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Volumn 31, Issue 3, 2007, Pages 473-484

Lysosomotropic compounds and spermine enzymatic oxidation products in cancer therapy (review)

Author keywords

Colon adenocarcinoma; Lysosomes; Lysosomotropic compounds; MDL 72527; Multidrug resistance; Polyamines

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HYDROGEN PEROXIDE; OXYGEN; REACTIVE OXYGEN METABOLITE; SPERMINE;

EID: 38449100178     PISSN: 10196439     EISSN: 17912423     Source Type: Journal    
DOI: 10.3892/ijo.31.3.473     Document Type: Review
Times cited : (26)

References (114)
  • 1
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner MO: The biochemistry of apoptosis. Nature 407: 770-776, 2000.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 2
    • 9944222054 scopus 로고    scopus 로고
    • Exploiting death receptor signaling pathways for tumor therapy
    • DOI 10.1016/j.bbcan.2004.09.003, PII S0304419X04000599
    • Fulda S and Debatin KM: Exploiting death receptor signalling pathways for tumor therapy. Biochim Biophys Acta 1795: 27-41, 2004. (Pubitemid 39592904)
    • (2004) Biochimica et Biophysica Acta - Reviews on Cancer , vol.1705 , Issue.1 , pp. 27-41
    • Fulda, S.1    Debatin, K.-M.2
  • 3
    • 2442480795 scopus 로고    scopus 로고
    • Multiple cell death pathways as regulators of tumour initiation and progression
    • Jäättelä M: Multiple cell death pathways as regulators of tumour initiation and progression. Oncogene 23: 2746-2756, 2004.
    • (2004) Oncogene , vol.23 , pp. 2746-2756
    • Jäättelä, M.1
  • 4
    • 18244392443 scopus 로고    scopus 로고
    • Cell death independent of caspases: A review
    • Broker LE, Kruyt FA and Giaccone G: Cell death independent of caspases: a review. Clin Cancer Res 11: 3155-3162, 2005.
    • (2005) Clin Cancer Res , vol.11 , pp. 3155-3162
    • Broker, L.E.1    Kruyt, F.A.2    Giaccone, G.3
  • 5
    • 22544444514 scopus 로고    scopus 로고
    • Caspase-independent cell death
    • Kroemer G and Martin SJ: Caspase-independent cell death. Nat Med 11: 723-730, 2005.
    • (2005) Nat Med , vol.11 , pp. 723-730
    • Kroemer, G.1    Martin, S.J.2
  • 6
    • 0141907718 scopus 로고    scopus 로고
    • Destination 'lysosome': A target organelle for tumor cell killing
    • Castino R, Demoz M and Isidoro C: Destination 'lysosome': a target organelle for tumor cell killing. J Mol Recognit 16: 337-348, 2003.
    • (2003) J Mol Recognit , vol.16 , pp. 337-348
    • Castino, R.1    Demoz, M.2    Isidoro, C.3
  • 8
    • 0442323561 scopus 로고    scopus 로고
    • Autophagy in sickness and in health
    • Cuervo AM: Autophagy in sickness and in health. Trends Cell Biol 14: 70-77, 2004.
    • (2004) Trends Cell Biol , vol.14 , pp. 70-77
    • Cuervo, A.M.1
  • 9
    • 27644471129 scopus 로고    scopus 로고
    • Doctor Jekyll and Mister Hyde: Autophagy can promote both cell survival and cell death
    • Eskelinen EL: Doctor Jekyll and Mister Hyde: Autophagy can promote both cell survival and cell death. Cell Death Differ 12: 1468-1472, 2005.
    • (2005) Cell Death Differ , vol.12 , pp. 1468-1472
    • Eskelinen, E.L.1
  • 10
    • 28544435485 scopus 로고    scopus 로고
    • Lysosomes and autophagy in cell death control
    • DOI 10.1038/nrc1738
    • Kroemer G and Jäättelä M: Lysosomes and autophagy in cell death control. Nat Rev Cancer 5: 886-897, 2005. (Pubitemid 41746033)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.11 , pp. 886-897
    • Kroemer, G.1    Jaattela, M.2
  • 11
    • 17144361820 scopus 로고    scopus 로고
    • Lysosomes as targets in cancer therapy
    • Fehrenbacher N and Jäättelä M: Lysosomes as targets in cancer therapy. Cancer Res 65: 2993-2995, 2005.
    • (2005) Cancer Res , vol.65 , pp. 2993-2995
    • Fehrenbacher, N.1    Jäättelä, M.2
  • 12
    • 21344455498 scopus 로고    scopus 로고
    • Lysosomal cysteine proteinases: Structural features and their role in apoptosis
    • Stoka V, Turk B and Turk V: Lysosomal cysteine proteinases: structural features and their role in apoptosis. IUBMB Life 57: 347-353, 2005.
    • (2005) IUBMB Life , vol.57 , pp. 347-353
    • Stoka, V.1    Turk, B.2    Turk, V.3
  • 13
    • 0025413403 scopus 로고
    • The role of cathepsin L in malignant transformation
    • Kane SE and Gottesman MM: The role of cathepsin L in malignant transformation. Semin Cancer Biol 1: 127-136, 1990.
    • (1990) Semin Cancer Biol , vol.1 , pp. 127-136
    • Kane, S.E.1    Gottesman, M.M.2
  • 14
    • 0034651996 scopus 로고    scopus 로고
    • Unravelling the role of proteases in cancer
    • Koblinski JE, Ahram M and Sloane BF: Unravelling the role of proteases in cancer. Clin Chim Acta 291: 113-135, 2000.
