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Volumn 109, Issue 37, 2012, Pages

Discovery and validation of small-molecule heat-shock protein 90 inhibitors through multimodality molecular imaging in living subjects

Author keywords

Bioluminescence imaging; Co chaperone p23; Drug development; PET computed tomography imaging; Small molecule inhibitors

Indexed keywords

FIREFLY LUCIFERASE; FLUORODEOXYGLUCOSE F 18; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 ALPHA; HEAT SHOCK PROTEIN 90 BETA; HEAT SHOCK PROTEIN 90 INHIBITOR; N (5 METHYLISOXAZOL 3 YL) 2 [4 (THIOPHEN 2 YL) 6 (TRIFLUOROMETHYL)PYRIMIDIN 2 YLTHIO]ACETAMIDE; PROTEIN P23; RENILLA LUCIFERIN 2 MONOOXYGENASE; THYMIDINE KINASE; UNCLASSIFIED DRUG;

EID: 84866272310     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1205459109     Document Type: Article
Times cited : (24)

References (50)
  • 1
    • 4344674482 scopus 로고    scopus 로고
    • Targeting multiple signal transduction pathways through inhibition of Hsp90
    • Zhang H, Burrows F (2004) Targeting multiple signal transduction pathways through inhibition of Hsp90. J Mol Med (Berl) 82:488-499.
    • (2004) J Mol Med (Berl) , vol.82 , pp. 488-499
    • Zhang, H.1    Burrows, F.2
  • 3
    • 0032955897 scopus 로고    scopus 로고
    • Expression of hsp90 and cyclin D1 in human breast cancer
    • Yano M, et al. (1999) Expression of hsp90 and cyclin D1 in human breast cancer. Cancer Lett 137:45-51.
    • (1999) Cancer Lett , vol.137 , pp. 45-51
    • Yano, M.1
  • 5
    • 3142545683 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of a new class of geldanamycin derivatives as potent inhibitors of Hsp90
    • Le Brazidec JY, et al. (2004) Synthesis and biological evaluation of a new class of geldanamycin derivatives as potent inhibitors of Hsp90. J Med Chem 47:3865-3873.
    • (2004) J Med Chem , vol.47 , pp. 3865-3873
    • Le Brazidec, J.Y.1
  • 6
    • 33746365169 scopus 로고    scopus 로고
    • Discovery and development of purine-scaffold Hsp90 inhibitors
    • Chiosis G (2006) Discovery and development of purine-scaffold Hsp90 inhibitors. Curr Top Med Chem 6:1183-1191.
    • (2006) Curr Top Med Chem , vol.6 , pp. 1183-1191
    • Chiosis, G.1
  • 7
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal A, et al. (2003) A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 425:407-410.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1
  • 8
    • 17444371717 scopus 로고    scopus 로고
    • Rapid engineering of the geldanamycin biosynthesis pathway by Red/ET recombination and gene complementation
    • Vetcher L, et al. (2005) Rapid engineering of the geldanamycin biosynthesis pathway by Red/ET recombination and gene complementation. Appl Environ Microbiol 71(4):1829-1835.
    • (2005) Appl Environ Microbiol , vol.71 , Issue.4 , pp. 1829-1835
    • Vetcher, L.1
  • 9
    • 3042553538 scopus 로고    scopus 로고
    • Targeting wide-range oncogenic transformation via PU24FCl, a specific inhibitor of tumor Hsp90
    • Vilenchik M, et al. (2004) Targeting wide-range oncogenic transformation via PU24FCl, a specific inhibitor of tumor Hsp90. Chem Biol 11:787-797.
    • (2004) Chem Biol , vol.11 , pp. 787-797
    • Vilenchik, M.1
  • 10
    • 33746222909 scopus 로고    scopus 로고
    • Synthesis of a red-shifted fluorescence polarization probe for Hsp90
    • Moulick K, et al. (2006) Synthesis of a red-shifted fluorescence polarization probe for Hsp90. Bioorg Med Chem Lett 16:4515-4518.
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 4515-4518
    • Moulick, K.1
  • 11
    • 17444416142 scopus 로고    scopus 로고
    • Evaluation of 8-arylsulfanyl, 8-arylsulfoxyl, and 8-arylsulfonyl adenine derivatives as inhibitors of the heat shock protein 90
    • Llauger L, et al. (2005) Evaluation of 8-arylsulfanyl, 8-arylsulfoxyl, and 8-arylsulfonyl adenine derivatives as inhibitors of the heat shock protein 90. J Med Chem 48:2892-2905.
