메뉴 건너뛰기




Volumn 26, Issue 12, 2013, Pages 1782-1800

Toxicity of polyamines and their metabolic products

Author keywords

[No Author keywords available]

Indexed keywords

1,3 PROPANEDIAMINE; ACROLEIN; AMINE OXIDASE (COPPER CONTAINING); AMINE OXIDASE (FLAVIN CONTAINING); C REACTIVE PROTEIN; CADAVERINE; DIAMINE; GLUTATHIONE REDUCTASE; GLUTATHIONYLSPERMIDINE; HYDROGEN PEROXIDE; INTERLEUKIN 6; N METHYL DEXTRO ASPARTIC ACID RECEPTOR BLOCKING AGENT; N,N' BIS(2,3 BUTADIENYL)PUTRESCINE; N1 ACETYLSPERMIDINE; ORGANIC CATION TRANSPORTER; ORNITHINE; POLYAMINE DERIVATIVE; POLYAMINE OXIDASE; PROTECTIVE AGENT; PROTEIN; PUTRESCINE; REACTIVE OXYGEN METABOLITE; SMALL INTERFERING RNA; SPERMIDINE; SPERMINE; SUPEROXIDE DISMUTASE; TRYPANOTHIONE; TRYPANOTHIONE REDUCTASE; UNCLASSIFIED DRUG; POLYAMINE;

EID: 84890459089     PISSN: 0893228X     EISSN: 15205010     Source Type: Journal    
DOI: 10.1021/tx400316s     Document Type: Review
Times cited : (238)

References (243)
  • 2
    • 34547697846 scopus 로고    scopus 로고
    • Unique polyamines produced by an extreme thermophile, Thermus thermophilus
    • DOI 10.1007/s00726-007-0526-z, Special Issue: Polyamines and their Analogs in Cancer and other Diseases
    • Oshima, T. (2007) Unique polyamines produced by an extreme thermophile, Thermus thermophilus Amino Acids 33, 367-372 (Pubitemid 47222972)
    • (2007) Amino Acids , vol.33 , Issue.2 , pp. 367-372
    • Oshima, T.1
  • 5
    • 0037814710 scopus 로고    scopus 로고
    • Polycationic peptides from diatom biosilica that direct silica nanosphere formation
    • Kroger, N., Deutzmann, R., and Sumper, M. (1999) Polycationic peptides from diatom biosilica that direct silica nanosphere formation Science 286, 1129-1132
    • (1999) Science , vol.286 , pp. 1129-1132
    • Kroger, N.1    Deutzmann, R.2    Sumper, M.3
  • 7
    • 32944472627 scopus 로고    scopus 로고
    • Polyamine modulon in Escherichia coli: Genes involved in the stimulation of cell growth by polyamines
    • DOI 10.1093/jb/mvj020
    • Igarashi, K. and Kashiwagi, K. (2006) Polyamine modulon in Escherichia coli: Genes involved in the stimulation of cell growth by polyamines J. Biochem. (Tokyo) 139, 11-16 (Pubitemid 43258841)
    • (2006) Journal of Biochemistry , vol.139 , Issue.1 , pp. 11-16
    • Igarashi, K.1    Kashiwagi, K.2
  • 8
    • 70350344714 scopus 로고    scopus 로고
    • Polyamine modulon in yeast-Stimulation of COX4 synthesis by spermidine at the level of translation
    • Uemura, T., Higashi, K., Takigawa, M., Toida, T., Kashiwagi, K., and Igarashi, K. (2009) Polyamine modulon in yeast-Stimulation of COX4 synthesis by spermidine at the level of translation Int. J. Biochem. Cell Biol. 41, 2538-2545
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 2538-2545
    • Uemura, T.1    Higashi, K.2    Takigawa, M.3    Toida, T.4    Kashiwagi, K.5    Igarashi, K.6
  • 9
    • 65549167195 scopus 로고    scopus 로고
    • Hypusine-containing protein eIF5A promotes translation elongation
    • Saini, P., Eyler, D. E., Green, R., and Dever, T. E. (2009) Hypusine-containing protein eIF5A promotes translation elongation Nature 459, 118-121
    • (2009) Nature , vol.459 , pp. 118-121
    • Saini, P.1    Eyler, D.E.2    Green, R.3    Dever, T.E.4
  • 10
    • 84890496173 scopus 로고    scopus 로고