    • (2000) Clin Chim Acta , vol.291 , pp. 113-135
    • Koblinski, J.E.1    Ahram, M.2    Sloane, B.F.3
  • 15
    • 10044296973 scopus 로고    scopus 로고
    • Cathepsins in human cancer
    • Jedeszko C and Sloan BF: Cathepsins in human cancer. Biol Chem 385: 1017-1027, 2004.
    • (2004) Biol Chem , vol.385 , pp. 1017-1027
    • Jedeszko, C.1    Sloan, B.F.2
  • 16
    • 0034948738 scopus 로고    scopus 로고
    • The autophagosomal-lysosomal compartment in programmed cell death
    • Bursch W: The autophagosomal-lysosomal compartment in programmed cell death. Cell Death Differ 8: 569-581, 2001.
    • (2001) Cell Death Differ , vol.8 , pp. 569-581
    • Bursch, W.1
  • 17
    • 0030757986 scopus 로고    scopus 로고
    • Photo-oxidative disruption of lysosomal membranes causes apoptosis of cultured human fibroblasts
    • Brunk UT, Dalen H, Roberg K and Hellquist HB: Photo-oxidative disruption of lysosomal membranes causes apoptosis of cultured human fibroblasts. Free Radic Biol Med 23: 616-626, 1997.
    • (1997) Free Radic Biol Med , vol.23 , pp. 616-626
    • Brunk, U.T.1    Dalen, H.2    Roberg, K.3    Hellquist, H.B.4
  • 18
    • 27744529221 scopus 로고    scopus 로고
    • Polyamines and apoptosis
    • Seiler N and Raul F: Polyamines and apoptosis. J Cell Mol Med 9: 623-642, 2005.
    • (2005) J Cell Mol Med , vol.9 , pp. 623-642
    • Seiler, N.1    Raul, F.2
  • 19
    • 0033214906 scopus 로고    scopus 로고
    • The polyamine oxidase inhibitor MDL-72,527 selectively induces apoptosis of transformed hematopoietic cells through lysosomotropic effects
    • Dai H, Kramer DL, Yanag C, Murti KG, Porter CW and Cleveland JL: The polyamine oxidase inhibitor MDL 72527 selectively induces apoptosis of transformed haematopoietic cells through lysosomotropic effects. Cancer Res 59: 4844-4954, 1999. (Pubitemid 29472900)
    • (1999) Cancer Research , vol.59 , Issue.19 , pp. 4944-4954
    • Dai, H.1    Kramer, D.L.2    Yang, C.3    Murti, K.G.4    Porter, C.W.5    Cleveland, J.L.6
  • 21
    • 26944475263 scopus 로고    scopus 로고
    • The lysosome turns fifty
    • de Duve C: The lysosome turns fifty. Nat Cell Biol 7: 847-849, 2005.
    • (2005) Nat Cell Biol , vol.7 , pp. 847-849
    • De Duve, C.1
  • 22
    • 27644466759 scopus 로고    scopus 로고
    • Autophagy and signalling: Their role in cell survival and cell death
    • Codogno P and Meijer AJ: Autophagy and signalling: their role in cell survival and cell death. Cell Death Differ 12: 1509-1518, 2005.
    • (2005) Cell Death Differ , vol.12 , pp. 1509-1518
    • Codogno, P.1    Meijer, A.J.2
  • 23
    • 0016904754 scopus 로고
    • The secretion of lysosomal enzymes
    • Davies P and Allison AC: The secretion of lysosomal enzymes. Front Biol 45: 61-98, 1976.
    • (1976) Front Biol , vol.45 , pp. 61-98
    • Davies, P.1    Allison, A.C.2
  • 24
    • 0033016291 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and pathogenesis of human diseases
    • Schwartz AL and Ciechanover A: The ubiquitin-proteasome pathway and pathogenesis of human diseases. Annu Rev Med 50: 57-74, 1999.
    • (1999) Annu Rev Med , vol.50 , pp. 57-74
    • Schwartz, A.L.1    Ciechanover, A.2
  • 25
    • 4544385218 scopus 로고    scopus 로고
    • Autophagy: Many paths to the same end
    • Cuervo AM: Autophagy: Many paths to the same end. Mol Cell Biochem 263: 55-72, 2004.
    • (2004) Mol Cell Biochem , vol.263 , pp. 55-72
    • Cuervo, A.M.1
  • 26
    • 0031685364 scopus 로고    scopus 로고
    • Cysteine proteinases and their endogenous inhibitors: Target proteins for prognosis, diagnosis and therapy in cancer
    • review
    • Kos J and Lah TT: Cysteine proteinases and their endogenous inhibitors: target proteins for prognosis, diagnosis and therapy in cancer (review). Oncol Rep 5: 1349-1361, 1998.
    • (1998) Oncol Rep , vol.5 , pp. 1349-1361
    • Kos, J.1    Lah, T.T.2
  • 27
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: More than scavengers
    • Turk B, Turk D and Turk V: Lysosomal cysteine proteases: more than scavengers. Biochim Biophys Acta 1477: 89-111, 2000.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 89-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 28
    • 4344673498 scopus 로고    scopus 로고
    • Mechanisms of chaperone-mediated autophagy
    • Majeski AE and Dice JF: Mechanisms of chaperone-mediated autophagy. Int J Biochem Cell Biol 36: 2435-2444, 2004.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2435-2444
    • Majeski, A.E.1    Dice, J.F.2
  • 30
    • 0037451783 scopus 로고    scopus 로고
    • Autophagy: A barrier or an adaptive response to cancer
    • Ogier-Denis and Codogno: Autophagy: a barrier or an adaptive response to cancer. Biochim Biophys Acta 1603: 113-128, 2003.