    • (2005) J Med Chem , vol.48 , pp. 2892-2905
    • Llauger, L.1
  • 12
    • 33746914732 scopus 로고    scopus 로고
    • Structural and quantum chemical studies of 8-aryl-sulfanyl adenine class Hsp90 inhibitors
    • Immormino RM, Kang Y, Chiosis G, Gewirth DT (2006) Structural and quantum chemical studies of 8-aryl-sulfanyl adenine class Hsp90 inhibitors. J Med Chem 49:4953-4960.
    • (2006) J Med Chem , vol.49 , pp. 4953-4960
    • Immormino, R.M.1    Kang, Y.2    Chiosis, G.3    Gewirth, D.T.4
  • 13
    • 30444447639 scopus 로고    scopus 로고
    • Identification of potent water soluble purine-scaffold inhibitors of the heat shock protein 90
    • He H, et al. (2006) Identification of potent water soluble purine-scaffold inhibitors of the heat shock protein 90. J Med Chem 49(1):381-390.
    • (2006) J Med Chem , vol.49 , Issue.1 , pp. 381-390
    • He, H.1
  • 14
    • 0036836964 scopus 로고    scopus 로고
    • Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase
    • Chiosis G, Lucas B, Shtil A, Huezo H, Rosen N (2002) Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase. Bioorg Med Chem 10:3555-3564.
    • (2002) Bioorg Med Chem , vol.10 , pp. 3555-3564
    • Chiosis, G.1    Lucas, B.2    Shtil, A.3    Huezo, H.4    Rosen, N.5
  • 15
    • 0141485327 scopus 로고    scopus 로고
    • Development of purine-scaffold small molecule inhibitors of Hsp90
    • Chiosis G, et al. (2003) Development of purine-scaffold small molecule inhibitors of Hsp90. Curr Cancer Drug Targets 3:371-376.
    • (2003) Curr Cancer Drug Targets , vol.3 , pp. 371-376
    • Chiosis, G.1
  • 16
    • 33244484848 scopus 로고    scopus 로고
    • Targeting chaperones in transformed systems- A focus on Hsp90 and cancer
    • Chiosis G (2006) Targeting chaperones in transformed systems- a focus on Hsp90 and cancer. Expert Opin Ther Targets 10:37-50.
    • (2006) Expert Opin Ther Targets , vol.10 , pp. 37-50
    • Chiosis, G.1
  • 19
    • 33750986790 scopus 로고    scopus 로고
    • Inhibition of Hsp90 with synthetic macrolactones: Synthesis and structural and biological evaluation of ring and conformational analogs of radicicol
    • Proisy N, et al. (2006) Inhibition of Hsp90 with synthetic macrolactones: Synthesis and structural and biological evaluation of ring and conformational analogs of radicicol. Chem Biol 13:1203-1215.
    • (2006) Chem Biol , vol.13 , pp. 1203-1215
    • Proisy, N.1
  • 20
    • 37649024109 scopus 로고    scopus 로고
    • Development and application of Hsp90 inhibitors
    • Solit DB, Chiosis G (2008) Development and application of Hsp90 inhibitors. Drug Discov Today 13:38-43.
    • (2008) Drug Discov Today , vol.13 , pp. 38-43
    • Solit, D.B.1    Chiosis, G.2
  • 21
    • 74849111762 scopus 로고    scopus 로고
    • Heat shock protein 90: Inhibitors in clinical trials
    • Biamonte MA, et al. (2010) Heat shock protein 90: Inhibitors in clinical trials. J Med Chem 53:3-17.
    • (2010) J Med Chem , vol.53 , pp. 3-17
    • Biamonte, M.A.1
  • 22
    • 74249085361 scopus 로고    scopus 로고
    • Update on Hsp90 inhibitors in clinical trial
    • Kim YS, et al. (2009) Update on Hsp90 inhibitors in clinical trial. Curr Top Med Chem 9: 1479-1492.
