메뉴 건너뛰기




Volumn 9, Issue 1, 2009, Pages 62-77

Antiproliferative and proapoptotic effects of proteasome inhibitors and their combination with histone deacetylase inhibitors on leukemia cells

Author keywords

Apoptosis; Histone deacetylase inhibitors; Leukemia; Proteasome; Proteasome inhibitors

Indexed keywords

3 PHENYLSULFAMOYLCINNAMOHYDROXAMIC ACID; 4 [N (2 HYDROXYETHYL) N [2 (3 INDOLYL)ETHYL]AMINOMETHYL]CINNAMOHYDROXAMIC ACID; BORTEZOMIB; CARFILZOMIB; CASPASE 3; CASPASE 9; CYTARABINE; CYTOCHROME C; DOXORUBICIN; FR 23522; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID; IDARUBICIN; IMMUNOSUPPRESSIVE AGENT; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; N (2 AMINOPHENYL) 4 [4 (3 PYRIDINYL) 2 PYRIMIDINYLAMINOMETHYL]BENZAMIDE; PANOBINOSTAT; PR 171; PROTEASOME INHIBITOR; PROTEINASE INHIBITOR; REACTIVE NITROGEN SPECIES; ROMIDEPSIN; SALINOSPORAMIDE A; UNCLASSIFIED DRUG; VALPROATE SEMISODIUM; VALPROIC ACID; VORINOSTAT; ANTINEOPLASTIC AGENT; BORONIC ACID DERIVATIVE; ENZYME INHIBITOR; HISTONE DEACETYLASE; LACTONE; OLIGOPEPTIDE; PYRAZINE DERIVATIVE; PYRROLE DERIVATIVE;

EID: 65549136174     PISSN: 1871529X     EISSN: None     Source Type: Journal    
DOI: 10.2174/187152909787581372     Document Type: Article
Times cited : (23)

References (137)
  • 2
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem., 2001, 70, 503-533.
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 3
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M.H.; Ciechanover, A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev., 2002, 82, 373-428.
    • (2002) Physiol. Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 4
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • Pickart, C.M.; Cohen R.E. Proteasomes and their kin: proteases in the machine age. Nat. Rev. Mol. Cell Biol., 2004, 5, 177-187.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 5
    • 23944471680 scopus 로고    scopus 로고
    • Nobel Lecture. The ubiquitin system for protein degradation and some of its roles in the control of the cell division cycle
    • Hershko, A. Rev.: Nobel Lecture. The ubiquitin system for protein degradation and some of its roles in the control of the cell division cycle. Cell Death Differ., 2005, 12, 1191-1197.
    • (2005) Cell Death Differ , vol.12 , pp. 1191-1197
    • Hershko, A.R.1
  • 6
    • 37249026703 scopus 로고    scopus 로고
    • Intracellular protein degradation from a vague idea through the lysosome and the ubiquitin-proteasome system and on to human diseases and drug targeting: Nobel Lecture, December 8, 2004
    • Ciechanover, A. Intracellular protein degradation from a vague idea through the lysosome and the ubiquitin-proteasome system and on to human diseases and drug targeting: Nobel Lecture, December 8, 2004. Ann. N. Y. Acad. Sci., 2007, 1116, 1-28.
    • (2007) Ann. N. Y. Acad. Sci , vol.1116 , pp. 1-28
    • Ciechanover, A.1
  • 7
    • 23944526888 scopus 로고    scopus 로고
    • Nobel Lecture. Ubiquitin at Fox Chase
    • Rose, I. Rev.: Nobel Lecture. Ubiquitin at Fox Chase. Cell Death Differ., 2005, 12, 1162-1166.
    • (2005) Cell Death Differ , vol.12 , pp. 1162-1166
    • Rose, I.R.1
  • 8
    • 10944267182 scopus 로고    scopus 로고
    • Ubiquitin: A Nobel protein
    • Wilkinson, K.D. Ubiquitin: A Nobel protein. Cell, 2004, 119, 741-745.
    • (2004) Cell , vol.119 , pp. 741-745
    • Wilkinson, K.D.1
  • 9
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl, M.; Hoppe, T.; Schlenker, S.; Ulrich, H.D.; Mayer, T.U.; Jentsch, S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell, 1999, 96, 635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 10
    • 33645854348 scopus 로고    scopus 로고
    • Role of ubiquitylation in cellular membrane transport
    • Staub, O.; Rotin, D. Role of ubiquitylation in cellular membrane transport. Physiol. Rev., 2006, 86, 669-707.
    • (2006) Physiol. Rev , vol.86 , pp. 669-707
    • Staub, O.1    Rotin, D.2
  • 11
    • 0027446410 scopus 로고
    • Leupeptin-binding site(s) in the mammalian multicatalytic proteinase complex
    • Savory, P.J.; Rivett, A.J. Leupeptin-binding site(s) in the mammalian multicatalytic proteinase complex. Biochem. J., 1993, 289, 45-48.
    • (1993) Biochem. J , vol.289 , pp. 45-48
    • Savory, P.J.1    Rivett, A.J.2
  • 12
    • 0028150688 scopus 로고
    • Inhibition of the proteolytic activity of the multicatalytic proteinase complex (proteasome) by substrate-related peptidyl aldehydes
    • Vinitsky, A.; Cardozo, C.; Sepp-Lorenzino, L.; Michaud, C.; Orlowski, M. Inhibition of the proteolytic activity of the multicatalytic proteinase complex (proteasome) by substrate-related peptidyl aldehydes. J. Biol. Chem., 1994, 269, 29860-29866.
    • (1994) J. Biol. Chem , vol.269 , pp. 29860-29866
    • Vinitsky, A.1    Cardozo, C.2    Sepp-Lorenzino, L.3    Michaud, C.4    Orlowski, M.5
  • 13
    • 0029564960 scopus 로고    scopus 로고
    • Imajoh-Ohmi, S.; Kawaguchi, T.; Sugiyama, S.; Tanaka, K.; Omura, S.; Kikuchi, H. Lactacystin, a specific inhibitor of the proteasome, induces apoptosis in human monoblast U937 cells. Biochem. Biophys. Res. Commun., 1995, 217, 1070-1077.
    • Imajoh-Ohmi, S.; Kawaguchi, T.; Sugiyama, S.; Tanaka, K.; Omura, S.; Kikuchi, H. Lactacystin, a specific inhibitor of the proteasome, induces apoptosis in human monoblast U937 cells. Biochem. Biophys. Res. Commun., 1995, 217, 1070-1077.
  • 15
    • 0031906567 scopus 로고    scopus 로고
    • The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-alphainitiated apoptosis
    • Delic, J.; Masdehors, P.; Omura, S.; Cosset, J.M.; Dumont, J.; Binet, J.L.; Magdelénat, H. The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-alphainitiated apoptosis. Br. J. Cancer., 1998, 77, 1103-1107.