    • (2003) Biochim Biophys Acta , vol.1603 , pp. 113-128
    • Ogier-Denis1    Codogno2
  • 31
    • 2442482810 scopus 로고    scopus 로고
    • Autophagy as a cell death and tumor suppressor mechanism
    • DOI 10.1038/sj.onc.1207521
    • Gozuacik D and Kimchi A: Autophagy as a cell death and tumor suppressor mechanism. Oncogene 23: 2891-2906, 2004. (Pubitemid 38638851)
    • (2004) Oncogene , vol.23 , Issue.16 REV. ISS. 2 , pp. 2891-2906
    • Gozuacik, D.1    Kimchi, A.2
  • 32
    • 0037448105 scopus 로고    scopus 로고
    • Intralysosomal iron: A major determinant of oxidant-induced cell death
    • DOI 10.1016/S0891-5849(03)00109-6
    • Yu Z, Persson HL, Eaton JW and Brunk UT: Intralysosomal iron, a major determinant of oxidant-induced cell death. Free Radic Biol Med 34: 1243-1252, 2003. (Pubitemid 36513967)
    • (2003) Free Radical Biology and Medicine , vol.34 , Issue.10 , pp. 1243-1252
    • Yu, Z.1    Persson, H.L.2    Eaton, J.W.3    Brunk, U.T.4
  • 33
    • 0022336763 scopus 로고
    • Lysosomal origin of the iron required for cell killing by hydrogen peroxide
    • Starke PE, Gilberton JD and Farber JL: Lysosomal origin of the iron required for cell killing by hydrogen peroxide. Biochem Biophys Res Commun 133(2): 371-379, 1985.
    • (1985) Biochem Biophys Res Commun , vol.133 , Issue.2 , pp. 371-379
    • Starke, P.E.1    Gilberton, J.D.2    Farber, J.L.3
  • 34
    • 0032988381 scopus 로고    scopus 로고
    • Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak
    • Brunk UT and Svensson I: Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak. Redox Rep 4: 3-11, 1999.
    • (1999) Redox Rep , vol.4 , pp. 3-11
    • Brunk, U.T.1    Svensson, I.2
  • 36
    • 0141447370 scopus 로고    scopus 로고
    • Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis
    • Zhao M, Antunes F, Eaton JW and Brunk UT: Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis. Eur J Biochem 270: 3778-3786, 2003.
    • (2003) Eur J Biochem , vol.270 , pp. 3778-3786
    • Zhao, M.1    Antunes, F.2    Eaton, J.W.3    Brunk, U.T.4
  • 37
    • 3042777753 scopus 로고    scopus 로고
    • Human neuroblastoma (SH-SY5Y) is highly sensitive to the lysosomotropic aldehyde 3-aminopropanal
    • Yu Z, Li W, Hillman J and Brunk UT: Human neuroblastoma (SH-SY5Y) is highly sensitive to the lysosomotropic aldehyde 3-aminopropanal. Brain Res 1016: 163-169, 2004.
    • (2004) Brain Res , vol.1016 , pp. 163-169
    • Yu, Z.1    Li, W.2    Hillman, J.3    Brunk, U.T.4
  • 39
    • 0029782494 scopus 로고    scopus 로고
    • Cathepsin D protease mediates programmed cell death induced by interferon-γ, Fas/Apo-1 and TNF-α
    • Deiss LP, Galinka H, Berissi H, Cohen O and Kimchi A: Cathepsin D protease mediates programmed cell death induced by interferon-γ, Fas/Apo-1 and TNF-α. EMBO J 15: 3861-3870, 1996.
    • (1996) EMBO J , vol.15 , pp. 3861-3870
    • Deiss, L.P.1    Galinka, H.2    Berissi, H.3    Cohen, O.4    Kimchi, A.5
  • 40
    • 0035408169 scopus 로고    scopus 로고
    • The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress
    • Kågedal K, Johansson U and Ollinger K: The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress. FASEB J 15: 1592-1594, 2001.
    • (2001) FASEB J , vol.15 , pp. 1592-1594
    • Kågedal, K.1    Johansson, U.2    Ollinger, K.3
  • 41
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • DOI 10.1074/jbc.M301911200
    • Bidere N, Lorenzo HK, Carmona S, Ladorge M, Harper F, Dumont C and Senik A: Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J Biol Chem 278: 31401-31411, 2003. (Pubitemid 36994661)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 31401-31411
    • Bidere, N.1    Lorenzo, H.K.2    Carmona, S.3    Laforge, M.4    Harper, F.5    Dumont, C.6    Senik, A.7
  • 42
    • 11844294713 scopus 로고    scopus 로고
    • Induction of lysosomal membrane permeabilization by compounds that activate p53-independent apoptosis
    • Erdal H, Berndtsson M, Castro J, Brunk U, Shoshan MC and Linder S: Induction of lysosomal membrane permeabilization by compounds that activate p53-independent apoptosis. Proc Natl Acad Sci USA 102: 192-197, 2005.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 192-197
    • Erdal, H.1    Berndtsson, M.2    Castro, J.3    Brunk, U.4    Shoshan, M.C.5    Linder, S.6
  • 43
    • 0035018235 scopus 로고    scopus 로고
    • Evidence for a lysosomal pathway for apoptosis induced by the synthetic retinoid CD437 in human leukaemia HL-60 cells
    • Zang Y, Beard RL, Chandraratna RA and Kanag JX: Evidence for a lysosomal pathway for apoptosis induced by the synthetic retinoid CD437 in human leukaemia HL-60 cells. Cell Death Differ 8: 477-485, 2001.
    • (2001) Cell Death Differ , vol.8 , pp. 477-485
    • Zang, Y.1    Beard, R.L.2    Chandraratna, R.A.3    Kanag, J.X.4
  • 44
    • 0026021362 scopus 로고
    • Production of large amounts of hydrogen peroxide by human tumor cells
    • Szatrowsky TP and Nathan CE: Production of large amounts of hydrogen peroxide by human tumor cells. Cancer Res 51: 794-798, 1991.
