메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

The proteasome deubiquitinase inhibitor VLX1570 shows selectivity for ubiquitin-specific protease-14 and induces apoptosis of multiple myeloma cells

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; AZEPINE DERIVATIVE; BENZYLIDENE DERIVATIVE; POLYUBIQUITIN; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN BINDING; UBIQUITIN THIOLESTERASE; UCHL5 PROTEIN, HUMAN; USP14 PROTEIN, HUMAN; VLX1570;

EID: 84974705319     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep26979     Document Type: Article
Times cited : (132)

References (52)
  • 2
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 A resolution
    • Groll, M. et al. Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 386, 463-471 (1997).
    • (1997) Nature , vol.386 , pp. 463-471
    • Groll, M.1
  • 3
    • 33847066706 scopus 로고    scopus 로고
    • Functions of the proteasome: From protein degradation and immune surveillance to cancer therapy
    • Goldberg, A. L. Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy. Biochem Soc Trans 35, 12-17 (2007).
    • (2007) Biochem Soc Trans , vol.35 , pp. 12-17
    • Goldberg, A.L.1
  • 4
    • 0033613196 scopus 로고    scopus 로고
    • The catalytic sites of 20S proteasomes and their role in subunit maturation: A mutational and crystallographic study
    • Groll, M. et al. The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study. Proc Natl Acad Sci USA 96, 10976-10983 (1999).
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10976-10983
    • Groll, M.1
  • 5
    • 79955470830 scopus 로고    scopus 로고
    • Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes
    • Lee, M. J., Lee, B. H., Hanna, J., King, R. W. & Finley, D. Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes. Mol Cell Proteomics 10, R110 003871 (2011).
    • (2011) Mol Cell Proteomics , vol.10 R110 , pp. 3871
    • Lee, M.J.1    Lee, B.H.2    Hanna, J.3    King, R.W.4    Finley, D.5
  • 6
    • 84922605325 scopus 로고    scopus 로고
    • Deubiquitinase inhibition as a cancer therapeutic strategy
    • D'Arcy, P., Wang, X. & Linder, S. Deubiquitinase inhibition as a cancer therapeutic strategy. Pharmacolgy & Therapeutics 15, 32-54 (2014).
    • (2014) Pharmacolgy & Therapeutics , vol.15 , pp. 32-54
    • D'Arcy, P.1    Wang, X.2    Linder, S.3
  • 7
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao, T. & Cohen, R. E. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419, 403-407 (2002).
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 8
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • Adams, J. The development of proteasome inhibitors as anticancer drugs. Cancer Cell 5, 417-421 (2004).
    • (2004) Cancer Cell , vol.5 , pp. 417-421
    • Adams, J.1
  • 9
    • 20444433230 scopus 로고    scopus 로고
    • Bortezomib or high-dose dexamethasone for relapsed multiple myeloma
    • Richardson, P. G. et al. Bortezomib or high-dose dexamethasone for relapsed multiple myeloma. New Engl J Med 352, 2487-2498 (2005).
    • (2005) New Engl J Med , vol.352 , pp. 2487-2498
    • Richardson, P.G.1
  • 10
    • 84912521891 scopus 로고    scopus 로고
    • Novel targeted agents in the treatment of multiple myeloma
    • Varga, C. et al. Novel targeted agents in the treatment of multiple myeloma. Hematol Oncol Clin North Am 28, 903-925 (2014).
    • (2014) Hematol Oncol Clin North Am , vol.28 , pp. 903-925
    • Varga, C.1
  • 11
    • 77953163141 scopus 로고    scopus 로고
    • Genome-wide siRNA screen for modulators of cell death induced by proteasome inhibitor bortezomib
    • Chen, S. et al. Genome-wide siRNA screen for modulators of cell death induced by proteasome inhibitor bortezomib. Cancer Res 70, 4318-4326 (2010).
    • (2010) Cancer Res , vol.70 , pp. 4318-4326
    • Chen, S.1
  • 12
    • 84856085129 scopus 로고    scopus 로고
    • Inhibition of proteasome deubiquitinating activity as a new cancer therapy
    • D'Arcy, P. et al. Inhibition of proteasome deubiquitinating activity as a new cancer therapy. Nat Med 17, 1636-1640 (2011).
