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

This study explores the suppression mechanism of amsacrine (4‐(9‐Acridinylamino)‐N‐(methanesulfonyl)‐m‐anisidine hydrochloride) on matrix metalloproteinase‐2 (MMP‐2) and MMP‐9 expression in human leukemia cells. Amsacrine attenuated cell invasion with decreased MMP‐2/MMP‐9 protein expression and mRN...

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Published inJournal of cellular physiology Vol. 229; no. 5; pp. 588 - 598
Main Authors Liu, Wen-Hsin, Chen, Ying-Jung, Chien, Jen-Hung, Chang, Long-Sen
Format Journal Article
LanguageEnglish
Published United States Blackwell Publishing Ltd 01.05.2014
Wiley Subscription Services, Inc
Subjects
Amsacrine - chemistry
Amsacrine - pharmacology
Decay
Down-Regulation
Enzyme Inhibitors - pharmacology
Gene Expression Regulation, Neoplastic
Humans
Inactivation
Leukemia
Leukemia - enzymology
MAP Kinase Kinase 4 - genetics
MAP Kinase Kinase 4 - metabolism
Matrix Metalloproteinase 2 - genetics
Matrix Metalloproteinase 2 - metabolism
Matrix Metalloproteinase 9 - genetics
Matrix Metalloproteinase 9 - metabolism
Molecular Structure
p38 Mitogen-Activated Protein Kinases - genetics
p38 Mitogen-Activated Protein Kinases - metabolism
Protein Phosphatase 2 - classification
Protein Phosphatase 2 - genetics
Protein Phosphatase 2 - metabolism
RNA, Messenger - genetics
RNA, Messenger - metabolism
U937 Cells
Up-Regulation
Online AccessGet full text

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Abstract This study explores the suppression mechanism of amsacrine (4‐(9‐Acridinylamino)‐N‐(methanesulfonyl)‐m‐anisidine hydrochloride) on matrix metalloproteinase‐2 (MMP‐2) and MMP‐9 expression in human leukemia cells. Amsacrine attenuated cell invasion with decreased MMP‐2/MMP‐9 protein expression and mRNA levels in U937, Jurkat, HL‐60, K562, KU812, and MEG‐01 cells. Moreover, amsacrine reduced both MMP‐2/MMP‐9 promoter luciferase activity and MMP‐2/MMP‐9 mRNA stability in leukemia cells. Studies on amsacrine‐treated U937 cells revealed that amsacrine‐elicited ROS generation induced JNK and p38 MAPK activation but reduced the phospho‐ERK level. Amsacrine‐induced ERK inactivation and p38 MAPK/JNK activation were demonstrated to suppress MMP‐2/MMP‐9 promoter luciferase activity and promote MMP‐2/MMP‐9 mRNA decay, respectively. p38 MAPK/JNK activation led to up‐regulation of protein phosphatase 2A catalytic subunit α (PP2Acα) in amsacrine‐treated U937 cells. Okadaic acid (PP2A inhibitor) treatment increased MMP‐2/MMP‐9 mRNA stability in amsacrine‐treated cells, whereas PP2Acα over‐expression increased MMP‐2/MMP‐9 mRNA decay. Amsacrine‐induced MMP‐2/MMP‐9 down‐regulation was also related to PP2Acα up‐regulation on Jurkat, HL‐60, K562, KU812, and MEG‐01 cells. Collectively, our data indicate that amsacrine induces MMP‐2/MMP‐9 down‐regulation via simultaneous suppression of genetic transcription and mRNA stability in human leukemia cells. J. Cell. Physiol. 229: 588–598, 2014. © 2013 Wiley Periodicals, Inc.
AbstractList This study explores the suppression mechanism of amsacrine (4-(9-Acridinylamino)-N-(methanesulfonyl)-m-anisidine hydrochloride) on matrix metalloproteinase-2 (MMP-2) and MMP-9 expression in human leukemia cells. Amsacrine attenuated cell invasion with decreased MMP-2/MMP-9 protein expression and mRNA levels in U937, Jurkat, HL-60, K562, KU812, and MEG-01 cells. Moreover, amsacrine reduced both MMP-2/MMP-9 promoter luciferase activity and MMP-2/MMP-9 mRNA stability in leukemia cells. Studies on amsacrine-treated U937 cells revealed that amsacrine-elicited ROS generation induced JNK and p38 MAPK activation but reduced the phospho-ERK level. Amsacrine-induced ERK inactivation and p38 MAPK/JNK activation were demonstrated to suppress MMP-2/MMP-9 promoter luciferase activity and promote MMP-2/MMP-9 mRNA decay, respectively. p38 MAPK/JNK activation led to up-regulation of protein phosphatase 2A catalytic subunit α (PP2Acα) in amsacrine-treated U937 cells. Okadaic acid (PP2A inhibitor) treatment increased MMP-2/MMP-9 mRNA stability in amsacrine-treated cells, whereas PP2Acα over-expression increased MMP-2/MMP-9 mRNA decay. Amsacrine-induced MMP-2/MMP-9 down-regulation was also related to PP2Acα up-regulation on Jurkat, HL-60, K562, KU812, and MEG-01 cells. Collectively, our data indicate that amsacrine induces MMP-2/MMP-9 down-regulation via simultaneous suppression of genetic transcription and mRNA stability in human leukemia cells.
