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Volumn 229, Issue 5, 2014, Pages 588-598

Amsacrine suppresses matrix metalloproteinase-2 (MMP-2)/MMP-9 expression in human leukemia cells

Author keywords

[No Author keywords available]

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; 4 (4 FLUOROPHENYL) 2 (4 HYDROXYPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; ACETYLCYSTEINE; AMSACRINE; ANTHRA[1,9 CD]PYRAZOL 6(2H) ONE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CYCLOHEXIMIDE; DACTINOMYCIN; GELATINASE A; GELATINASE B; LUCIFERASE; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE P38; OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE 2A; STRESS ACTIVATED PROTEIN KINASE;

EID: 84892634974     PISSN: 00219541     EISSN: 10974652     Source Type: Journal    
DOI: 10.1002/jcp.24481     Document Type: Article
Times cited : (31)

References (44)
  • 2
    • 35748981505 scopus 로고    scopus 로고
    • Mechanisms of cellular resistance to imatinib in human chronic myeloid leukemia cells
    • Baran Y, Ural AU, Gunduz U. 2007. Mechanisms of cellular resistance to imatinib in human chronic myeloid leukemia cells. Hematology 12:497-503.
    • (2007) Hematology , vol.12 , pp. 497-503
    • Baran, Y.1    Ural, A.U.2    Gunduz, U.3
  • 3
    • 0035992304 scopus 로고    scopus 로고
    • Gene expression profiling in chronic myeloid leukemia patients treated with hydroxyurea
    • Bruchova H, Borovanova T, Klamova H, Brdicka R. 2002. Gene expression profiling in chronic myeloid leukemia patients treated with hydroxyurea. Leuk Lymphoma 43:1289-1295.
    • (2002) Leuk Lymphoma , vol.43 , pp. 1289-1295
    • Bruchova, H.1    Borovanova, T.2    Klamova, H.3    Brdicka, R.4
  • 4
    • 79960196862 scopus 로고    scopus 로고
    • Discovery of 4-anilinofuro[2,3-b]quinoline derivatives as selective and orally active compounds against non-small-cell lung cancers
    • Chen YW, Chen YL, Tseng CH, Liang CC, Yang CN, Yao YC, Lu PJ, Tzeng CC. 2011. Discovery of 4-anilinofuro[2, 3-b]quinoline derivatives as selective and orally active compounds against non-small-cell lung cancers. J Med Chem 54:4446-4461.
    • (2011) J Med Chem , vol.54 , pp. 4446-4461
    • Chen, Y.W.1    Chen, Y.L.2    Tseng, C.H.3    Liang, C.C.4    Yang, C.N.5    Yao, Y.C.6    Lu, P.J.7    Tzeng, C.C.8
  • 5
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M, Werb Z. 2002. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2:161-174.
    • (2002) Nat Rev Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 6
    • 79955799029 scopus 로고    scopus 로고
    • Beyond DNA binding-A review of the potential mechanisms mediating quinacrine's therapeutic activities in parasitic infections, inflammation, and cancers
    • Ehsanian R, Van Waes C, Feller SM. 2011. Beyond DNA binding-A review of the potential mechanisms mediating quinacrine's therapeutic activities in parasitic infections, inflammation, and cancers. Cell Commun Signal 15:9-13.
    • (2011) Cell Commun Signal , vol.15 , pp. 9-13
    • Ehsanian, R.1    Van Waes, C.2    Feller, S.M.3
  • 9
    • 13244290068 scopus 로고    scopus 로고
    • CIL-102 interacts with microtubule polymerization and causes mitotic arrest following apoptosis in the human prostate cancer PC-3 cell line
    • Huang YT, Huang DM, Guh JH, Chen IL, Tzeng CC, Teng CM. 2005. CIL-102 interacts with microtubule polymerization and causes mitotic arrest following apoptosis in the human prostate cancer PC-3 cell line. J Biol Chem 280:2771-2779.