    • Functional significance of eIF5A and its hypusine modification in eukaryotes
    • Park, M. H., Nishimura, K., Zanelli, C. F., and Valentini, S. R. (2010) Functional significance of eIF5A and its hypusine modification in eukaryotes Amino Acids 41, 2538-2545
    • (2010) Amino Acids , vol.41 , pp. 2538-2545
    • Park, M.H.1    Nishimura, K.2    Zanelli, C.F.3    Valentini, S.R.4
  • 11
    • 0027984375 scopus 로고
    • Potassium channel block by cytoplasmic polyamines as the mechanism of intrinsic rectification
    • DOI 10.1038/372366a0
    • Lopatin, A. N., N., M. E., and Nichols, C. G. (1994) Potassium channel block by cytoplasmic polyamines as the mechanism of intrinsic rectification Nature 372, 366-369 (Pubitemid 24363439)
    • (1994) Nature , vol.372 , Issue.6504 , pp. 366-369
    • Lopatin, A.N.1    Makhina, E.N.2    Nichols, C.G.3
  • 12
    • 0030899291 scopus 로고    scopus 로고
    • Modulation and block of ion channels: A new biology of polyamines
    • DOI 10.1016/S0898-6568(96)00089-7, PII S0898656896000897
    • Williams, K. (1997) Modulation and block of ion channels: a new biology of polyamines Cell. Signalling 9, 1-13 (Pubitemid 27120861)
    • (1997) Cellular Signalling , vol.9 , Issue.1 , pp. 1-13
    • Williams, K.1
  • 13
    • 70350780368 scopus 로고    scopus 로고
    • Mammalian polyamine metabolism and function
    • Pegg, A. E. (2009) Mammalian polyamine metabolism and function IUBMB Life 61, 880-894
    • (2009) IUBMB Life , vol.61 , pp. 880-894
    • Pegg, A.E.1
  • 15
    • 0036163891 scopus 로고    scopus 로고
    • Essential role of S-adenosylmethionine decarboxylase in mouse embryonic development
    • DOI 10.1046/j.1356-9597.2001.00494.x
    • Nishimura, K., Nakatsu, F., Kashiwagi, K., Ohno, H., Saito, H., Saito, T., and Igarashi, K. (2002) Essential role of S -adenosylmethionine decarboxylase in mouse embryonic development Genes Cells 7, 41-47 (Pubitemid 34121304)
    • (2002) Genes to Cells , vol.7 , Issue.1 , pp. 41-47
    • Nishimura, K.1    Nakatsu, F.2    Kashiwagi, K.3    Ohno, H.4    Saito, T.5    Igarashi, K.6
  • 16
    • 10944225039 scopus 로고    scopus 로고
    • Spermine synthesis is required for normal viability, growth, and fertility in the mouse
    • DOI 10.1074/jbc.M410471200
    • Wang, X., Ikeguchi, Y., McCloskey, D. E., Nelson, P., and Pegg, A. E. (2004) Spermine synthesis is required for normal viability, growth and fertility in the mouse J. Biol. Chem. 49, 51370-51375 (Pubitemid 40017884)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 51370-51375
    • Wang, X.1    Ikeguchi, Y.2    McCloskey, D.E.3    Nelson, P.4    Pegg, A.E.5
  • 17
    • 73749085773 scopus 로고    scopus 로고
    • Mouse models to investigate the function of spermine
    • Pegg, A. E. and Wang, X. (2009) Mouse models to investigate the function of spermine Commun. Integr. Biol. 2, 271-274
    • (2009) Commun. Integr. Biol. , vol.2 , pp. 271-274
    • Pegg, A.E.1    Wang, X.2
  • 20
    • 79956280817 scopus 로고    scopus 로고
    • Spermine synthase deficiency resulting in X-linked intellectual disability (Snyder-Robinson syndrome)
    • Schwartz, C. E., Wang, X., Stevenson, R. E., and Pegg, A. E. (2011) Spermine synthase deficiency resulting in X-linked intellectual disability (Snyder-Robinson syndrome) Methods Mol. Biol. 720, 437-445
    • (2011) Methods Mol. Biol. , vol.720 , pp. 437-445
