메뉴 건너뛰기




Volumn 33, Issue 2, 2007, Pages 273-281

Anticancer drugs and hyperthermia enhance cytotoxicity induced by polyamine enzymatic oxidation products

Author keywords

Amine oxidase; Docetaxel; Eukaryotic initiation factor 5A; IFN ; Multidrug resistance; Polyamines

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; ALDEHYDE; ALPHA INTERFERON; AMINE OXIDASE (FLAVIN CONTAINING); ANTINEOPLASTIC AGENT; BACTERIAL TOXIN; DOCETAXEL; ETOPOSIDE; HYBRID PROTEIN; HYDROGEN PEROXIDE; HYPUSINE; INITIATION FACTOR 5A; N,N' BIS(2,3 BUTADIENYL)PUTRESCINE; POLYAMINE; PROTEIN SYNTHESIS INHIBITOR; SPERMINE; TRANSFORMING GROWTH FACTOR ALPHA;

EID: 34547662506     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-007-0536-x     Document Type: Review
Times cited : (6)

References (62)
  • 1
    • 0023871286 scopus 로고
    • Developmental pattern for deoxyhypusine hydroxylase in rat brain
    • A Abbruzzese 1988 Developmental pattern for deoxyhypusine hydroxylase in rat brain J Neurochem 50 695 699
    • (1988) J Neurochem , vol.50 , pp. 695-699
    • Abbruzzese, A.1
  • 2
    • 0024462317 scopus 로고
    • Inhibition of deoxyhypusine hydroxylase by polyamines and by a deoxyhypusine peptide
    • A Abbruzzese MH Park S Beninati JE Folk 1989 Inhibition of deoxyhypusine hydroxylase by polyamines and by a deoxyhypusine peptide Biochem Biophys Acta 997 248 255
    • (1989) Biochem Biophys Acta , vol.997 , pp. 248-255
    • Abbruzzese, A.1    Park, M.H.2    Beninati, S.3    Folk, J.E.4
  • 3
    • 0642317017 scopus 로고    scopus 로고
    • Drugs affecting the cell cycle via actions of the polyamine metabolic pathway
    • JM Ackermann AE Pegg DE McCloskey 2003 Drugs affecting the cell cycle via actions of the polyamine metabolic pathway Prog Cell Cycle Res 5 461 468
    • (2003) Prog Cell Cycle Res , vol.5 , pp. 461-468
    • Ackermann, J.M.1    Pegg, A.E.2    McCloskey, D.E.3
  • 4
    • 12144282794 scopus 로고    scopus 로고
    • The biological functions of polyamine oxidation products by amine oxidases: Perspectives of clinical applications
    • E Agostinelli G Arancia L Dalla Vedova F Belli M Marra M Salvi A Toninello 2004 The biological functions of polyamine oxidation products by amine oxidases: perspectives of clinical applications Amino Acids 27 347 358
    • (2004) Amino Acids , vol.27 , pp. 347-358
    • Agostinelli, E.1    Arancia, G.2    Dalla Vedova, L.3    Belli, F.4    Marra, M.5    Salvi, M.6    Toninello, A.7
  • 5
    • 33747113715 scopus 로고    scopus 로고
    • Hyperthermia enhances cytotoxicity of amine oxidase and spermine on drug-resistant LoVo colon adenocarcinoma cells
    • E Agostinelli F Belli L Dalla Vedova M Marra P Crateri G Arancia 2006a Hyperthermia enhances cytotoxicity of amine oxidase and spermine on drug-resistant LoVo colon adenocarcinoma cells Int J Oncol 28 1543 1553
    • (2006) Int J Oncol , vol.28 , pp. 1543-1553
    • Agostinelli, E.1    Belli, F.2    Dalla Vedova, L.3    Marra, M.4    Crateri, P.5    Arancia, G.6
  • 6
    • 33749044114 scopus 로고    scopus 로고
    • Sensitization of human colon adenocarcinoma cells (LoVo) to reactive oxygen species by a lysosomotropic compound
    • E Agostinelli L Dalla Vedova F Belli M Condello G Arancia N Seiler 2006b Sensitization of human colon adenocarcinoma cells (LoVo) to reactive oxygen species by a lysosomotropic compound Int J Oncol 29 947 955
