메뉴 건너뛰기




Volumn 288, Issue 47, 2013, Pages 34181-34189

The antiparasitic clioquinol induces apoptosis in leukemia and myeloma cells by inhibiting histone deacetylase activity

Author keywords

[No Author keywords available]

Indexed keywords

CELL-CYCLE ARREST; COMPUTER MODELING; COORDINATE BONDS; HEMATOLOGICAL MALIGNANCIES; HISTONE DEACETYLASES; MECHANISTIC STUDIES; MOLECULAR MECHANISM; OXYGEN AND NITROGENS;

EID: 84888329493     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.472563     Document Type: Article
Times cited : (42)

References (48)
  • 1
    • 79952384705 scopus 로고    scopus 로고
    • Cancer epigenetics reaches mainstream oncology
    • Rodríguez-Paredes, M., and Esteller, M. (2011) Cancer epigenetics reaches mainstream oncology. Nat. Med. 17, 330-339
    • (2011) Nat. Med. , vol.17 , pp. 330-339
    • Rodríguez-Paredes, M.1    Esteller, M.2
  • 3
    • 34547924046 scopus 로고    scopus 로고
    • HATs and HDACs. From structure, function and regulation to novel strategies for therapy and prevention
    • Yang, X. J., and Seto, E. (2007) HATs and HDACs. From structure, function and regulation to novel strategies for therapy and prevention. Oncogene 26, 5310-5318
    • (2007) Oncogene , vol.26 , pp. 5310-5318
    • Yang, X.J.1    Seto, E.2
  • 4
    • 33947313218 scopus 로고    scopus 로고
    • HDACs, histone deacetylation and gene transcription. From molecular biology to cancer therapeutics
    • Gallinari, P., Di Marco, S., Jones, P., Pallaoro, M., and Steinkühler, C. (2007) HDACs, histone deacetylation and gene transcription. From molecular biology to cancer therapeutics. Cell Res. 17, 195-211
    • (2007) Cell Res. , vol.17 , pp. 195-211
    • Gallinari, P.1    Di Marco, S.2    Jones, P.3    Pallaoro, M.4    Steinkühler, C.5
  • 5
    • 77953170728 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase in cancer cells slows down replication forks, activates dormant origins, and induces DNA damage
    • Conti, C., Leo, E., Eichler, G. S., Sordet, O., Martin, M. M., Fan, A., Aladjem, M. I., and Pommier, Y. (2010) Inhibition of histone deacetylase in cancer cells slows down replication forks, activates dormant origins, and induces DNA damage. Cancer Res. 70, 4470-4480
    • (2010) Cancer Res. , vol.70 , pp. 4470-4480
    • Conti, C.1    Leo, E.2    Eichler, G.S.3    Sordet, O.4    Martin, M.M.5    Fan, A.6    Aladjem, M.I.7    Pommier, Y.8
  • 6
    • 73949128107 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy
    • Lane, A. A., and Chabner, B. A. (2009) Histone deacetylase inhibitors in cancer therapy. J. Clin. Oncol. 27, 5459-5468
    • (2009) J. Clin. Oncol. , vol.27 , pp. 5459-5468
    • Lane, A.A.1    Chabner, B.A.2
  • 7
    • 39449138853 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylase (HDAC) restore the p53 pathway in neuroblastoma cells
    • Condorelli, F., Gnemmi, I., Vallario, A., Genazzani, A. A., and Canonico, P. L. (2008) Inhibitors of histone deacetylase (HDAC) restore the p53 pathway in neuroblastoma cells. Br. J. Pharmacol. 153, 657-668
    • (2008) Br. J. Pharmacol. , vol.153 , pp. 657-668
    • Condorelli, F.1    Gnemmi, I.2    Vallario, A.3    Genazzani, A.A.4    Canonico, P.L.5
  • 8
    • 79952996842 scopus 로고    scopus 로고
    • The tricyclic antidepressant amitriptyline inhibits D-cyclin transactivation and induces myeloma cell apoptosis by inhibiting histone deacetylases. In vitro and in silico evidence
    • Mao, X., Hou, T., Cao, B., Wang, W., Li, Z., Chen, S., Fei, M., Hurren, R., Gronda, M., Wu, D., Trudel, S., and Schimmer, A. D. (2011) The tricyclic antidepressant amitriptyline inhibits D-cyclin transactivation and induces myeloma cell apoptosis by inhibiting histone deacetylases. In vitro and in silico evidence. Mol. Pharmacol. 79, 672-680
    • (2011) Mol. Pharmacol. , vol.79 , pp. 672-680