    • Schwartz, C.E.1    Wang, X.2    Stevenson, R.E.3    Pegg, A.E.4
  • 21
    • 18344418431 scopus 로고    scopus 로고
    • Spermine is not essential for growth of Saccharomyces cerevisiae: Identification of the SPE4 gene (spermine synthase) and characterization of a spe4 deletion mutant
    • Hamasaki-Katagiri, N., Katagiri, Y., Tabor, C. W., and Tabor, H. (1998) Spermine is not essential for growth of Saccharomyces cerevisiae: identification of the SPE4 gene (spermine synthase) and characterization of a spe4 deletion mutant Gene 210, 195-210
    • (1998) Gene , vol.210 , pp. 195-210
    • Hamasaki-Katagiri, N.1    Katagiri, Y.2    Tabor, C.W.3    Tabor, H.4
  • 22
    • 23944478337 scopus 로고    scopus 로고
    • Oxidative metabolites are involved in polyamine-induced microglial cell death
    • DOI 10.1016/j.neuroscience.2005.05.014, PII S0306452205005531
    • Takano, K., Ogura, M., Yoneda, Y., and Nakamura, Y. (2005) Oxidative metabolites are involved in polyamine-induced microglial cell death Neuroscience 134, 1123-1131 (Pubitemid 41207365)
    • (2005) Neuroscience , vol.134 , Issue.4 , pp. 1123-1131
    • Takano, K.1    Ogura, M.2    Yoneda, Y.3    Nakamura, Y.4
  • 25
    • 79955606518 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor (eIF) 5A stimulates protein synthesis in Saccharomyces cerevisiae
    • Henderson, A. and Hershey, J. W. (2011) Eukaryotic translation initiation factor (eIF) 5A stimulates protein synthesis in Saccharomyces cerevisiae Proc. Natl. Acad. Sci. U.S.A. 108, 6415-6419
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 6415-6419
    • Henderson, A.1    Hershey, J.W.2
  • 27
  • 28
    • 0014010850 scopus 로고
    • Multiple pathways of putrescine biosynthesis in Escherichia coli
    • Morris, D. R. and Pardee, A. B. (1966) Multiple pathways of putrescine biosynthesis in Escherichia coli J. Biol. Chem. 241, 3129-3135
    • (1966) J. Biol. Chem. , vol.241 , pp. 3129-3135
    • Morris, D.R.1    Pardee, A.B.2
  • 29
    • 0036402941 scopus 로고    scopus 로고
    • Regulation of enzymes of the urea cycle and arginine metabolism
    • Morris, S. M. J. (2002) Regulation of enzymes of the urea cycle and arginine metabolism Annu. Rev. Nutr. 22, 87-105
    • (2002) Annu. Rev. Nutr. , vol.22 , pp. 87-105
    • Morris, S.M.J.1
  • 30
    • 9644279544 scopus 로고    scopus 로고
    • Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily
    • DOI 10.1074/jbc.M409246200
    • Ahn, H. J., Kim, K. H., Lee, J., Ha, J. Y., Lee, H. H., Kim, D., Yoon, H. J., Kwon, A. R., and Suh, S. W. (2004) Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily J. Biol. Chem. 279, 50505-50513 (Pubitemid 39577869)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.48 , pp. 50505-50513
    • Hyung, J.A.1    Kyoung, H.K.2    Lee, J.3    Ha, J.-Y.4    Hyung, H.L.5    Kim, D.6    Yoon, H.-J.7    Kwon, A.-R.8    Se, W.S.9
  • 31
    • 79953185435 scopus 로고    scopus 로고
    • The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase
    • Landete, J. M., Arena, M. E., Pardo, I., Manca de Nadra, M. C., and Ferrer, S. (2010) The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase Int. Microbiol. 13, 169-177
    • (2010) Int. Microbiol. , vol.13 , pp. 169-177
    • Landete, J.M.1    Arena, M.E.2    Pardo, I.3    Manca De Nadra, M.C.4    Ferrer, S.5
