메뉴 건너뛰기




Volumn 22, Issue 3, 2015, Pages 391-403

A small molecule inhibitor of ATPase activity of HSP70 induces apoptosis and has antitumor activities

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ANTINEOPLASTIC AGENT; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; APOPTOZOLE; CASPASE; CHAPERONIN 60; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; UNCLASSIFIED DRUG; ENZYME INHIBITOR; HEAT SHOCK PROTEIN 70L1, HUMAN; IMIDAZOLE DERIVATIVE; PROTEIN BINDING;

EID: 84925463299     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2015.02.004     Document Type: Article
Times cited : (89)

References (56)
  • 1
    • 84859135431 scopus 로고    scopus 로고
    • Autophagy-regulating small molecules and their therapeutic applications
    • K.-H. Baek, J. Park, and I. Shin Autophagy-regulating small molecules and their therapeutic applications Chem. Soc. Rev. 41 2012 3245 3263
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 3245-3263
    • Baek, K.-H.1    Park, J.2    Shin, I.3
  • 3
    • 26444495615 scopus 로고    scopus 로고
    • Death versus survival: functional interaction between the apoptotic and stress-inducible heat shock protein pathways
    • H.M. Beere Death versus survival: functional interaction between the apoptotic and stress-inducible heat shock protein pathways J. Clin. Invest. 115 2005 2633 2639
    • (2005) J. Clin. Invest. , vol.115 , pp. 2633-2639
    • Beere, H.M.1
  • 5
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • B. Bukau, and A.L. Horwich The Hsp70 and Hsp60 chaperone machines Cell 92 1998 351 366
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 6
    • 83755171532 scopus 로고    scopus 로고
    • A small molecule that binds to an ATPase domain of Hsc70 promotes membrane trafficking of mutant cystic fibrosis transmembrane conductance regulator
    • H.J. Cho, H.Y. Gee, K.H. Baek, S.K. Ko, J.M. Park, H. Lee, N.D. Kim, M.G. Lee, and I. Shin A small molecule that binds to an ATPase domain of Hsc70 promotes membrane trafficking of mutant cystic fibrosis transmembrane conductance regulator J. Am. Chem. Soc. 133 2011 20267 20276
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 20267-20276
    • Cho, H.J.1    Gee, H.Y.2    Baek, K.H.3    Ko, S.K.4    Park, J.M.5    Lee, H.6    Kim, N.D.7    Lee, M.G.8    Shin, I.9
  • 7
    • 84925527464 scopus 로고    scopus 로고
    • Probing of effect of an inhibitor of an ATPase domain of Hsc70 on clathrin-mediated endocytosis
    • H.J. Cho, G.-H. Kim, S.-H. Park, J.Y. Hyun, N.-K. Kim, and I. Shin Probing of effect of an inhibitor of an ATPase domain of Hsc70 on clathrin-mediated endocytosis Mol. BioSyst. 2015 10.1039/c4mb00695j
    • (2015) Mol. BioSyst.
    • Cho, H.J.1    Kim, G.-H.2    Park, S.-H.3    Hyun, J.Y.4    Kim, N.-K.5    Shin, I.6
  • 8
    • 21744445069 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications
    • D.R. Ciocca, and S.K. Calderwood Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications Cell Stress Chaperones 10 2005 86 103
    • (2005) Cell Stress Chaperones , vol.10 , pp. 86-103
    • Ciocca, D.R.1    Calderwood, S.K.2
  • 9
    • 34447528828 scopus 로고    scopus 로고
    • The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions
    • M. Daugaard, M. Rohde, and M. Jaattela The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions FEBS Lett. 581 2007 3702 3710
    • (2007) FEBS Lett. , vol.581 , pp. 3702-3710
    • Daugaard, M.1    Rohde, M.2    Jaattela, M.3
  • 10
    • 33747041690 scopus 로고    scopus 로고
    • Pharmacological induction of Hsp70 protects apoptosis-prone cells from doxorubicin: comparison with caspase-inhibitor- and cycle-arrest-mediated cytoprotection
    • Z.N. Demidenko, C. Vivo, H.D. Halicka, C.J. Li, K. Bhalla, E.V. Broude, and M.V. Blagosklonny Pharmacological induction of Hsp70 protects apoptosis-prone cells from doxorubicin: comparison with caspase-inhibitor- and cycle-arrest-mediated cytoprotection Cell Death Differ. 13 2006 1434 1441