    • (1998) Br. J. Cancer , vol.77 , pp. 1103-1107
    • Delic, J.1    Masdehors, P.2    Omura, S.3    Cosset, J.M.4    Dumont, J.5    Binet, J.L.6    Magdelénat, H.7
  • 16
    • 0032189685 scopus 로고    scopus 로고
    • Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor
    • Orlowski, R.Z.; Eswara, J.R.; Lafond-Walker, A.; Grever, M.R.; Orlowski, M.; Dang, C.V. Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor. Cancer Res., 1998, 58, 4342-4348.
    • (1998) Cancer Res , vol.58 , pp. 4342-4348
    • Orlowski, R.Z.1    Eswara, J.R.2    Lafond-Walker, A.3    Grever, M.R.4    Orlowski, M.5    Dang, C.V.6
  • 17
    • 0026786503 scopus 로고
    • Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex
    • Vinitsky, A.; Michaud, C.; Powers, J.C.; Orlowski, M. Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. Biochemistry, 1992, 31, 9421-9428.
    • (1992) Biochemistry , vol.31 , pp. 9421-9428
    • Vinitsky, A.1    Michaud, C.2    Powers, J.C.3    Orlowski, M.4
  • 18
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NFkappa B1 precursor protein and the activation of NF-kappa
    • Palombella, V.J.; Rando, O.J.; Goldberg, A.L.; Maniatis, T. The ubiquitin-proteasome pathway is required for processing the NFkappa B1 precursor protein and the activation of NF-kappa B. Cell, 1994, 78, 773-785.
    • (1994) B. Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 19
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock K.L.; Gramm, C.; Rothstein, L.; Clark, K.; Stein, R.; Dick, L.; Hwang, D.; Goldberg, A.L. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell, 1994, 78, 761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 21
    • 2642551603 scopus 로고    scopus 로고
    • Development of the proteasome inhibitor Velcade (Bortezomib)
    • Adams, J.; Kauffman, M. Development of the proteasome inhibitor Velcade (Bortezomib). Cancer Invest., 2004, 22, 304-311.
    • (2004) Cancer Invest , vol.22 , pp. 304-311
    • Adams, J.1    Kauffman, M.2
  • 22
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: A suitable antineoplastic target
    • Adams, J. The proteasome: a suitable antineoplastic target. Nat. Rev. Cancer., 2004, 4, 349-360.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 349-360
    • Adams, J.1
  • 23
    • 0345447210 scopus 로고    scopus 로고
    • Kane, R.C.; Bross, P.F.; Farrell, A.T.; Pazdur, R. Velcade: U.S. FDA approval for the treatment of multiple myeloma progressing on prior therapy. Oncologist., 2003, 8, 508-551.
    • Kane, R.C.; Bross, P.F.; Farrell, A.T.; Pazdur, R. Velcade: U.S. FDA approval for the treatment of multiple myeloma progressing on prior therapy. Oncologist., 2003, 8, 508-551.
  • 24
    • 33744832401 scopus 로고    scopus 로고
    • United States Food and Drug Administration approval summary: Bortezomib for the treatment of progressive multiple myeloma after one prior therapy
    • Kane, R.C.; Farrell, A.T.; Sridhara, R.; Pazdur, R. United States Food and Drug Administration approval summary: bortezomib for the treatment of progressive multiple myeloma after one prior therapy. Clin. Cancer Res., 2006, 12, 2955-2960.
    • (2006) Clin. Cancer Res , vol.12 , pp. 2955-2960
    • Kane, R.C.1    Farrell, A.T.2    Sridhara, R.3    Pazdur, R.4
  • 27
    • 43249127114 scopus 로고    scopus 로고
    • Targeting proteasomes as therapy in multiple myeloma
    • Chauhan, D.; Hideshima, T.; Anderson, K.C. Targeting proteasomes as therapy in multiple myeloma. Adv. Exp. Med. Biol., 2008, 615, 251-260.
    • (2008) Adv. Exp. Med. Biol , vol.615 , pp. 251-260
    • Chauhan, D.1    Hideshima, T.2    Anderson, K.C.3
  • 30
    • 43049115407 scopus 로고    scopus 로고
    • Bortezomib in mantle cell lymphoma
    • Suh, K.S.; Gay, A. Bortezomib in mantle cell lymphoma. Future Oncol., 2008, 4, 149-168.
    • (2008) Future Oncol , vol.4 , pp. 149-168
    • Suh, K.S.1    Gay, A.2
  • 32
    • 0035300479 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells
    • Hideshima, T.; Richardson, P.; Chauhan, D.; Palombella, V.J.; Elliott, P.J.; Adams, J.; Anderson, K.C. The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells. Cancer Res., 2001, 61, 3071-3076.
    • (2001) Cancer Res , vol.61 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3    Palombella, V.J.4    Elliott, P.J.5    Adams, J.6    Anderson, K.C.7
  • 36
    • 29244470510 scopus 로고    scopus 로고
    • Bortezomib inhibits PKR-like endoplasmic reticulum (ER) kinase and induces apoptosis via ER stress in human pancreatic cancer cells
    • Nawrocki, S.T.; Carew, J.S.; Dunner, K., Jr., Boise, L.H.; Chiao, P.J.; Huang, P.; Abbruzzese, J.L.; McConkey, D.J. Bortezomib inhibits PKR-like endoplasmic reticulum (ER) kinase and induces apoptosis via ER stress in human pancreatic cancer cells. Cancer Res., 2005, 65, 11510-11519.
    • (2005) Cancer Res , vol.65 , pp. 11510-11519
    • Nawrocki, S.T.1    Carew, J.S.2    Dunner Jr., K.3    Boise, L.H.4    Chiao, P.J.5    Huang, P.6    Abbruzzese, J.L.7    McConkey, D.J.8
  • 38
    • 0043193876 scopus 로고    scopus 로고
    • Proteasome inhibitors disrupt the unfolded protein response in myeloma cells
    • Lee, A.H.; Iwakoshi, N.N.; Anderson, K.C.; Glimcher, L.H. Proteasome inhibitors disrupt the unfolded protein response in myeloma cells. Proc. Natl. Acad. Sci. USA, 2003, 100, 9946-9951.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9946-9951
    • Lee, A.H.1    Iwakoshi, N.N.2    Anderson, K.C.3    Glimcher, L.H.4
  • 39
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • Obeng, E.A.; Carlson, L.M.; Gutman, D.M.; Harrington, W.J., Jr., Lee, K.P.; Boise, H. Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. Blood, 2006, 107, 4907-4916.
    • (2006) Blood , vol.107 , pp. 4907-4916
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3    Harrington Jr., W.J.4    Lee, K.P.5    Boise, H.6
  • 40
    • 0036020941 scopus 로고    scopus 로고
    • NF-κB as a therapeutic target in cancer
    • Orlowski, R.Y.; Baldwin, A.S. NF-κB as a therapeutic target in cancer.Trends Mol. Med., 2002, 8, 385-389.
