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Volumn 75, Issue 23, 2015, Pages 5130-5142

Naturally occurring isothiocyanates exert anticancer effects by inhibiting deubiquitinating enzymes

Author keywords

[No Author keywords available]

Indexed keywords

BCR ABL PROTEIN; BENZYL ISOTHIOCYANATE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; DEUBIQUITINASE; ENZYME INHIBITOR; HYBRID PROTEIN; ISOTHIOCYANIC ACID DERIVATIVE; PHENETHYL ISOTHIOCYANATE; PROTEIN MCL 1; SULFORAPHANE; UNCLASSIFIED DRUG; WP 1130; PROTEINASE; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN THIOLESTERASE; UCHL5 PROTEIN, HUMAN; UCHL5 PROTEIN, MOUSE; USP9X PROTEIN, HUMAN; USP9X PROTEIN, MOUSE;

EID: 84955493429     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-15-1544     Document Type: Article
Times cited : (67)

References (50)
  • 1
    • 80053154634 scopus 로고    scopus 로고
    • Proteins as binding targets of isothiocyanates in cancer prevention
    • Mi L, Di Pasqua AJ, Chung FL. Proteins as binding targets of isothiocyanates in cancer prevention. Carcinogenesis 2011;32:1405-13.
    • (2011) Carcinogenesis , vol.32 , pp. 1405-1413
    • Mi, L.1    Di Pasqua, A.J.2    Chung, F.L.3
  • 2
    • 84866122895 scopus 로고    scopus 로고
    • Cancer chemoprevention with dietary isothiocyanates mature for clinical translational research
    • Singh SV, Singh K. Cancer chemoprevention with dietary isothiocyanates mature for clinical translational research. Carcinogenesis 2012;33: 1833-42.
    • (2012) Carcinogenesis , vol.33 , pp. 1833-1842
    • Singh, S.V.1    Singh, K.2
  • 3
    • 84904649739 scopus 로고    scopus 로고
    • Molecular targets ofisothiocyanates in cancer: Recent advances
    • Gupta P, Kim B, Kim SH, Srivastava SK. Molecular targets ofisothiocyanates in cancer: recent advances. Mol Nutr Food Res 2014;58:1685-707.
    • (2014) Mol Nutr Food Res , vol.58 , pp. 1685-1707
    • Gupta, P.1    Kim, B.2    Kim, S.H.3    Srivastava, S.K.4
  • 4
    • 84876702379 scopus 로고    scopus 로고
    • Enhancing sulforaphane absorption and excretion in healthy men through the combined consumption of fresh broccoli sprouts and a glucoraphanin-rich powder
    • Cramer JM, Teran-Garcia M, Jeffery EH. Enhancing sulforaphane absorption and excretion in healthy men through the combined consumption of fresh broccoli sprouts and a glucoraphanin-rich powder. Br J Nutr 2012; 107:1333-8.
    • (2012) Br J Nutr , vol.107 , pp. 1333-1338
    • Cramer, J.M.1    Teran-Garcia, M.2    Jeffery, E.H.3
  • 5
    • 1942451371 scopus 로고    scopus 로고
    • Selected isothiocyanates rapidly induce growth inhibition of cancer cells
    • Zhang Y, Tang L, Gonzalez V. Selected isothiocyanates rapidly induce growth inhibition of cancer cells. Mol Cancer Ther 2003;2:1045-52.
    • (2003) Mol Cancer Ther , vol.2 , pp. 1045-1052
    • Zhang, Y.1    Tang, L.2    Gonzalez, V.3
  • 6
    • 84922393807 scopus 로고    scopus 로고
    • Ubiquitination in disease pathogenesis and treatment
    • Popovic D, Vucic D, Dikic I. Ubiquitination in disease pathogenesis and treatment. Nat Med 2014;20:1242-53.