    • (2006) Cell Death Differ. , vol.13 , pp. 1434-1441
    • Demidenko, Z.N.1    Vivo, C.2    Halicka, H.D.3    Li, C.J.4    Bhalla, K.5    Broude, E.V.6    Blagosklonny, M.V.7
  • 11
    • 77953734857 scopus 로고    scopus 로고
    • Heat shock protein 70 (hsp70) as an emerging drug target
    • C.G. Evans, L. Chang, and J.E. Gestwicki Heat shock protein 70 (hsp70) as an emerging drug target J. Med. Chem. 53 2010 4585 4602
    • (2010) J. Med. Chem. , vol.53 , pp. 4585-4602
    • Evans, C.G.1    Chang, L.2    Gestwicki, J.E.3
  • 13
    • 18844378888 scopus 로고    scopus 로고
    • Increased expression of the major heat shock protein Hsp72 in human prostate carcinoma cells is dispensable for their viability but confers resistance to a variety of anticancer agents
    • V.L. Gabai, K.R. Budagova, and M.Y. Sherman Increased expression of the major heat shock protein Hsp72 in human prostate carcinoma cells is dispensable for their viability but confers resistance to a variety of anticancer agents Oncogene 24 2005 3328 3338
    • (2005) Oncogene , vol.24 , pp. 3328-3338
    • Gabai, V.L.1    Budagova, K.R.2    Sherman, M.Y.3
  • 14
    • 33751203833 scopus 로고    scopus 로고
    • Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties
    • C. Garrido, M. Brunet, C. Didelot, Y. Zermati, E. Schmitt, and G. Kroemer Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties Cell Cycle 5 2006 2592 2601
    • (2006) Cell Cycle , vol.5 , pp. 2592-2601
    • Garrido, C.1    Brunet, M.2    Didelot, C.3    Zermati, Y.4    Schmitt, E.5    Kroemer, G.6
  • 15
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • Y. Gavrieli, Y. Sherman, and S.A. Ben-Sasson Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation J. Cell Biol. 119 1992 493 501
    • (1992) J. Cell Biol. , vol.119 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 16
    • 1842843854 scopus 로고    scopus 로고
    • hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria
    • T. Gotoh, K. Terada, S. Oyadomari, and M. Mori hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria Cell Death Differ. 11 2004 390 402
    • (2004) Cell Death Differ. , vol.11 , pp. 390-402
    • Gotoh, T.1    Terada, K.2    Oyadomari, S.3    Mori, M.4
  • 17
    • 0028961801 scopus 로고
    • Over-expression of hsp70 confers tumorigenicity to mouse fibrosarcoma cells
    • M. Jaattela Over-expression of hsp70 confers tumorigenicity to mouse fibrosarcoma cells Int. J. Cancer 60 1995 689 693
    • (1995) Int. J. Cancer , vol.60 , pp. 689-693
    • Jaattela, M.1
  • 19
    • 84906780734 scopus 로고    scopus 로고
    • Imidazole-based small molecules that promote neurogenesis in pluripotent cells
    • G.H. Kim, D. Halder, J. Park, W. Namkung, and I. Shin Imidazole-based small molecules that promote neurogenesis in pluripotent cells Angew. Chem. Int. Ed. Engl. 53 2014 9271 9274
    • (2014) Angew. Chem. Int. Ed. Engl. , vol.53 , pp. 9271-9274
    • Kim, G.H.1    Halder, D.2    Park, J.3    Namkung, W.4    Shin, I.5
  • 22
    • 70349768075 scopus 로고    scopus 로고
    • A small molecule inhibitor of inducible heat shock protein 70
    • J.I. Leu, J. Pimkina, A. Frank, M.E. Murphy, and D.L. George A small molecule inhibitor of inducible heat shock protein 70 Mol. Cell 36 2009 15 27
    • (2009) Mol. Cell , vol.36 , pp. 15-27
    • Leu, J.I.1    Pimkina, J.2    Frank, A.3    Murphy, M.E.4    George, D.L.5
  • 23
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • P. Li, D. Nijhawan, I. Budihardjo, S.M. Srinivasula, M. Ahmad, E.S. Alnemri, and X. Wang Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade Cell 91 1997 479 489
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 24
    • 33845637791 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits the nuclear import of apoptosis-inducing factor to avoid DNA fragmentation in TF-1 cells during erythropoiesis