    • (2002) Trends Mol. Med , vol.8 , pp. 385-389
    • Orlowski, R.Y.1    Baldwin, A.S.2
  • 41
    • 4544224979 scopus 로고    scopus 로고
    • Inhibition of NF-kappaB in cancer cells converts inflammation- induced tumor growth mediated by TNFalpha to TRAIL-mediated tumor regression
    • Luo, J.L.; Maeda, S.; Hsu, L.C.; Yagita, H.; Karin, M. Inhibition of NF-kappaB in cancer cells converts inflammation- induced tumor growth mediated by TNFalpha to TRAIL-mediated tumor regression. Cancer Cell, 2004, 6, 297-305.
    • (2004) Cancer Cell , vol.6 , pp. 297-305
    • Luo, J.L.1    Maeda, S.2    Hsu, L.C.3    Yagita, H.4    Karin, M.5
  • 43
    • 0029858387 scopus 로고    scopus 로고
    • TNF- and cancer therapy-induced apoptosis: Potentiation by inhibition of NFkappaB
    • Wang, C.Y.; Mayo, M.W.; Baldwin, A.S., Jr. TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NFkappaB. Science, 1996, 274, 784-787.
    • (1996) Science , vol.274 , pp. 784-787
    • Wang, C.Y.1    Mayo, M.W.2    Baldwin Jr., A.S.3
  • 44
    • 0032905030 scopus 로고    scopus 로고
    • Wang, C.Y.; Cusack, J.C., Jr., Liu, R.; Baldwin, A.S., Jr. Control of inducible chemoresistance: enhanced anti-tumor therapy through increased apoptosis by inhibition of NF-kappaB. Nat. Med., 1999, 5, 412-417.
    • Wang, C.Y.; Cusack, J.C., Jr., Liu, R.; Baldwin, A.S., Jr. Control of inducible chemoresistance: enhanced anti-tumor therapy through increased apoptosis by inhibition of NF-kappaB. Nat. Med., 1999, 5, 412-417.
  • 45
    • 0035328584 scopus 로고    scopus 로고
    • Cusack, J.C., Jr., Liu, R.; Houston, M.; Abendroth, K.; Elliott, P.J.; Adams, J.; Baldwin, A.S., Jr. Enhanced chemosensitivity to CPT-11 with proteasome inhibitor PS-341: implications for systemic nuclear factor-kappaB inhibition. Cancer Res., 2001, 61, 3535-3540.
    • Cusack, J.C., Jr., Liu, R.; Houston, M.; Abendroth, K.; Elliott, P.J.; Adams, J.; Baldwin, A.S., Jr. Enhanced chemosensitivity to CPT-11 with proteasome inhibitor PS-341: implications for systemic nuclear factor-kappaB inhibition. Cancer Res., 2001, 61, 3535-3540.
  • 46
    • 0033177897 scopus 로고    scopus 로고
    • NF- kappa B and chemoresistance: Potentiation of cancer drugs via inhibition of NF- kappa B
    • Cusack, J.C.; Liu, R.; Baldwin, A.S. NF- kappa B and chemoresistance: potentiation of cancer drugs via inhibition of NF- kappa B. Drug Resist. Updat., 1999, 2, 271-273.
    • (1999) Drug Resist. Updat , vol.2 , pp. 271-273
    • Cusack, J.C.1    Liu, R.2    Baldwin, A.S.3
  • 47
    • 0035341494 scopus 로고    scopus 로고
    • Russo, S.M.; Tepper, J.E.; Baldwin, A.S., Jr., Liu, R.; Adams, J.; Elliott, P.; Cusack, J.C., Jr. Enhancement of radiosensitivity by proteasome inhibition: implications for a role of NF-kappaB. Int. J. Radiat. Oncol. Biol. Phys., 2001, 50, 183-193.
    • Russo, S.M.; Tepper, J.E.; Baldwin, A.S., Jr., Liu, R.; Adams, J.; Elliott, P.; Cusack, J.C., Jr. Enhancement of radiosensitivity by proteasome inhibition: implications for a role of NF-kappaB. Int. J. Radiat. Oncol. Biol. Phys., 2001, 50, 183-193.
  • 49
    • 0345357773 scopus 로고    scopus 로고
    • Gene silencing in cancer in association with promoter hypermethylation
    • Herman, J.G.; Baylin, S.B. Gene silencing in cancer in association with promoter hypermethylation. N. Eng. J. Med., 2003, 349, 2042-2054.
    • (2003) N. Eng. J. Med , vol.349 , pp. 2042-2054
    • Herman, J.G.1    Baylin, S.B.2
  • 50
  • 51
    • 55749110754 scopus 로고    scopus 로고
    • Demethylating agents in myeloid malignancies
    • Garcia-Manero, G. Demethylating agents in myeloid malignancies. Curr. Opin. Oncol. 2008, 20, 705-710.
    • (2008) Curr. Opin. Oncol , vol.20 , pp. 705-710
    • Garcia-Manero, G.1
  • 53
    • 34547660308 scopus 로고    scopus 로고
    • Keats, J.J.; Fonseca, R.; Chesi, M.; Schop, R.; Baker, A.; Chng, W.J.; Van Wier, S.; Tiedemann, R.; Shi, C.X.; Sebag, M.; Braggio, E.; Henry, T.; Zhu, Y.X.; Fogle, H.; Price-Troska, T.; Ahmann, G.; Mancini, C.; Brents, L.A.; Kumar, S.; Greipp, P.; Dispenzieri, A.; Bryant, B.; Mulligan, G.; Bruhn, L.; Barrett, M.; Valdez, R.; Trent, J.; Stewart, A.K.; Carpten, J.; Bergsagel, P.L. Promiscuous mutations activate the noncanonical NF-kappaB pathway in multiple myeloma. Cancer Cell, 2007, 12, 131-144.
    • Keats, J.J.; Fonseca, R.; Chesi, M.; Schop, R.; Baker, A.; Chng, W.J.; Van Wier, S.; Tiedemann, R.; Shi, C.X.; Sebag, M.; Braggio, E.; Henry, T.; Zhu, Y.X.; Fogle, H.; Price-Troska, T.; Ahmann, G.; Mancini, C.; Brents, L.A.; Kumar, S.; Greipp, P.; Dispenzieri, A.; Bryant, B.; Mulligan, G.; Bruhn, L.; Barrett, M.; Valdez, R.; Trent, J.; Stewart, A.K.; Carpten, J.; Bergsagel, P.L. Promiscuous mutations activate the noncanonical NF-kappaB pathway in multiple myeloma. Cancer Cell, 2007, 12, 131-144.
  • 54
    • 33746840548 scopus 로고    scopus 로고
    • Proteasome inhibitors induce death but activate NF-kappaB on endometrial carcinoma cell lines and primary culture explants
    • Dolcet, X.; Llobet, D.; Encinas, M.; Pallares, J.; Cabero, A.; Schoenenberger, J.A.; Comella, J.X.; Matias-Guiu, X. Proteasome inhibitors induce death but activate NF-kappaB on endometrial carcinoma cell lines and primary culture explants. J. Biol. Chem., 2006, 281, 22118-22130.