    • (1991) Cancer Res , vol.51 , pp. 794-798
    • Szatrowsky, T.P.1    Nathan, C.E.2
  • 45
  • 48
    • 0030561552 scopus 로고    scopus 로고
    • Drug-induced lysosomal storage of sulphated glycosaminoglycans
    • DOI 10.1016/S0306-3623(96)00150-4, PII S0306362396001504
    • Fischer J, Lullmann H and Lullman-Rauch R: Drug-induced lysosomal storage of sulphated glycosaminoglycans. Gen Pharmacol 27: 1317-1324, 1996. (Pubitemid 26419688)
    • (1996) General Pharmacology , vol.27 , Issue.8 , pp. 1317-1324
    • Fischer, J.1    Lullmann, H.2    Lullmann-Rauch, R.3
  • 49
    • 0021925321 scopus 로고
    • Regulation of human natural killing by lysosomotropic and thiol-reactive agents
    • Shau H and Dawson JR: Regulation of human natural killing by lysosomotropic and thiol-reactive agents. Immunology 55: 647-654, 1985. (Pubitemid 15237672)
    • (1985) Immunology , vol.55 , Issue.4 , pp. 647-654
    • Shau, H.1    Dawson, J.R.2
  • 50
    • 0000391671 scopus 로고
    • Decrease in macrophage antigen metabolism caused by ammonia and chloroquine is associated with inhibition of antigen presentation to T cells
    • Ziegler HK and Unanue ER: Decrease in macrophage antigen metabolism caused by ammonia and chloroquine is associated with inhibition of antigen presentation to T cells. Proc Natl Acad Sci USA 79: 175-178, 1982.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 175-178
    • Ziegler, H.K.1    Unanue, E.R.2
  • 51
    • 0028007124 scopus 로고
    • Cellular transport of drugs
    • Steinberg TH: Cellular transport of drugs. Clin Infect Dis 19: 916-921, 1994.
    • (1994) Clin Infect Dis , vol.19 , pp. 916-921
    • Steinberg, T.H.1
  • 53
    • 0040117958 scopus 로고    scopus 로고
    • Bafilomycins and concanamycins as inhibitors of V-ATPases
    • Drose S and Altendorf K: Bafilomycins and concanamycins as inhibitors of V-ATPases. J Exp Biol 200: 1-8, 1997.
    • (1997) J Exp Biol , vol.200 , pp. 1-8
    • Drose, S.1    Altendorf, K.2
  • 54
    • 0031931983 scopus 로고    scopus 로고
    • +-translocating vacuolartype ATPase in the anterior silk gland cell of Bombyx mori during metamorphosis
    • +-translocating vacuolartype ATPase in the anterior silk gland cell of Bombyx mori during metamorphosis. J Exp Biol 201: 479-486, 1998.
    • (1998) J Exp Biol , vol.201 , pp. 479-486
    • Azuma, M.1    Ohta, Y.2
  • 56
    • 0037468160 scopus 로고    scopus 로고
    • In bafilomycin A1-resistant cells, bafilomycin A1 raised lysosomal pH and both prodigiosins and concanamycin A inhibited growth through apoptosis
    • Tanigaki K, Sasaki S and Ohkuma S: In bafilomycin A1-resistant cells, bafilomycin A1 raised lysosomal pH and both prodigiosins and concanamycin A inhibited growth through apoptosis. FEBS Lett 537: 79-84, 2003.
    • (2003) FEBS Lett , vol.537 , pp. 79-84
    • Tanigaki, K.1    Sasaki, S.2    Ohkuma, S.3
  • 58
    • 12144282794 scopus 로고    scopus 로고
    • The biological functions of polyamine oxidation products by amine oxidases. Perspectives of clinical applications
    • Agostinelli E, Arancia G, Dalla Vedova L, Belli F, Marra M, Salvi M and Toninello A: The biological functions of polyamine oxidation products by amine oxidases. Perspectives of clinical applications. Amino Acids 27: 347-358, 2004.
    • (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
  • 59
    • 3042837762 scopus 로고    scopus 로고
    • Reactive oxygen species mediate chloroquine-induced expression of chemokines by human astroglial cells
    • Park J, Choi K, Jeong E, Kwon D, Benveniste EN and Choi C: Reactive oxygen species mediate chloroquine-induced expression of chemokines by human astroglial cells. Glia 47: 9-20, 2004.
    • (2004) Glia , vol.47 , pp. 9-20
    • Park, J.1    Choi, K.2    Jeong, E.3    Kwon, D.4    Benveniste, E.N.5    Choi, C.6
  • 62
    • 0035878846 scopus 로고    scopus 로고
    • Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure
    • Wang Y, Devereux W, Woster PM, Stewart TM, Hacker A and Casero RA Jr: Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure. Cancer Res 64: 5370-5373, 2001.
    • (2001) Cancer Res , vol.64 , pp. 5370-5373
    • Wang, Y.1    Devereux, W.2    Woster, P.M.3    Stewart, T.M.4    Hacker, A.5    Casero Jr., R.A.6
  • 63
    • 0024555496 scopus 로고
    • Selective growth inhibition of ductal pancreatic adenocarcinoma cells by the lysosomotropic agent chloroquine
    • Zeilhofer HU, Mollenhauer J and Brune K: Selective growth inhibition of ductal pancreatic adenocarcinoma cells by the lysosomotropic agent chloroquine. Cancer Lett 44: 61-66, 1989. (Pubitemid 19050963)
    • (1989) Cancer Letters , vol.44 , Issue.1 , pp. 61-66
    • Zeilhofer, H.U.1    Mollenhauer, J.2    Brune, K.3
  • 64
    • 33750719583 scopus 로고    scopus 로고
    • Synergism between apple procyanidins and lysosomotropic drugs: Potential in chemoprevention
    • Seiler N, Chaabi M, Roussi S, Gosse F, Lobstein A and Raul F: Synergism between apple procyanidins and lysosomotropic drugs: potential in chemoprevention. Anticancer Res 26: 3381-3385, 2006.