    • (2005) J Biol Chem , vol.280 , pp. 2771-2779
    • Huang, Y.T.1    Huang, D.M.2    Guh, J.H.3    Chen, I.L.4    Tzeng, C.C.5    Teng, C.M.6
  • 10
    • 17244377668 scopus 로고    scopus 로고
    • α3β1 integrin regulates MMP-9 mRNA stability in immortalized keratinocytes: A novel mechanism of integrin-mediated MMP gene expression
    • Iyer V, Pumiglia K, DiPersio CM. 2005. α3β1 integrin regulates MMP-9 mRNA stability in immortalized keratinocytes: A novel mechanism of integrin-mediated MMP gene expression. J Cell Sci 118:1185-1195.
    • (2005) J Cell Sci , vol.118 , pp. 1185-1195
    • Iyer, V.1    Pumiglia, K.2    DiPersio, C.M.3
  • 11
    • 84864284116 scopus 로고    scopus 로고
    • Assessment of amsacrine binding with DNA using UV-visible, circular dichroism and Raman spectroscopic techniques
    • Jangir DK, Dey SK, Kundu S, Mehrotra R. 2012. Assessment of amsacrine binding with DNA using UV-visible, circular dichroism and Raman spectroscopic techniques. J Photochem Photobiol B 114:38-43.
    • (2012) J Photochem Photobiol B , vol.114 , pp. 38-43
    • Jangir, D.K.1    Dey, S.K.2    Kundu, S.3    Mehrotra, R.4
  • 12
    • 77953533783 scopus 로고    scopus 로고
    • Inhibition of NF-κB signaling by quinacrine is cytotoxic to human colon carcinoma cell lines and is synergistic in combination with tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) or oxaliplatin
    • Jani TS, DeVecchio J, Mazumdar T, Agyeman A, Houghton JA. 2010. Inhibition of NF-κB signaling by quinacrine is cytotoxic to human colon carcinoma cell lines and is synergistic in combination with tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) or oxaliplatin. J Biol Chem 285:19162-19172.
    • (2010) J Biol Chem , vol.285 , pp. 19162-19172
    • Jani, T.S.1    DeVecchio, J.2    Mazumdar, T.3    Agyeman, A.4    Houghton, J.A.5
  • 13
    • 0033032626 scopus 로고    scopus 로고
    • Specific cutaneous infiltrates in patients with myelogenous leukemia: A clinicopathologic study of 26 patients with assessment of diagnostic criteria
    • Kaddu S, Zenahlik P, Beham-Schmid C, Kerl H, Cerroni L. 1999. Specific cutaneous infiltrates in patients with myelogenous leukemia: A clinicopathologic study of 26 patients with assessment of diagnostic criteria. J Am Acad Dermatol 40:966-978.
    • (1999) J Am Acad Dermatol , vol.40 , pp. 966-978
    • Kaddu, S.1    Zenahlik, P.2    Beham-Schmid, C.3    Kerl, H.4    Cerroni, L.5
  • 14
    • 35648950010 scopus 로고    scopus 로고
    • New concepts in antimalarial use and mode of action in dermatology
    • Kalia S, Dutz JP. 2007. New concepts in antimalarial use and mode of action in dermatology. Dermatol Ther 20:160-174.
    • (2007) Dermatol Ther , vol.20 , pp. 160-174
    • Kalia, S.1    Dutz, J.P.2
  • 15
    • 4444333253 scopus 로고    scopus 로고
    • Genome-wide analysis of gene-expression profiles in chronic myeloid leukemia cells using a cDNA microarray
    • Kaneta Y, Kagami Y, Tsunoda T, Ohno R, Nakamura Y, Katagiri T. 2003. Genome-wide analysis of gene-expression profiles in chronic myeloid leukemia cells using a cDNA microarray. Int J Oncol 23:681-691.