    • (2011) Nat Med , vol.17 , pp. 1636-1640
    • D'Arcy, P.1
  • 13
    • 41649091606 scopus 로고    scopus 로고
    • Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome
    • Koulich, E., Li, X. & DeMartino, G. N. Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome. Mol Biol Cell 19, 1072-1082 (2008).
    • (2008) Mol Biol Cell , vol.19 , pp. 1072-1082
    • Koulich, E.1    Li, X.2    DeMartino, G.N.3
  • 14
    • 84902986661 scopus 로고    scopus 로고
    • The 19S Deubiquitinase inhibitor b-AP15 is enriched in cells and elicits rapid commitment to cell death
    • Wang, X. et al. The 19S Deubiquitinase inhibitor b-AP15 is enriched in cells and elicits rapid commitment to cell death. Mol Pharm 85, 932-945 (2014).
    • (2014) Mol Pharm , vol.85 , pp. 932-945
    • Wang, X.1
  • 15
    • 84902668793 scopus 로고    scopus 로고
    • Small-molecule RA-9 inhibits proteasome-associated DUBs and ovarian cancer in vitro and in vivo via exacerbating unfolded protein responses
    • Coughlin, K. et al. Small-molecule RA-9 inhibits proteasome-associated DUBs and ovarian cancer in vitro and in vivo via exacerbating unfolded protein responses. Clin Cancer Res 20, 3174-3186 (2014).
    • (2014) Clin Cancer Res , vol.20 , pp. 3174-3186
    • Coughlin, K.1
  • 16
    • 84906249813 scopus 로고    scopus 로고
    • Clinically used antirheumatic agent auranofin is a proteasomal deubiquitinase inhibitor and inhibits tumor growth
    • Liu, N. et al. Clinically used antirheumatic agent auranofin is a proteasomal deubiquitinase inhibitor and inhibits tumor growth. Oncotarget 5, 5453-5471 (2014).
    • (2014) Oncotarget , vol.5 , pp. 5453-5471
    • Liu, N.1
  • 17
    • 78549247880 scopus 로고    scopus 로고
    • Deubiquitinase inhibition by small-molecule WP1130 triggers aggresome formation and tumor cell apoptosis
    • Kapuria, V. et al. Deubiquitinase inhibition by small-molecule WP1130 triggers aggresome formation and tumor cell apoptosis. Cancer Res 70, 9265-9276 (2010).
    • (2010) Cancer Res , vol.70 , pp. 9265-9276
    • Kapuria, V.1
  • 18
    • 84882265186 scopus 로고    scopus 로고
    • Deubiquitinase inhibition of 19S regulatory particles by 4-arylidene curcumin analog AC17 causes NF-kappaB inhibition and p53 reactivation in human lung cancer cells
    • Zhou, B. et al. Deubiquitinase inhibition of 19S regulatory particles by 4-arylidene curcumin analog AC17 causes NF-kappaB inhibition and p53 reactivation in human lung cancer cells. Mol Cancer Ther 12, 1381-1392 (2013).
    • (2013) Mol Cancer Ther , vol.12 , pp. 1381-1392
    • Zhou, B.1
  • 19
    • 84944164063 scopus 로고    scopus 로고
    • Synthesis and evaluation of derivatives of the proteasome deubiquitinase inhibitor b-AP15
    • Wang, X. et al. Synthesis and evaluation of derivatives of the proteasome deubiquitinase inhibitor b-AP15. Chem Biol Drug Des 86, 1036-1048 (2015).
    • (2015) Chem Biol Drug des , vol.86 , pp. 1036-1048
    • Wang, X.1
  • 20
    • 0035903538 scopus 로고    scopus 로고
    • A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14
    • Borodovsky, A. et al. A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14. EMBO J 20, 5187-5196 (2001).
    • (2001) EMBO J , vol.20 , pp. 5187-5196
    • Borodovsky, A.1
  • 21
    • 33749482993 scopus 로고    scopus 로고
    • Identification of new compounds that trigger apoptosomeindependent caspase activation and apoptosis
    • Aleo, E., Henderson, C. J., Fontanini, A., Solazzo, B. & Brancolini, C. Identification of new compounds that trigger apoptosomeindependent caspase activation and apoptosis. Cancer Res 66, 9235-9244 (2006).