    • (2006) J. Biol. Chem , vol.281 , pp. 22118-22130
    • Dolcet, X.1    Llobet, D.2    Encinas, M.3    Pallares, J.4    Cabero, A.5    Schoenenberger, J.A.6    Comella, J.X.7    Matias-Guiu, X.8
  • 58
    • 34548183776 scopus 로고    scopus 로고
    • Neurotoxicity of bortezomib therapy in multiple myeloma: A single-center experience and review of the literature
    • Badros, A.; Goloubeva, O.; Dalal, J.S.; Can, I.; Thompson, J.; Rapoport, A.P.; Heyman, M.; Akpek, G.; Fenton, R.G. Neurotoxicity of bortezomib therapy in multiple myeloma: a single-center experience and review of the literature. Cancer, 2007, 110, 1042-1049.
    • (2007) Cancer , vol.110 , pp. 1042-1049
    • Badros, A.1    Goloubeva, O.2    Dalal, J.S.3    Can, I.4    Thompson, J.5    Rapoport, A.P.6    Heyman, M.7    Akpek, G.8    Fenton, R.G.9
  • 60
    • 0037455147 scopus 로고    scopus 로고
    • Feling, R.H.; Buchanan, G.O.; Mincer, T.J.; Kauffman, C.A.; Jensen, P.R.; Fenical, W. Salinosporamide A: a highly cytotoxic proteasome inhibitor from a novel microbial source, a marine bacterium of the new genus salinospora. Angew. Chem. Int. Ed. Engl., 2003, 42, 355-357.
    • Feling, R.H.; Buchanan, G.O.; Mincer, T.J.; Kauffman, C.A.; Jensen, P.R.; Fenical, W. Salinosporamide A: a highly cytotoxic proteasome inhibitor from a novel microbial source, a marine bacterium of the new genus salinospora. Angew. Chem. Int. Ed. Engl., 2003, 42, 355-357.
  • 63
    • 33750209537 scopus 로고    scopus 로고
    • A novel proteasome inhibitor NPI-0052 as an anticancer therapy
    • Chauhan, D.; Hideshima T.; Anderson K.C. A novel proteasome inhibitor NPI-0052 as an anticancer therapy. Br. J. Cancer, 2006, 95, 961-965.
    • (2006) Br. J. Cancer , vol.95 , pp. 961-965
    • Chauhan, D.1    Hideshima, T.2    Anderson, K.C.3
  • 65
    • 34347375499 scopus 로고    scopus 로고
    • NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemia cells
    • Miller, C.P.; Ban, K.; Dujka, M.E.; McConkey, D.J.; Munsell, M.; Palladino, M.; Chandra, J. NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemia cells. Blood, 2007, 110, 267-277.
    • (2007) Blood , vol.110 , pp. 267-277
    • Miller, C.P.1    Ban, K.2    Dujka, M.E.3    McConkey, D.J.4    Munsell, M.5    Palladino, M.6    Chandra, J.7
  • 66
    • 38949125853 scopus 로고    scopus 로고
    • Combination of proteasome inhibitors bortezomib and NPI-0052 trigger in vivo synergistic cytotoxicity in multiple myeloma
    • Chauhan, D.; Singh, A.; Brahmandam, M.; Podar, K.; Hideshima, T.; Richardson, P.; Munshi, N.; Palladino, M.A.; Anderson, K.C. Combination of proteasome inhibitors bortezomib and NPI-0052 trigger in vivo synergistic cytotoxicity in multiple myeloma. Blood, 2008, 111, 1654-1664.
    • (2008) Blood , vol.111 , pp. 1654-1664
    • Chauhan, D.1    Singh, A.2    Brahmandam, M.3    Podar, K.4    Hideshima, T.5    Richardson, P.6    Munshi, N.7    Palladino, M.A.8    Anderson, K.C.9
  • 68
    • 33847410207 scopus 로고    scopus 로고
    • The proteasome inhibitors bortezomib and PR-171 have antiproliferative and proapoptotic effects on primary human acute myeloid leukaemia cells
    • Stapnes, C.; Døskeland, A.P.; Hatfield, K.; Ersvaer, E.; Ryningen, A.; Lorens J.B.; Gjertsen, B.T.; Bruserud, O. The proteasome inhibitors bortezomib and PR-171 have antiproliferative and proapoptotic effects on primary human acute myeloid leukaemia cells. Br. J. Haematol., 2007, 136 814-828.
    • (2007) Br. J. Haematol , vol.136 , pp. 814-828
    • Stapnes, C.1    Døskeland, A.P.2    Hatfield, K.3    Ersvaer, E.4    Ryningen, A.5    Lorens, J.B.6    Gjertsen, B.T.7    Bruserud, O.8
  • 70
    • 41549133200 scopus 로고    scopus 로고
    • Proteasome inhibitors in cancer therapy: Lessons from the first decade
    • Orlowski, R.Z.; Kuhn, D.J. Proteasome inhibitors in cancer therapy: lessons from the first decade. Clin. Cancer Res., 2008, 14, 1649-1657.
    • (2008) Clin. Cancer Res , vol.14 , pp. 1649-1657
    • Orlowski, R.Z.1    Kuhn, D.J.2
  • 71
    • 34948881265 scopus 로고    scopus 로고
    • Salinosporamide A (NPI-0052) potentiates apoptosis, suppresses osteoclastogenesis, and inhibits invasion through down-modulation of NFkappaB regulated gene products
    • Ahn, K.S.; Sethi, G.; Chao, T.H.; Neuteboom, S.T.; Chaturvedi, M.M.; Palladino, M.A.; Younes, A.; Aggarwal, B.B. Salinosporamide A (NPI-0052) potentiates apoptosis, suppresses osteoclastogenesis, and inhibits invasion through down-modulation of NFkappaB regulated gene products. Blood, 2007, 110, 2286-2295.
    • (2007) Blood , vol.110 , pp. 2286-2295
    • Ahn, K.S.1    Sethi, G.2    Chao, T.H.3    Neuteboom, S.T.4    Chaturvedi, M.M.5    Palladino, M.A.6    Younes, A.7    Aggarwal, B.B.8
  • 72
    • 33748300908 scopus 로고    scopus 로고
    • The proteasome inhibitor NPI-0052 is a more effective inducer of apoptosis than bortezomib in lymphocytes from patients with chronic lymphocytic leukemia
    • Ruiz, S.; Krupnik, Y.; Keating, M.; Chandra, J.; Palladino, M.; McConkey, D. The proteasome inhibitor NPI-0052 is a more effective inducer of apoptosis than bortezomib in lymphocytes from patients with chronic lymphocytic leukemia. Mol. Cancer Ther., 2006, 5, 1836-1843.
    • (2006) Mol. Cancer Ther , vol.5 , pp. 1836-1843
    • Ruiz, S.1    Krupnik, Y.2    Keating, M.3    Chandra, J.4    Palladino, M.5    McConkey, D.6
  • 74
    • 34547864236 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Molecular mechanisms of action
    • Xu, W.S.; Parmigiani, R.B.; Marks, P.A. Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene, 2007, 26, 5541-5552.