  • 32
    • 80051572800 scopus 로고    scopus 로고
    • Independent evolutionary origins of functional polyamine biosynthetic enzyme fusions catalysing de novo diamine to triamine formation
    • Green, R., Hanfrey, C. C., Elliott, K. A., McCloskey, D. E., Wang, X., Kanugula, S., Pegg, A. E., and Michael, A. J. (2011) Independent evolutionary origins of functional polyamine biosynthetic enzyme fusions catalysing de novo diamine to triamine formation Mol. Microbiol. 81, 1109-1124
    • (2011) Mol. Microbiol. , vol.81 , pp. 1109-1124
    • Green, R.1    Hanfrey, C.C.2    Elliott, K.A.3    McCloskey, D.E.4    Wang, X.5    Kanugula, S.6    Pegg, A.E.7    Michael, A.J.8
  • 33
    • 65649147535 scopus 로고    scopus 로고
    • An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae
    • Lee, J., Sperandio, V., Frantz, D. E., Longgood, J., Camilli, A., Phillips, M. A., and Michael, A. J. (2009) An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae J. Biol. Chem. 284, 9899-9907
    • (2009) J. Biol. Chem. , vol.284 , pp. 9899-9907
    • Lee, J.1    Sperandio, V.2    Frantz, D.E.3    Longgood, J.4    Camilli, A.5    Phillips, M.A.6    Michael, A.J.7
  • 34
    • 0027244509 scopus 로고
    • Purification and characterization of homospermidine synthase in Acinetobacter tartarogenes ATCC 31105
    • Yamamoto, S., Nagata, S., and Kusaba, K. (1993) Purification and characterization of homospermidine synthase in Acinetobacter tartarogenes ATCC 31105 J. Biochem. 114, 45-49 (Pubitemid 23235630)
    • (1993) Journal of Biochemistry , vol.114 , Issue.1 , pp. 45-49
    • Yamamoto, S.1    Nagata, S.2    Kusaba, K.3
  • 35
    • 0038305967 scopus 로고    scopus 로고
    • Molecular evolution by change of function: Alkaloid-specific homospermidine synthase retained all properties of deoxyhypusine synthase except binding the eIF5a precursor protein
    • DOI 10.1074/jbc.M207112200
    • Ober, D., Harms, R., Witte, L., and Hartmann, T. (2003) Molecular evolution by change of function. Alkaloid-specific homospermidine synthase retained all properties of deoxyhypusine synthase except binding the eIF5A precursor protein J. Biol. Chem. 278, 12805-12812 (Pubitemid 36800044)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 12805-12812
    • Ober, D.1    Harms, R.2    Witte, L.3    Hartmann, T.4
  • 36
    • 0000470880 scopus 로고
    • The biosynthesis of spermidine and spermine from putrescine and methionine
    • Tabor, H., Rosenthal, S. M., and Tabor, C. W. (1958) The biosynthesis of spermidine and spermine from putrescine and methionine J. Biol. Chem. 233, 907-914
    • (1958) J. Biol. Chem. , vol.233 , pp. 907-914
    • Tabor, H.1    Rosenthal, S.M.2    Tabor, C.W.3
  • 37
    • 0020215250 scopus 로고
    • Polyamine metabolism and function
    • Pegg, A. E. and McCann, P. P. (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
  • 38
    • 0022450919 scopus 로고
    • Recent advances in the biochemistry of polyamines in eukaryocytes
    • Pegg, A. E. (1986) Recent advances in the biochemistry of polyamines in eukaryotes Biochem. J. 234, 249-262 (Pubitemid 16049822)
    • (1986) Biochemical Journal , vol.234 , Issue.2 , pp. 249-262
    • Pegg, A.E.1
  • 40
    • 32944472945 scopus 로고    scopus 로고
    • Aminopropyltransferases: Function, structure and genetics
    • DOI 10.1093/jb/mvj019
