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Volumn 34, Issue 7, 2013, Pages 1442-1449

Pure curcumin increases the expression of SOCS1 and SOCS3 in myeloproliferative neoplasms through suppressing class I histone deacetylases

Author keywords

[No Author keywords available]

Indexed keywords

CURCUMIN; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 3; HISTONE DEACETYLASE 8; JANUS KINASE 2; SMALL INTERFERING RNA; STAT5 PROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING 1; SUPPRESSOR OF CYTOKINE SIGNALING 3; TRICHOSTATIN A;

EID: 84880286355     PISSN: 01433334     EISSN: 14602180     Source Type: Journal    
DOI: 10.1093/carcin/bgt070     Document Type: Article
Times cited : (67)

References (46)
  • 1
    • 0034841006 scopus 로고    scopus 로고
    • Negative regulation of cytokine signaling
    • Greenhalgh, C.J. et al. (2001) Negative regulation of cytokine signaling. J. Leukoc. Biol., 70, 348-356.
    • (2001) J. Leukoc. Biol , vol.70 , pp. 348-356
    • Greenhalgh, C.J.1
  • 2
    • 0038807434 scopus 로고    scopus 로고
    • Negative regulation of interleukin-12 signaling by suppressor of cytokine signaling-1
    • Eyles, J.L. et al. (2002) Negative regulation of interleukin-12 signaling by suppressor of cytokine signaling-1. J. Biol. Chem., 277, 43735-43740.
    • (2002) J. Biol. Chem , vol.277 , pp. 43735-43740
    • Eyles, J.L.1
  • 3
    • 0036233985 scopus 로고    scopus 로고
    • Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1
    • Ungureanu, D. et al. (2002) Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1. Mol. Cell. Biol., 22, 3316-3326.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 3316-3326
    • Ungureanu, D.1
  • 4
    • 0034703097 scopus 로고    scopus 로고
    • CIS3/SOCS-3 suppresses erythropoietin (EPO) signaling by binding the EPO receptor and JAK2
    • Sasaki, A. et al. (2000) CIS3/SOCS-3 suppresses erythropoietin (EPO) signaling by binding the EPO receptor and JAK2. J. Biol. Chem., 275, 29338-29347.
    • (2000) J. Biol. Chem , vol.275 , pp. 29338-29347
    • Sasaki, A.1
  • 5
    • 17844383458 scopus 로고    scopus 로고
    • A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera
    • James, C. et al. (2005) A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera. Nature, 434, 1144-1148.
    • (2005) Nature , vol.434 , pp. 1144-1148
    • James, C.1
  • 6
    • 33750534561 scopus 로고    scopus 로고
    • MPL515 mutations in myeloproliferative and other myeloid disorders: a study of 1182 patients
    • Pardanani, A.D. et al. (2006) MPL515 mutations in myeloproliferative and other myeloid disorders: a study of 1182 patients. Blood, 108, 3472-3476.
    • (2006) Blood , vol.108 , pp. 3472-3476
    • Pardanani, A.D.1
  • 7
    • 34249728880 scopus 로고    scopus 로고
    • The myeloproliferative disorder-associated JAK2 V617F mutant escapes negative regulation by suppressor of cytokine signaling 3
    • Hookham, M.B. et al. (2007) The myeloproliferative disorder-associated JAK2 V617F mutant escapes negative regulation by suppressor of cytokine signaling 3. Blood, 109, 4924-4929.
    • (2007) Blood , vol.109 , pp. 4924-4929
    • Hookham, M.B.1
  • 8
    • 84860257685 scopus 로고    scopus 로고
    • Roles of histone deacetylases in epigenetic regulation: emerging paradigms from studies with inhibitors
    • Clin. Epigenetics
    • Delcuve, G.P. et al. (2012) Roles of histone deacetylases in epigenetic regulation: emerging paradigms from studies with inhibitors. Clin. Epigenetics, 4, 5.
    • (2012) , vol.4 , pp. 5
    • Delcuve, G.P.1
  • 9
    • 34347339526 scopus 로고    scopus 로고
    • Role for histone deacetylase 1 in human tumor cell proliferation
    • Senese, S. et al. (2007) Role for histone deacetylase 1 in human tumor cell proliferation. Mol. Cell. Biol., 27, 4784-4795.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 4784-4795
    • Senese, S.1
  • 10
    • 1842631408 scopus 로고    scopus 로고
    • Upregulation and nuclear recruitment of HDAC1 in hormone refractory prostate cancer
    • Halkidou, K. et al. (2004) Upregulation and nuclear recruitment of HDAC1 in hormone refractory prostate cancer. Prostate, 59, 177-189.