    • Mao, X.1    Hou, T.2    Cao, B.3    Wang, W.4    Li, Z.5    Chen, S.6    Fei, M.7    Hurren, R.8    Gronda, M.9    Wu, D.10    Trudel, S.11    Schimmer, A.D.12
  • 9
    • 10044280340 scopus 로고    scopus 로고
    • Histone deacetylase inhibition-mediated post-translational elevation of p27KIP1 protein levels is required for G1 arrest in fibroblasts
    • Chen, J. S., and Faller, D. V. (2005) Histone deacetylase inhibition-mediated post-translational elevation of p27KIP1 protein levels is required for G1 arrest in fibroblasts. J. Cell. Physiol. 202, 87-99
    • (2005) J. Cell. Physiol. , vol.202 , pp. 87-99
    • Chen, J.S.1    Faller, D.V.2
  • 10
    • 79951571473 scopus 로고    scopus 로고
    • Role of HDAC3 on p53 expression and apoptosis in T cells of patients with multiple sclerosis
    • Zhang, F., Shi, Y., Wang, L., and Sriram, S. (2011) Role of HDAC3 on p53 expression and apoptosis in T cells of patients with multiple sclerosis. PLoS One 6, e16795
    • (2011) PLoS One , vol.6
    • Zhang, F.1    Shi, Y.2    Wang, L.3    Sriram, S.4
  • 12
    • 3042785975 scopus 로고    scopus 로고
    • A review ofdepsipeptide and other histone deacetylase inhibitors in clinical trials
    • Piekarz, R., and Bates, S. (2004) A review ofdepsipeptide and other histone deacetylase inhibitors in clinical trials. Curr. Pharm. Des. 10, 2289-2298
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 2289-2298
    • Piekarz, R.1    Bates, S.2
  • 13
    • 43049104161 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship of histone deacetylase (HDAC) inhibitors with triazole-linked cap group
    • Chen, P. C., Patil, V., Guerrant, W., Green, P., and Oyelere, A. K. (2008) Synthesis and structure-activity relationship of histone deacetylase (HDAC) inhibitors with triazole-linked cap group. Bioorg. Med. Chem. 16, 4839-4853
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 4839-4853
    • Chen, P.C.1    Patil, V.2    Guerrant, W.3    Green, P.4    Oyelere, A.K.5
  • 15
    • 54949124884 scopus 로고    scopus 로고
    • The toxicology ofclioquinol
    • Mao, X., and Schimmer, A. D. (2008) The toxicology ofclioquinol. Toxicol. Lett. 182, 1-6
    • (2008) Toxicol. Lett. , vol.182 , pp. 1-6
    • Mao, X.1    Schimmer, A.D.2
  • 16
    • 84901648175 scopus 로고    scopus 로고
    • Clioquinol and pyrrolidine dithiocarbamate complex with copper to form proteasome inhibitors and apoptosis inducers in human breast cancer cells
    • Daniel, K. G., Chen, D., Orlu, S., Cui, Q. C., Miller, F. R., and Dou, Q. P. (2005) Clioquinol and pyrrolidine dithiocarbamate complex with copper to form proteasome inhibitors and apoptosis inducers in human breast cancer cells. Breast Cancer Res. 7, R897-908
    • (2005) Breast Cancer Res. , vol.7
    • Daniel, K.G.1    Chen, D.2    Orlu, S.3    Cui, Q.C.4    Miller, F.R.5    Dou, Q.P.6
  • 18
    • 33847746963 scopus 로고    scopus 로고
    • Clioquinol, a therapeutic agent for Alzheimer's disease, has proteasome-inhibitory, androgen receptor-suppressing, apoptosis-inducing, and antitumor activities in human prostate cancer cells and xenografts
    • Chen, D., Cui, Q. C., Yang, H., Barrea, R. A., Sarkar, F. H., Sheng, S., Yan, B., Reddy, G. P., and Dou, Q. P. (2007) Clioquinol, a therapeutic agent for Alzheimer's disease, has proteasome-inhibitory, androgen receptor-suppressing, apoptosis-inducing, and antitumor activities in human prostate cancer cells and xenografts. Cancer Res. 67, 1636-1644
    • (2007) Cancer Res. , vol.67 , pp. 1636-1644
    • Chen, D.1    Cui, Q.C.2    Yang, H.3    Barrea, R.A.4    Sarkar, F.H.5    Sheng, S.6    Yan, B.7    Reddy, G.P.8    Dou, Q.P.9
  • 21
    • 84856280358 scopus 로고    scopus 로고
    • Clioquinol. Review of its mechanisms of action and clinical uses in neurodegenerative disorders
    • Bareggi, S. R., and Cornelli, U. (2012) Clioquinol. Review of its mechanisms of action and clinical uses in neurodegenerative disorders. CNS Neurosci. Ther. 18, 41-46