    • (2006) Int J Oncol , vol.29 , pp. 947-955
    • Agostinelli, E.1    Dalla Vedova, L.2    Belli, F.3    Condello, M.4    Arancia, G.5    Seiler, N.6
  • 9
    • 0027293584 scopus 로고
    • Cytotoxicity and kinetic analysis of purified bovine serum amine oxidase in the presence of spermine in Chinese hamster ovary cells
    • DA Averill-Bates E Agostinelli E Przybytkowski MA Mateescu B Mondovì 1993 Cytotoxicity and kinetic analysis of purified bovine serum amine oxidase in the presence of spermine in Chinese hamster ovary cells Arch Biochem Biophys 300 75 79
    • (1993) Arch Biochem Biophys , vol.300 , pp. 75-79
    • Averill-Bates, D.A.1    Agostinelli, E.2    Przybytkowski, E.3    Mateescu, M.A.4    Mondovì, B.5
  • 10
    • 20344392399 scopus 로고    scopus 로고
    • Anti-tumoral effect of native and immobilized bovine serum amine oxidase in a mouse melanoma model
    • DA Averill-Bates A Cherif E Agostinelli A Tanel G Fortier 2005 Anti-tumoral effect of native and immobilized bovine serum amine oxidase in a mouse melanoma model Biochem Pharmacol 69 1693 1704
    • (2005) Biochem Pharmacol , vol.69 , pp. 1693-1704
    • Averill-Bates, D.A.1    Cherif, A.2    Agostinelli, E.3    Tanel, A.4    Fortier, G.5
  • 11
    • 0018083955 scopus 로고
    • Enhancement of thermal killing by polyamines. II. Uptake and metabolism of exogenous polyamines in hyperthermic Chinese hamster cells
    • E Ben-Hur E Riklis 1978 Enhancement of thermal killing by polyamines. II. Uptake and metabolism of exogenous polyamines in hyperthermic Chinese hamster cells Int J Cancer 22 607 610
    • (1978) Int J Cancer , vol.22 , pp. 607-610
    • Ben-Hur, E.1    Riklis, E.2
  • 12
    • 0033213831 scopus 로고    scopus 로고
    • Topoisomerase II is non-functional in polyamine-depleted cells
    • AK Berntsson SM Oredsson 1999 Topoisomerase II is non-functional in polyamine-depleted cells J Cell Biochem 75 46 55
    • (1999) J Cell Biochem , vol.75 , pp. 46-55
    • Berntsson, A.K.1    Oredsson, S.M.2
  • 14
    • 0003018426 scopus 로고
    • Inhibition of basic amino acid decarboxylases involved in polyamine biosynthesis
    • PP McCann AE Pegg A Sjoerdsma. Academic Press Orlando
    • P Bey C Danzin M Jung 1987 Inhibition of basic amino acid decarboxylases involved in polyamine biosynthesis PP McCann AE Pegg A Sjoerdsma Inhibition of polyamine metabolism Academic Press Orlando 1 31
    • (1987) Inhibition of Polyamine Metabolism , pp. 1-31
    • Bey, P.1    Danzin, C.2    Jung, M.3
  • 15
    • 0026076137 scopus 로고
    • Mechanisms of spermine toxicity in baby-hamster kidney (BHK) cells. the role of amine oxidases and oxidative stress
    • VG Brunton MH Grant HM Wallace 1991 Mechanisms of spermine toxicity in baby-hamster kidney (BHK) cells. The role of amine oxidases and oxidative stress Biochem J 280 193 198
    • (1991) Biochem J , vol.280 , pp. 193-198
    • Brunton, V.G.1    Grant, M.H.2    Wallace, H.M.3
  • 16
    • 0026446891 scopus 로고
    • Cytostasis induced in L1210 murine leukemia cells by the S-adenosyl-L-methionine decarboxylase inhibitor 5′-{[(Z)-4-amino-2- butenyl]methylamino}-5′-deoxyadenosine may be due to hypusine depletion
    • TL Byers B Ganem AE Pegg 1992 Cytostasis induced in L1210 murine leukemia cells by the S-adenosyl-L-methionine decarboxylase inhibitor 5′-{[(Z)-4-amino-2-butenyl]methylamino}-5′-deoxyadenosine may be due to hypusine depletion Biochem J 287 717 724