    • (2004) Prostate , vol.59 , pp. 177-189
    • Halkidou, K.1
  • 11
    • 73849103589 scopus 로고    scopus 로고
    • Targeting of HDAC8 and investigational inhibitors in neuroblastoma
    • Oehme, I. et al. (2009) Targeting of HDAC8 and investigational inhibitors in neuroblastoma. Expert Opin. Investig. Drugs, 18, 1605-1617.
    • (2009) Expert Opin. Investig. Drugs , vol.18 , pp. 1605-1617
    • Oehme, I.1
  • 12
    • 77955643796 scopus 로고    scopus 로고
    • The clinical development of histone deacetylase inhibitors as targeted anticancer drugs
    • Marks, P.A. (2010) The clinical development of histone deacetylase inhibitors as targeted anticancer drugs. Expert Opin. Investig. Drugs, 19, 1049-1066.
    • (2010) Expert Opin. Investig. Drugs , vol.19 , pp. 1049-1066
    • Marks, P.A.1
  • 13
    • 67449127082 scopus 로고    scopus 로고
    • Clinical studies of histone deacetylase inhibitors
    • Prince, H.M. et al. (2009) Clinical studies of histone deacetylase inhibitors. Clin. Cancer Res., 15, 3958-3969.
    • (2009) Clin. Cancer Res , vol.15 , pp. 3958-3969
    • Prince, H.M.1
  • 15
    • 84863011392 scopus 로고    scopus 로고
    • Green tea polyphenols causes cell cycle arrest and apoptosis in prostate cancer cells by suppressing class I histone deacetylases
    • Thakur, V.S. et al. (2012) Green tea polyphenols causes cell cycle arrest and apoptosis in prostate cancer cells by suppressing class I histone deacetylases. Carcinogenesis, 33, 377-384.
    • (2012) Carcinogenesis , vol.33 , pp. 377-384
    • Thakur, V.S.1
  • 16
    • 0022357855 scopus 로고
    • Potential anticancer activity of turmeric (Curcuma longa)
    • Kuttan, R. et al. (1985) Potential anticancer activity of turmeric (Curcuma longa). Cancer Lett., 29, 197-202.
    • (1985) Cancer Lett , vol.29 , pp. 197-202
    • Kuttan, R.1
  • 17
    • 33845973732 scopus 로고    scopus 로고
    • Curcumin-induced cell cycle arrest and apoptosis in human acute promyelocytic leukemia HL-60 cells via MMP changes and caspase-3 activation
    • Tan, T.W. et al. (2006) Curcumin-induced cell cycle arrest and apoptosis in human acute promyelocytic leukemia HL-60 cells via MMP changes and caspase-3 activation. Anticancer Res., 26, 4361-4371.
    • (2006) Anticancer Res , vol.26 , pp. 4361-4371
    • Tan, T.W.1
  • 18
    • 61349105913 scopus 로고    scopus 로고
    • Wilms' tumour gene 1 (WT1) as a target in curcumin treatment of pancreatic cancer cells
    • Glienke, W. et al. (2009) Wilms' tumour gene 1 (WT1) as a target in curcumin treatment of pancreatic cancer cells. Eur. J. Cancer, 45, 874-880.
    • (2009) Eur. J. Cancer , vol.45 , pp. 874-880
    • Glienke, W.1
  • 19
    • 0037305821 scopus 로고    scopus 로고
    • Curcumin (diferuloylmethane) down-regulates the constitutive activation of nuclear factor-kappa B and IkappaBalpha kinase in human multiple myeloma cells
    • Bharti, A.C. et al. (2003) Curcumin (diferuloylmethane) down-regulates the constitutive activation of nuclear factor-kappa B and IkappaBalpha kinase in human multiple myeloma cells, leading to suppression of proliferation and induction of apoptosis. Blood, 101, 1053-1062.