    • (2003) Int J Oncol , vol.23 , pp. 681-691
    • Kaneta, Y.1    Kagami, Y.2    Tsunoda, T.3    Ohno, R.4    Nakamura, Y.5    Katagiri, T.6
  • 16
    • 84857609733 scopus 로고    scopus 로고
    • Amsacrine as a topoisomerase II poison: Importance of drug-DNA interactions
    • Ketron AC, Denny WA, Graves DE, Osheroff N. 2012. Amsacrine as a topoisomerase II poison: Importance of drug-DNA interactions. Biochemistry 51:1730-1739.
    • (2012) Biochemistry , vol.51 , pp. 1730-1739
    • Ketron, A.C.1    Denny, W.A.2    Graves, D.E.3    Osheroff, N.4
  • 18
    • 56549091431 scopus 로고    scopus 로고
    • The complexity of mitogen activated protein kinases (MAPKs) made simple
    • Krishna M, Narang H. 2008. The complexity of mitogen activated protein kinases (MAPKs) made simple. Cell Mol Life Sci 65:3525-3544.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 3525-3544
    • Krishna, M.1    Narang, H.2
  • 19
    • 0031587929 scopus 로고    scopus 로고
    • Novel homologues of CSBP/p38 MAP kinase activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles
    • Kumar S, McDonnell PC, Gum RJ, Hand AT, Lee JC, Young PR. 1997. Novel homologues of CSBP/p38 MAP kinase activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles. Biochem Biophys Res Commun 235:533-538.
    • (1997) Biochem Biophys Res Commun , vol.235 , pp. 533-538
    • Kumar, S.1    McDonnell, P.C.2    Gum, R.J.3    Hand, A.T.4    Lee, J.C.5    Young, P.R.6
  • 20
    • 33646357488 scopus 로고    scopus 로고
    • Src oncogene activates MMP-2 expression via the ERK/Sp1 pathway
    • Kuo L, Chang HC, Leu TH, Maa MC, Hung WC. 2006. Src oncogene activates MMP-2 expression via the ERK/Sp1 pathway. J Cell Physiol 207:729-734.
    • (2006) J Cell Physiol , vol.207 , pp. 729-734
    • Kuo, L.1    Chang, H.C.2    Leu, T.H.3    Maa, M.C.4    Hung, W.C.5
  • 21
    • 0036277708 scopus 로고    scopus 로고
    • Marrow matrix metalloproteinases (MMPs) and tissue inhibitors of MMP in acute leukaemia: Potential role of MMP-9 as a surrogate marker to monitor leukaemic status in patients ith acute myelogenous leukaemia
    • Lin LI, Lin DT, Chang CJ, Lee CY, Tang JL, Tien HF. 2002. Marrow matrix metalloproteinases (MMPs) and tissue inhibitors of MMP in acute leukaemia: Potential role of MMP-9 as a surrogate marker to monitor leukaemic status in patients ith acute myelogenous leukaemia. Br J Haematol 117:835-841.
    • (2002) Br J Haematol , vol.117 , pp. 835-841
    • Lin, L.I.1    Lin, D.T.2    Chang, C.J.3    Lee, C.Y.4    Tang, J.L.5    Tien, H.F.6
  • 22
    • 77954599546 scopus 로고    scopus 로고
    • 2+/ROS-mediated suppression of ERK/c-fos pathway and activation of p38 MAPK/c-Jun pathway
    • 2+/ROS-mediated suppression of ERK/c-fos pathway and activation of p38 MAPK/c-Jun pathway. J Cell Physiol 224:775-785.
    • (2010) J Cell Physiol , vol.224 , pp. 775-785
    • Liu, W.H.1    Chang, L.S.2
  • 23
    • 0345167810 scopus 로고    scopus 로고
    • Mechanism of inhibition of matrix metalloproteinase-2 expression by doxycycline in human aortic smooth muscle cells
    • Liu J, Xiong W, Baca-Regen L, Nagase H, Baxter BT. 2003. Mechanism of inhibition of matrix metalloproteinase-2 expression by doxycycline in human aortic smooth muscle cells. J Vasc Surg 38:1376-1383.