    • (2006) Anticancer Res , vol.26 , pp. 3381-3385
    • Seiler, N.1    Chaabi, M.2    Roussi, S.3    Gosse, F.4    Lobstein, A.5    Raul, F.6
  • 65
    • 0022971454 scopus 로고
    • Chloroquine enhancement of anticancer drug cytotoxicity in drug-resistant human leukaemia cells
    • Zamora JM and Beck WT: Chloroquine enhancement of anticancer drug cytotoxicity in drug-resistant human leukaemia cells. Biochem Pharmacol 35(23): 4303-4310, 1986.
    • (1986) Biochem Pharmacol , vol.35 , Issue.23 , pp. 4303-4310
    • Zamora, J.M.1    Beck, W.T.2
  • 66
    • 0022612462 scopus 로고
    • Lysosomotropic agents reverse multiple drug resistance in human cancer cells
    • DOI 10.1016/0304-3835(86)90049-2
    • Shiraishi N, Akiyama S, Kobayashi M and Kuwano M: Lysosomotropic agents reverse multidrug resistance in human cancer cells. Cancer Lett 30: 251-259, 1986. (Pubitemid 16141895)
    • (1986) Cancer Letters , vol.30 , Issue.3 , pp. 251-259
    • Shiraishi, N.1    Akiyama, S.-I.2    Kobayashi, M.3    Kuwano, M.4
  • 67
    • 0036389837 scopus 로고    scopus 로고
    • The polyamine oxidase inactivator MDL 72527
    • Seiler N, Duranton B and Raul F: The polyamine oxidase inactivator MDL 72527. Prog Drug Res 59: 1-40, 2002.
    • (2002) Prog Drug Res , vol.59 , pp. 1-40
    • Seiler, N.1    Duranton, B.2    Raul, F.3
  • 68
    • 0026076137 scopus 로고
    • Mechanism of spermine toxicity in baby hamster kidney (BHK) cells
    • Brunton VG, Grant MH and Wallace HM: Mechanism of spermine toxicity in baby hamster kidney (BHK) cells. Biochem J 280: 193-198, 1991.
    • (1991) Biochem J , vol.280 , pp. 193-198
    • Brunton, V.G.1    Grant, M.H.2    Wallace, H.M.3
  • 69
    • 0033949077 scopus 로고    scopus 로고
    • Spermine cytotoxicity to human colon carcinoma-derived cells (CaCo-2)
    • Seiler N, Duranton B, Gossé F and Raul F: Spermine cytotoxicity to human colon carcinoma-derived cells (CaCo-2). Cell Biol Toxicol 16: 117-130, 2000.
    • (2000) Cell Biol Toxicol , vol.16 , pp. 117-130
    • Seiler, N.1    Duranton, B.2    Gossé, F.3    Raul, F.4
  • 72
    • 33644829741 scopus 로고    scopus 로고
    • Cytotoxicity of the polyamine oxidase inactivator MDL 72527 to cancer cells: Comparison with a saturated structural analogue
    • Seiler N, Renault J, Gossé F, Roussi S and Raul F: Cytotoxicity of the polyamine oxidase inactivator MDL 72527 to cancer cells: comparison with a saturated structural analogue. Int J Oncol 27: 1669-1676, 2005.
    • (2005) Int J Oncol , vol.27 , pp. 1669-1676
    • Seiler, N.1    Renault, J.2    Gossé, F.3    Roussi, S.4    Raul, F.5
  • 73
    • 1842848009 scopus 로고    scopus 로고
    • Cytotoxic effects of the polyamine oxidase inactivator MDL 72527 on two human colon carcinoma cell lines SW 440 and SW 620
    • Duranton B, Holl V, Schneider Y, Carnesecchi S, Gosse F, Raul F and Seiler N: Cytotoxic effects of the polyamine oxidase inactivator MDL 72527 on two human colon carcinoma cell lines SW 440 and SW 620. Cell Biol Toxicol 18: 381-396, 2002.
    • (2002) Cell Biol Toxicol , vol.18 , pp. 381-396
    • Duranton, B.1    Holl, V.2    Schneider, Y.3    Carnesecchi, S.4    Gosse, F.5    Raul, F.6    Seiler, N.7
  • 74
    • 33749044114 scopus 로고    scopus 로고
    • Sensitization of human colon adenocarcinoma cells (LoVo) to reactive oxygen species by a lysosomotropic compound
    • Agostinelli E, Dalla Vedova L, Belli F, Condello M, Arancia G and Seiler N: Sensitization of human colon adenocarcinoma cells (LoVo) to reactive oxygen species by a lysosomotropic compound. Int J Oncol 29: 947-955, 2006.
    • (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
  • 76
    • 32044453808 scopus 로고    scopus 로고
    • Recent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux
    • Loo TW and Clarke DM: Recent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux. J Membr Biol 206: 173-185, 2005.
    • (2005) J Membr Biol , vol.206 , pp. 173-185
    • Loo, T.W.1    Clarke, D.M.2
  • 77
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman MM and Pastan I: Biochemistry of multidrug resistance mediated by the multidrug transporter. Annu Rev Biochem 62: 385-427, 1993. (Pubitemid 23237876)
    • (1993) Annual Review of Biochemistry , vol.62 , pp. 385-427
    • Gottesman, M.M.1    Pastan, I.2
  • 78
    • 23844521998 scopus 로고    scopus 로고
    • P-glycoprotein: Implications of metabolism of neoplastic cells and cancer therapy
    • Breier A, Barancik M, Sulova Z and Uhrik B: P-glycoprotein: implications of metabolism of neoplastic cells and cancer therapy. Curr Cancer Drug Targets 5: 457-468, 2005.