This study explores the suppression mechanism of amsacrine (4‐(9‐Acridinylamino)‐N‐(methanesulfonyl)‐m‐anisidine hydrochloride) on matrix metalloproteinase‐2 (MMP‐2) and MMP‐9 expression in human leukemia cells. Amsacrine attenuated cell invasion with decreased MMP‐2/MMP‐9 protein expression and mRNA levels in U937, Jurkat, HL‐60, K562, KU812, and MEG‐01 cells. Moreover, amsacrine reduced both MMP‐2/MMP‐9 promoter luciferase activity and MMP‐2/MMP‐9 mRNA stability in leukemia cells. Studies on amsacrine‐treated U937 cells revealed that amsacrine‐elicited ROS generation induced JNK and p38 MAPK activation but reduced the phospho‐ERK level. Amsacrine‐induced ERK inactivation and p38 MAPK/JNK activation were demonstrated to suppress MMP‐2/MMP‐9 promoter luciferase activity and promote MMP‐2/MMP‐9 mRNA decay, respectively. p38 MAPK/JNK activation led to up‐regulation of protein phosphatase 2A catalytic subunit α (PP2Acα) in amsacrine‐treated U937 cells. Okadaic acid (PP2A inhibitor) treatment increased MMP‐2/MMP‐9 mRNA stability in amsacrine‐treated cells, whereas PP2Acα over‐expression increased MMP‐2/MMP‐9 mRNA decay. Amsacrine‐induced MMP‐2/MMP‐9 down‐regulation was also related to PP2Acα up‐regulation on Jurkat, HL‐60, K562, KU812, and MEG‐01 cells. Collectively, our data indicate that amsacrine induces MMP‐2/MMP‐9 down‐regulation via simultaneous suppression of genetic transcription and mRNA stability in human leukemia cells. J. Cell. Physiol. 229: 588–598, 2014. © 2013 Wiley Periodicals, Inc.
This study explores the suppression mechanism of amsacrine (4-(9-Acridinylamino)-N-(methanesulfonyl)-m-anisidine hydrochloride) on matrix metalloproteinase-2 (MMP-2) and MMP-9 expression in human leukemia cells. Amsacrine attenuated cell invasion with decreased MMP-2/MMP-9 protein expression and mRNA levels in U937, Jurkat, HL-60, K562, KU812, and MEG-01 cells. Moreover, amsacrine reduced both MMP-2/MMP-9 promoter luciferase activity and MMP-2/MMP-9 mRNA stability in leukemia cells. Studies on amsacrine-treated U937 cells revealed that amsacrine-elicited ROS generation induced JNK and p38 MAPK activation but reduced the phospho-ERK level. Amsacrine-induced ERK inactivation and p38 MAPK/JNK activation were demonstrated to suppress MMP-2/MMP-9 promoter luciferase activity and promote MMP-2/MMP-9 mRNA decay, respectively. p38 MAPK/JNK activation led to up-regulation of protein phosphatase 2A catalytic subunit α (PP2Acα) in amsacrine-treated U937 cells. Okadaic acid (PP2A inhibitor) treatment increased MMP-2/MMP-9 mRNA stability in amsacrine-treated cells, whereas PP2Acα over-expression increased MMP-2/MMP-9 mRNA decay. Amsacrine-induced MMP-2/MMP-9 down-regulation was also related to PP2Acα up-regulation on Jurkat, HL-60, K562, KU812, and MEG-01 cells. Collectively, our data indicate that amsacrine induces MMP-2/MMP-9 down-regulation via simultaneous suppression of genetic transcription and mRNA stability in human leukemia cells.This study explores the suppression mechanism of amsacrine (4-(9-Acridinylamino)-N-(methanesulfonyl)-m-anisidine hydrochloride) on matrix metalloproteinase-2 (MMP-2) and MMP-9 expression in human leukemia cells. Amsacrine attenuated cell invasion with decreased MMP-2/MMP-9 protein expression and mRNA levels in U937, Jurkat, HL-60, K562, KU812, and MEG-01 cells. Moreover, amsacrine reduced both MMP-2/MMP-9 promoter luciferase activity and MMP-2/MMP-9 mRNA stability in leukemia cells. Studies on amsacrine-treated U937 cells revealed that