    • (2003) J Vasc Surg , vol.38 , pp. 1376-1383
    • Liu, J.1    Xiong, W.2    Baca-Regen, L.3    Nagase, H.4    Baxter, B.T.5
  • 24
    • 84866778284 scopus 로고    scopus 로고
    • CIL-102 induces matrix metalloproteinase-2 (MMP-2)/MMP-9 down-regulation via simultaneous suppression of genetic transcription and mRNA stability
    • Liu WH, Chen YL, Chang LS. 2012. CIL-102 induces matrix metalloproteinase-2 (MMP-2)/MMP-9 down-regulation via simultaneous suppression of genetic transcription and mRNA stability. Int J Biochem Cell Biol 44:2212-2222.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 2212-2222
    • Liu, W.H.1    Chen, Y.L.2    Chang, L.S.3
  • 25
    • 84875928387 scopus 로고    scopus 로고
    • p38 MAPK/PP2Acα/TTP pathway on the connection of TNF-α and caspases activation on hydroquinone-induced apoptosis
    • Liu WH, Chou WM, Chang LS. 2013a. p38 MAPK/PP2Acα/TTP pathway on the connection of TNF-α and caspases activation on hydroquinone-induced apoptosis. Carcinogenesis 34:818-827.
    • (2013) Carcinogenesis , vol.34 , pp. 818-827
    • Liu, W.H.1    Chou, W.M.2    Chang, L.S.3
  • 26
    • 84879268502 scopus 로고    scopus 로고
    • Cross talk between p38MAPK and ERK is mediated through MAPK-mediated protein phosphatase 2A catalytic subunit a and MAPK phosphatase-1 expression in human leukemia U937 cells
    • Liu WH, Chen YJ, Cheng TL, Lin SR, Chang LS. 2013b. Cross talk between p38MAPK and ERK is mediated through MAPK-mediated protein phosphatase 2A catalytic subunit a and MAPK phosphatase-1 expression in human leukemia U937 cells. Cell Signal 25:1845-1851.
    • (2013) Cell Signal , vol.25 , pp. 1845-1851
    • Liu, W.H.1    Chen, Y.J.2    Cheng, T.L.3    Lin, S.R.4    Chang, L.S.5
  • 27
    • 34548785032 scopus 로고    scopus 로고
    • Topoisomerase IIβ mediated DNA double-strand breaks: implications in doxorubicin cardiotoxicity and prevention by dexrazoxane
    • Lyu YL, Kerrigan JE, Lin CP, Azarova AM, Tsai YC, Ban Y, Liu LF. 2007. Topoisomerase IIβ mediated DNA double-strand breaks: implications in doxorubicin cardiotoxicity and prevention by dexrazoxane. Cancer Res 67:8839-8846.
    • (2007) Cancer Res , vol.67 , pp. 8839-8846
    • Lyu, Y.L.1    Kerrigan, J.E.2    Lin, C.P.3    Azarova, A.M.4    Tsai, Y.C.5    Ban, Y.6    Liu, L.F.7
  • 28
    • 84863192311 scopus 로고    scopus 로고
    • SP-1 regulation of MMP-9 expression requires Ser586 in the PEST domain
    • Murthy S, Ryan AJ, Carter AB. 2012. SP-1 regulation of MMP-9 expression requires Ser586 in the PEST domain. Biochem J 445:229-236.
    • (2012) Biochem J , vol.445 , pp. 229-236
    • Murthy, S.1    Ryan, A.J.2    Carter, A.B.3
  • 29
    • 43549115238 scopus 로고    scopus 로고
    • Cell-surface MMP-9 regulates the invasive capacity of leukemia blast cells with monocytic features
    • Paupert J, Mansat-De Mas V, Demur C, Salles B, Muller C. 2008. Cell-surface MMP-9 regulates the invasive capacity of leukemia blast cells with monocytic features. Cell Cycle 7:1047-1053.