    • (2012) CNS Neurosci. Ther. , vol.18 , pp. 41-46
    • Bareggi, S.R.1    Cornelli, U.2
  • 22
    • 58249091525 scopus 로고    scopus 로고
    • Clioquinol targets zinc to lysosomes in human cancer cells
    • Yu, H., Zhou, Y., Lind, S. E., and Ding, W. Q. (2009) Clioquinol targets zinc to lysosomes in human cancer cells. Biochem. J. 417, 133-139
    • (2009) Biochem. J. , vol.417 , pp. 133-139
    • Yu, H.1    Zhou, Y.2    Lind, S.E.3    Ding, W.Q.4
  • 23
    • 71749090438 scopus 로고    scopus 로고
    • Synthesis and pharmacological exploitation of clioquinol-derived copper-binding apoptosis inducers triggering reactive oxygen species generation and MAPK pathway activation
    • Chen, H. L., Chang, C. Y., Lee, H. T., Lin, H. H., Lu, P. J., Yang, C. N., Shiau, C. W., and Shaw, A. Y. (2009) Synthesis and pharmacological exploitation of clioquinol-derived copper-binding apoptosis inducers triggering reactive oxygen species generation and MAPK pathway activation. Bioorg. Med. Chem. 17, 7239-7247
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 7239-7247
    • Chen, H.L.1    Chang, C.Y.2    Lee, H.T.3    Lin, H.H.4    Lu, P.J.5    Yang, C.N.6    Shiau, C.W.7    Shaw, A.Y.8
  • 24
    • 79951717280 scopus 로고    scopus 로고
    • Clioquinol. A novel copper-dependent and independent proteasome inhibitor
    • Schimmer, A. D. (2011) Clioquinol. A novel copper-dependent and independent proteasome inhibitor. Curr. Cancer Drug Targets 11, 325-331
    • (2011) Curr. Cancer Drug Targets , vol.11 , pp. 325-331
    • Schimmer, A.D.1
  • 29
    • 3042524904 scopus 로고
    • A wellbehaved electrostatic potential based method using charge restraints for deriving atomic charges
    • Bayly, C. I., Cieplak, P., Cornell, W. D., and Kollman, P. A. (1993) A wellbehaved electrostatic potential based method using charge restraints for deriving atomic charges. The Resp model. J. Phys. Chem. 97, 10269-10280
    • (1993) The Resp Model. J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 33
    • 77952853306 scopus 로고    scopus 로고
    • Histone deacetylases and epigenetic therapies of hematological malignancies
    • Mercurio, C, Minucci, S., and Pelicci, P. G. (2010) Histone deacetylases and epigenetic therapies of hematological malignancies. Pharmacol. Res. 62, 18-34
    • (2010) Pharmacol. Res. , vol.62 , pp. 18-34
    • Mercurio, C.1    Minucci, S.2    Pelicci, P.G.3
  • 34
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • Bolden, J. E., Peart, M. J., and Johnstone, R. W. (2006) Anticancer activities of histone deacetylase inhibitors. Nat Rev. Drug. Discov. 5, 769-784
    • (2006) Nat Rev. Drug. Discov. , vol.5 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 35
    • 0242624636 scopus 로고    scopus 로고
    • Epigenetic targets in hematopoietic malignancies
    • Claus, R., and Lübbert, M. (2003) Epigenetic targets in hematopoietic malignancies. Oncogene 22, 6489-6496
    • (2003) Oncogene , vol.22 , pp. 6489-6496
    • Claus, R.1    Lübbert, M.2
  • 36
    • 0036014986 scopus 로고    scopus 로고
    • Histone deacetylases as therapeutic targets in hematologic malignancies
    • Melnick, A., and Licht, J. D. (2002) Histone deacetylases as therapeutic targets in hematologic malignancies. Curr. Opin. Hematol. 9, 322-332
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 322-332
    • Melnick, A.1    Licht, J.D.2
  • 37
    • 50049108874 scopus 로고    scopus 로고
    • Prognostic significance of the therapeutic targets histone deacetylase 1, 2, 6 and acetylated histone H4 in cutaneous T-cell lymphoma
    • Marquard, L., Gjerdrum, L. M., Christensen, I. J., Jensen, P. B., Sehested, M., and Ralfkiaer, E. (2008) Prognostic significance of the therapeutic targets histone deacetylase 1, 2, 6 and acetylated histone H4 in cutaneous T-cell lymphoma. Histopathology 53, 267-277
    • (2008) Histopathology , vol.53 , pp. 267-277