    • (2009) Curr Top Med Chem , vol.9 , pp. 1479-1492
    • Kim, Y.S.1
  • 23
    • 1642503079 scopus 로고    scopus 로고
    • High-throughput screening assay for inhibitors of heatshock protein 90 ATPase activity
    • Rowlands MG, et al. (2004) High-throughput screening assay for inhibitors of heatshock protein 90 ATPase activity. Anal Biochem 327:176-183.
    • (2004) Anal Biochem , vol.327 , pp. 176-183
    • Rowlands, M.G.1
  • 24
    • 0038730655 scopus 로고    scopus 로고
    • Comparative analysis of the ATPbinding sites of Hsp90 by nucleotide affinity cleavage: A distinct nucleotide specificity of the C-terminal ATP-binding site
    • Soti C, Vermes A, Haystead TA, Csermely P (2003) Comparative analysis of the ATPbinding sites of Hsp90 by nucleotide affinity cleavage: A distinct nucleotide specificity of the C-terminal ATP-binding site. Eur J Biochem 270:2421-2428.
    • (2003) Eur J Biochem , vol.270 , pp. 2421-2428
    • Soti, C.1    Vermes, A.2    Haystead, T.A.3    Csermely, P.4
  • 25
    • 2542643923 scopus 로고    scopus 로고
    • Imaging the pharmacodynamics of HER2 degradation in response to Hsp90 inhibitors
    • Smith-Jones PM, et al. (2004) Imaging the pharmacodynamics of HER2 degradation in response to Hsp90 inhibitors. Nat Biotechnol 22(6):701-706.
    • (2004) Nat Biotechnol , vol.22 , Issue.6 , pp. 701-706
    • Smith-Jones, P.M.1
  • 26
    • 75149113119 scopus 로고    scopus 로고
    • (89)Zr-trastuzumab PET visualises HER2 downregulation by the HSP90 inhibitor NVP-AUY922 in a human tumour xenograft
    • Oude Munnink TH, et al. (2010) (89)Zr-trastuzumab PET visualises HER2 downregulation by the HSP90 inhibitor NVP-AUY922 in a human tumour xenograft. Eur J Cancer 46:678-684.
    • (2010) Eur J Cancer , vol.46 , pp. 678-684
    • Oude Munnink, T.H.1
  • 28
    • 51849088295 scopus 로고    scopus 로고
    • Non-invasive MRI tumor imaging and synergistic anticancer effect of HSP90 inhibitor and glycolysis inhibitor in RIP1-Tag2 transgenic pancreatic tumor model
    • Cao X, et al. (2008) Non-invasive MRI tumor imaging and synergistic anticancer effect of HSP90 inhibitor and glycolysis inhibitor in RIP1-Tag2 transgenic pancreatic tumor model. Cancer Chemother Pharmacol 62:985-994.
    • (2008) Cancer Chemother Pharmacol , vol.62 , pp. 985-994
    • Cao, X.1
  • 30
    • 39149109163 scopus 로고    scopus 로고
    • Molecular imaging of the efficacy of heat shock protein 90 inhibitors in living subjects
    • Chan CT, et al. (2008) Molecular imaging of the efficacy of heat shock protein 90 inhibitors in living subjects. Cancer Res 68:216-226.
    • (2008) Cancer Res , vol.68 , pp. 216-226
    • Chan, C.T.1
  • 31
    • 33746789921 scopus 로고    scopus 로고
    • Quantitative high-throughput screening: A titration-based approach that efficiently identifies biological activities in large chemical libraries
    • Inglese J, et al. (2006) Quantitative high-throughput screening: A titration-based approach that efficiently identifies biological activities in large chemical libraries. Proc Natl Acad Sci USA 103:11473-11478.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11473-11478
    • Inglese, J.1
  • 32
    • 33746417580 scopus 로고    scopus 로고
    • Hsp90: A novel target for cancer therapy
    • Solit DB, Rosen N (2006) Hsp90: A novel target for cancer therapy. Curr Top Med Chem 6:1205-1214.
    • (2006) Curr Top Med Chem , vol.6 , pp. 1205-1214
    • Solit, D.B.1    Rosen, N.2
  • 33
    • 34447550488 scopus 로고    scopus 로고
    • Chaperoning cell death: A critical dual role for Hsp90 in small-cell lung cancer
    • Workman P, Powers MV (2007) Chaperoning cell death: A critical dual role for Hsp90 in small-cell lung cancer. Nat Chem Biol 3:455-457.