amsacrine-elicited ROS generation induced JNK and p38 MAPK activation but reduced the phospho-ERK level. Amsacrine-induced ERK inactivation and p38 MAPK/JNK activation were demonstrated to suppress MMP-2/MMP-9 promoter luciferase activity and promote MMP-2/MMP-9 mRNA decay, respectively. p38 MAPK/JNK activation led to up-regulation of protein phosphatase 2A catalytic subunit α (PP2Acα) in amsacrine-treated U937 cells. Okadaic acid (PP2A inhibitor) treatment increased MMP-2/MMP-9 mRNA stability in amsacrine-treated cells, whereas PP2Acα over-expression increased MMP-2/MMP-9 mRNA decay. Amsacrine-induced MMP-2/MMP-9 down-regulation was also related to PP2Acα up-regulation on Jurkat, HL-60, K562, KU812, and MEG-01 cells. Collectively, our data indicate that amsacrine induces MMP-2/MMP-9 down-regulation via simultaneous suppression of genetic transcription and mRNA stability in human leukemia cells.
This study explores the suppression mechanism of amsacrine (4-(9-Acridinylamino)-N-(methanesulfonyl)-m-anisidine hydrochloride) on matrix metalloproteinase-2 (MMP-2) and MMP-9 expression in human leukemia cells. Amsacrine attenuated cell invasion with decreased MMP-2/MMP-9 protein expression and mRNA levels in U937, Jurkat, HL-60, K562, KU812, and MEG-01 cells. Moreover, amsacrine reduced both MMP-2/MMP-9 promoter luciferase activity and MMP-2/MMP-9 mRNA stability in leukemia cells. Studies on amsacrine-treated U937 cells revealed that amsacrine-elicited ROS generation induced JNK and p38 MAPK activation but reduced the phospho-ERK level. Amsacrine-induced ERK inactivation and p38 MAPK/JNK activation were demonstrated to suppress MMP-2/MMP-9 promoter luciferase activity and promote MMP-2/MMP-9 mRNA decay, respectively. p38 MAPK/JNK activation led to up-regulation of protein phosphatase 2A catalytic subunit [alpha] (PP2Ac[alpha]) in amsacrine-treated U937 cells. Okadaic acid (PP2A inhibitor) treatment increased MMP-2/MMP-9 mRNA stability in amsacrine-treated cells, whereas PP2Ac[alpha] over-expression increased MMP-2/MMP-9 mRNA decay. Amsacrine-induced MMP-2/MMP-9 down-regulation was also related to PP2Ac[alpha] up-regulation on Jurkat, HL-60, K562, KU812, and MEG-01 cells. Collectively, our data indicate that amsacrine induces MMP-2/MMP-9 down-regulation via simultaneous suppression of genetic transcription and mRNA stability in human leukemia cells. J. Cell. Physiol. 229: 588-598, 2014. © 2013 Wiley Periodicals, Inc. [PUBLICATION ABSTRACT]
Author Chen, Ying-Jung
Chang, Long-Sen
Liu, Wen-Hsin
Chien, Jen-Hung
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  email: Correspondence to: Long-Sen Chang, Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung 804, Taiwan., lschang@mail.nsysu.edu.tw
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Gurova KV, Hill JE, Guo C, Prokvolit A, Burdelya LG, Samoylova E, Khodyakova AV, Ganapathi R, Ganapathi M, Tararova ND, Bosykh D, Lvovskiy D, Webb TR, Stark GR, Gudkov AV. 2005. Small molecules that reactivate p53 in renal cell carcinoma reveal a NF-κB-dependent mechanism of p53 suppression in tumors. Proc Natl Acad Sci USA 102:17448-17453.
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.
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.
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.
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.
Ketron AC, Denny WA, Graves DE, Osheroff N. 2012. Amsacrine as a topoisomerase II poison: Importance of drug-DNA interactions. Biochemistry 51:1730-1739.