    • (1992) Biochem J , vol.287 , pp. 717-724
    • Byers, T.L.1    Ganem, B.2    Pegg, A.E.3
  • 17
    • 0036568479 scopus 로고    scopus 로고
    • Enzymatic oxidation product of spermine induce greater cytotoxic effects on human multidrug-resistant colon carcinoma cells (LoVo) than on their wild type counterparts
    • A Calcabrini G Arancia M Marra P Crateri O Befani A Martone E Agostinelli 2002 Enzymatic oxidation product of spermine induce greater cytotoxic effects on human multidrug-resistant colon carcinoma cells (LoVo) than on their wild type counterparts Int J Cancer 99 43 52
    • (2002) Int J Cancer , vol.99 , pp. 43-52
    • Calcabrini, A.1    Arancia, G.2    Marra, M.3    Crateri, P.4    Befani, O.5    Martone, A.6    Agostinelli, E.7
  • 19
    • 0041810592 scopus 로고    scopus 로고
    • The eukaryotic initiation factor 5A is involved in the regulation of proliferation and apoptosis induced by interferon-α and EGF in human cancer cells
    • M Caraglia M Marra G Giuberti AM D'Alessandro A Baldi P Tassone S Venuta P Tagliaferri A Abbruzzese 2003a The eukaryotic initiation factor 5A is involved in the regulation of proliferation and apoptosis induced by interferon-α and EGF in human cancer cells J Biochem 133 757 765
    • (2003) J Biochem , vol.133 , pp. 757-765
    • Caraglia, M.1    Marra, M.2    Giuberti, G.3    D'Alessandro, A.M.4    Baldi, A.5    Tassone, P.6    Venuta, S.7    Tagliaferri, P.8    Abbruzzese, A.9
  • 23
    • 0023710185 scopus 로고
    • Regulation of ornithine decarboxylase and other cell cycle-dependent genes during enescence of IMR-90 human diploid fibroblasts
    • ZF Chang KY Chen 1988 Regulation of ornithine decarboxylase and other cell cycle-dependent genes during enescence of IMR-90 human diploid fibroblasts J Biol Chem 263 11431 11435
    • (1988) J Biol Chem , vol.263 , pp. 11431-11435
    • Chang, Z.F.1    Chen, K.Y.2
  • 25
    • 0034992341 scopus 로고    scopus 로고
    • Immobilization of native and polyethyleneglycol-treated ("PEGylated") bovine serum amine oxidase into a biocompatible hydrogel
    • N Demers E Agostinelli DA Averill-Bates G Fortier 2001 Immobilization of native and polyethyleneglycol-treated ("PEGylated") bovine serum amine oxidase into a biocompatible hydrogel Biotechnol Appl Biochem 33 201 207
    • (2001) Biotechnol Appl Biochem , vol.33 , pp. 201-207
    • Demers, N.1    Agostinelli, E.2    Averill-Bates, D.A.3    Fortier, G.4
  • 28
    • 4944242891 scopus 로고    scopus 로고
    • Polyamines and cancer: Old molecules, new understanding
    • EW Gerner FL Meyskens Jr 2004 Polyamines and cancer: old molecules, new understanding Nat Rev Cancer 4 781 792
    • (2004) Nat Rev Cancer , vol.4 , pp. 781-792
    • Gerner, E.W.1    Meyskens Jr., F.L.2
  • 30
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • JWB Hershey 1991 Translational control in mammalian cells Annu Rev Biochem 61 717 755
    • (1991) Annu Rev Biochem , vol.61 , pp. 717-755
    • Hershey, J.W.B.1
  • 31
    • 0343127454 scopus 로고
    • Polyamine requirement for polyribosome formation and protein synthesis in human lymphocytes
    • Akademiai Kiado Budapest