    • (2006) Cancer Res , vol.66 , pp. 9235-9244
    • Aleo, E.1    Henderson, C.J.2    Fontanini, A.3    Solazzo, B.4    Brancolini, C.5
  • 22
    • 78751659623 scopus 로고    scopus 로고
    • Alphabeta-Unsaturated carbonyl system of chalcone-based derivatives is responsible for broad inhibition of proteasomal activity and preferential killing of human papilloma virus (HPV) positive cervical cancer cells
    • Bazzaro, M. et al. alpha,beta-Unsaturated carbonyl system of chalcone-based derivatives is responsible for broad inhibition of proteasomal activity and preferential killing of human papilloma virus (HPV) positive cervical cancer cells. J Med Chem 54, 449-456 (2011).
    • (2011) J Med Chem , vol.54 , pp. 449-456
    • Bazzaro, M.1
  • 23
    • 84879748358 scopus 로고    scopus 로고
    • Monitoring drug target engagement in cells and tissues using the cellular thermal shift assay
    • Martinez Molina, D. et al. Monitoring drug target engagement in cells and tissues using the cellular thermal shift assay. Science 341, 84-87 (2013).
    • (2013) Science , vol.341 , pp. 84-87
    • Martinez Molina, D.1
  • 25
    • 84897022669 scopus 로고    scopus 로고
    • A novel small molecule inhibitor of deubiquitylating enzyme USP14 and UCHL5 induces apoptosis in multiple myeloma and overcomes bortezomib resistance
    • Tian, Z. et al. A novel small molecule inhibitor of deubiquitylating enzyme USP14 and UCHL5 induces apoptosis in multiple myeloma and overcomes bortezomib resistance. Blood 125, 706-716 (2013).
    • (2013) Blood , vol.125 , pp. 706-716
    • Tian, Z.1
  • 26
    • 35348818721 scopus 로고    scopus 로고
    • Induction of heme oxygenase-1 by cobalt protoporphyrin enhances the antitumour effect of bortezomib in adult T-cell leukaemia cells
    • Hamamura, R. S. et al. Induction of heme oxygenase-1 by cobalt protoporphyrin enhances the antitumour effect of bortezomib in adult T-cell leukaemia cells. Br J Cancer 97, 1099-1105 (2007).
    • (2007) Br J Cancer , vol.97 , pp. 1099-1105
    • Hamamura, R.S.1
  • 27
    • 84912529600 scopus 로고    scopus 로고
    • Induction of tumor cell apoptosis by a proteasome deubiquitinase inhibitor is associated with oxidative stress
    • Brnjic, S. et al. Induction of tumor cell apoptosis by a proteasome deubiquitinase inhibitor is associated with oxidative stress. Antiox Redox Signal 21, 2271-2285 (2014).
    • (2014) Antiox Redox Signal , vol.21 , pp. 2271-2285
    • Brnjic, S.1
  • 29
    • 84891913291 scopus 로고    scopus 로고
    • A bis-benzylidine piperidone targeting proteasome ubiquitin receptor RPN13/ADRM1 as a therapy for cancer
    • Anchoori, R. K. et al. A bis-benzylidine piperidone targeting proteasome ubiquitin receptor RPN13/ADRM1 as a therapy for cancer. Cancer Cell 24, 791-805 (2013).
    • (2013) Cancer Cell , vol.24 , pp. 791-805
    • Anchoori, R.K.1
  • 30
    • 33748188085 scopus 로고    scopus 로고
    • Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1
    • Yao, T. et al. Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1. Nature Cell Biol 8, 994-1002 (2006).
    • (2006) Nature Cell Biol , vol.8 , pp. 994-1002
    • Yao, T.1
  • 31
    • 33947380146 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the affinity-purified human 26S proteasome complex
    • Wang, X. et al. Mass spectrometric characterization of the affinity-purified human 26S proteasome complex. Biochemistry 46, 3553-3565 (2007).
    • (2007) Biochemistry , vol.46 , pp. 3553-3565
    • Wang, X.1
  • 32
    • 57649167477 scopus 로고    scopus 로고
    • Necroptosis: A specialized pathway of programmed necrosis
    • Galluzzi, L. & Kroemer, G. Necroptosis: a specialized pathway of programmed necrosis. Cell 135, 1161-1163 (2008).