    • (2007) Oncogene , vol.26 , pp. 5541-5552
    • Xu, W.S.1    Parmigiani, R.B.2    Marks, P.A.3
  • 75
    • 33750596313 scopus 로고    scopus 로고
    • Epigenetic cancer therapy makes headway
    • Mack, G.S. Epigenetic cancer therapy makes headway. J. Natl. Cancer Inst., 2006, 1443-1444.
    • (2006) J. Natl. Cancer Inst , pp. 1443-1444
    • Mack, G.S.1
  • 78
    • 0035962644 scopus 로고    scopus 로고
    • Histone deacetylases: A common molecular target for differentiation treatment of acute myeloid leukemias?
    • Minucci, S.; Nervi, C.; Lo Coco, F.; Pelicci, P.G. Histone deacetylases: a common molecular target for differentiation treatment of acute myeloid leukemias? Oncogene, 2001, 20, 3110-3115.
    • (2001) Oncogene , vol.20 , pp. 3110-3115
    • Minucci, S.1    Nervi, C.2    Lo Coco, F.3    Pelicci, P.G.4
  • 79
    • 27144475816 scopus 로고    scopus 로고
    • Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors
    • Bradbury, C.A.; Khanim, F.L.; Hayden, R.; Bunce, C.M.; White, D.A.; Drayson, M.T.; Craddock, C.; Turner, B.M. Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors. Leukemia, 2005, 19, 1751-1759.
    • (2005) Leukemia , vol.19 , pp. 1751-1759
    • Bradbury, C.A.1    Khanim, F.L.2    Hayden, R.3    Bunce, C.M.4    White, D.A.5    Drayson, M.T.6    Craddock, C.7    Turner, B.M.8
  • 80
    • 34547897023 scopus 로고    scopus 로고
    • Histone deacetylases and cancer
    • Glozak, M.A.; Seto, E. Histone deacetylases and cancer. Oncogene, 2007, 26, 5420-5432.
    • (2007) Oncogene , vol.26 , pp. 5420-5432
    • Glozak, M.A.1    Seto, E.2
  • 81
    • 34547924046 scopus 로고    scopus 로고
    • HATs and HDACs: From structure, function and regulation to novel strategies for therapy and prevention
    • Yang, X.-J.; Seto, E. HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention. Oncogene, 2007, 26, 5310-5318.
    • (2007) Oncogene , vol.26 , pp. 5310-5318
    • Yang, X.-J.1    Seto, E.2
  • 83
    • 36048958965 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Overview and perspectives
    • Dokmanovic, M.; Clarke, C.; Marks, P.A. Histone deacetylase inhibitors: overview and perspectives. Mol. Cancer Res., 2007, 5, 981-989.
    • (2007) Mol. Cancer Res , vol.5 , pp. 981-989
    • Dokmanovic, M.1    Clarke, C.2    Marks, P.A.3
  • 84
    • 33846122993 scopus 로고    scopus 로고
    • Dimethyl sulfoxide to vorinostat: Development of this histone deacetylase inhibitor as an anticancer drug
    • Marks, P.A.; Breslow, R. Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug. Nat. Biotechnol., 2007, 25, 84-90.
    • (2007) Nat. Biotechnol , vol.25 , pp. 84-90
    • Marks, P.A.1    Breslow, R.2
  • 85
    • 34547122494 scopus 로고    scopus 로고
    • HDAC inhibitors: Clinical update and mechanismbased potential
    • Glaser, K.B. HDAC inhibitors: clinical update and mechanismbased potential. Biochem. Pharmacol., 2007, 74, 659-671.
    • (2007) Biochem. Pharmacol , vol.74 , pp. 659-671
    • Glaser, K.B.1
  • 86
    • 34250171437 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Signalling towards p21cip1/waf1
    • Ocker, M.; Schneider-Stock, R. Histone deacetylase inhibitors: signalling towards p21cip1/waf1. Int. J. Biochem. Cell Biol., 2007, 39, 1367-1374.
    • (2007) Int. J. Biochem. Cell Biol , vol.39 , pp. 1367-1374
    • Ocker, M.1    Schneider-Stock, R.2
  • 87
    • 40949162039 scopus 로고    scopus 로고
    • Modulation of cell cycles and apoptosis by apicidin in estrogen receptor (ER)-positive and-negative human breast cancer cells
    • Im, J.Y.; Park, H.; Kang, K.W.; Choi, W.S.; Kim, H.S. Modulation of cell cycles and apoptosis by apicidin in estrogen receptor (ER)-positive and-negative human breast cancer cells. Chem. Biol. Interact., 2008, 172, 235-244.
    • (2008) Chem. Biol. Interact , vol.172 , pp. 235-244
    • Im, J.Y.1    Park, H.2    Kang, K.W.3    Choi, W.S.4    Kim, H.S.5
  • 88
    • 0038677606 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase activity increases chromosomal instability by the aberrant regulation of mitotic checkpoint activation
    • Shin, H.J.; Baek, K.H.; Jeon, A.H.; Kim, S.J.; Jang, K.L.; Sung, Y.C.; Kim, C.M.; Lee, C.W. Inhibition of histone deacetylase activity increases chromosomal instability by the aberrant regulation of mitotic checkpoint activation. Oncogene, 2003, 22, 3853-3858.
    • (2003) Oncogene , vol.22 , pp. 3853-3858
    • Shin, H.J.1    Baek, K.H.2    Jeon, A.H.3    Kim, S.J.4    Jang, K.L.5    Sung, Y.C.6    Kim, C.M.7    Lee, C.W.8
  • 89
    • 25144513926 scopus 로고    scopus 로고
    • Mitotic spindle checkpoint inactivation by trichostatin a defines a mechanism for increasing cancer cell killing by microtubule-disrupting agents
    • Dowling, M.; Voong, K.R.; Kim, M.; Keutmann, M.K.; Harris, E.; Kao, G.D. Mitotic spindle checkpoint inactivation by trichostatin a defines a mechanism for increasing cancer cell killing by microtubule-disrupting agents. Cancer Biol. Ther., 2005, 4, 197-206.
    • (2005) Cancer Biol. Ther , vol.4 , pp. 197-206
    • Dowling, M.1    Voong, K.R.2    Kim, M.3    Keutmann, M.K.4    Harris, E.5    Kao, G.D.6
  • 90
    • 0035845541 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species
    • Ruefli, A.A.; Ausserlechner, M.J.; Bernhard, D.; Sutton, V.R.; Tainton, K.M.; Kofler, R.; Smyth, M.J.; Johnstone, R.W. The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species. Proc. Natl. Acad. Sci USA, 2001, 98, 10833-10838.
    • (2001) Proc. Natl. Acad. Sci USA , vol.98 , pp. 10833-10838
    • Ruefli, A.A.1    Ausserlechner, M.J.2    Bernhard, D.3    Sutton, V.R.4    Tainton, K.M.5    Kofler, R.6    Smyth, M.J.7    Johnstone, R.W.8
  • 91
    • 0038485588 scopus 로고    scopus 로고
    • Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA)
    • Henderson, C.; Mizzau, M.; Paroni, G.; Maestro, R.; Schneider, C.; Brancolini, C. Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA). J. Biol. Chem., 2003, 278, 12579-12589.
