Bona, R.D.3
  • 21
    • 79960983822 scopus 로고    scopus 로고
    • AUY922, a novel HSP90 inhibitor: Final results of a first-in-human study in patients with advanced solid malignancies
    • Samuel TA, Sessa C, Britten C, et al. AUY922, a novel HSP90 inhibitor: final results of a first-in-human study in patients with advanced solid malignancies.J Clin Oncol 2010; 28:2528.
    • (2010) J Clin Oncol , vol.28 , pp. 2528
    • Samuel, T.A.1    Sessa, C.2    Britten, C.3
  • 22
    • 84859741308 scopus 로고    scopus 로고
    • SNX 2112 An oral Hsp-90 inhibitor exerts antiproliferative effects in combination with bortezomib and rituximab in ritux-imab resistant non-Hodgkin's lymphoma
    • Reddy N, Hicks D, Jagasia M, et al. SNX 2112, An oral Hsp-90 inhibitor exerts antiproliferative effects in combination with bortezomib and rituximab in ritux-imab resistant non-Hodgkin's lymphoma. Blood (abstr) 2009; 114:3733.
    • (2009) Blood (Abstr) , vol.114 , pp. 3733
    • Reddy, N.1    Hicks, D.2    Jagasia, M.3
  • 23
    • 79955619964 scopus 로고    scopus 로고
    • The safety, pharmacokinetics and pharmaco-dynamics of KW-2478, a novel Hsp90 antagonist, in patients with B-cell malignancies: A first-in-man, phase I, multicentre, open-label, dose escalation study
    • Cavenagh JD, Yong K, Byrne J, et al. The safety, pharmacokinetics and pharmaco-dynamics of KW-2478, a novel Hsp90 antagonist, in patients with B-cell malignancies: a first-in-man, phase I, multicentre, open-label, dose escalation study. Blood (abstr) 2008; 112:2777.
    • (2008) Blood (Abstr) , vol.112 , pp. 2777
    • Cavenagh, J.D.1    Yong, K.2    Byrne, J.3
  • 24
    • 3242777803 scopus 로고    scopus 로고
    • Advances in biology of multiple myeloma: Clinical applications
    • Hideshima T, Bergsagel PL, Kuehl WM, et al. Advances in biology of multiple myeloma: clinical applications. Blood 2004; 104:607-18.
    • (2004) Blood , vol.104 , pp. 607-618
    • Hideshima, T.1    Bergsagel, P.L.2    Kuehl, W.M.3
  • 25
    • 31544436323 scopus 로고    scopus 로고
    • Antimyeloma activity of heat shock protein-90 inhibition
    • Mitsiades CS, Mitsiades NS, McMullan CJ, et al. Antimyeloma activity of heat shock protein-90 inhibition. Blood 2006; 107:1092-100.
    • (2006) Blood , vol.107 , pp. 1092-1100
    • Mitsiades, C.S.1    Mitsiades, N.S.2    McMullan, C.J.3
  • 26
    • 41049105321 scopus 로고    scopus 로고
    • IPI-504, a novel and soluble HSP-90 inhibitor, blocks the unfolded protein response in multiple myeloma cells
    • Patterson J, Palombella VJ, Fritz C, et al. IPI-504, a novel and soluble HSP-90 inhibitor, blocks the unfolded protein response in multiple myeloma cells. Cancer Chemother Pharmacol 2008; 61:923-32.
    • (2008) Cancer Chemother Pharmacol , vol.61 , pp. 923-932
    • Patterson, J.1    Palombella, V.J.2    Fritz, C.3
  • 27
    • 77955737063 scopus 로고    scopus 로고
    • Activity of new heat shock protein 90 (hsp90) inhibitor NVP-AUY922 against myeloma cells sensitive and resistant to conventional agents
    • McMillin DW, Negri J, Delmore J, et al. Activity of new heat shock protein 90 (hsp90) inhibitor NVP-AUY922 against myeloma cells sensitive and resistant to conventional agents. Blood 2007; 110:1587.
    • (2007) Blood , vol.110 , pp. 1587
    • McMillin, D.W.1    Negri, J.2    Delmore, J.3
  • 28
    • 33747679267 scopus 로고    scopus 로고
    • Analysis of expression of heat shock protein-90 (HSP90) and the effects of HSP90 inhibitor (17-AAG) in multiple myeloma
    • Duus J, Bahar HI, Venkataraman G, et al. Analysis of expression of heat shock protein-90 (HSP90) and the effects of HSP90 inhibitor (17-AAG) in multiple myeloma. Leuk Lymphoma 2006; 47:1369-78.
    • (2006) Leuk Lymphoma , vol.47 , pp. 1369-1378
    • Duus, J.1    Bahar, H.I.2    Venkataraman, G.3
  • 29
    • 33845348883 scopus 로고    scopus 로고
    • Combination mammalian target of rapa-mycin inhibitor rapamycin and HSP90 inhibitor 17-allylamino-17-demethoxy-geldanamycin has synergistic activity in multiple myeloma
    • Francis LK, Alsayed Y, Leleu X, et al. Combination mammalian target of rapa-mycin inhibitor rapamycin and HSP90 inhibitor 17-allylamino-17-demethoxy- geldanamycin has synergistic activity in multiple myeloma. Clin Cancer Res 2006; 12:6826-35.