    • (2008) Cell , vol.135 , pp. 1161-1163
    • Galluzzi, L.1    Kroemer, G.2
  • 33
    • 65549091495 scopus 로고    scopus 로고
    • Deubiquitination of CXCR4 by USP14 is critical for both CXCL12-induced CXCR4 degradation and chemotaxis but not ERK ativation
    • Mines, M. A., Goodwin, J. S., Limbird, L. E., Cui, F. F. & Fan, G. H. Deubiquitination of CXCR4 by USP14 is critical for both CXCL12-induced CXCR4 degradation and chemotaxis but not ERK ativation. J Biol Chem 284, 5742-5752 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 5742-5752
    • Mines, M.A.1    Goodwin, J.S.2    Limbird, L.E.3    Cui, F.F.4    Fan, G.H.5
  • 34
    • 84919883904 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 14 (USP14) regulates cellular proliferation and apoptosis in epithelial ovarian cancer
    • Wang, Y. et al. Ubiquitin-specific protease 14 (USP14) regulates cellular proliferation and apoptosis in epithelial ovarian cancer. Med Oncol 32, 379 (2015).
    • (2015) Med Oncol , vol.32 , pp. 379
    • Wang, Y.1
  • 35
    • 84943742662 scopus 로고    scopus 로고
    • USP14 activation promotes tumor progression in hepatocellular carcinoma
    • Huang, G., Li, L. & Zhou, W. USP14 activation promotes tumor progression in hepatocellular carcinoma. Oncol Rep 34, 2917-2924 (2015).
    • (2015) Oncol Rep , vol.34 , pp. 2917-2924
    • Huang, G.1    Li, L.2    Zhou, W.3
  • 36
    • 84897022669 scopus 로고    scopus 로고
    • A novel small molecule inhibitor of deubiquitylating enzyme USP14 and UCHL5 induces apoptosis in multiple myeloma and overcomes bortezomib resistance
    • Tian, Z. et al. A novel small molecule inhibitor of deubiquitylating enzyme USP14 and UCHL5 induces apoptosis in multiple myeloma and overcomes bortezomib resistance. Blood 123, 706-716 (2014).
    • (2014) Blood , vol.123 , pp. 706-716
    • Tian, Z.1
  • 38
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • Obeng, E. A. et al. Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. Blood 107, 4907-4916 (2006).
    • (2006) Blood , vol.107 , pp. 4907-4916
    • Obeng, E.A.1
  • 39
    • 77956527159 scopus 로고    scopus 로고
    • Enhancement of proteasome activity by a small-molecule inhibitor of USP14
    • Lee, B. H. et al. Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature 467, 179-184 (2010).
    • (2010) Nature , vol.467 , pp. 179-184
    • Lee, B.H.1
  • 40
    • 84931263257 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 14 modulates degradation of cellular prion protein
    • Homma, T. et al. Ubiquitin-specific protease 14 modulates degradation of cellular prion protein. Sci Reports 5, 11028 (2015).
    • (2015) Sci Reports , vol.5 , pp. 11028
    • Homma, T.1
  • 41
    • 0036842130 scopus 로고    scopus 로고
    • Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease
    • Wilson, S. M. et al. Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease. Nat Genet 32, 420-425 (2002).
    • (2002) Nat Genet , vol.32 , pp. 420-425
    • Wilson, S.M.1
  • 42
    • 84928747278 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 14 regulates c-Jun N-terminal kinase signaling at the neuromuscular junction
    • Vaden, J. H. et al. Ubiquitin-specific protease 14 regulates c-Jun N-terminal kinase signaling at the neuromuscular junction. Mol Neurodegener 10, 3 (2015).
    • (2015) Mol Neurodegener , vol.10 , pp. 3
    • Vaden, J.H.1
  • 43
    • 0036070772 scopus 로고    scopus 로고
    • Pharmacophore model for novel inhibitors of ubiquitin isopeptidases that induce p53-independent cell death
    • Mullally, J. E. & Fitzpatrick, F. A. Pharmacophore model for novel inhibitors of ubiquitin isopeptidases that induce p53-independent cell death. Mol Pharm 62, 351-358 (2002).