    • (2014) Nat Med , vol.20 , pp. 1242-1253
    • Popovic, D.1    Vucic, D.2    Dikic, I.3
  • 7
    • 79959982112 scopus 로고    scopus 로고
    • Phenethyl isothiocyanate exhibits antileukemic activity in vitro and in vivo by inactivation of akt and activation of JNK pathways
    • Gao N, Budhraja A, Cheng S, Liu EH, Chen J, Yang Z, et al. Phenethyl isothiocyanate exhibits antileukemic activity in vitro and in vivo by inactivation of Akt and activation of JNK pathways. Cell Death Dis 2011;2:e140.
    • (2011) Cell Death Dis , vol.2 , pp. e140
    • Gao, N.1    Budhraja, A.2    Cheng, S.3    Liu, E.H.4    Chen, J.5    Yang, Z.6
  • 8
    • 84876005782 scopus 로고    scopus 로고
    • Downregulation of mcl-1 through inhibition of translation contributes to benzyl isothiocyanate-induced cell cycle arrest and apoptosis in human leukemia cells
    • Zhou T, Li G, Cao B, Liu L, Cheng Q, Kong H, et al. Downregulation of Mcl-1 through inhibition of translation contributes to benzyl isothiocyanate-induced cell cycle arrest and apoptosis in human leukemia cells. Cell Death Dis 2013;4:e515.
    • (2013) Cell Death Dis , vol.4 , pp. e515
    • Zhou, T.1    Li, G.2    Cao, B.3    Liu, L.4    Cheng, Q.5    Kong, H.6
  • 9
    • 52649153465 scopus 로고    scopus 로고
    • Effective elimination of fludarabine-resistant CLL cells by PEITC through a redoxmediated mechanism
    • Trachootham D, Zhang H, Zhang W, Feng L, Du M, Zhou Y, et al. Effective elimination of fludarabine-resistant CLL cells by PEITC through a redoxmediated mechanism. Blood 2008;112:1912-22.
    • (2008) Blood , vol.112 , pp. 1912-1922
    • Trachootham, D.1    Zhang, H.2    Zhang, W.3    Feng, L.4    Du, M.5    Zhou, Y.6
  • 10
    • 45149100643 scopus 로고    scopus 로고
    • Effective killing of gleevec-resistant CML cells with T315I mutation by a natural compound PEITC through redox-mediated mechanism
    • Zhang H, Trachootham D, Lu W, Carew J, Giles FJ, Keating MJ, et al. Effective killing of Gleevec-resistant CML cells with T315I mutation by a natural compound PEITC through redox-mediated mechanism. Leukemia 2008;22:1191-9.
    • (2008) Leukemia , vol.22 , pp. 1191-1199
    • Zhang, H.1    Trachootham, D.2    Lu, W.3    Carew, J.4    Giles, F.J.5    Keating, M.J.6
  • 11
    • 77957958015 scopus 로고    scopus 로고
    • Overcoming resistance to histone deacetylase inhibitors in human leukemia with the redox modulating compound beta-phenylethyl isothiocyanate
    • Hu Y, Lu W, Chen G, Zhang H, Jia Y, Wei Y, et al. Overcoming resistance to histone deacetylase inhibitors in human leukemia with the redox modulating compound beta-phenylethyl isothiocyanate. Blood 2010;116: 2732-41.
    • (2010) Blood , vol.116 , pp. 2732-2741
    • Hu, Y.1    Lu, W.2    Chen, G.3    Zhang, H.4    Jia, Y.5    Wei, Y.6
  • 12
    • 84901372958 scopus 로고    scopus 로고
    • No evident dose-response relationship between cellular ROS level and its cytotoxicity - A paradoxical issue in ROS-based cancer therapy
    • Zhu C, Hu W, Wu H, Hu X. No evident dose-response relationship between cellular ROS level and its cytotoxicity - a paradoxical issue in ROS-based cancer therapy. Sci Rep 2014;4:5029.
    • (2014) Sci Rep , vol.4 , pp. 5029
    • Zhu, C.1    Hu, W.2    Wu, H.3    Hu, X.4
  • 13
    • 0017163293 scopus 로고
    • Inhibition of papain by isothiocyanates
    • Tang CS, Tang WJ. Inhibition of papain by isothiocyanates. Biochim Biophys Acta 1976;452:510-20.