    • E Hölttä 1985 Polyamine requirement for polyribosome formation and protein synthesis in human lymphocytes L Selmeci ME Brosnan N Seiler Recent progress in polyamine research Akademiai Kiado Budapest 137 150
    • (1985) Recent Progress in Polyamine Research , pp. 137-150
    • Hölttä, E.1    Selmeci, L.2    Brosnan, M.E.3    Seiler, N.4
  • 32
    • 1842481509 scopus 로고    scopus 로고
    • The chemopreventive agent α-difluoromethylornithine blocks K-ras dependent tumor formation and specific gene expression in Caco-2 cells
    • NA Ignatenko H Zhang GS Watts BA Skovan DE Stringer EW Gerner 2004 The chemopreventive agent α-difluoromethylornithine blocks K-ras dependent tumor formation and specific gene expression in Caco-2 cells Mol Carcinog 39 221 233
    • (2004) Mol Carcinog , vol.39 , pp. 221-233
    • Ignatenko, N.A.1    Zhang, H.2    Watts, G.S.3    Skovan, B.A.4    Stringer, D.E.5    Gerner, E.W.6
  • 33
    • 1542284582 scopus 로고    scopus 로고
    • Genetic approaches to the cellular functions of polyamines in mammals
    • J Janne L Alhonen M Pietila TA Keinanen 2004 Genetic approaches to the cellular functions of polyamines in mammals Eur J Biochem 271 877 894
    • (2004) Eur J Biochem , vol.271 , pp. 877-894
    • Janne, J.1    Alhonen, L.2    Pietila, M.3    Keinanen, T.A.4
  • 34
    • 0027518126 scopus 로고
    • Features of the spermidine binding site of deoxyhypusine synthase as derived from inhibition studies. Effective inhibition by bis- and mono-guanylated diamines and polyamines
    • J Jakus EC Wolff MH Park JE Folk 1993 Features of the spermidine binding site of deoxyhypusine synthase as derived from inhibition studies. Effective inhibition by bis- and mono-guanylated diamines and polyamines J Biol Chem 268 13151 13159
    • (1993) J Biol Chem , vol.268 , pp. 13151-13159
    • Jakus, J.1    Wolff, E.C.2    Park, M.H.3    Folk, J.E.4
  • 35
    • 0031064613 scopus 로고    scopus 로고
    • Efficacy, safety, and risk-benefit analysis of adjuvant interferon alfa-2b in melanoma
    • JM Kirkwood GD Resnick BF Cole 1997 Efficacy, safety, and risk-benefit analysis of adjuvant interferon alfa-2b in melanoma Semin Oncol 24 S16 S23
    • (1997) Semin Oncol , vol.24
    • Kirkwood, J.M.1    Resnick, G.D.2    Cole, B.F.3
  • 37
    • 0035503697 scopus 로고    scopus 로고
    • Polyamine depletion in human melanoma cells leads to G1 arrest associated with induction of p21WAF1/ CIP1/SDI1, changes in the expression of p21-regulated genes, and a senescence-like phenotype
    • DL Kramer BD Chang Y Chen P Diegelman K Alm AR Black IB Roninson CW Porter 2001 Polyamine depletion in human melanoma cells leads to G1 arrest associated with induction of p21WAF1/ CIP1/SDI1, changes in the expression of p21-regulated genes, and a senescence-like phenotype Cancer Res 61 7754 7762
    • (2001) Cancer Res , vol.61 , pp. 7754-7762
    • Kramer, D.L.1    Chang, B.D.2    Chen, Y.3    Diegelman, P.4    Alm, K.5    Black, A.R.6    Roninson, I.B.7    Porter, C.W.8
  • 38
    • 0034672221 scopus 로고    scopus 로고
    • Human deoxyhypusine synthase: Interrelationship between binding of NAD and substrates
    • CH Lee MH Park 2000 Human deoxyhypusine synthase: interrelationship between binding of NAD and substrates Biochem J 352 851 857
    • (2000) Biochem J , vol.352 , pp. 851-857
    • Lee, C.H.1    Park, M.H.2
  • 39
    • 0032529637 scopus 로고    scopus 로고