    • (2003) J. Biol. Chem , vol.278 , pp. 12579-12589
    • Henderson, C.1    Mizzau, M.2    Paroni, G.3    Maestro, R.4    Schneider, C.5    Brancolini, C.6
  • 92
    • 0032555716 scopus 로고    scopus 로고
    • Luo, X.; Budihardjo, I.; Zou, H.; Slaughter, C.; Wang, X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell, 1998, 94, 481-490.
    • Luo, X.; Budihardjo, I.; Zou, H.; Slaughter, C.; Wang, X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell, 1998, 94, 481-490.
  • 93
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li, H.; Zhu, H.; Xu, C.J.; Yuan, J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell, 1998, 94, 491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 94
    • 2942584501 scopus 로고    scopus 로고
    • Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochondrial damage and apoptosis in human leukemia cells
    • Rosato, R.R.; Almenara, J.A.; Dai, Y.; Grant, S. Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochondrial damage and apoptosis in human leukemia cells. Mol. Cancer Ther., 2003, 2, 1273-1284.
    • (2003) Mol. Cancer Ther , vol.2 , pp. 1273-1284
    • Rosato, R.R.1    Almenara, J.A.2    Dai, Y.3    Grant, S.4
  • 95
    • 33846199978 scopus 로고    scopus 로고
    • Trichostatin A induces apoptosis in lung cancer cells via simultaneous activation of the death receptormediated and mitochondrial pathway?
    • Kim, H.R.; Kim, E.J.;Yang, S.H.; Jeong, E.T.; Park, C.; Lee, J.H.; Youn, M.J.; So, H.S.; Park, R. Trichostatin A induces apoptosis in lung cancer cells via simultaneous activation of the death receptormediated and mitochondrial pathway? Exp. Mol. Med., 2006, 38, 616-624.
    • (2006) Exp. Mol. Med , vol.38 , pp. 616-624
    • Kim, H.R.1    Kim, E.J.2    Yang, S.H.3    Jeong, E.T.4    Park, C.5    Lee, J.H.6    Youn, M.J.7    So, H.S.8    Park, R.9
  • 96
    • 36749029400 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor suberoylanilide hydroxamic acid induces apoptosis through both mitochondrial and Fas (Cd95) signaling in head and neck squamous carcinoma cells
    • Gillenwater, A.M.; Zhong, M.; Lotan, R. Histone deacetylase inhibitor suberoylanilide hydroxamic acid induces apoptosis through both mitochondrial and Fas (Cd95) signaling in head and neck squamous carcinoma cells. Mol. Cancer Ther., 2007, 6, 2967-2975.
    • (2007) Mol. Cancer Ther , vol.6 , pp. 2967-2975
    • Gillenwater, A.M.1    Zhong, M.2    Lotan, R.3
  • 97
    • 20744449274 scopus 로고    scopus 로고
    • Blockade of histone deacetylase inhibitor-induced RelA/p65 acetylation and NFkappaB activation potentiates apoptosis in leukemia cells through a process mediated by oxidative damage, XIAP downregulation, and c-Jun N-terminal kinase 1 activation
    • Dai, Y.; Rahmani, M.; Dent, P.; Grant, S. Blockade of histone deacetylase inhibitor-induced RelA/p65 acetylation and NFkappaB activation potentiates apoptosis in leukemia cells through a process mediated by oxidative damage, XIAP downregulation, and c-Jun N-terminal kinase 1 activation. Mol. Cell Biol., 2005, 25, 5429-5444.
    • (2005) Mol. Cell Biol , vol.25 , pp. 5429-5444
    • Dai, Y.1    Rahmani, M.2    Dent, P.3    Grant, S.4
  • 98
    • 0036690648 scopus 로고    scopus 로고
    • PS-341, a novel proteasome inhibitor, induces Bcl-2 phosphorylation and cleavage in association with G2-M phase arrest and apoptosis
    • Ling, Y.-H.; Liebes, L.; Ng, B.; Buckley, M.; Elliott, P.J.; Adams, J.; Jiang, J.-D.; Muggia, F.M.; Perez-Soler, R. PS-341, a novel proteasome inhibitor, induces Bcl-2 phosphorylation and cleavage in association with G2-M phase arrest and apoptosis. Mol. Cancer Ther., 2002, 1, 841-849.
    • (2002) Mol. Cancer Ther , vol.1 , pp. 841-849
    • Ling, Y.-H.1    Liebes, L.2    Ng, B.3    Buckley, M.4    Elliott, P.J.5    Adams, J.6    Jiang, J.-D.7    Muggia, F.M.8    Perez-Soler, R.9
  • 99
    • 2542523228 scopus 로고    scopus 로고
    • Synergistic induction of oxidative injury and apoptosis in human multiple myeloma cells by the proteasome inhibitor bortezomib and histone deacetylase inhibitors
    • Pei, X.-Y.; Dai, Y.; Grant, S. Synergistic induction of oxidative injury and apoptosis in human multiple myeloma cells by the proteasome inhibitor bortezomib and histone deacetylase inhibitors. Clin. Cancer Res., 2004, 10, 3839-3852.
    • (2004) Clin. Cancer Res , vol.10 , pp. 3839-3852
    • Pei, X.-Y.1    Dai, Y.2    Grant, S.3
  • 110
    • 34248377893 scopus 로고    scopus 로고
    • Bortezomib activity and in vitro interactions with anthracyclines and cytarabine in acute myeloid leukemia cells are independent of multidrug resistance mechanisms and p53 status
    • Minderman, H.; Zhou, Y.; O'Loughlin, K.L.; Baer, M.R. Bortezomib activity and in vitro interactions with anthracyclines and cytarabine in acute myeloid leukemia cells are independent of multidrug resistance mechanisms and p53 status. Cancer Chemother. Pharmacol., 2007, 60, 245-255.
    • (2007) Cancer Chemother. Pharmacol , vol.60 , pp. 245-255
    • Minderman, H.1    Zhou, Y.2    O'Loughlin, K.L.3    Baer, M.R.4
  • 111
    • 38449109278 scopus 로고    scopus 로고
    • Functional characteristics and gene expression profiles of primary acute myeloid leukaemia cells identify patient subgroups that differ in susceptibility to histone deacetylase inhibitors
    • Stapnes, C.; Ryningen, A.; Hatfield, K.; Øyan, A.M.; Eide, G.E.; Corbascio, M.; Kalland, K.H.; Gjertsen, B.T.; Bruserud, Ø. Functional characteristics and gene expression profiles of primary acute myeloid leukaemia cells identify patient subgroups that differ in susceptibility to histone deacetylase inhibitors. Int. J. Oncol., 2007, 31, 1529-1538.
    • (2007) Int. J. Oncol , vol.31 , pp. 1529-1538
    • Stapnes, C.1    Ryningen, A.2    Hatfield, K.3    Øyan, A.M.4    Eide, G.E.5    Corbascio, M.6    Kalland, K.H.7    Gjertsen, B.T.8    Bruserud, Ø.9
  • 112
    • 37249032404 scopus 로고    scopus 로고
    • Epigenetic targeting in acute myeloid leukemia: Use of flow cytometry in monitoring therapeutic effects
    • Ryningen, A.; Bruserud, Ø. Epigenetic targeting in acute myeloid leukemia: use of flow cytometry in monitoring therapeutic effects. Curr. Pharm. Biotechnol., 2007, 8, 401-411.