    • (1976) Biochim Biophys Acta , vol.452 , pp. 510-520
    • Tang, C.S.1    Tang, W.J.2
  • 16
    • 0036775490 scopus 로고    scopus 로고
    • Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family
    • Borodovsky A, Ovaa H, Kolli N, Gan-Erdene T, Wilkinson KD, Ploegh HL, et al. Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family. Chem Biol 2002;9:1149-59.
    • (2002) Chem Biol , vol.9 , pp. 1149-1159
    • Borodovsky, A.1    Ovaa, H.2    Kolli, N.3    Gan-Erdene, T.4    Wilkinson, K.D.5    Ploegh, H.L.6
  • 17
    • 0033197542 scopus 로고    scopus 로고
    • Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown
    • Kisselev AF, Akopian TN, Castillo V, Goldberg AL. Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol Cell 1999;4:395-402.
    • (1999) Mol Cell , vol.4 , pp. 395-402
    • Kisselev, A.F.1    Akopian, T.N.2    Castillo, V.3    Goldberg, A.L.4
  • 18
  • 19
    • 34250746414 scopus 로고    scopus 로고
    • Tandem orthogonal proteolysis-activity-based protein profiling (TOP-ABPP) - A general method for mapping sites of probe modification in proteomes
    • Weerapana E, Speers AE, Cravatt BF. Tandem orthogonal proteolysis-activity-based protein profiling (TOP-ABPP) - a general method for mapping sites of probe modification in proteomes. Nat Protoc 2007;2: 1414-25.
    • (2007) Nat Protoc , vol.2 , pp. 1414-1425
    • Weerapana, E.1    Speers, A.E.2    Cravatt, B.F.3
  • 20
    • 0032533620 scopus 로고    scopus 로고
    • Bcr-abl efficiently induces a myeloproliferative disease and production of excess interleukin-3 and granulocyte-macrophage colony-stimulating factor in mice: A novel model for chronic myelogenous leukemia
    • Zhang X, Ren R. Bcr-Abl efficiently induces a myeloproliferative disease and production of excess interleukin-3 and granulocyte-macrophage colony-stimulating factor in mice: a novel model for chronic myelogenous leukemia. Blood 1998;92:3829-40.
    • (1998) Blood , vol.92 , pp. 3829-3840
    • Zhang, X.1    Ren, R.2
  • 21
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells
    • Dantuma NP, Lindsten K, Glas R, Jellne M, Masucci MG. Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells. Nat Biotechnol 2000;18:538-43.
    • (2000) Nat Biotechnol , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 22
    • 79961023008 scopus 로고    scopus 로고
    • EGF signalling activates the ubiquitin proteasome system to modulate C. Elegans lifespan
    • Liu G, Rogers J, Murphy CT, Rongo C. EGF signalling activates the ubiquitin proteasome system to modulate C. elegans lifespan. EMBO J 2011;30: 2990-3003.
    • (2011) EMBO J , vol.30 , pp. 2990-3003
    • Liu, G.1    Rogers, J.2    Murphy, C.T.3    Rongo, C.4
  • 23
    • 77956254963 scopus 로고    scopus 로고
    • Parkin directly modulates 26S proteasome activity
    • Um JW, Im E, Lee HJ, Min B, Yoo L, Yoo J, et al. Parkin directly modulates 26S proteasome activity. J Neurosci 2010;30:11805-14.
    • (2010) J Neurosci , vol.30 , pp. 11805-11814
    • Um, J.W.1    Im, E.2    Lee, H.J.3    Min, B.4    Yoo, L.5    Yoo, J.6
  • 24
    • 79251567380 scopus 로고    scopus 로고
    • Isothiocyanates inhibit proteasome activity and proliferation of multiple myeloma cells
    • Mi L, Gan N, Chung FL. Isothiocyanates inhibit proteasome activity and proliferation of multiple myeloma cells. Carcinogenesis 2011;32: 216-23.