    • (2006) Clin Cancer Res , vol.12 , pp. 6826-6835
    • Francis, L.K.1    Alsayed, Y.2    Leleu, X.3
  • 30
    • 59649086503 scopus 로고    scopus 로고
    • SNX-2112, a selective Hsp90 inhibitor, potently inhibits tumor cell growth, angiogenesis, and osteoclastogenesis inmultiple myeloma and other hematologic tumors by abrogating signaling via Akt and ERK
    • Okawa Y, Hideshima T, Steed P, et al. SNX-2112, a selective Hsp90 inhibitor, potently inhibits tumor cell growth, angiogenesis, and osteoclastogenesis inmultiple myeloma and other hematologic tumors by abrogating signaling via Akt and ERK. Blood 2009; 113:846-55.
    • (2009) Blood , vol.113 , pp. 846-855
    • Okawa, Y.1    Hideshima, T.2    Steed, P.3
  • 31
    • 77949443606 scopus 로고    scopus 로고
    • Synergistic action of the novel HSP90 inhibitor NVP-AUY922 with histone deacetylase inhibitors, melphalan, or doxorubicin in multiple myeloma
    • Kaiser M, Lamottke B, Mieth M, et al. Synergistic action of the novel HSP90 inhibitor NVP-AUY922 with histone deacetylase inhibitors, melphalan, or doxorubicin in multiple myeloma. Eur J Haematol 2010; 84:337-44.
    • (2010) Eur J Haematol , vol.84 , pp. 337-344
    • Kaiser, M.1    Lamottke, B.2    Mieth, M.3
  • 32
    • 49449105426 scopus 로고    scopus 로고
    • Signalling profile and antitumour activity of the novel Hsp90 inhibitor NVP-AUY922 in multiple myeloma
    • Stühmer T, Zöllinger A, Siegmund D, et al. Signalling profile and antitumour activity of the novel Hsp90 inhibitor NVP-AUY922 in multiple myeloma. Leukemia 2008; 22:1604-12.
    • (2008) Leukemia , vol.22 , pp. 1604-1612
    • Stühmer, T.1    Zöllinger, A.2    Siegmund, D.3
  • 33
    • 34948890040 scopus 로고    scopus 로고
    • Heat shock protein inhibition is associated with activation of the unfolded protein response pathway in myeloma plasma cells
    • Davenport EL, Moore HE, Dunlop AS, et al. Heat shock protein inhibition is associated with activation of the unfolded protein response pathway in myeloma plasma cells. Blood 2007; 110:2641-9.
    • (2007) Blood , vol.110 , pp. 2641-2649
    • Davenport, E.L.1    Moore, H.E.2    Dunlop, A.S.3
  • 34
    • 77952383375 scopus 로고    scopus 로고
    • New molecular and biological mechanism of antitumor activities of KW-2478, a novel nonansamycin heat shock protein 90 inhibitor, in multiple myeloma cells
    • Nakashima T, Ishii T, Tagaya H, et al. New molecular and biological mechanism of antitumor activities of KW-2478, a novel nonansamycin heat shock protein 90 inhibitor, in multiple myeloma cells. Clin Cancer Res 2010; 16:2792-802.
    • (2010) Clin Cancer Res , vol.16 , pp. 2792-2802
    • Nakashima, T.1    Ishii, T.2    Tagaya, H.3
  • 35
    • 77955141041 scopus 로고    scopus 로고
    • Tanespimycin monotherapy in relapsed multiple myeloma: Results of a phase 1 dose-escalation study
    • Richardson PG, Chanan-Khan AA, Alsina M, et al. Tanespimycin monotherapy in relapsed multiple myeloma: results of a phase 1 dose-escalation study. Br J Haematol 2010; 150:438-45.
    • (2010) Br J Haematol , vol.150 , pp. 438-445
    • Richardson, P.G.1    Chanan-Khan, A.A.2    Alsina, M.3
  • 36
    • 77956548752 scopus 로고    scopus 로고
    • Tanespimycin + bortezomib demonstrates safety, activity, and effective target inhibition in relapsed/refractory myeloma patients: Updated results of a phase 1/2 study
    • Richrdson PG, Chanan-Khan AA, Lonial S, et al. Tanespimycin + bortezomib demonstrates safety, activity, and effective target inhibition in relapsed/refractory myeloma patients: updated results of a phase 1/2 study. Blood (abstr) 2009; 114:2890.
    • (2009) Blood (Abstr) , vol.114 , pp. 2890
    • Richrdson, P.G.1    Chanan-Khan, A.A.2    Lonial, S.3
  • 37
    • 77955144862 scopus 로고    scopus 로고
    • Tanespimycin with bortezomib: Activity in relapsed/refractory patients with multiple myeloma
    • Richardson PG, Badros AZ, Jagannath S, et al. Tanespimycin with bortezomib: activity in relapsed/refractory patients with multiple myeloma. Br J Haematol 2010; 150:428-37.
    • (2010) Br J Haematol , vol.150 , pp. 428-437
    • Richardson, P.G.1    Badros, A.Z.2    Jagannath, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.