    • Ikeguchi, Y., Bewley, M., and Pegg, A. E. (2006) Aminopropyltransferases: function, structure and genetics J. Biochem. (Tokyo) 139, 1-9 (Pubitemid 43258840)
    • (2006) Journal of Biochemistry , vol.139 , Issue.1 , pp. 1-9
    • Ikeguchi, Y.1    Bewley, M.C.2    Pegg, A.E.3
  • 42
    • 84859743777 scopus 로고    scopus 로고
    • Thermospermine is not a minor polyamine in the plant kingdom
    • Takano, A., Kakehi, J., and Takahashi, T. (2012) Thermospermine is not a minor polyamine in the plant kingdom Plant Cell Physiol. 53, 606-616
    • (2012) Plant Cell Physiol. , vol.53 , pp. 606-616
    • Takano, A.1    Kakehi, J.2    Takahashi, T.3
  • 43
    • 84961011913 scopus 로고
    • Pharmacology of spermine and spermidine; Some effects on animals and bacteria
    • Tabor, C. W. and Rosenthal, S. M. (1956) Pharmacology of spermine and spermidine; some effects on animals and bacteria J. Pharmacol. Exp. Ther. 116, 139-155
    • (1956) J. Pharmacol. Exp. Ther. , vol.116 , pp. 139-155
    • Tabor, C.W.1    Rosenthal, S.M.2
  • 44
    • 0022001625 scopus 로고
    • Polyamines in microorganisms
    • Tabor, C. W. and Tabor, H. (1985) Polyamines in microorganisms Microbiol. Rev. 49, 81-99 (Pubitemid 15134122)
    • (1985) Microbiological Reviews , vol.49 , Issue.1 , pp. 81-99
    • Tabor, C.W.1    Tabor, H.2
  • 45
    • 0025872465 scopus 로고
    • A new perspective on ornithine decarboxylase regulation: Prevention of polyamine toxicity is the overriding theme
    • Morris, D. R., Davis, R., and Coffino, P. (1991) A new perspective on ornithine decarboxylase regulation: Prevention of polyamine toxicity is the overriding theme J. Cell. Biochem. 46, 102-105
    • (1991) J. Cell. Biochem. , vol.46 , pp. 102-105
    • Morris, D.R.1    Davis, R.2    Coffino, P.3
  • 46
    • 76549179643 scopus 로고
    • Nicolas Louis Vauquelin (1763-1829)
    • Williams-Ashman, H. G. (1965) Nicolas Louis Vauquelin (1763-1829) Invest. Urol. 2, 605-613
    • (1965) Invest. Urol. , vol.2 , pp. 605-613
    • Williams-Ashman, H.G.1
  • 47
    • 0000029613 scopus 로고
    • Observationes D. Antonii Lewenhoeck, de Natis e semine genitali Animalculis
    • Leeuwenhoek, A. (1678) Observationes D. Antonii Lewenhoeck, de Natis e semine genitali Animalculis Philos. Trans. R. Soc. 12, 1040-1048
    • (1678) Philos. Trans. R. Soc. , vol.12 , pp. 1040-1048
    • Leeuwenhoek, A.1
  • 48
    • 0016593558 scopus 로고
    • Oxidation of polymines by diamine oxidase from human seminal plasma
    • Hölttä, E., Pulkkinen, P., Elfving, K., and Jänne, J. (1975) Oxidation of polymines by diamine oxidase from human seminal plasma Biochem. J. 145, 373-378
    • (1975) Biochem. J. , vol.145 , pp. 373-378
    • Hölttä, E.1    Pulkkinen, P.2    Elfving, K.3    Jänne, J.4
  • 49
    • 84883367140 scopus 로고    scopus 로고
    • Identification of a role for a mouse sperm surface aldo-keto reductase (AKR1B7) and its human analogue in the detoxification of the reactive aldehyde, acrolein
    • Jagoe, W. N., Howe, K., O'Brien, S. C., and Carroll, J. (2013) Identification of a role for a mouse sperm surface aldo-keto reductase (AKR1B7) and its human analogue in the detoxification of the reactive aldehyde, acrolein Andrologia 45, 326-331
    • (2013) Andrologia , vol.45 , pp. 326-331
    • Jagoe, W.N.1    Howe, K.2    O'Brien, S.C.3    Carroll, J.4