    • Apoptosis, reproductive failure, and oxidative stress in Chinese hamster ovary cells with compromised genomic integrity
    • CL Limoli A Hartmann L Shephard CR Yang DA Boothman J Bartholomew WF Morgan 1998 Apoptosis, reproductive failure, and oxidative stress in Chinese hamster ovary cells with compromised genomic integrity Cancer Res 58 3712 3718
    • (1998) Cancer Res , vol.58 , pp. 3712-3718
    • Limoli, C.L.1    Hartmann, A.2    Shephard, L.3    Yang, C.R.4    Boothman, D.A.5    Bartholomew, J.6    Morgan, W.F.7
  • 40
    • 28144445570 scopus 로고    scopus 로고
    • Docetaxel: A review of its use in metastatic breast cancer
    • KA Lyseng-Williamson C Fenton 2005 Docetaxel: a review of its use in metastatic breast cancer Drugs 65 2513 2531
    • (2005) Drugs , vol.65 , pp. 2513-2531
    • Lyseng-Williamson, K.A.1    Fenton, C.2
  • 42
    • 0018097605 scopus 로고
    • Anti-proliferate properties of DL-α-difuloromethylornithine in cultured cells. a consequence of the irreversible inhibition of ornithine decarboxylase
    • PS Mamont MC Duchesne J Grove P Bey 1978 Anti-proliferate properties of DL-α-difuloromethylornithine in cultured cells. A consequence of the irreversible inhibition of ornithine decarboxylase Biochem Biophys Res Commun 81 58 66
    • (1978) Biochem Biophys Res Commun , vol.81 , pp. 58-66
    • Mamont, P.S.1    Duchesne, M.C.2    Grove, J.3    Bey, P.4
  • 43
    • 0028956729 scopus 로고
    • Polyamines as targets for therapeutic intervention
    • LJ Marton AE Pegg 1995 Polyamines as targets for therapeutic intervention Annu Rev Pharmacol Toxicol 35 55 91
    • (1995) Annu Rev Pharmacol Toxicol , vol.35 , pp. 55-91
    • Marton, L.J.1    Pegg, A.E.2
  • 44
    • 0021031297 scopus 로고
    • A mouse lymphoma cell mutant whose major protein product is ornithine decarboxylase
    • L McConlogue P Coffino 1983 A mouse lymphoma cell mutant whose major protein product is ornithine decarboxylase J Biol Chem 258 12083 12086
    • (1983) J Biol Chem , vol.258 , pp. 12083-12086
    • McConlogue, L.1    Coffino, P.2
  • 45
    • 0023126357 scopus 로고
    • Oxidized polyamines and the growth of human vascular endothelial cells
    • DML Morgan 1987 Oxidized polyamines and the growth of human vascular endothelial cells Biochem J 242 347 352
    • (1987) Biochem J , vol.242 , pp. 347-352
    • Morgan, D.M.L.1
  • 47
    • 0027197906 scopus 로고
    • Hypusine: Its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation
    • MH Park EC Wolff JE Folk 1993 Hypusine: its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation Biofactors 4 95 104
    • (1993) Biofactors , vol.4 , pp. 95-104
    • Park, M.H.1    Wolff, E.C.2    Folk, J.E.3
  • 48
    • 0020215250 scopus 로고
    • Polyamine metabolism and function
    • AE Pegg PP McCann 1982 Polyamine metabolism and function Am J Physiol 243 C212 C221
    • (1982) Am J Physiol , vol.243
    • Pegg, A.E.1    McCann, P.P.2
  • 50
  • 51
    • 0018900891 scopus 로고
    • Ornithine decarboxylase as a biological and pharmacological tool
    • DH Russell 1980 Ornithine decarboxylase as a biological and pharmacological tool Pharmacology 20 117 129
    • (1980) Pharmacology , vol.20 , pp. 117-129
    • Russell, D.H.1
  • 52
    • 0034045972 scopus 로고    scopus 로고
    • Involvement of polyamines in apoptosis. Facts and controversies: Effectors or protectors?