    • (2007) Curr. Pharm. Biotechnol , vol.8 , pp. 401-411
    • Ryningen, A.1    Bruserud, Ø.2
  • 113
    • 34249887679 scopus 로고    scopus 로고
    • Clonogenic acute myelogenous leukemia cells are heterogeneous with regard to regulation of differentiation and effect of epigenetic pharmacological targeting
    • Ryningen, A.; Stapnes, C.; Bruserud, Ø. Clonogenic acute myelogenous leukemia cells are heterogeneous with regard to regulation of differentiation and effect of epigenetic pharmacological targeting. Leuk. Res., 2007, 31, 1303-1313.
    • (2007) Leuk. Res , vol.31 , pp. 1303-1313
    • Ryningen, A.1    Stapnes, C.2    Bruserud, Ø.3
  • 114
    • 31144449861 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor depsipeptide (FK228) induces apoptosis in leukemic cells by facilitating mitochondrial translocation of Bax, which is enhanced by the proteasome inhibitor bortezomib
    • Sutheesophon, K.; Kobayashi, Y.; Takatoku, M.A.; Ozawa, K.; Kano, Y.; Ishii, H.; Furukawa, Y. Histone deacetylase inhibitor depsipeptide (FK228) induces apoptosis in leukemic cells by facilitating mitochondrial translocation of Bax, which is enhanced by the proteasome inhibitor bortezomib. Acta Haematol., 2006, 115, 78-90.
    • (2006) Acta Haematol , vol.115 , pp. 78-90
    • Sutheesophon, K.1    Kobayashi, Y.2    Takatoku, M.A.3    Ozawa, K.4    Kano, Y.5    Ishii, H.6    Furukawa, Y.7
  • 116
    • 68349087709 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib as better inductor of apoptosis than transforming growth factor beta in human acute myeloid cell lines
    • Abstract PP7A-24
    • Fuchs, O.; Provaznikova, D.; Marinov, I.; Kuzelova, K.; Spicka, I. The proteasome inhibitor bortezomib as better inductor of apoptosis than transforming growth factor beta in human acute myeloid cell lines. FEBS J., 2008, 275(Suppl. 1), 305, Abstract PP7A-24.
    • (2008) FEBS J , vol.275 , Issue.SUPPL. 1 , pp. 305
    • Fuchs, O.1    Provaznikova, D.2    Marinov, I.3    Kuzelova, K.4    Spicka, I.5
  • 118
    • 0242493856 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib interacts synergistically with histone deacetylase inhibitors to induce apoptosis in Bcr/Abl+ cells sensitive and resistant to STI571
    • Yu, C.; Rahmani, M.; Conrad, D.; Subler, M.; Dent, P.; Grant, S. The proteasome inhibitor bortezomib interacts synergistically with histone deacetylase inhibitors to induce apoptosis in Bcr/Abl+ cells sensitive and resistant to STI571. Blood, 2003, 102, 3765-3774.
    • (2003) Blood , vol.102 , pp. 3765-3774
    • Yu, C.1    Rahmani, M.2    Conrad, D.3    Subler, M.4    Dent, P.5    Grant, S.6
  • 119
    • 3142554015 scopus 로고    scopus 로고
    • Bortezomib and flavopiridol interact synergistically to induce apoptosis in chronic myeloid leukemia cells resistant to imatinib mesylate through both Bcr/ Abl-dependent and -independent mechanisms
    • Dai, Y.; Rahmani, M.; Pei, X.Y.; Dent, P.; Grant, S. Bortezomib and flavopiridol interact synergistically to induce apoptosis in chronic myeloid leukemia cells resistant to imatinib mesylate through both Bcr/ Abl-dependent and -independent mechanisms. Blood, 2004, 104, 509-518.
    • (2004) Blood , vol.104 , pp. 509-518
    • Dai, Y.1    Rahmani, M.2    Pei, X.Y.3    Dent, P.4    Grant, S.5
  • 120
    • 0141960411 scopus 로고    scopus 로고
    • Effects of the proteasome inhibitor, bortezomib, on apoptosis in isolated lymphocytes obtained from patients with chronic lymphocytic leukemia
    • Pahler, J.C.; Ruiz, S.; Niemer, I.; Calvert, L.R.; Andreeff, M.; Keating, M.; Faderl, S.; McConkey, D.J. Effects of the proteasome inhibitor, bortezomib, on apoptosis in isolated lymphocytes obtained from patients with chronic lymphocytic leukemia. Clin. Cancer Res., 2003, 9, 4570-4577.
    • (2003) Clin. Cancer Res , vol.9 , pp. 4570-4577
    • Pahler, J.C.1    Ruiz, S.2    Niemer, I.3    Calvert, L.R.4    Andreeff, M.5    Keating, M.6    Faderl, S.7    McConkey, D.J.8
  • 121
    • 2942594286 scopus 로고    scopus 로고
    • Treatment of human chronic lymphocytic leukemia cells with the proteasome inhibitor bortezomib promotes apoptosis
    • Kelley,T.W.; Alkan, S.; Srkalovic, G.; Hsi, E.D. Treatment of human chronic lymphocytic leukemia cells with the proteasome inhibitor bortezomib promotes apoptosis. Leuk Res., 2004, 28, 845-850.
    • (2004) Leuk Res , vol.28 , pp. 845-850
    • Kelley, T.W.1    Alkan, S.2    Srkalovic, G.3    Hsi, E.D.4
  • 122
    • 17444405587 scopus 로고    scopus 로고
    • In vitro cytotoxic effect of proteasome inhibitor bortezomib in combination with purine nucleoside analogues on chronic lymphocytic leukaemia cells
    • Duechler, M.; Linke, A.; Cebula, B.; Shehata, M.; Schwarzmeier, J.D.; Robak, T.; Smolewski, P. In vitro cytotoxic effect of proteasome inhibitor bortezomib in combination with purine nucleoside analogues on chronic lymphocytic leukaemia cells. Eur. J. Haematol., 2005, 74, 407-417.
    • (2005) Eur. J. Haematol , vol.74 , pp. 407-417
    • Duechler, M.1    Linke, A.2    Cebula, B.3    Shehata, M.4    Schwarzmeier, J.D.5    Robak, T.6    Smolewski, P.7
  • 123
    • 33745810978 scopus 로고    scopus 로고
    • The TRAIL apoptotic pathway mediates proteasome inhibitor induced apoptosis in primary chronic lymphocytic leukemia cells
    • Kabore, A.F.; Sun, J.; Hu, X.; McCrea, K.; Johnston, J.B.; Gibson, S.B. The TRAIL apoptotic pathway mediates proteasome inhibitor induced apoptosis in primary chronic lymphocytic leukemia cells. Apoptosis, 2006, 11, 1175-1193.