    • (2005) Curr Cancer Drug Targets , vol.5 , pp. 457-468
    • Breier, A.1    Barancik, M.2    Sulova, Z.3    Uhrik, B.4
  • 79
    • 0034477126 scopus 로고    scopus 로고
    • Reversal of multidrug resistance of tumor cells
    • Szabo D, Keyzer H, Kaiser HE and Molnar J: Reversal of multidrug resistance of tumor cells. Anticancer Res 20: 4261-4274, 2000.
    • (2000) Anticancer Res , vol.20 , pp. 4261-4274
    • Szabo, D.1    Keyzer, H.2    Kaiser, H.E.3    Molnar, J.4
  • 80
    • 0030988015 scopus 로고    scopus 로고
    • Biophysical aspects of P-glycoprotein-mediated multidrug resistance
    • Wadkins RM and Roepe PD: Biophysical aspects of Pglycoprotein-mediated multidrug resistance. Int Rev Cytol 171: 121-165, 1997. (Pubitemid 127742465)
    • (1997) International Review of Cytology , vol.171 , pp. 121-165
    • Wadkins, R.M.1    Roepe, P.D.2
  • 81
    • 0023898749 scopus 로고
    • Physical chemical properties shared by compounds that modulate multidrug-resistance in human leukaemic cells
    • Zamora JM, Pearce HL and Beck WT: Physical chemical properties shared by compounds that modulate multidrug-resistance in human leukaemic cells. Mol Pharmacol 33: 454-462, 1988.
    • (1988) Mol Pharmacol , vol.33 , pp. 454-462
    • Zamora, J.M.1    Pearce, H.L.2    Beck, W.T.3
  • 82
    • 0021550950 scopus 로고
    • Chemosensitizers counteracting acquired resistance to anthracyclines and Vinca alkaloids in vivo. A new treatment principle
    • Skovsgaard T, Dano K and Nissen NI: Chemosensitizers counteracting acquired resistance to anthracyclines and Vinca alkaloids in vivo. A new treatment principle. Cancer Treat Rev 11 (Suppl A9): 63-72, 1984.
    • (1984) Cancer Treat Rev , vol.11 , Issue.SUPPL. A9 , pp. 63-72
    • Skovsgaard, T.1    Dano, K.2    Nissen, N.I.3
  • 84
    • 7144259744 scopus 로고    scopus 로고
    • The bisbenzylisoquinoline alkaloids, tetrandine and fangchinoline, enhance the cytotoxicity of multidrug resistance-related drugs via modulation of P-glycoprotein
    • Choi SU, Park SH, Kim KH, Choi EJ, Kim S, Park WK, Zhang YH, Kim HS, Jung NP and Lee CO: The bisbenzylisoquinoline alkaloids, tetrandine and fangchinoline, enhance the cytotoxicity of multidrug resistance-related drugs via modulation of P-glycoprotein. Anticancer Drugs 9: 255-261, 1998.
    • (1998) Anticancer Drugs , vol.9 , pp. 255-261
    • Choi, S.U.1    Park, S.H.2    Kim, K.H.3    Choi, E.J.4    Kim, S.5    Park, W.K.6    Zhang, Y.H.7    Kim, H.S.8    Jung, N.P.9    Lee, C.O.10
  • 86
    • 0032530924 scopus 로고    scopus 로고
    • Direct binding of chloroquine to the multidrug resistance protein (MRP): Possible role for MRP in chloroquine drug transport and resistance in tumor cells
    • Vezmar M and Georges E: Direct binding of chloroquine to the multidrug resistance protein (MRP): possible role for MRP in chloroquine drug transport and resistance in tumor cells. Biochem Pharmacol 56: 733-742, 1998.
    • (1998) Biochem Pharmacol , vol.56 , pp. 733-742
    • Vezmar, M.1    Georges, E.2
  • 87
    • 0021151666 scopus 로고
    • Verapamil enhances the toxicity of conjugates of epidermal growth factor with Pseudomonas exotoxin and antitransferrin receptor with Pseudomonas exotoxin
    • Akiyama S, Gottesman MM, Hanover JA, Fitzgerald DJP, Willingham MC and Pastan I: Verapamil enhances the toxicity of conjugates of epidermal growth factor with Pseudomonas exotoxin and antitransferrin receptor with Pseudomonas exotoxin. J Cell Physiol 120: 271-279, 1984.
    • (1984) J Cell Physiol , vol.120 , pp. 271-279
    • Akiyama, S.1    Gottesman, M.M.2    Hanover, J.A.3    Fitzgerald, D.J.P.4    Willingham, M.C.5    Pastan, I.6
  • 88
    • 0021810158 scopus 로고
    • The effect of calcium antagonists on the proteolytic degradation of low-density lipoprotein in HeLa cells
    • DOI 10.1016/0014-4827(85)90443-4
    • Akiyama S, Tomita K and Kuwano M: The effect of calcium antagonists on the proteolytic degradation of low density lipoprotein in HeLa cells. Exp Cell Res 158: 192-204, 1985. (Pubitemid 15045832)
    • (1985) Experimental Cell Research , vol.158 , Issue.1 , pp. 192-204
    • Akiyama, S.1    Tomita, K.2    Kuwano, M.3
  • 89
    • 0029944732 scopus 로고    scopus 로고
    • Reversal of doxorubicin, etoposide, vinblastine and taxol resistance in multidrug resistant human sarcoma cells by a polymer of spermine
    • Gosland MP, Gillespie MN, Tsuboi CP, Tofig S, Olson JW, Crooks PA and Aziz SM: Reversal of doxorubicin, etoposide, vinblastine and taxol resistance in multidrug resistant human sarcoma cells by a polymer of spermine. Cancer Chemother Pharmacol 37: 593-600, 1996.