    • Marquard, L.1    Gjerdrum, L.M.2    Christensen, I.J.3    Jensen, P.B.4    Sehested, M.5    Ralfkiaer, E.6
  • 39
    • 13944274571 scopus 로고    scopus 로고
    • Histone deacetylase inhibition downregulates cyclin D1 transcription by inhibiting nuclear factor-B/p65 DNA binding
    • Hu, J., and Colburn, N. H. (2005) Histone deacetylase inhibition downregulates cyclin D1 transcription by inhibiting nuclear factor-B/p65 DNA binding. Mol. Cancer Res. 3, 100-109
    • (2005) Mol. Cancer Res. , vol.3 , pp. 100-109
    • Hu, J.1    Colburn, N.H.2
  • 40
    • 0037053375 scopus 로고    scopus 로고
    • Ubiquitin/proteasome-dependent degradation of D-type cyclins is linked to tumor necrosis factor-induced cell cycle arrest
    • Hu, X., Bryington, M., Fisher, A. B., Liang, X., Zhang, X., Cui, D., Datta, I., and Zuckerman, K. S. (2002) Ubiquitin/proteasome-dependent degradation of D-type cyclins is linked to tumor necrosis factor-induced cell cycle arrest. J. Biol. Chem. 277, 16528-16537
    • (2002) J. Biol. Chem. , vol.277 , pp. 16528-16537
    • Hu, X.1    Bryington, M.2    Fisher, A.B.3    Liang, X.4    Zhang, X.5    Cui, D.6    Datta, I.7    Zuckerman, K.S.8
  • 41
    • 77949267166 scopus 로고    scopus 로고
    • Tumor cellular proteasome inhibition and growth suppression by 8-hydroxyquinoline and clioquinol requires their capabilities to bind copper and transport copper into cells
    • Zhai, S., Yang, L., Cui, Q. C, Sun, Y., Dou, Q. P., and Yan, B. (2010) Tumor cellular proteasome inhibition and growth suppression by 8-hydroxyquinoline and clioquinol requires their capabilities to bind copper and transport copper into cells. J. Biol. Inorg Chem. 15, 259-269
    • (2010) J. Biol. Inorg Chem. , vol.15 , pp. 259-269
    • Zhai, S.1    Yang, L.2    Cui, Q.C.3    Sun, Y.4    Dou, Q.P.5    Yan, B.6
  • 42
    • 0017199809 scopus 로고
    • Hydroxyquinolines inhibit ribonucleic acid-dependent deoxyribonucleic acid polymerase and inactivate Rous sarcoma virus and herpes simplex virus
    • Rohde, W., Mikelens, P., Jackson, J., Blackman, J., Whitcher, J., and Levinson, W. (1976) Hydroxyquinolines inhibit ribonucleic acid-dependent deoxyribonucleic acid polymerase and inactivate Rous sarcoma virus and herpes simplex virus. Antimicrob. Agents. Chemother. 10, 234-240
    • (1976) Antimicrob. Agents. Chemother. , vol.10 , pp. 234-240
    • Rohde, W.1    Mikelens, P.2    Jackson, J.3    Blackman, J.4    Whitcher, J.5    Levinson, W.6
  • 45
    • 43049163953 scopus 로고    scopus 로고
    • Acetylation is indispensable for p53 activation
    • Tang, Y., Zhao, W., Chen, Y., Zhao, Y., and Gu, W. (2008) Acetylation is indispensable for p53 activation. Cell 133, 612-626
    • (2008) Cell , vol.133 , pp. 612-626
    • Tang, Y.1    Zhao, W.2    Chen, Y.3    Zhao, Y.4    Gu, W.5
  • 46
    • 1442330508 scopus 로고    scopus 로고
    • Acetylation of p53 augments its site-specific DNA binding both in vitro and in vivo
    • Luo, J., Li, M., Tang, Y., Laszkowska, M., Roeder, R. G., and Gu, W. (2004) Acetylation of p53 augments its site-specific DNA binding both in vitro and in vivo. Proc. Natl. Acad. Sci. U. S. A. 101, 2259-2264
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2259-2264
    • Luo, J.1    Li, M.2    Tang, Y.3    Laszkowska, M.4    Roeder, R.G.5    Gu, W.6
  • 47
    • 37349020313 scopus 로고    scopus 로고
    • Clioquinol promotes cancer cell toxicity through tumor necrosis factor a release from macrophages
    • Du, T., Filiz, G., Caragounis, A., Crouch, P. J., and White, A. R. (2008) Clioquinol promotes cancer cell toxicity through tumor necrosis factor a release from macrophages. J. Pharmacol. Exp. Ther. 324, 360-367
    • (2008) J. Pharmacol. Exp. Ther. , vol.324 , pp. 360-367
    • Du, T.1    Filiz, G.2    Caragounis, A.3    Crouch, P.J.4    White, A.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.