Kalia S, Dutz JP. 2007. New concepts in antimalarial use and mode of action in dermatology. Dermatol Ther 20:160-174.
Baran Y, Ural AU, Gunduz U. 2007. Mechanisms of cellular resistance to imatinib in human chronic myeloid leukemia cells. Hematology 12:497-503.
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.
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.
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.
Stuhlmeier KM. 2003. Mepacrine inhibits matrix metalloproteinases-1 (MMP-1) and MMP-9 activation in human fibroblast-like synoviocytes. J Rheumatol 30:2330-2337.
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.
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.
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.
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.
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.
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.
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.
Krishna M, Narang H. 2008. The complexity of mitogen activated protein kinases (MAPKs) made simple. Cell Mol Life Sci 65:3525-3544.
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.
Wang W, Ho WC, Dicker DT, MacKinnon C, Winkler JD, Marmorstein R, El-Deiry WS. 2005. Acridine derivatives activate p53 and induce tumor cell death through Bax. Cancer Biol Ther 4:893-898.
Akool el-S, Kleinert H, Hamada FM, Abdelwahab MH, Förstermann U, Pfeilschifter J, Eberhardt W. 2003. Nitric oxide increases the decay of matrix metalloproteinase 9 mRNA by inhibiting the expression of mRNA-stabilizing factor HuR. Mol Cell Biol 23:4901-4916.
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.
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.
Guo C, Gasparian AV, Zhuang Z, Bosykh DA, Komar AA, Gudkov AV, Gurova KV. 2009. 9-Aminoacridine-based anticancer drugs target the PI3K/AKT/mTOR, NF-κB and p53 pathways. Oncogene 28:1151-1161.
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.
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.
Van den Steen PE, Dubois B, Nelissen I, Rudd PM, Dwek RA, Opdenakker G. 2002. Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9). Crit Rev Biochem Mol Biol 37:375-536.
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.
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.
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.
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.
Liu WH, Chang LS. 2010. Caffeine induces matrix metalloproteinase-2 (MMP-2) and MMP-9 down-regulation in human leukemia U937 cells via Ca2+/ROS-mediated suppression of ERK/c-fos pathway and activation of p38 MAPK/c-Jun pathway. J Cell Physiol 224:775-785.
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.
Spallarossa P, Altieri P, Garibaldi S, Ghigliotti G, Barisione C, Manca V, Fabbi P, Ballestrero A, Brunelli C, Barsotti A. 2006. Matrix metalloproteinase-2 and -9 are induced differently by doxorubicin in H9c2 cells: The role of MAP kinases and NAD(P)H oxidase. Cardiovasc Res 69:736-745.
1997; 235
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  year: 2005
  end-page: 898
  article-title: Acridine derivatives activate p53 and induce tumor cell death through Bax
  publication-title: Cancer Biol Ther
– volume: 117
  start-page: 835
  year: 2002
  end-page: 841
  article-title: 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
  publication-title: Br J Haematol
– volume: 2
  start-page: 161
  year: 2002
  end-page: 174
  article-title: New functions for the matrix metalloproteinases in cancer progression
  publication-title: Nat Rev Cancer
– volume: 2011
  start-page: 792639
  year: 2011
  article-title: Mitogen‐activated protein kinases and reactive oxygen species: How can ROS activate MAPK pathways
  publication-title: J Signal Transduct
– volume: 54
  start-page: 4446
  year: 2011
  end-page: 4461
  article-title: Discovery of 4‐anilinofuro[2,3‐b]quinoline derivatives as selective and orally active compounds against non‐small‐cell lung cancers
  publication-title: J Med Chem
– volume: 33
  start-page: 472
  year: 2006
  end-page: 480
  article-title: Quinacrine but not chloroquine inhibits PMA induced upregulation of matrix metalloproteinases in leukocytes: Quinacrine acts at the transcriptional level through a PLA2‐independent mechanism
  publication-title: J Rheumatol
– volume: 15
  start-page: 9
  year: 2011
  end-page: 13
  article-title: Beyond DNA binding—A review of the potential mechanisms mediating quinacrine's therapeutic activities in parasitic infections, inflammation, and cancers
  publication-title: Cell Commun Signal
– volume: 48
  start-page: 1931
  year: 2007
  end-page: 1941
  article-title: Platelet‐activating factor overturns the transcriptional repressor disposition of Sp1 in the expression of MMP‐9 in human corneal epithelial cells