    • (1996) Cancer Chemother Pharmacol , vol.37 , pp. 593-600
    • Gosland, M.P.1    Gillespie, M.N.2    Tsuboi, C.P.3    Tofig, S.4    Olson, J.W.5    Crooks, P.A.6    Aziz, S.M.7
  • 90
    • 0028914767 scopus 로고
    • Potentiation of anticancer drug cytotoxicity by multidrug-resistance chemosensitizers involves alterations in membrane fluidity leading to increased membrane permeability
    • Drori S, Eytan GD and Assaraf YG: Potentiation of anticancer drug cytotoxicity by multidrug-resistance chemosensitizers involves alterations in membrane fluidity leading to increased membrane permeability. Eur J Biochem 228: 1020-1029, 1995.
    • (1995) Eur J Biochem , vol.228 , pp. 1020-1029
    • Drori, S.1    Eytan, G.D.2    Assaraf, Y.G.3
  • 91
    • 0025973575 scopus 로고
    • Modulation of Mitomycin C-induced multidrug resistance in vitro
    • Dorr RT and Liddil ID: Modulation of Mitomycin C-induced multidrug resistance in vitro. Cancer Chemother Pharmacol 27: 290-294, 1991.
    • (1991) Cancer Chemother Pharmacol , vol.27 , pp. 290-294
    • Dorr, R.T.1    Liddil, I.D.2
  • 92
    • 0023785754 scopus 로고
    • The effect of lysosomotropic agents and secretory inhibitors on anthracycline retention and activity of multiple drug-resistant cells
    • Klohs WD and Steinkampf RW: The effect of lysosomotropic agents and secretory inhibitors on anthracycline retention and activity of multiple drug-resistant cells. Mol Pharmacol 34: 180-185, 1988.
    • (1988) Mol Pharmacol , vol.34 , pp. 180-185
    • Klohs, W.D.1    Steinkampf, R.W.2
  • 94
    • 20344392399 scopus 로고    scopus 로고
    • Antitumoral effect of native and immobilized bovine serum amine oxidase in a mouse melanoma model
    • Averill-Bates DA, Cherif A, Agostinelli E, Tanel A and Fortier G: Antitumoral effect of native and immobilized bovine serum amine oxidase in a mouse melanoma model. Biochem Pharmacol 69: 1693-1700, 2005.
    • (2005) Biochem Pharmacol , vol.69 , pp. 1693-1700
    • Averill-Bates, D.A.1    Cherif, A.2    Agostinelli, E.3    Tanel, A.4    Fortier, G.5
  • 95
    • 0033807445 scopus 로고    scopus 로고
    • Hydrogen peroxide inhibits activation, not activity, of cellular caspase-3 in vivo
    • Lee YJ and Shacter E: Hydrogen peroxide inhibits activation, not activity, of cellular caspase-3 in vivo. Free Radic Biol Med 29: 684-692, 2000.
    • (2000) Free Radic Biol Med , vol.29 , pp. 684-692
    • Lee, Y.J.1    Shacter, E.2
  • 96
    • 0033005384 scopus 로고    scopus 로고
    • Hydrogen peroxide-induced apoptosis and necrosis in human lung fibroblasts: Protective roles of glutathione
    • Teramoto S, Tomita T, Matsui H, Ohga E, Matsuse T and Ouchi Y: Hydrogen peroxide-induced apoptosis and necrosis in human lung fibroblasts: protective roles of glutathione. Jpn J Pharmacol 79: 33-40, 1999.
    • (1999) Jpn J Pharmacol , vol.79 , pp. 33-40
    • Teramoto, S.1    Tomita, T.2    Matsui, H.3    Ohga, E.4    Matsuse, T.5    Ouchi, Y.6
  • 97
    • 0037154352 scopus 로고    scopus 로고
    • Acrolein-induced cell death: A caspase-influenced decision between apoptosis and oncosis/necrosis
    • Kern JC and Kehrer JP: Acrolein-induced cell death: a caspase-influenced decision between apoptosis and oncosis/necrosis. Chem Biol Interact 139: 79-95, 2002.
    • (2002) Chem Biol Interact , vol.139 , pp. 79-95
    • Kern, J.C.1    Kehrer, J.P.2
  • 98
    • 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
    • Calcabrini A, Arancia G, Marra M, Crateri P, Befani O, Martone A and Agostinelli E: 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.
    • (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
  • 100
    • 33747113715 scopus 로고    scopus 로고
    • Hyperthermia enhances cytotoxicity of amine oxidase and spermine on drug-resistant colon adenocarcinoma cells (LoVo)
    • Agostinelli E, Belli F, Dalla Vedova L, Marra M, Crateri P and Arancia G: Hyperthermia enhances cytotoxicity of amine oxidase and spermine on drug-resistant colon adenocarcinoma cells (LoVo). Int J Oncol 28: 1543-1553, 2006.
    • (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
  • 101
    • 0034992341 scopus 로고    scopus 로고
    • Immobilization of native and poly(ethylene glycol)-treated ('PEGylated') bovine serum amine oxidase into a biocompatible hydrogel
    • Demers N, Agostinelli E, Averill-Bates DA and Fortier G: Immobilization of native and poly(ethylene glycol)-treated ('PEGylated') bovine serum amine oxidase into a biocompatible hydrogel. Biotechnol Appl Biochem 33: 201-207, 2001.