    • (2011) Carcinogenesis , vol.32 , pp. 216-223
    • Mi, L.1    Gan, N.2    Chung, F.L.3
  • 25
    • 84866992804 scopus 로고    scopus 로고
    • Detection of ubiquitin-proteasome enzymatic activities in cells: Application of activity-based probes to inhibitor development
    • Kramer HB, Nicholson B, Kessler BM, Altun M. Detection of ubiquitin-proteasome enzymatic activities in cells: application of activity-based probes to inhibitor development. Biochim Biophys Acta 2012;1823: 2029-37.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 2029-2037
    • Kramer, H.B.1    Nicholson, B.2    Kessler, B.M.3    Altun, M.4
  • 26
    • 84867193114 scopus 로고    scopus 로고
    • Ubiquitin-based probes prepared bytotal synthesis to profile the activity of deubiquitinating enzymes
    • de Jong A, Merkx R, Berlin I, Rodenko B, Wijdeven RH, ElAtmioui D, et al. Ubiquitin-based probes prepared bytotal synthesis to profile the activity of deubiquitinating enzymes. Chembiochem 2012;13:2251-8.
    • (2012) Chembiochem , vol.13 , pp. 2251-2258
    • De Jong, A.1    Merkx, R.2    Berlin, I.3    Rodenko, B.4    Wijdeven, R.H.5    ElAtmioui, D.6
  • 28
    • 84876105929 scopus 로고    scopus 로고
    • Covalent inhibition of SUMO and ubiquitin-specific cysteine proteases by an in situ thiol-alkyne addition
    • Sommer S, Weikart ND, Linne U, Mootz HD. Covalent inhibition of SUMO and ubiquitin-specific cysteine proteases by an in situ thiol-alkyne addition. Bioorg Med Chem 2013;21:2511-7.
    • (2013) Bioorg Med Chem , vol.21 , pp. 2511-2517
    • Sommer, S.1    Weikart, N.D.2    Linne, U.3    Mootz, H.D.4
  • 29
    • 78549247880 scopus 로고    scopus 로고
    • Deubiquitinase inhibition by small-molecule WP1130 triggers aggresome formation and tumor cell apoptosis
    • Kapuria V, Peterson LF, Fang D, Bornmann WG, Talpaz M, Donato NJ. Deubiquitinase inhibition by small-molecule WP1130 triggers aggresome formation and tumor cell apoptosis. Cancer Res 2010;70:9265-76.
    • (2010) Cancer Res , vol.70 , pp. 9265-9276
    • Kapuria, V.1    Peterson, L.F.2    Fang, D.3    Bornmann, W.G.4    Talpaz, M.5    Donato, N.J.6
  • 30
    • 84880278583 scopus 로고    scopus 로고
    • Power and promise of ubiquitin carboxyl-terminal hydrolase 37 as a target of cancer therapy
    • Chen YJ, Ma YS, Fang Y, Wang Y, Fu D, Shen XZ. Power and promise of ubiquitin carboxyl-terminal hydrolase 37 as a target of cancer therapy. Asian Pac J Cancer Prev 2013;14:2173-9.
    • (2013) Asian Pac J Cancer Prev , vol.14 , pp. 2173-2179
    • Chen, Y.J.1    Ma, Y.S.2    Fang, Y.3    Wang, Y.4    Fu, D.5    Shen, X.Z.6
  • 31
    • 84886037235 scopus 로고    scopus 로고
    • USP9X expression correlates with tumor progression and poor prognosis in esophageal squamous cell carcinoma
    • Peng J, Hu Q, Liu W, He X, Cui L, Chen X, et al. USP9X expression correlates with tumor progression and poor prognosis in esophageal squamous cell carcinoma. Diagn Pathol 2013;8:177.