    • (2006) Apoptosis , vol.11 , pp. 1175-1193
    • Kabore, A.F.1    Sun, J.2    Hu, X.3    McCrea, K.4    Johnston, J.B.5    Gibson, S.B.6
  • 124
    • 33748300908 scopus 로고    scopus 로고
    • The proteasome inhibitor NPI-0052 is a more effective inducer of apoptosis than bortezomib in lymphocytes from patients with chronic lymphocytic leukemia
    • Ruiz, S.; Krupnik, Y.; Keating, M.; Chandra, J.; Palladino, M.; McConkey, D. The proteasome inhibitor NPI-0052 is a more effective inducer of apoptosis than bortezomib in lymphocytes from patients with chronic lymphocytic leukemia. Mol. Cancer Ther., 2006, 5, 1836-1843.
    • (2006) Mol. Cancer Ther , vol.5 , pp. 1836-1843
    • Ruiz, S.1    Krupnik, Y.2    Keating, M.3    Chandra, J.4    Palladino, M.5    McConkey, D.6
  • 125
    • 38949105902 scopus 로고    scopus 로고
    • Interactions between bortezomib and romidepsin and belinostat in chronic lymphocytic leukemia cells
    • Dai, Y.; Chen, S.; Kramer, L.B.; Funk, V.L.; Dent, P.; Grant, S. Interactions between bortezomib and romidepsin and belinostat in chronic lymphocytic leukemia cells. Clin Cancer Res., 2008, 14, 549-558.
    • (2008) Clin Cancer Res , vol.14 , pp. 549-558
    • Dai, Y.1    Chen, S.2    Kramer, L.B.3    Funk, V.L.4    Dent, P.5    Grant, S.6
  • 126
    • 0036172154 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341, a potential therapeutic agent for adult T-cell leukemia
    • Tan, C.; Waldmann, T.A. Proteasome inhibitor PS-341, a potential therapeutic agent for adult T-cell leukemia. Cancer Res., 2002, 62, 1083-1086.
    • (2002) Cancer Res , vol.62 , pp. 1083-1086
    • Tan, C.1    Waldmann, T.A.2
  • 127
    • 4344643781 scopus 로고    scopus 로고
    • Proteasome inhibitor, bortezomib, potently inhibits the growth of adult T-cell leukemia cells both in vivo and in vitro
    • Satou, Y.; Nosaka, K.; Koya, Y.; Yasunaga, J.I.; Toyokuni, S.; Matsuoka, M. Proteasome inhibitor, bortezomib, potently inhibits the growth of adult T-cell leukemia cells both in vivo and in vitro. Leukemia, 2004, 18, 1357-1363.
    • (2004) Leukemia , vol.18 , pp. 1357-1363
    • Satou, Y.1    Nosaka, K.2    Koya, Y.3    Yasunaga, J.I.4    Toyokuni, S.5    Matsuoka, M.6
  • 129
    • 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.; Ohyashiki, J.H.; Kurashina, R.; Kobayashi, C.; Zhang, Y.; Takaku, T.; Ohyashiki, K. Induction of heme oxygenase-1 by cobalt protoporphyrin enhances the antitumour effect of bortezomib in adult T-cell leukaemia cells. Br. J. Cancer, 2007, 97, 1099-1105.
    • (2007) Br. J. Cancer , vol.97 , pp. 1099-1105
    • Hamamura, R.S.1    Ohyashiki, J.H.2    Kurashina, R.3    Kobayashi, C.4    Zhang, Y.5    Takaku, T.6    Ohyashiki, K.7
  • 130
    • 36048981351 scopus 로고    scopus 로고
    • Bortezomib induces apoptosis in T-cell prolymphocytic leukemia (TPLL)
    • Ozpuyan, F.; Meyer, P.; Ni, H.; Al-Masri, H.; Alkan, S. Bortezomib induces apoptosis in T-cell prolymphocytic leukemia (TPLL). Leuk. Lymphoma, 2007, 48, 2247-2250.
    • (2007) Leuk. Lymphoma , vol.48 , pp. 2247-2250
    • Ozpuyan, F.1    Meyer, P.2    Ni, H.3    Al-Masri, H.4    Alkan, S.5
  • 131
    • 39149111265 scopus 로고    scopus 로고
    • Treatment of adult T-cell leukemia/lymphoma: Past, present, and future
    • Ishitsuka, K.; Tamura, K. Treatment of adult T-cell leukemia/lymphoma: past, present, and future. Eur. J. Haematol., 2008, 80, 185-196.
    • (2008) Eur. J. Haematol , vol.80 , pp. 185-196
    • Ishitsuka, K.1    Tamura, K.2
  • 132
    • 33845532759 scopus 로고    scopus 로고
    • Activity patterns of proteasome subunits reflect bortezomib sensitivity of hematologic malignancies and are variable in primary human leukemia cells
    • Kraus, M.; Ruckrich, T.; Reich, M.; Gogel, J.; Beck, A.; Kammer, W.; Berkers, C.R.; Burg, D.; Overkleeft, H.; Ovaa, H.; Driessen, C. Activity patterns of proteasome subunits reflect bortezomib sensitivity of hematologic malignancies and are variable in primary human leukemia cells. Leukemia, 2007, 21, 84-92.
    • (2007) Leukemia , vol.21 , pp. 84-92
    • Kraus, M.1    Ruckrich, T.2    Reich, M.3    Gogel, J.4    Beck, A.5    Kammer, W.6    Berkers, C.R.7    Burg, D.8    Overkleeft, H.9    Ovaa, H.10    Driessen, C.11
  • 134
    • 33745621044 scopus 로고    scopus 로고
    • Proteasome inhibition as novel treatment strategy in leukaemia
    • Vink, J.; Cloos, J.; Kaspers, G.J. Proteasome inhibition as novel treatment strategy in leukaemia. Br. J. Haematol., 2006, 134, 253-262.
    • (2006) Br. J. Haematol , vol.134 , pp. 253-262
    • Vink, J.1    Cloos, J.2    Kaspers, G.J.3
  • 137
    • 27644477944 scopus 로고    scopus 로고
    • Differential effects of proteasome inhibition by bortezomib on murine acute graft-versus-host disease (GVHD): Delayed administration of bortezomib results in increased GVHD-dependent gastrointestinal toxicity
    • Sun, K.; Wilkins, D.E.; Anver, M.R.; Sayers, T.J.; Panoskaltsis-Mortari, A.; Blazar, B.R.; Welniak, L.A.; Murphy, W.J. Differential effects of proteasome inhibition by bortezomib on murine acute graft-versus-host disease (GVHD): delayed administration of bortezomib results in increased GVHD-dependent gastrointestinal toxicity. Blood, 2005, 106, 3293-3299.
    • (2005) Blood , vol.106 , pp. 3293-3299
    • Sun, K.1    Wilkins, D.E.2    Anver, M.R.3    Sayers, T.J.4    Panoskaltsis-Mortari, A.5    Blazar, B.R.6    Welniak, L.A.7    Murphy, W.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.