    • (2001) Biotechnol Appl Biochem , vol.33 , pp. 201-207
    • Demers, N.1    Agostinelli, E.2    Averill-Bates, D.A.3    Fortier, G.4
  • 102
    • 0025325255 scopus 로고
    • Molecular genetics of polyamine synthesis in eukaryotic cells
    • Heby O and Persson L: Molecular genetics of polyamine synthesis in eukaryotic cells. Trends Biochem Sci 15: 153-158, 1990. (Pubitemid 20186844)
    • (1990) Trends in Biochemical Sciences , vol.15 , Issue.4 , pp. 153-158
    • Heby, O.1    Persson, L.2
  • 104
    • 0032984266 scopus 로고    scopus 로고
    • For the clinical application of thermochemotherapy given at mild temperatures
    • Urano M, Kuroda M and Nishimura Y: For the clinical application of thermochemotherapy given at mild temperatures. Int J Hyperthermia 15: 79-107, 1999.
    • (1999) Int J Hyperthermia , vol.15 , pp. 79-107
    • Urano, M.1    Kuroda, M.2    Nishimura, Y.3
  • 105
    • 23944504811 scopus 로고    scopus 로고
    • Should chloroquine be laid to rest?
    • Ginsburg H: Should chloroquine be laid to rest? Acta Trop 96: 16-23, 2005.
    • (2005) Acta Trop , vol.96 , pp. 16-23
    • Ginsburg, H.1
  • 107
    • 4444313754 scopus 로고    scopus 로고
    • Therapy of glioblastoma multiforme improved by the antimutagenic chloroquine
    • Briceno E, Reyes S and Sotelo J: Therapy of glioblastoma multiforme improved by the antimutagenic chloroquine. Neurosurg Focus 14: e3, 2003.
    • (2003) Neurosurg Focus , vol.14
    • Briceno, E.1    Reyes, S.2    Sotelo, J.3
  • 108
    • 0025267832 scopus 로고
    • Morphological evidence for an apparent lysosomotropic activity by unsaturated putrescine analogues
    • Porter CW, Stanek J, Black J, Vaughan M, Ganis B and Pleshkewych A: Morphological evidence for an apparent lysosomotropic activity by unsaturated putrescine analogues. Cancer Res 50: 1929-1935, 1990.
    • (1990) Cancer Res , vol.50 , pp. 1929-1935
    • Porter, C.W.1    Stanek, J.2    Black, J.3    Vaughan, M.4    Ganis, B.5    Pleshkewych, A.6
  • 109
    • 0028267047 scopus 로고
    • Antileukemic activity of phenylalanine methyl ester (PME): A lysosomotropic peptide methyl ester
    • Rosenfeld CS: Antileukemic activity of phenylalanine methyl ester (PME): a lysosomotropic peptide methyl ester. Stem Cells 12: 198-204, 1994.
    • (1994) Stem Cells , vol.12 , pp. 198-204
    • Rosenfeld, C.S.1
  • 111
    • 0032728949 scopus 로고    scopus 로고
    • Mechanism of apoptosis induced by lysosomotropic agent L-leucyl-L-leucine methyl ester
    • Uchimoto T, Nohara H, Kamehara R, Iwamura M, Watanabe N and Kobayashi T: Mechanism of apoptosis induced by lysosomotropic agent L-leucyl-L-leucine methyl ester. Apoptosis 4: 357-362, 1999.
    • (1999) Apoptosis , vol.4 , pp. 357-362
    • Uchimoto, T.1    Nohara, H.2    Kamehara, R.3    Iwamura, M.4    Watanabe, N.5    Kobayashi, T.6
  • 112
    • 0036152653 scopus 로고    scopus 로고
    • Design, synthesis, photochemical properties and cytotoxic activities of water-Soluble caged L-Leucyl-L-leucine methyl esters that control apoptosis of immune cells
    • DOI 10.1016/S0968-0896(01)00323-6, PII S0968089601003236
    • Mizuta H, Watanabe S, Sakurai Y, Nishiyama K, Furuta T, Kobayashi Y and Iwamura M: Design, synthesis, photochemical properties and cytotoxic activities of water-soluble caged Lleucyl-L-leucine methyl esters that control apoptosis of immune cells. Bioorg Med Chem 10: 675-683, 2002. (Pubitemid 34112460)
    • (2002) Bioorganic and Medicinal Chemistry , vol.10 , Issue.3 , pp. 675-683
    • Mizuta, H.1    Watanabe, S.2    Sakurai, Y.3    Nishiyama, K.4    Furuta, T.5    Kobayashi, Y.6    Iwamura, M.7
  • 113
    • 0028990047 scopus 로고
    • Tilorone-induced lysosomal storage of sulphated glycosaminoglycans can be separated from tilorone-induced enhancement of lysosomal enzyme secretion
    • Lullmann-Rauch R, Pods R and Von Witzendorff B: Tilorone-induced lysosomal storage of sulphated glycosaminoglycans can be separated from tilorone-induced enhancement of lysosomal enzyme secretion. Biochem Pharmacol 49: 1223-1233, 1995.
    • (1995) Biochem Pharmacol , vol.49 , pp. 1223-1233
    • Lullmann-Rauch, R.1    Pods, R.2    Von Witzendorff, B.3
  • 114
    • 0038641715 scopus 로고    scopus 로고
    • 3-Aminopropanal, formed during cerebral ischaemia, is a potent lysosomotropic neurotoxin
    • Li W, Yuan XM, Ivanova S, Tracey KJ, Eaton JW and Brunk UT: 3-Aminopropanal, formed during cerebral ischaemia, is a potent lysosomotropic neurotoxin. Biochem J 371: 429-436, 2003.
    • (2003) Biochem J , vol.371 , pp. 429-436
    • Li, W.1    Yuan, X.M.2    Ivanova, S.3    Tracey, K.J.4    Eaton, J.W.5    Brunk, U.T.6


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