    • (2008) Cell Cycle , vol.7 , pp. 1047-1053
    • Paupert, J.1    Mansat-De Mas, V.2    Demur, C.3    Salles, B.4    Muller, C.5
  • 30
    • 84856328050 scopus 로고    scopus 로고
    • Quinacrine has anticancer activity in breast cancer cells through inhibition of topoisomerase activity
    • Preet R, Mohapatra P, Mohanty S, Sahu SK, Choudhuri T, Wyatt MD, Kundu CN. 2012. Quinacrine has anticancer activity in breast cancer cells through inhibition of topoisomerase activity. Int J Cancer 130:1660-1670.
    • (2012) Int J Cancer , vol.130 , pp. 1660-1670
    • Preet, R.1    Mohapatra, P.2    Mohanty, S.3    Sahu, S.K.4    Choudhuri, T.5    Wyatt, M.D.6    Kundu, C.N.7
  • 31
    • 0037200088 scopus 로고    scopus 로고
    • Activation of p38α MAPK enhances collagenase-1 (matrix metalloproteinase (MMP)-1) and stromelysin-1 (MMP-3) expression by mRNA stabilization
    • Reunanen N, Li SP, Ahonen M, Foschi M, Han J, Kähäri VM. 2002. Activation of p38α MAPK enhances collagenase-1 (matrix metalloproteinase (MMP)-1) and stromelysin-1 (MMP-3) expression by mRNA stabilization. J Biol Chem 277:32360-32368.
    • (2002) J Biol Chem , vol.277 , pp. 32360-32368
    • Reunanen, N.1    Li, S.P.2    Ahonen, M.3    Foschi, M.4    Han, J.5    Kähäri, V.M.6
  • 32
    • 0031800908 scopus 로고    scopus 로고
    • Expression of the active form of MMP-2 on the surface of leukemic cells accounts for their in vitro invasion
    • Sawicki G, Matsuzaki A, Janowska-Wieczorek A. 1998. Expression of the active form of MMP-2 on the surface of leukemic cells accounts for their in vitro invasion, J Cancer Res Clin Oncol 124:245-252.
    • (1998) J Cancer Res Clin Oncol , vol.124 , pp. 245-252
    • Sawicki, G.1    Matsuzaki, A.2    Janowska-Wieczorek, A.3
  • 33
    • 80054993459 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases and reactive oxygen species: How can ROS activate MAPK pathways
    • Son Y, Cheong YK, Kim NH, Chung HT, Kang DG, Pae HO. 2011. Mitogen-activated protein kinases and reactive oxygen species: How can ROS activate MAPK pathways? J Signal Transduct 2011:792639.
    • (2011) J Signal Transduct , vol.2011 , pp. 792639
    • Son, Y.1    Cheong, Y.K.2    Kim, N.H.3    Chung, H.T.4    Kang, D.G.5    Pae, H.O.6
  • 35
    • 33748189347 scopus 로고    scopus 로고
    • Cell-surface association between matrix metalloproteinases and integrins: Role of the complexes in leukocyte migration and cancer progression
    • Stefanidakis M, Koivunen E. 2006. Cell-surface association between matrix metalloproteinases and integrins: Role of the complexes in leukocyte migration and cancer progression. Blood 108:1441-1450.
    • (2006) Blood , vol.108 , pp. 1441-1450
    • Stefanidakis, M.1    Koivunen, E.2
  • 36
    • 0242693161 scopus 로고    scopus 로고
    • Mepacrine inhibits matrix metalloproteinases-1 (MMP-1) and MMP-9 activation in human fibroblast-like synoviocytes
    • Stuhlmeier KM. 2003. Mepacrine inhibits matrix metalloproteinases-1 (MMP-1) and MMP-9 activation in human fibroblast-like synoviocytes. J Rheumatol 30:2330-2337.