  publication-title: Invest Ophthalmol Vis Sci
– volume: 31
  start-page: 1437
  year: 2007
  end-page: 1440
  article-title: Expression of matrix metalloproteinase (MMP) and tissue inhibitor of MMP (TIMP) genes in blasts of infant acute lymphoblastic leukemia with organ involvement
  publication-title: Leuk Res
– volume: 50
  start-page: 87
  year: 2004
  end-page: 100
  article-title: The possible role of matrix metalloproteinase (MMP)‐2 and MMP‐9 in cancer, e.g. acute leukemia
  publication-title: Critical Rev Oncol Hematol
– volume: 23
  start-page: 4901
  year: 2003
  end-page: 4916
  article-title: Nitric oxide increases the decay of matrix metalloproteinase 9 mRNA by inhibiting the expression of mRNA‐stabilizing factor HuR
  publication-title: Mol Cell Biol
– volume: 285
  start-page: 19162
  year: 2010
  end-page: 19172
  article-title: 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
  publication-title: J Biol Chem
– volume: 20
  start-page: 160
  year: 2007
  end-page: 174
  article-title: New concepts in antimalarial use and mode of action in dermatology
  publication-title: Dermatol Ther
– volume: 207
  start-page: 729
  year: 2006
  end-page: 734
  article-title: Src oncogene activates MMP‐2 expression via the ERK/Sp1 pathway
  publication-title: J Cell Physiol
– volume: 44
  start-page: 2212
  year: 2012
  end-page: 2222
  article-title: CIL‐102 induces matrix metalloproteinase‐2 (MMP‐2)/MMP‐9 down‐regulation via simultaneous suppression of genetic transcription and mRNA stability
  publication-title: Int J Biochem Cell Biol
– volume: 38
  start-page: 1376
  year: 2003
  end-page: 1383
  article-title: Mechanism of inhibition of matrix metalloproteinase‐2 expression by doxycycline in human aortic smooth muscle cells
  publication-title: J Vasc Surg
– volume: 108
  start-page: 1441
  year: 2006
  end-page: 1450
  article-title: Cell‐surface association between matrix metalloproteinases and integrins: Role of the complexes in leukocyte migration and cancer progression
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  year: 2007
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  year: 2003
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  year: 2013a
  end-page: 827
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  publication-title: Carcinogenesis
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  year: 2012
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  article-title: SP‐1 regulation of MMP‐9 expression requires Ser586 in the PEST domain
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– volume: 37
  start-page: 375
  year: 2002
  end-page: 536
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  publication-title: Crit Rev Biochem Mol Biol
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  start-page: 2771
  year: 2005
  end-page: 2779
  article-title: CIL‐102 interacts with microtubule polymerization and causes mitotic arrest following apoptosis in the human prostate cancer PC‐3 cell line
  publication-title: J Biol Chem
– volume: 114
  start-page: 38
  year: 2012
  end-page: 43
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Snippet This study explores the suppression mechanism of amsacrine (4‐(9‐Acridinylamino)‐N‐(methanesulfonyl)‐m‐anisidine hydrochloride) on matrix metalloproteinase‐2...
This study explores the suppression mechanism of amsacrine (4-(9-Acridinylamino)-N-(methanesulfonyl)-m-anisidine hydrochloride) on matrix metalloproteinase-2...
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SubjectTerms Amsacrine - chemistry
Amsacrine - pharmacology
Decay
Down-Regulation
Enzyme Inhibitors - pharmacology
Gene Expression Regulation, Neoplastic
Humans
Inactivation
Leukemia
Leukemia - enzymology
MAP Kinase Kinase 4 - genetics
MAP Kinase Kinase 4 - metabolism
Matrix Metalloproteinase 2 - genetics
Matrix Metalloproteinase 2 - metabolism
Matrix Metalloproteinase 9 - genetics
Matrix Metalloproteinase 9 - metabolism
Molecular Structure
p38 Mitogen-Activated Protein Kinases - genetics
p38 Mitogen-Activated Protein Kinases - metabolism
Protein Phosphatase 2 - classification
Protein Phosphatase 2 - genetics
Protein Phosphatase 2 - metabolism
RNA, Messenger - genetics
RNA, Messenger - metabolism
U937 Cells
Up-Regulation
Title Amsacrine suppresses matrix metalloproteinase-2 (MMP-2)/MMP-9 expression in human leukemia cells
URI https://api.istex.fr/ark:/67375/WNG-B04VRDJQ-P/fulltext.pdf
https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fjcp.24481
https://www.ncbi.nlm.nih.gov/pubmed/24122234
https://www.proquest.com/docview/1490648386
https://www.proquest.com/docview/1491064291
Volume 229
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