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Volumn 22, Issue 4, 2005, Pages 331-339

Inhibitors of polyamine biosynthesis decrease the expression of the metalloproteases meprin α and MMP-7 in hormone-independent human breast cancer cells

Author keywords

Breast cancer invasion; DFMO; Metalloproteases; Polyamines; SAM486A

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; ACTINONIN; ADENOSYLMETHIONINE DECARBOXYLASE; DECARBOXYLASE INHIBITOR; EFLORNITHINE; GELATINASE A; HORMONE; INTERSTITIAL COLLAGENASE; MATRILYSIN; MATRIX METALLOPROTEINASE 14; MEPRIN; MESSENGER RNA; METALLOPROTEINASE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; POLYAMINE; PUTRESCINE; SAM 486 A; STROMELYSIN; UNCLASSIFIED DRUG;

EID: 25444454560     PISSN: 02620898     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10585-005-0660-5     Document Type: Article
Times cited : (42)

References (31)
  • 1
  • 2
    • 0032766004 scopus 로고    scopus 로고
    • Prognostic value of ornithine decarboxylase and polyamines in human breast cancer: Correlation with clinicopathologic parameters
    • F Canizares J Salinas M de las Heras 1999 Prognostic value of ornithine decarboxylase and polyamines in human breast cancer: Correlation with clinicopathologic parameters Clin Cancer Res 5 2035 41
    • (1999) Clin Cancer Res , vol.5 , pp. 2035-41
    • Canizares, F.1    Salinas, J.2    De Las Heras, M.3
  • 3
    • 0029832374 scopus 로고    scopus 로고
    • Prognostic influence on survival of increased ornithine decarboxylase activity in human breast cancer
    • A Manni D Mauger P Gimotty 1996 Prognostic influence on survival of increased ornithine decarboxylase activity in human breast cancer Clin Cancer Res 2 1901 6
    • (1996) Clin Cancer Res , vol.2 , pp. 1901-6
    • Manni, A.1    Mauger, D.2    Gimotty, P.3
  • 4
    • 0036211154 scopus 로고    scopus 로고
    • Influence of polyamines on in vitro and in vivo features of aggressive and metastatic behavior by human breast cancer cells
    • A Manni S Washington JW Griffith 2002 Influence of polyamines on in vitro and in vivo features of aggressive and metastatic behavior by human breast cancer cells Clin Exp Metast 19 95 105
    • (2002) Clin Exp Metast , vol.19 , pp. 95-105
    • Manni, A.1    Washington, S.2    Griffith, J.W.3
  • 5
    • 0038199842 scopus 로고    scopus 로고
    • Effects of α-difluoromethylornithine on local recurrence and pulmonary metastasis from MDA-MB-435 breast cancer xenografts in nude mice
    • A Manni S Washington L Craig 2003 Effects of α- difluoromethylornithine on local recurrence and pulmonary metastasis from MDA-MB-435 breast cancer xenografts in nude mice Clin Exp Metast 20 321 5
    • (2003) Clin Exp Metast , vol.20 , pp. 321-5
    • Manni, A.1    Washington, S.2    Craig, L.3
  • 6
    • 16644386863 scopus 로고    scopus 로고
    • Biological activity of the S-adenosylmethionine decarboxylase inhibitor SAM486A in human breast cancer cell in vitro and in vivo
    • X Hu S Washington MF Verderame 2004 Biological activity of the S-adenosylmethionine decarboxylase inhibitor SAM486A in human breast cancer cell in vitro and in vivo Int J Oncology 25 1831 8
    • (2004) Int J Oncology , vol.25 , pp. 1831-8
    • Hu, X.1    Washington, S.2    Verderame, M.F.3
  • 7
    • 12444340846 scopus 로고    scopus 로고
    • Cellular mechanisms mediating the anti-invasive properties of the ornithine decarboxylase inhibitor α-difluoromethylornithine (DFMO) in breast cancer cells
    • A Manni S Washington D Mauger 2004 Cellular mechanisms mediating the anti-invasive properties of the ornithine decarboxylase inhibitor α-difluoromethylornithine (DFMO) in breast cancer cells Clin Exp Metast 21 461 7
    • (2004) Clin Exp Metast , vol.21 , pp. 461-7
    • Manni, A.1    Washington, S.2    Mauger, D.3
  • 8
    • 0025171017 scopus 로고
    • Specific inhibition of endothelial cell proliferation by thrombospondin
    • P Bagavandoss JW Wilks 1990 Specific inhibition of endothelial cell proliferation by thrombospondin Biochem Biophys Res Commun 170 867 72
    • (1990) Biochem Biophys Res Commun , vol.170 , pp. 867-72
    • Bagavandoss, P.1    Wilks, J.W.2
  • 9
    • 0025853349 scopus 로고
    • Thrombospondin exerts an antiangiogenic effect on cord formation by endothelial cells in vitro
    • ML Iruela-Arispe P Bornstein H Sage 1991 Thrombospondin exerts an antiangiogenic effect on cord formation by endothelial cells in vitro Proc Natl Acad Sci USA 88 5026 30