    • (2002) Mol Pharm , vol.62 , pp. 351-358
    • Mullally, J.E.1    Fitzpatrick, F.A.2
  • 44
    • 84907358982 scopus 로고    scopus 로고
    • Screening of DUB activity and specificity by MALDI-TOF mass spectrometry
    • Ritorto, M. S. et al. Screening of DUB activity and specificity by MALDI-TOF mass spectrometry. Nat Comms 5, 4763 (2014).
    • (2014) Nat Comms , vol.5 , pp. 4763
    • Ritorto, M.S.1
  • 45
    • 0024456697 scopus 로고
    • Biological interactions of alpha,beta-unsaturated aldehydes
    • Witz, G. Biological interactions of alpha,beta-unsaturated aldehydes. Free Rad Biology Med 7, 333-349 (1989).
    • (1989) Free Rad Biology Med , vol.7 , pp. 333-349
    • Witz, G.1
  • 46
    • 0028209437 scopus 로고
    • Reversible conjugation of ethacrynic acid with glutathione and human glutathione S-transferase P1-1
    • Ploemen, J. H., Van Schanke, A., Van Ommen, B. & Van Bladeren, P. J. Reversible conjugation of ethacrynic acid with glutathione and human glutathione S-transferase P1-1. Cancer Res 54, 915-919 (1994).
    • (1994) Cancer Res , vol.54 , pp. 915-919
    • Ploemen, J.H.1    Van Schanke, A.2    Van Ommen, B.3    Van Bladeren, P.J.4
  • 47
    • 44349116590 scopus 로고    scopus 로고
    • Proteasome subunit Rpn13 is a novel ubiquitin receptor
    • Husnjak, K. et al. Proteasome subunit Rpn13 is a novel ubiquitin receptor. Nature 453, 481-488 (2008).
    • (2008) Nature , vol.453 , pp. 481-488
    • Husnjak, K.1
  • 48
    • 84907020021 scopus 로고    scopus 로고
    • The cellular thermal shift assay for evaluating drug target interactions in cells
    • Jafari, R. et al. The cellular thermal shift assay for evaluating drug target interactions in cells. Nat Protoc 9, 2100-2122 (2014).
    • (2014) Nat Protoc , vol.9 , pp. 2100-2122
    • Jafari, R.1
  • 49
    • 35148838586 scopus 로고    scopus 로고
    • A reliable tool to determine cell viability in complex 3-d culture: The acid phosphatase assay
    • Friedrich, J. et al. A reliable tool to determine cell viability in complex 3-d culture: the acid phosphatase assay. J Biomol Screen 12, 925-937 (2007).
    • (2007) J Biomol Screen , vol.12 , pp. 925-937
    • Friedrich, J.1
  • 50
    • 84902477582 scopus 로고    scopus 로고
    • Efficient transient transfection of human multiple myeloma cells by electroporation-an appraisal
    • Steinbrunn, T., Chatterjee, M., Bargou, R. C. & Stuhmer, T. Efficient transient transfection of human multiple myeloma cells by electroporation-an appraisal. PloS one 9, e97443 (2014).
    • (2014) PloS One , vol.9 , pp. e97443
    • Steinbrunn, T.1    Chatterjee, M.2    Bargou, R.C.3    Stuhmer, T.4
  • 51
    • 12444342652 scopus 로고    scopus 로고
    • A novel assay for discovery and characterization of pro-apoptotic drugs and for monitoring apoptosis in patient sera
    • Biven, K. et al. A novel assay for discovery and characterization of pro-apoptotic drugs and for monitoring apoptosis in patient sera. Apoptosis 8, 263-268 (2003).
    • (2003) Apoptosis , vol.8 , pp. 263-268
    • Biven, K.1
  • 52
    • 84922252107 scopus 로고    scopus 로고
    • Molecular basis of resistance to proteasome inhibitors in hematological malignancies
    • Niewerth, D. et al. Molecular basis of resistance to proteasome inhibitors in hematological malignancies. Drug Res Updates 18, 18-35 (2015).
    • (2015) Drug Res Updates , vol.18 , pp. 18-35
    • Niewerth, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.