  • 50
    • 33744951504 scopus 로고    scopus 로고
    • Regulation of ornithine decarboxylase
    • DOI 10.1074/jbc.R500031200
    • Pegg, A. E. (2006) Regulation of ornithine decarboxylase J. Biol. Chem. 281, 14529-14532 (Pubitemid 43855154)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.21 , pp. 14529-14532
    • Pegg, A.E.1
  • 51
    • 69249245459 scopus 로고    scopus 로고
    • Polyamine catabolism and disease
    • Casero, R. A., Jr. and Pegg, A. E. (2009) Polyamine catabolism and disease Biochem. J. 421, 323-338
    • (2009) Biochem. J. , vol.421 , pp. 323-338
    • Casero Jr., R.A.1    Pegg, A.E.2
  • 52
    • 77449090048 scopus 로고    scopus 로고
    • Regulation of cellular polyamine levels and cellular proliferation by antizyme and antizyme inhibitor
    • Kahana, C. (2009) Regulation of cellular polyamine levels and cellular proliferation by antizyme and antizyme inhibitor Essays Biochem. 46, 47-61
    • (2009) Essays Biochem. , vol.46 , pp. 47-61
    • Kahana, C.1
  • 53
    • 77449159833 scopus 로고    scopus 로고
    • S -Adenosylmethionine decarboxylase
    • Pegg, A. E. (2009) S -Adenosylmethionine decarboxylase Essays Biochem. 46, 25-45
    • (2009) Essays Biochem. , vol.46 , pp. 25-45
    • Pegg, A.E.1
  • 54
    • 0032433866 scopus 로고    scopus 로고
    • S-adenosylmethionine decarboxylase: Structure, function and regulation by polyamines
    • Pegg, A. E., Xiong, H., Feith, D., and Shantz, L. M. (1998) S -Adenosylmethionine decarboxylase: structure, function and regulation by polyamines Biochem. Soc. Trans. 26, 580-586 (Pubitemid 29008128)
    • (1998) Biochemical Society Transactions , vol.26 , Issue.4 , pp. 580-586
    • Pegg, A.E.1    Xiong, H.2    Feith, D.J.3    Shantz, L.M.4
  • 55
    • 0037155130 scopus 로고    scopus 로고
    • Regulated translation termination at the upstream open reading frame in S-adenosylmethionine decarboxylase mRNA
    • DOI 10.1074/jbc.M108375200
    • Raney, A., Law, G. L., Mize, G. J., and Morris, D. R. (2002) Regulated translation termination at the upstream open reading frame in S -adenosylmethionine decarboxylase mRNA J. Biol. Chem. 277, 5988-5994 (Pubitemid 34968381)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.8 , pp. 5988-5994
    • Raney, A.1    Lynn Law, G.2    Mize, G.J.3    Morris, D.R.4
  • 56
    • 28244500966 scopus 로고    scopus 로고
    • A dual upstream open reading frame-based autoregulatory circuit controlling polyamine-responsive translation
    • DOI 10.1074/jbc.M509340200
    • Hanfrey, C., Elliott, K. A., Franceschetti, M., Mayer, M. J., Illingworth, C., and Michael, A. J. (2005) A dual upstream open reading frame-based autoregulatory circuit controlling polyamine-responsive translation J. Biol. Chem. 280, 39229-39237 (Pubitemid 41713875)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39229-39237
    • Hanfrey, C.1    Elliott, K.A.2    Franceschetti, M.3    Mayer, M.J.4    Illingworth, C.5    Michael, A.J.6
  • 57
    • 34547671110 scopus 로고    scopus 로고
    • Ubiquitin dependent and independent protein degradation in the regulation of cellular polyamines
    • DOI 10.1007/s00726-007-0519-y, Special Issue: Polyamines and their Analogs in Cancer and other Diseases
    • Kahana, C. (2007) Ubiquitin dependent and independent protein degradation in the regulation of cellular polyamines Amino Acids 33, 225-230 (Pubitemid 47222965)