    • (2003) Leading to suppression of proliferation and induction of apoptosis. Blood , vol.101 , pp. 1053-1062
    • Bharti, A.C.1
  • 20
    • 43949131788 scopus 로고    scopus 로고
    • Curcumin induces cell-arrest and apoptosis in association with the inhibition of constitutively active NF-kappaB and STAT3 pathways in Hodgkin's lymphoma cells
    • Mackenzie, G.G. et al. (2008) Curcumin induces cell-arrest and apoptosis in association with the inhibition of constitutively active NF-kappaB and STAT3 pathways in Hodgkin's lymphoma cells. Int. J. Cancer, 123, 56-65.
    • (2008) Int. J. Cancer , vol.123 , pp. 56-65
    • Mackenzie, G.G.1
  • 21
    • 33750520736 scopus 로고    scopus 로고
    • Curcumin regulates signal transducer and activator of transcription (STAT) expression in K562 cells
    • Blasius, R. et al. (2006) Curcumin regulates signal transducer and activator of transcription (STAT) expression in K562 cells. Biochem. Pharmacol., 72, 1547-1554.
    • (2006) Biochem. Pharmacol , vol.72 , pp. 1547-1554
    • Blasius, R.1
  • 22
    • 78349269863 scopus 로고    scopus 로고
    • Development of curcumin as an epigenetic agent
    • Fu, S. et al. (2010) Development of curcumin as an epigenetic agent. Cancer, 116, 4670-4676.
    • (2010) Cancer , vol.116 , pp. 4670-4676
    • Fu, S.1
  • 23
    • 84860240764 scopus 로고    scopus 로고
    • Curcumin causes promoter hypomethylation and increased expression of FANCF gene in SiHa cell line
    • Parashar, G. et al. (2012) Curcumin causes promoter hypomethylation and increased expression of FANCF gene in SiHa cell line. Mol. Cell. Biochem., 365, 29-35.
    • (2012) Mol. Cell. Biochem , vol.365 , pp. 29-35
    • Parashar, G.1
  • 24
    • 18744403080 scopus 로고    scopus 로고
    • Curcumin
    • is a novel histone deacetylase inhibitor regulating B-NHL cell line Raji proliferation. Acta Pharmacol. Sin
    • Liu, H.L. et al. (2005) Curcumin, a potent anti-tumor reagent, is a novel histone deacetylase inhibitor regulating B-NHL cell line Raji proliferation. Acta Pharmacol. Sin., 26, 603-609.
    • (2005) A potent anti-tumor reagent , vol.26 , pp. 603-609
    • Liu, H.L.1
  • 25
    • 84859865097 scopus 로고    scopus 로고
    • Essential role for Stat5a/b in myeloproliferative neoplasms induced by BCR-ABL1 and JAK2(V617F) in mice
    • Walz, C. et al. (2012) Essential role for Stat5a/b in myeloproliferative neoplasms induced by BCR-ABL1 and JAK2(V617F) in mice. Blood, 119, 3550-3560.
    • (2012) Blood , vol.119 , pp. 3550-3560
    • Walz, C.1
  • 26
    • 0033544899 scopus 로고    scopus 로고
    • SOCS/CIS protein inhibition of growth hormonestimulated STAT5 signaling by multiple mechanisms
    • Ram, P.A. et al. (1999) SOCS/CIS protein inhibition of growth hormonestimulated STAT5 signaling by multiple mechanisms. J. Biol. Chem., 274, 35553-35561.
    • (1999) J. Biol. Chem , vol.274 , pp. 35553-35561
    • Ram, P.A.1
  • 27
    • 79955117246 scopus 로고    scopus 로고
    • Curcumin-induced HDAC inhibition and attenuation of medulloblastoma growth in vitro and in vivo
    • Lee, S.J. et al. (2011) Curcumin-induced HDAC inhibition and attenuation of medulloblastoma growth in vitro and in vivo. BMC Cancer, 11, 144.
    • (2011) BMC Cancer , vol.11 , pp. 144
    • Lee, S.J.1
  • 28
    • 84861476075 scopus 로고    scopus 로고
    • Curcumin blocks small cell lung cancer cells migration, invasion, angiogenesis, cell cycle and neoplasia through Janus kinase-STAT3 signalling pathway
    • e37960
    • Yang, C.L. et al. (2012) Curcumin blocks small cell lung cancer cells migration, invasion, angiogenesis, cell cycle and neoplasia through Janus kinase-STAT3 signalling pathway. PLoS ONE, 7, e37960.