    • J.C. Lui, and S.K. Kong Heat shock protein 70 inhibits the nuclear import of apoptosis-inducing factor to avoid DNA fragmentation in TF-1 cells during erythropoiesis FEBS Lett. 581 2007 109 117
    • (2007) FEBS Lett. , vol.581 , pp. 109-117
    • Lui, J.C.1    Kong, S.K.2
  • 25
    • 0037463033 scopus 로고    scopus 로고
    • NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors
    • B. Meyer, and T. Peters NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors Angew. Chem. Int. Ed. Engl. 42 2003 864 890
    • (2003) Angew. Chem. Int. Ed. Engl. , vol.42 , pp. 864-890
    • Meyer, B.1    Peters, T.2
  • 26
    • 2342651518 scopus 로고    scopus 로고
    • Molecular chaperones and the stress of oncogenesis
    • D.D. Mosser, and R.I. Morimoto Molecular chaperones and the stress of oncogenesis Oncogene 23 2004 2907 2918
    • (2004) Oncogene , vol.23 , pp. 2907-2918
    • Mosser, D.D.1    Morimoto, R.I.2
  • 27
    • 0030739208 scopus 로고    scopus 로고
    • Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis
    • D.D. Mosser, A.W. Caron, L. Bourget, C. Denis-Larose, and B. Massie Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis Mol. Cell. Biol. 17 1997 5317 5327
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5317-5327
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3    Denis-Larose, C.4    Massie, B.5
  • 28
    • 34848848499 scopus 로고    scopus 로고
    • Fluorine in pharmaceuticals: looking beyond intuition
    • K. Muller, C. Faeh, and F. Diederich Fluorine in pharmaceuticals: looking beyond intuition Science 317 2007 1881 1886
    • (2007) Science , vol.317 , pp. 1881-1886
    • Muller, K.1    Faeh, C.2    Diederich, F.3
  • 29
    • 0026526303 scopus 로고
    • Interaction of the immunosuppressant deoxyspergualin with a member of the Hsp70 family of heat shock proteins
    • S.G. Nadler, M.A. Tepper, B. Schacter, and C.E. Mazzucco Interaction of the immunosuppressant deoxyspergualin with a member of the Hsp70 family of heat shock proteins Science 258 1992 484 486
    • (1992) Science , vol.258 , pp. 484-486
    • Nadler, S.G.1    Tepper, M.A.2    Schacter, B.3    Mazzucco, C.E.4
  • 30
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: releasing power for life and unleashing the machineries of death
    • D.D. Newmeyer, and S. Ferguson-Miller Mitochondria: releasing power for life and unleashing the machineries of death Cell 112 2003 481 490
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 32
    • 0035254227 scopus 로고    scopus 로고
    • Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase
    • H.S. Park, J.S. Lee, S.H. Huh, J.S. Seo, and E.J. Choi Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase EMBO J. 20 2001 446 456
    • (2001) EMBO J. , vol.20 , pp. 446-456
    • Park, H.S.1    Lee, J.S.2    Huh, S.H.3    Seo, J.S.4    Choi, E.J.5
  • 36
    • 34447507818 scopus 로고    scopus 로고
    • Inhibitors of the heat shock response: biology and pharmacology
    • M.V. Powers, and P. Workman Inhibitors of the heat shock response: biology and pharmacology FEBS Lett. 581 2007 3758 3769
    • (2007) FEBS Lett. , vol.581 , pp. 3758-3769
    • Powers, M.V.1    Workman, P.2
  • 37
    • 50349096803 scopus 로고    scopus 로고
    • Dual targeting of Hsc70 and Hsp72 inhibits Hsp90 function and induces tumor-specific apoptosis
    • M.V. Powers, P.A. Clarke, and P. Workman Dual targeting of Hsc70 and Hsp72 inhibits Hsp90 function and induces tumor-specific apoptosis Cancer Cell 14 2008 250 262
    • (2008) Cancer Cell , vol.14 , pp. 250-262
    • Powers, M.V.1    Clarke, P.A.2    Workman, P.3
  • 39
    • 33745001797 scopus 로고    scopus 로고
    • Pharmacokinetics and biodistribution studies of doxorubicin loaded poly(butyl cyanoacrylate) nanoparticles synthesized by two different techniques