    • (2003) J Rheumatol , vol.30 , pp. 2330-2337
    • Stuhlmeier, K.M.1
  • 37
    • 33644665938 scopus 로고    scopus 로고
    • Quinacrine but not chloroquine inhibits PMA induced upregulation of matrix metalloproteinases in leukocytes: Quinacrine acts at the transcriptional level through a PLA2-independent mechanism
    • Stuhlmeier KM, Pollaschek C. 2006. Quinacrine but not chloroquine inhibits PMA induced upregulation of matrix metalloproteinases in leukocytes: Quinacrine acts at the transcriptional level through a PLA2-independent mechanism. J Rheumatol 33:472-480.
    • (2006) J Rheumatol , vol.33 , pp. 472-480
    • Stuhlmeier, K.M.1    Pollaschek, C.2
  • 38
    • 34547678257 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase (MMP) and tissue inhibitor of MMP (TIMP) genes in blasts of infant acute lymphoblastic leukemia with organ involvement
    • Suminoe A, Matsuzaki A, Hattori H, Koga Y, Ishii E, Hara T. 2007. Expression of matrix metalloproteinase (MMP) and tissue inhibitor of MMP (TIMP) genes in blasts of infant acute lymphoblastic leukemia with organ involvement. Leuk Res 31:1437-1440.
    • (2007) Leuk Res , vol.31 , pp. 1437-1440
    • Suminoe, A.1    Matsuzaki, A.2    Hattori, H.3    Koga, Y.4    Ishii, E.5    Hara, T.6
  • 39
    • 34250219975 scopus 로고    scopus 로고
    • Platelet-activating factor overturns the transcriptional repressor disposition of Sp1 in the expression of MMP-9 in human corneal epithelial cells
    • Taheri F, Bazan HE. 2007. Platelet-activating factor overturns the transcriptional repressor disposition of Sp1 in the expression of MMP-9 in human corneal epithelial cells. Invest Ophthalmol Vis Sci 48:1931-1941.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 1931-1941
    • Taheri, F.1    Bazan, H.E.2
  • 40
    • 80455131069 scopus 로고    scopus 로고
    • Acridine and acridinones: Old and new structures with antimalarial activity
    • Valdes AF. 2011. Acridine and acridinones: Old and new structures with antimalarial activity. Open Med Chem J 5:11-20.
    • (2011) Open Med Chem J , vol.5 , pp. 11-20
    • Valdes, A.F.1
  • 43
    • 84860289206 scopus 로고    scopus 로고
    • ADAM17 targets MMP-2 and MMP-9 via EGFR-MEK-ERK pathway activation to promote prostate cancer cell invasion
    • Xiao LJ, Lin P, Lin F, Liu X, Qin W, Zou HF, Guo L, Liu W, Wang SJ, Yu XG. 2012. ADAM17 targets MMP-2 and MMP-9 via EGFR-MEK-ERK pathway activation to promote prostate cancer cell invasion. Int J Oncol 40:1714-1724.
    • (2012) Int J Oncol , vol.40 , pp. 1714-1724
    • Xiao, L.J.1    Lin, P.2    Lin, F.3    Liu, X.4    Qin, W.5    Zou, H.F.6    Guo, L.7    Liu, W.8    Wang, S.J.9    Yu, X.G.10
  • 44
    • 0026546254 scopus 로고
    • Relative activity of structural analogues of amsacrine against human leukemia cell lines containing amsacrine-sensitive or -resistant forms of topoisomerase II: Use of computer simulations in new drug development
    • Zwelling LA, Mitchell MJ, Satitpunwaycha P, Mayes J, Altschuler E, Hinds M, Baguley BC. 1992. Relative activity of structural analogues of amsacrine against human leukemia cell lines containing amsacrine-sensitive or -resistant forms of topoisomerase II: Use of computer simulations in new drug development. Cancer Res 52:209-217.
    • (1992) Cancer Res , vol.52 , pp. 209-217
    • Zwelling, L.A.1    Mitchell, M.J.2    Satitpunwaycha, P.3    Mayes, J.4    Altschuler, E.5    Hinds, M.6    Baguley, B.C.7


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