    • (2007) Nat Chem Biol , vol.3 , pp. 455-457
    • Workman, P.1    Powers, M.V.2
  • 34
    • 53049093524 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 inhibition induces glioma cell death through c-MYC, nuclear factor-kappaB, and glucose regulation
    • Kotliarova S, et al. (2008) Glycogen synthase kinase-3 inhibition induces glioma cell death through c-MYC, nuclear factor-kappaB, and glucose regulation. Cancer Res 68:6643-6651.
    • (2008) Cancer Res , vol.68 , pp. 6643-6651
    • Kotliarova, S.1
  • 35
    • 47249083512 scopus 로고    scopus 로고
    • Differential modulation of Akt/GSK-3beta pathway regulates apoptotic and cytoprotective signaling responses
    • Nair VD, Olanow CW (2008) Differential modulation of Akt/GSK-3beta pathway regulates apoptotic and cytoprotective signaling responses. J Biol Chem 283(22):15469-15478.
    • (2008) J Biol Chem , vol.283 , Issue.22 , pp. 15469-15478
    • Nair, V.D.1    Olanow, C.W.2
  • 36
    • 34248594167 scopus 로고    scopus 로고
    • Reproducibility of 18F-FDG microPET studies in mouse tumor xenografts
    • Dandekar M, Tseng JR, Gambhir SS (2007) Reproducibility of 18F-FDG microPET studies in mouse tumor xenografts. J Nucl Med 48:602-607.
    • (2007) J Nucl Med , vol.48 , pp. 602-607
    • Dandekar, M.1    Tseng, J.R.2    Gambhir, S.S.3
  • 37
    • 2942715274 scopus 로고    scopus 로고
    • Optical imaging of Renilla luciferase, synthetic Renilla luciferase, and firefly luciferase reporter gene expression in living mice
    • Bhaumik S, Lewis XZ, Gambhir SS (2004) Optical imaging of Renilla luciferase, synthetic Renilla luciferase, and firefly luciferase reporter gene expression in living mice. J Biomed Opt 9:578-586.
    • (2004) J Biomed Opt , vol.9 , pp. 578-586
    • Bhaumik, S.1    Lewis, X.Z.2    Gambhir, S.S.3
  • 38
    • 0037039437 scopus 로고    scopus 로고
    • Optical imaging of Renilla luciferase reporter gene expression in living mice
    • Bhaumik S, Gambhir SS (2002) Optical imaging of Renilla luciferase reporter gene expression in living mice. Proc Natl Acad Sci USA 99:377-382.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 377-382
    • Bhaumik, S.1    Gambhir, S.S.2
  • 39
    • 34248225421 scopus 로고    scopus 로고
    • A small animal positron emission tomography study of the effect of chemotherapy and hormonal therapy on the uptake of 2-deoxy-2-[F-18] fluoro-D-glucose in murine models of breast cancer
    • Aliaga A, et al. (2007) A small animal positron emission tomography study of the effect of chemotherapy and hormonal therapy on the uptake of 2-deoxy-2-[F-18] fluoro-D-glucose in murine models of breast cancer. Mol Imaging Biol 9:144-150.
    • (2007) Mol Imaging Biol , vol.9 , pp. 144-150
    • Aliaga, A.1
  • 40
    • 66149096269 scopus 로고    scopus 로고
    • Monitoring and predicting response to therapy with 18F-FDG PET in colorectal cancer: A systematic review
    • de Geus-Oei L-F, Vriens D, van Laarhoven HWM, van der Graaf WTA, Oyen WJG (2009) Monitoring and predicting response to therapy with 18F-FDG PET in colorectal cancer: A systematic review. J Nucl Med 50(Suppl 1):43S-54S.
    • (2009) J Nucl Med , vol.50 , Issue.SUPPL. 1
    • De Geus-Oei, L.-F.1    Vriens, D.2    Van Laarhoven, H.W.M.3    Van Der Graaf, W.T.A.4    Oyen, W.J.G.5
  • 41
    • 77749246666 scopus 로고    scopus 로고
    • Evaluation of the spatial dependence of the point spread function in 2D PET image reconstruction using LOROSEM
    • Wiant D, Gersh JA, Bennett M, Bourland JD (2010) Evaluation of the spatial dependence of the point spread function in 2D PET image reconstruction using LOROSEM. Med Phys 37:1169-1182.