    • (2012) PLoS ONE , vol.7
    • Yang, C.L.1
  • 29
    • 73649104449 scopus 로고    scopus 로고
    • Lysophosphatidic acid induces STAT3 phosphorylation and ovarian cancer cell motility: their inhibition by curcumin
    • Seo, J.H. et al. (2010) Lysophosphatidic acid induces STAT3 phosphorylation and ovarian cancer cell motility: their inhibition by curcumin. Cancer Lett., 288, 50-56.
    • (2010) Cancer Lett , vol.288 , pp. 50-56
    • Seo, J.H.1
  • 30
    • 29644438937 scopus 로고    scopus 로고
    • Curcumin induces growth-arrest and apoptosis in association with the inhibition of constitutively active JAK-STAT pathway in T cell leukemia
    • Rajasingh, J. et al. (2006) Curcumin induces growth-arrest and apoptosis in association with the inhibition of constitutively active JAK-STAT pathway in T cell leukemia. Biochem. Biophys. Res. Commun., 340, 359-368.
    • (2006) Biochem. Biophys. Res. Commun , vol.340 , pp. 359-368
    • Rajasingh, J.1
  • 31
    • 42349087790 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor ITF2357 selectively targets cells bearing mutated JAK2(V617F)
    • Guerini, V. et al. (2008) The histone deacetylase inhibitor ITF2357 selectively targets cells bearing mutated JAK2(V617F). Leukemia, 22, 740-747.
    • (2008) Leukemia , vol.22 , pp. 740-747
    • Guerini, V.1
  • 32
    • 61849163272 scopus 로고    scopus 로고
    • Molecular biology of bcr-abl1-positive chronic myeloid leukemia
    • Quintas-Cardama, A. et al.(2009) Molecular biology of bcr-abl1-positive chronic myeloid leukemia. Blood, 113, 1619-1630.
    • (2009) Blood , vol.113 , pp. 1619-1630
    • Quintas-Cardama, A.1
  • 33
    • 33746900778 scopus 로고    scopus 로고
    • Curcumin affects components of the chromosomal passenger complex and induces mitotic catastrophe in apoptosis-resistant Bcr-Abl-expressing cells
    • Wolanin, K. et al. (2006) Curcumin affects components of the chromosomal passenger complex and induces mitotic catastrophe in apoptosis-resistant Bcr-Abl-expressing cells. Mol. Cancer Res., 4, 457-469.
    • (2006) Mol. Cancer Res , vol.4 , pp. 457-469
    • Wolanin, K.1
  • 34
    • 42249115029 scopus 로고    scopus 로고
    • Epigenetic inactivation of suppressors of cytokine signalling in Philadelphia-negative chronic myeloproliferative disorders
    • Capello, D. et al. (2008) Epigenetic inactivation of suppressors of cytokine signalling in Philadelphia-negative chronic myeloproliferative disorders. Br. J. Haematol., 141, 504-511.
    • (2008) Br. J. Haematol , vol.141 , pp. 504-511
    • Capello, D.1
  • 35
    • 55549126446 scopus 로고    scopus 로고
    • Methylation of the suppressor of cytokine signaling 3 gene (SOCS3) in myeloproliferative disorders
    • Fourouclas, N. et al. (2008) Methylation of the suppressor of cytokine signaling 3 gene (SOCS3) in myeloproliferative disorders. Haematologica, 93, 1635-1644.
    • (2008) Haematologica , vol.93 , pp. 1635-1644
    • Fourouclas, N.1
  • 36
    • 84855242836 scopus 로고    scopus 로고
    • Trichostatin A
    • suppresses JAK2/STAT3 signaling via inducing the promoter-associated histone acetylation of SOCS1 and SOCS3 in human colorectal cancer cells. Mol. Carcinog.,
    • Xiong, H. et al. (2012) Trichostatin A, a histone deacetylase inhibitor, suppresses JAK2/STAT3 signaling via inducing the promoter-associated histone acetylation of SOCS1 and SOCS3 in human colorectal cancer cells. Mol. Carcinog., 51, 174-184.
    • (2012) A histone deacetylase inhibitor , vol.51 , pp. 174-184
    • Xiong, H.1
  • 37
    • 84860316991 scopus 로고    scopus 로고
    • Efficacy of vorinostat in a murine model of polycythemia vera
    • Akada, H. et al. (2012) Efficacy of vorinostat in a murine model of polycythemia vera. Blood, 119, 3779-3789.