    • (2013) Diagn Pathol , vol.8 , pp. 177
    • Peng, J.1    Hu, Q.2    Liu, W.3    He, X.4    Cui, L.5    Chen, X.6
  • 32
    • 84869217978 scopus 로고    scopus 로고
    • The downregulation of mcl-1 via USP9X inhibition sensitizes solid tumors to bcl-xl inhibition
    • Peddaboina C, Jupiter D, Fletcher S, Yap JL, Rai A, Tobin RP, et al. The downregulation of Mcl-1 via USP9X inhibition sensitizes solid tumors to Bcl-xl inhibition. BMC Cancer 2012;12:541.
    • (2012) BMC Cancer , vol.12 , pp. 541
    • Peddaboina, C.1    Jupiter, D.2    Fletcher, S.3    Yap, J.L.4    Rai, A.5    Tobin, R.P.6
  • 33
    • 73849083434 scopus 로고    scopus 로고
    • Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
    • Schwickart M, Huang X, Lill JR, Liu J, Ferrando R, French DM, et al. Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival. Nature 2010;463:103-7.
    • (2010) Nature , vol.463 , pp. 103-107
    • Schwickart, M.1    Huang, X.2    Lill, J.R.3    Liu, J.4    Ferrando, R.5    French, D.M.6
  • 34
    • 79953072934 scopus 로고    scopus 로고
    • Bcr-abl ubiquitination and usp9x inhibition block kinase signaling and promote CML cell apoptosis
    • Sun H, Kapuria V, Peterson LF, Fang D, Bornmann WG, Bartholomeusz G, et al. Bcr-Abl ubiquitination and Usp9x inhibition block kinase signaling and promote CML cell apoptosis. Blood 2011;117:3151-62.
    • (2011) Blood , vol.117 , pp. 3151-3162
    • Sun, H.1    Kapuria, V.2    Peterson, L.F.3    Fang, D.4    Bornmann, W.G.5    Bartholomeusz, G.6
  • 36
    • 84878353201 scopus 로고    scopus 로고
    • Mcl-1 as a therapeutic target in acute myelogenous leukemia (AML)
    • Bose P, Grant S. Mcl-1 as a therapeutic target in acute myelogenous leukemia (AML). Leuk Res Rep 2013;2:12-4.
    • (2013) Leuk Res Rep , vol.2 , pp. 12-14
    • Bose, P.1    Grant, S.2
  • 37
    • 77955271289 scopus 로고    scopus 로고
    • The fast-mobility isoform of mouse mcl-1 is a mitochondrial matrix-localized protein with attenuated anti-apoptotic activity
    • Huang CR, Yang-Yen HF. The fast-mobility isoform of mouse Mcl-1 is a mitochondrial matrix-localized protein with attenuated anti-apoptotic activity. FEBS Lett 2010;584:3323-30.
    • (2010) FEBS Lett , vol.584 , pp. 3323-3330
    • Huang, C.R.1    Yang-Yen, H.F.2
  • 38
    • 22244452016 scopus 로고    scopus 로고
    • Proteasome inhibitors trigger NOXA-mediated apoptosis in melanoma and myeloma cells
    • Qin JZ, Ziffra J, Stennett L, Bodner B, Bonish BK, Chaturvedi V, et al. Proteasome inhibitors trigger NOXA-mediated apoptosis in melanoma and myeloma cells. Cancer Res 2005;65:6282-93.
    • (2005) Cancer Res , vol.65 , pp. 6282-6293
    • Qin, J.Z.1    Ziffra, J.2    Stennett, L.3    Bodner, B.4    Bonish, B.K.5    Chaturvedi, V.6
  • 39
    • 30144442233 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib induces apoptosis in mantle-cell lymphoma through generation of ROS and noxa activation independent of p53 status
    • Perez-Galan P, Roue G, Villamor N, Montserrat E, Campo E, Colomer D. The proteasome inhibitor bortezomib induces apoptosis in mantle-cell lymphoma through generation of ROS and Noxa activation independent of p53 status. Blood 2006;107:257-64.