    • (2010) Med Phys , vol.37 , pp. 1169-1182
    • Wiant, D.1    Gersh, J.A.2    Bennett, M.3    Bourland, J.D.4
  • 42
    • 79955768389 scopus 로고    scopus 로고
    • Pharmacogenetics, pharmacogenomics, and individualized medicine
    • Ma Q, Lu AYH (2011) Pharmacogenetics, pharmacogenomics, and individualized medicine. Pharmacol Rev 63:437-459.
    • (2011) Pharmacol Rev , vol.63 , pp. 437-459
    • Ma, Q.1    Lu, A.Y.H.2
  • 43
    • 75149177573 scopus 로고    scopus 로고
    • Hsp90 and co-chaperones twist the functions of diverse client proteins
    • Zuehlke A, Johnson JL (2010) Hsp90 and co-chaperones twist the functions of diverse client proteins. Biopolymers 93:211-217.
    • (2010) Biopolymers , vol.93 , pp. 211-217
    • Zuehlke, A.1    Johnson, J.L.2
  • 44
    • 0036643521 scopus 로고    scopus 로고
    • Involvement of human heat shock protein 90 alpha in nicotine-induced apoptosis
    • Wu YP, Kita K, Suzuki N; Yu-ping Wu KKNS (2002) Involvement of human heat shock protein 90 alpha in nicotine-induced apoptosis. Int J Cancer 100:37-42.
    • (2002) Int J Cancer , vol.100 , pp. 37-42
    • Wu, Y.P.1    Kita, K.2    Suzuki, N.3    Yu-Ping Wu, K.K.N.S.4
  • 46
    • 34047240307 scopus 로고    scopus 로고
    • Effects of nontoxic heat shock protein 90 inhibitor peptide derivatives on reversal of MDR of tumor cells
    • Molnár J, et al. (2007) Effects of nontoxic heat shock protein 90 inhibitor peptide derivatives on reversal of MDR of tumor cells. In Vivo 21(2):429-433.
    • (2007) In Vivo , vol.21 , Issue.2 , pp. 429-433
    • Molnár, J.1
  • 47
    • 84860190466 scopus 로고    scopus 로고
    • A molecular imaging primer: Modalities, imaging agents, and applications
    • James ML, Gambhir SS (2012) A molecular imaging primer: Modalities, imaging agents, and applications. Physiol Rev 92(2):897-965.
    • (2012) Physiol Rev , vol.92 , Issue.2 , pp. 897-965
    • James, M.L.1    Gambhir, S.S.2
  • 48
    • 3242722132 scopus 로고    scopus 로고
    • A time-resolved fluorescence resonance energy transfer-based HTS assay and a surface plasmon resonance-based binding assay for heat shock protein 90 inhibitors
    • Zhou V, et al. (2004) A time-resolved fluorescence resonance energy transfer-based HTS assay and a surface plasmon resonance-based binding assay for heat shock protein 90 inhibitors. Anal Biochem 331:349-357.
    • (2004) Anal Biochem , vol.331 , pp. 349-357
    • Zhou, V.1
  • 49
    • 37649014199 scopus 로고    scopus 로고
    • Preclinical efficacy of the c-Met inhibitor CE-355621 in a U87 MG mouse xenograft model evaluated by 18F-FDG small-animal PET
    • Tseng JR, et al. (2008) Preclinical efficacy of the c-Met inhibitor CE-355621 in a U87 MG mouse xenograft model evaluated by 18F-FDG small-animal PET. J Nucl Med 49:129-134.
    • (2008) J Nucl Med , vol.49 , pp. 129-134
    • Tseng, J.R.1
  • 50
    • 33644831835 scopus 로고    scopus 로고
    • Reproducibility of 3?-deoxy-3?-(18)F-fluorothymidine microPET studies in tumor xenografts in mice
    • Tseng JR, et al. (2005) Reproducibility of 3?-deoxy-3?-(18)F- fluorothymidine microPET studies in tumor xenografts in mice. J Nucl Med 46:1851-1857.
    • (2005) J Nucl Med , vol.46 , pp. 1851-1857
    • Tseng, J.R.1


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