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5026-30
    • Iruela-Arispe, M.L.1    Bornstein, P.2    Sage, H.3
  • 10
    • 0035918152 scopus 로고    scopus 로고
    • Marked differences between metalloproteases meprin a and B in substrate and peptide bond specificity
    • G Bertenshaw B Turk S Hubbard 2001 Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity J Biol Chem 276 13248 55
    • (2001) J Biol Chem , vol.276 , pp. 13248-55
    • Bertenshaw, G.1    Turk, B.2    Hubbard, S.3
  • 11
    • 0037622285 scopus 로고    scopus 로고
    • Heterologously overexpressed, affinity-purified human meprin α is functionally active and cleaves components of the basement membrane in vitro
    • D Kohler M Kruse W Stocker 2000 Heterologously overexpressed, affinity-purified human meprin α is functionally active and cleaves components of the basement membrane in vitro FEBS Lett 465 2 7
    • (2000) FEBS Lett , vol.465 , pp. 2-7
    • Kohler, D.1    Kruse, M.2    Stocker, W.3
  • 12
    • 1642362446 scopus 로고    scopus 로고
    • Human meprin α and β homo-oligomers: Cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors
    • MN Kruse C Becker D Lottaz 2004 Human meprin α and β homo-oligomers: Cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors Biochem J 378 383 9
    • (2004) Biochem J , vol.378 , pp. 383-9
    • Kruse, M.N.1    Becker, C.2    Lottaz, D.3
  • 13
    • 0033104363 scopus 로고    scopus 로고
    • Nonpolarized secretion of human meprin α in colorectal cancer generates an increased proteolytic potential in the stroma
    • D Lottaz CA Maurer D Hahn 1999 Nonpolarized secretion of human meprin α in colorectal cancer generates an increased proteolytic potential in the stroma Cancer Res 59 1127 33
    • (1999) Cancer Res , vol.59 , pp. 1127-33
    • Lottaz, D.1    Maurer, C.A.2    Hahn, D.3
  • 14
    • 0037174846 scopus 로고    scopus 로고
    • Activation of human meprin-α in a cell culture model of colorectal cancer is triggered by the plasminogen activating system
    • S Rosmann D Hahn D Lottaz 2002 Activation of human meprin-α in a cell culture model of colorectal cancer is triggered by the plasminogen activating system J Biol Chem 277 40650 8
    • (2002) J Biol Chem , vol.277 , pp. 40650-8
    • Rosmann, S.1    Hahn, D.2    Lottaz, D.3
  • 15
    • 0037532953 scopus 로고    scopus 로고
    • Differences in the activation mechanism between the α and β subunits of human meprin
    • C Becker MN Kruse KA Slotty 2003 Differences in the activation mechanism between the α and β subunits of human meprin Biol Chem 384 825 31
    • (2003) Biol Chem , vol.384 , pp. 825-31
    • Becker, C.1    Kruse, M.N.2    Slotty, K.A.3
  • 16
    • 0033026426 scopus 로고    scopus 로고
    • Expression and regulation of the meprin β gene in human cancer cells
    • GL Matters JS Bond 1999 Expression and regulation of the meprin β gene in human cancer cells Mol Carcinogen 25 169 78
    • (1999) Mol Carcinogen , vol.25 , pp. 169-78
    • Matters, G.L.1    Bond, J.S.2
  • 17
    • 0037462760 scopus 로고    scopus 로고
    • Structure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular weight multimers
    • GP Bertenshaw MT Norcum JS Bond 2003 Structure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular weight multimers J Biol Chem 278 2522 32
    • (2003) J Biol Chem , vol.278 , pp. 2522-32
    • Bertenshaw, G.P.1    Norcum, M.T.2    Bond, J.S.3
  • 18
    • 0001082248 scopus 로고    scopus 로고
    • Secretion of human meprin from intestinal epithelial cells depends on differential expression of the α and β subunits
    • D Lottaz D Hahn S Muller 1999 Secretion of human meprin from intestinal epithelial cells depends on differential expression of the α and β subunits Eur J Biochem 259 496 504
    • (1999) Eur J Biochem , vol.259 , pp. 496-504
    • Lottaz, D.1    Hahn, D.2    Muller, S.3
  • 19
    • 0034012213 scopus 로고    scopus 로고
    • Heating greatly speeds Coomassie blue staining and destaining
    • C Wong S Sridhara JCA Bardwell 2000 Heating greatly speeds Coomassie blue staining and destaining BioTechniques 28 426 32
    • (2000) BioTechniques , vol.28 , pp. 426-32
    • Wong, C.1    Sridhara, S.2    Bardwell, J.C.A.3
  • 20
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • M Eglebad Z Werb 2002 New functions for the matrix metalloproteinases in cancer progression Nat Rev Cancer 2 163 76