    • L.H. Reddy, and R.S. Murthy Pharmacokinetics and biodistribution studies of doxorubicin loaded poly(butyl cyanoacrylate) nanoparticles synthesized by two different techniques Biomed. Pap. Med. Fac. Univ. Palacky Olomouc Czech. Repub. 148 2004 161 166
    • (2004) Biomed. Pap. Med. Fac. Univ. Palacky Olomouc Czech. Repub. , vol.148 , pp. 161-166
    • Reddy, L.H.1    Murthy, R.S.2
  • 45
    • 34047268015 scopus 로고    scopus 로고
    • Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker
    • J.F. Swain, G. Dinler, R. Sivendran, D.L. Montgomery, M. Stotz, and L.M. Gierasch Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker Mol. Cell 26 2007 27 39
    • (2007) Mol. Cell , vol.26 , pp. 27-39
    • Swain, J.F.1    Dinler, G.2    Sivendran, R.3    Montgomery, D.L.4    Stotz, M.5    Gierasch, L.M.6
  • 47
    • 79960069754 scopus 로고    scopus 로고
    • Saturation-transfer difference (STD) NMR: a simple and fast method for ligand screening and characterization of protein binding
    • A. Viegas, J.o. Manso, F.L. Nobrega, and E.J. Cabrita Saturation-transfer difference (STD) NMR: a simple and fast method for ligand screening and characterization of protein binding J. Chem. Educ. 88 2011 990 994
    • (2011) J. Chem. Educ. , vol.88 , pp. 990-994
    • Viegas, A.1    Manso, J.O.2    Nobrega, F.L.3    Cabrita, E.J.4
  • 48
    • 0033578065 scopus 로고    scopus 로고
    • Oncogenic potential of Hsp72
    • V.Z. Volloch, and M.Y. Sherman Oncogenic potential of Hsp72 Oncogene 18 1999 3648 3651
    • (1999) Oncogene , vol.18 , pp. 3648-3651
    • Volloch, V.Z.1    Sherman, M.Y.2
  • 49
    • 0034671731 scopus 로고    scopus 로고
    • Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function
    • R. Wadhwa, T. Sugihara, A. Yoshida, H. Nomura, R.R. Reddel, R. Simpson, H. Maruta, and S.C. Kaul Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function Cancer Res. 60 2000 6818 6821
    • (2000) Cancer Res. , vol.60 , pp. 6818-6821
    • Wadhwa, R.1    Sugihara, T.2    Yoshida, A.3    Nomura, H.4    Reddel, R.R.5    Simpson, R.6    Maruta, H.7    Kaul, S.C.8
  • 50
    • 0022976650 scopus 로고
    • Cellular and biochemical events in mammalian cells during and after recovery from physiological stress
    • W.J. Welch, and J.P. Suhan Cellular and biochemical events in mammalian cells during and after recovery from physiological stress J. Cell Biol. 103 1986 2035 2052
    • (1986) J. Cell Biol. , vol.103 , pp. 2035-2052
    • Welch, W.J.1    Suhan, J.P.2
  • 52
    • 43149116558 scopus 로고    scopus 로고
    • Fluorescent high-throughput screening of chemical inducers of neuronal differentiation in skeletal muscle cells
    • D.R. Williams, G.H. Kim, M.R. Lee, and I. Shin Fluorescent high-throughput screening of chemical inducers of neuronal differentiation in skeletal muscle cells Nat. Protoc. 3 2008 835 839
    • (2008) Nat. Protoc. , vol.3 , pp. 835-839
    • Williams, D.R.1    Kim, G.H.2    Lee, M.R.3    Shin, I.4
  • 53
  • 54
    • 0029564954 scopus 로고
    • Heat shock transcription factors: structure and regulation
    • C. Wu Heat shock transcription factors: structure and regulation Annu. Rev. Cell Dev. Biol. 11 1995 441 469
    • (1995) Annu. Rev. Cell Dev. Biol. , vol.11 , pp. 441-469
    • Wu, C.1
  • 55
    • 0033575187 scopus 로고    scopus 로고
    • The function of HSP72 in suppression of c-Jun N-terminal kinase activation can be dissociated from its role in prevention of protein damage
    • J.A. Yaglom, V.L. Gabai, A.B. Meriin, D.D. Mosser, and M.Y. Sherman The function of HSP72 in suppression of c-Jun N-terminal kinase activation can be dissociated from its role in prevention of protein damage J. Biol. Chem. 274 1999 20223 20228
    • (1999) J. Biol. Chem. , vol.274 , pp. 20223-20228
    • Yaglom, J.A.1    Gabai, V.L.2    Meriin, A.B.3    Mosser, D.D.4    Sherman, M.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.