    • (2006) Blood , vol.107 , pp. 257-264
    • Perez-Galan, P.1    Roue, G.2    Villamor, N.3    Montserrat, E.4    Campo, E.5    Colomer, D.6
  • 40
    • 69249211723 scopus 로고    scopus 로고
    • Proteasome inhibitor MG132 induces apoptosis and inhibits invasion of human malignant pleural mesothelioma cells
    • Yuan BZ, Chapman JA, Reynolds SH. Proteasome inhibitor MG132 induces apoptosis and inhibits invasion of human malignant pleural mesothelioma cells. Transl Oncol 2008;1:129-40.
    • (2008) Transl Oncol , vol.1 , pp. 129-140
    • Yuan, B.Z.1    Chapman, J.A.2    Reynolds, S.H.3
  • 43
    • 62549161305 scopus 로고    scopus 로고
    • Linkage-specific avidity defines the lysine 63-linked polyubiquitin-binding preference of rap80
    • Sims JJ, Cohen RE. Linkage-specific avidity defines the lysine 63-linked polyubiquitin-binding preference of rap80. Mol Cell 2009;33: 775-83.
    • (2009) Mol Cell , vol.33 , pp. 775-783
    • Sims, J.J.1    Cohen, R.E.2
  • 44
    • 85042098953 scopus 로고    scopus 로고
    • DUBs, the regulation of cell identity and disease
    • Heideker J, Wertz IE. DUBs, the regulation of cell identity and disease. Biochem J 2015;467:191.
    • (2015) Biochem J , vol.467 , pp. 191
    • Heideker, J.1    Wertz, I.E.2
  • 45
    • 84878710765 scopus 로고    scopus 로고
    • Regulation of T cell function by the ubiquitin-specific protease USP9X via modulating the carma1-bcl10-malt1 complex
    • Park Y, Jin HS, Liu YC. Regulation of T cell function by the ubiquitin-specific protease USP9X via modulating the Carma1-Bcl10-Malt1 complex. Proc Natl Acad Sci U S A 2013;110:9433-8.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 9433-9438
    • Park, Y.1    Jin, H.S.2    Liu, Y.C.3
  • 46
    • 76449094879 scopus 로고    scopus 로고
    • The therapeutic potential of deubiquitinating enzyme inhibitors
    • Colland F. The therapeutic potential of deubiquitinating enzyme inhibitors. Biochem Soc Trans 2010;38:137-43.
    • (2010) Biochem Soc Trans , vol.38 , pp. 137-143
    • Colland, F.1
  • 47
    • 33749482993 scopus 로고    scopus 로고
    • Identification of new compounds that trigger apoptosome-independent caspase activation and apoptosis
    • Aleo E, Henderson CJ, Fontanini A, Solazzo B, Brancolini C. Identification of new compounds that trigger apoptosome-independent caspase activation and apoptosis. Cancer Res 2006;66:9235-44.
    • (2006) Cancer Res , vol.66 , pp. 9235-9244
    • Aleo, E.1    Henderson, C.J.2    Fontanini, A.3    Solazzo, B.4    Brancolini, C.5
  • 49
    • 84864580657 scopus 로고    scopus 로고
    • Antiviral activity of a small molecule deubiquitinase inhibitor occurs via induction of the unfolded protein response
    • Perry JW, Ahmed M, Chang KO, Donato NJ, Showalter HD, Wobus CE. Antiviral activity of a small molecule deubiquitinase inhibitor occurs via induction of the unfolded protein response. PLoS Pathog 2012;8: e1002783.
    • (2012) PLoS Pathog , vol.8
    • Perry, J.W.1    Ahmed, M.2    Chang, K.O.3    Donato, N.J.4    Showalter, H.D.5    Wobus, C.E.6
  • 50
    • 84892365810 scopus 로고    scopus 로고
    • Development of inhibitors in the ubiquitination cascade
    • Zhang W, Sidhu SS. Development of inhibitors in the ubiquitination cascade. FEBS Lett 2014;588:356-67.
    • (2014) FEBS Lett , vol.588 , pp. 356-367
    • Zhang, W.1    Sidhu, S.S.2


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