    • (2002) Nat Rev Cancer , vol.2 , pp. 163-76
    • Eglebad, M.1    Werb, Z.2
  • 21
    • 0034176764 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Multifunctional contributors to tumor progression
    • LJ McCawley L Matrisian 2000 Matrix metalloproteinases: Multifunctional contributors to tumor progression Mol Med Today 6 149 56
    • (2000) Mol Med Today , vol.6 , pp. 149-56
    • McCawley, L.J.1    Matrisian, L.2
  • 22
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • LM Coussens B Fingleton LM Matrisian 2002 Matrix metalloproteinase inhibitors and cancer: Trials and tribulations Science (Wash DC) 295 2387 92
    • (2002) Science (Wash DC) , vol.295 , pp. 2387-92
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 23
    • 0038488950 scopus 로고    scopus 로고
    • A multigenic program mediating breast cancer metastasis to bone
    • Y Kang PM Siegel W Shu 2003 A multigenic program mediating breast cancer metastasis to bone Cancer Cell 3 537 49
    • (2003) Cancer Cell , vol.3 , pp. 537-49
    • Kang, Y.1    Siegel, P.M.2    Shu, W.3
  • 24
    • 0027997695 scopus 로고
    • Polyamine-dependent expression of the matrix metalloprotease matrilysin in a human colon cancer-derived cell line
    • UN Wallon LR Shassetz AE Cress 1994 Polyamine-dependent expression of the matrix metalloprotease matrilysin in a human colon cancer-derived cell line Mol Carcinog 11 138 44
    • (1994) Mol Carcinog , vol.11 , pp. 138-44
    • Wallon, U.N.1    Shassetz, L.R.2    Cress, A.E.3
  • 25
    • 0034673093 scopus 로고    scopus 로고
    • Actinonin, a naturally occurring antibacterial agent, is a potent deformylase inhibitor
    • DZ Chen DV Patel CJ Hackbarth 2000 Actinonin, a naturally occurring antibacterial agent, is a potent deformylase inhibitor Biochemistry 39 1256 62
    • (2000) Biochemistry , vol.39 , pp. 1256-62
    • Chen, D.Z.1    Patel, D.V.2    Hackbarth, C.J.3
  • 26
    • 0030048006 scopus 로고    scopus 로고
    • Inhibition of tumor cell invasion and matrix degradation by aminopeptidase inhibitors
    • H Fujii M Nakajima T Aoyagi 1996 Inhibition of tumor cell invasion and matrix degradation by aminopeptidase inhibitors Biol Pharm Bull 19 6 10
    • (1996) Biol Pharm Bull , vol.19 , pp. 6-10
    • Fujii, H.1    Nakajima, M.2    Aoyagi, T.3
  • 27
    • 0031930519 scopus 로고    scopus 로고
    • Antitumor activity of actinonin in vitro and in vivo
    • Y Xu LT Lai JL Gabrilove 1998 Antitumor activity of actinonin in vitro and in vivo Clin Cancer Res 4 171 6
    • (1998) Clin Cancer Res , vol.4 , pp. 171-6
    • Xu, Y.1    Lai, L.T.2    Gabrilove, J.L.3
  • 28
    • 9644268250 scopus 로고    scopus 로고
    • Human mitochondrial peptide deformylase, an new anti-cancer target of actinonin-based antibiotics
    • MD Lee Y She MJ Soskis 2004 Human mitochondrial peptide deformylase, an new anti-cancer target of actinonin-based antibiotics J Clin Invest 114 1107 16
    • (2004) J Clin Invest , vol.114 , pp. 1107-16
    • Lee, M.D.1    She, Y.2    Soskis, M.J.3
  • 29
    • 0036794934 scopus 로고    scopus 로고
    • A phase II breast cancer chemoprevention trial of oral α-difluoromethylornithine: Breast tissue, imaging, and serum and urine biomarkers
    • CJ Fabian BF Kimler DA Brady 2002 A phase II breast cancer chemoprevention trial of oral α-difluoromethylornithine: Breast tissue, imaging, and serum and urine biomarkers Clin Cancer Res 8 3105 17
    • (2002) Clin Cancer Res , vol.8 , pp. 3105-17
    • Fabian, C.J.1    Kimler, B.F.2    Brady, D.A.3
  • 30
    • 0032713928 scopus 로고    scopus 로고
    • α-difluoromethylornithine as treatment for metastatic breast cancer patients
    • JA O'Shaughnessy LM Demers SE Jones 1999 α-difluoromethylornithine as treatment for metastatic breast cancer patients Clin Cancer Res 5 3438 44
    • (1999) Clin Cancer Res , vol.5 , pp. 3438-44
    • O'Shaughnessy, J.A.1    Demers, L.M.2    Jones, S.E.3
  • 31
    • 0345535621 scopus 로고    scopus 로고
    • Development of difluoromethylornithine (DFMO) as a chemopreventive agent
    • FL Meyskens EW Gerner 1999 Development of difluoromethylornithine (DFMO) as a chemopreventive agent Clin Cancer Res 5 945 51
    • (1999) Clin Cancer Res , vol.5 , pp. 945-51
    • Meyskens, F.L.1    Gerner, E.W.2


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