    • RG Schipper LC Penning AA Verhofstad 2000 Involvement of polyamines in apoptosis. Facts and controversies: effectors or protectors? Semin Cancer Biol 10 55 68
    • (2000) Semin Cancer Biol , vol.10 , pp. 55-68
    • Schipper, R.G.1    Penning, L.C.2    Verhofstad, A.A.3
  • 53
    • 0141633535 scopus 로고    scopus 로고
    • Thirty years of polyamine-related approaches to cancer therapy. Retrospect and prospect: Part 1. Selective enzyme inhibitors
    • N Seiler 2003 Thirty years of polyamine-related approaches to cancer therapy. Retrospect and prospect: part 1. Selective enzyme inhibitors Curr Drug Targets 4 537 564
    • (2003) Curr Drug Targets , vol.4 , pp. 537-564
    • Seiler, N.1
  • 54
    • 0026603452 scopus 로고
    • The biochemistry, genetics, and regulation of polyamine biosynthesis in Saccharomyces decarboxylase and S-adenosylmethionine decarboxylase gene expression in rodent kidney and accessory sex organs
    • CW Tabor H Tabor AK Tyagi MS Cohn 1992 The biochemistry, genetics, and regulation of polyamine biosynthesis in Saccharomyces decarboxylase and S-adenosylmethionine decarboxylase gene expression in rodent kidney and accessory sex organs Endocrinology 130 1131 1144
    • (1992) Endocrinology , vol.130 , pp. 1131-1144
    • Tabor, C.W.1    Tabor, H.2    Tyagi, A.K.3    Cohn, M.S.4
  • 55
    • 0019196018 scopus 로고
    • Construction of an Escherichia coli strain unable to synthesize putrescine, spermidine, or cadaverine: Characterization of two genes controlling lysine decarboxylase
    • H Tabor EW Hafner CW Tabor 1980 Construction of an Escherichia coli strain unable to synthesize putrescine, spermidine, or cadaverine: characterization of two genes controlling lysine decarboxylase J Bacteriol 144 952 956
    • (1980) J Bacteriol , vol.144 , pp. 952-956
    • Tabor, H.1    Hafner, E.W.2    Tabor, C.W.3
  • 56
    • 0023136544 scopus 로고
    • Structural alterations and stabilization of rabbit uterine estrogen receptors by natural polyamines
    • T Thomas DT Kiang 1987 Structural alterations and stabilization of rabbit uterine estrogen receptors by natural polyamines Cancer Res 47 1799 1804
    • (1987) Cancer Res , vol.47 , pp. 1799-1804
    • Thomas, T.1    Kiang, D.T.2
  • 57
    • 0035099627 scopus 로고    scopus 로고
    • Polyamines in cell growth and cell death: Molecular mechanisms and therapeutic applications
    • T Thomas TJ Thomas 2001 Polyamines in cell growth and cell death: molecular mechanisms and therapeutic applications Cell Mol Life Sci 58 244 258
    • (2001) Cell Mol Life Sci , vol.58 , pp. 244-258
    • Thomas, T.1    Thomas, T.J.2
  • 60
    • 25444443392 scopus 로고    scopus 로고
    • Activation of TGF-β1/p38/Smad3 signaling in stromal cells requires ROS-mediated MMP-2 activity during bone marrow damage
    • L Wang S Clutter J Benincosa J Fortney LF Gibson 2005 Activation of TGF-β1/p38/Smad3 signaling in stromal cells requires ROS-mediated MMP-2 activity during bone marrow damage Stem Cells 23 1122 1134
    • (2005) Stem Cells , vol.23 , pp. 1122-1134
    • Wang, L.1    Clutter, S.2    Benincosa, J.3    Fortney, J.4    Gibson, L.F.5
  • 61
    • 10944225039 scopus 로고    scopus 로고
    • Spermine synthesis is required for normal viability, growth and fertility in the mouse
    • X Wang Y Ikeguchi DE McCloskey P Nelson AE Pegg 2004 Spermine synthesis is required for normal viability, growth and fertility in the mouse J Biol Chem 179 51370 51375
    • (2004) J Biol Chem , vol.179 , pp. 51370-51375
    • Wang, X.1    Ikeguchi, Y.2    McCloskey, D.E.3    Nelson, P.4    Pegg, A.E.5
  • 62
    • 0032790229 scopus 로고    scopus 로고
    • Subunit- and site-specific pharmacology of the NMDA receptor channel
    • T Yamakura K Shimoji 1999 Subunit- and site-specific pharmacology of the NMDA receptor channel Prog Neurobiol 59 279 298
    • (1999) Prog Neurobiol , vol.59 , pp. 279-298
    • Yamakura, T.1    Shimoji, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.