    • (2012) Blood , vol.119 , pp. 3779-3789
    • Akada, H.1
  • 38
    • 84876121166 scopus 로고    scopus 로고
    • Curcumin enhances the anticancer effects of trichostatin a in breast cancer cells
    • doi: 10.1002/mc.21875
    • Yan, G. et al. (2012) Curcumin enhances the anticancer effects of trichostatin a in breast cancer cells. Mol. Carcinog., doi: 10.1002/mc.21875.
    • (2012) Mol. Carcinog.,
    • Yan, G.1
  • 39
    • 77949503424 scopus 로고    scopus 로고
    • The enhancement of antiproliferative and proapoptotic activity of HDAC inhibitors by curcumin is mediated by Hsp90 inhibition
    • Giommarelli, C. et al. (2010) The enhancement of antiproliferative and proapoptotic activity of HDAC inhibitors by curcumin is mediated by Hsp90 inhibition. Cell. Mol. Life Sci., 67, 995-1004.
    • (2010) Cell. Mol. Life Sci , vol.67 , pp. 995-1004
    • Giommarelli, C.1
  • 40
    • 67650078931 scopus 로고    scopus 로고
    • Molecular modifications on carboxylic acid derivatives as potent histone deacetylase inhibitors: activity and docking studies
    • Bora-Tatar, G. et al. (2009) Molecular modifications on carboxylic acid derivatives as potent histone deacetylase inhibitors: activity and docking studies. Bioorg. Med. Chem., 17, 5219-5228.
    • (2009) Bioorg. Med. Chem , vol.17 , pp. 5219-5228
    • Bora-Tatar, G.1
  • 41
    • 0034725990 scopus 로고    scopus 로고
    • Cloning and characterization of human histone deacetylase 8
    • Van den Wyngaert, I. et al. (2000) Cloning and characterization of human histone deacetylase 8. FEBS Lett., 478, 77-83.
    • (2000) FEBS Lett , vol.478 , pp. 77-83
    • Van den Wyngaert, I.1
  • 42
    • 58849104486 scopus 로고    scopus 로고
    • Histone deacetylase 8 in neuroblastoma tumorigenesis
    • Oehme, I. et al. (2009) Histone deacetylase 8 in neuroblastoma tumorigenesis. Clin. Cancer Res., 15, 91-99.
    • (2009) Clin. Cancer Res , vol.15 , pp. 91-99
    • Oehme, I.1
  • 43
    • 84875163565 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors suppress mutant p53 transcription via histone deacetylase 8
    • Yan, W. et al. (2013) Histone deacetylase inhibitors suppress mutant p53 transcription via histone deacetylase 8. Oncogene, 32, 599-609.
    • (2013) Oncogene , vol.32 , pp. 599-609
    • Yan, W.1
  • 44
    • 6344222799 scopus 로고    scopus 로고
    • Crystal structure of a eukaryotic zinc-dependent histone deacetylase
    • complexed with a hydroxamic acid inhibitor. Proc. Natl Acad. Sci. U.S.A.,
    • Vannini, A. et al. (2004) Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor. Proc. Natl Acad. Sci. U.S.A., 101, 15064-15069.
    • (2004) Human HDAC8 , vol.101 , pp. 15064-15069
    • Vannini, A.1
  • 45
    • 43749109171 scopus 로고    scopus 로고
    • A novel histone deacetylase 8 (HDAC8)- specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas
    • Balasubramanian, S. et al. (2008) A novel histone deacetylase 8 (HDAC8)- specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas. Leukemia, 22, 1026-1034.
    • (2008) Leukemia , vol.22 , pp. 1026-1034
    • Balasubramanian, S.1
  • 46
    • 67650097017 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins isolated from dietary bitter melon induce apoptosis and inhibit histone deacetylase-1 selectively in premalignant and malignant prostate cancer cells
    • Xiong, S.D. et al. (2009) Ribosome-inactivating proteins isolated from dietary bitter melon induce apoptosis and inhibit histone deacetylase-1 selectively in premalignant and malignant prostate cancer cells. Int. J. Cancer, 125, 774-782.
    • (2009) Int. J. Cancer , vol.125 , pp. 774-782
    • Xiong, S.D.1


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