    • (2007) Amino Acids , vol.33 , Issue.2 , pp. 225-230
    • Kahana, C.1
  • 58
    • 57649134245 scopus 로고    scopus 로고
    • Structural basis for putrescine activation of human S-adenosylmethionine decarboxylase
    • Bale, S., Lopez, M. M., Makhatadze, G. I., Fang, Q., Pegg, A. E., and Ealick, S. E. (2008) Structural basis for putrescine activation of human S-adenosylmethionine decarboxylase Biochemistry 47, 13404-13417
    • (2008) Biochemistry , vol.47 , pp. 13404-13417
    • Bale, S.1    Lopez, M.M.2    Makhatadze, G.I.3    Fang, Q.4    Pegg, A.E.5    Ealick, S.E.6
  • 59
    • 68749099370 scopus 로고    scopus 로고
    • Cross-species activation of trypanosome S-adenosylmethionine decarboxylase by the regulatory subunit Prozyme
    • Willert, E. K. and Phillips, M. A. (2009) Cross-species activation of trypanosome S-adenosylmethionine decarboxylase by the regulatory subunit Prozyme Mol. Biochem. Parasitol. 168, 1-6
    • (2009) Mol. Biochem. Parasitol. , vol.168 , pp. 1-6
    • Willert, E.K.1    Phillips, M.A.2
  • 60
    • 0019876646 scopus 로고
    • Properties of spermidine N -acetyltransferase from livers of rats treated with carbon tetrachloride and its role in the conversion of spermidine into putrescine
    • Matsui, I., Wiegand, L., and Pegg, A. E. (1981) Properties of spermidine N -acetyltransferase from livers of rats treated with carbon tetrachloride and its role in the conversion of spermidine into putrescine J. Biol. Chem. 256, 2454-2459
    • (1981) J. Biol. Chem. , vol.256 , pp. 2454-2459
    • Matsui, I.1    Wiegand, L.2    Pegg, A.E.3
  • 61
    • 0027238083 scopus 로고
    • 1-acetyltransferase - The turning point in polyamine metabolism
    • 1-acetyltransferase: the turning point in polyamine metabolism FASEB J. 7, 653-661 (Pubitemid 23163600)
    • (1993) FASEB Journal , vol.7 , Issue.8 , pp. 653-661
    • Casero Jr., R.A.1    Pegg, A.E.2
  • 62
    • 47549106852 scopus 로고    scopus 로고
    • 1-acetyltransferase: A key metabolic regulator
    • 1-acetyltransferase: a key metabolic regulator Am. J. Physiol. Endocrinol. Metab. 294, E995-1010
    • (2008) Am. J. Physiol. Endocrinol. Metab. , vol.294 , pp. 995-1010
    • Pegg, A.E.1
  • 66
    • 1542284582 scopus 로고    scopus 로고
    • Genetic approaches to the cellular functions of polyamines in mammals
    • DOI 10.1111/j.1432-1033.2004.04009.x
    • Jänne, J., Alhonen, L., Pietilä, M., and Keinänen, T. (2004) Genetic approaches to the cellular functions of polyamines in mammals Eur. J. Biochem. 271, 877-894 (Pubitemid 38299643)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.5 , pp. 877-894
    • Janne, J.1    Alhonen, L.2    Pietila, M.3    Keinanen, T.A.4
  • 68
    • 77955649337 scopus 로고    scopus 로고
    • Polyamine transport is mediated by both endocytic and solute carrier transport mechanisms in the gastrointestinal tract
    • Uemura, T., Stringer, D. E., Blohm-Mangone, K. A., and Gerner, E. W. (2010) Polyamine transport is mediated by both endocytic and solute carrier transport mechanisms in the gastrointestinal tract Am. J. Physiol. Gastrointest. Liver Physiol. 299, G517-522
    • (2010) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.299 , pp. 517-522
    • Uemura, T.1    Stringer, D.E.2    Blohm-Mangone, K.A.3    Gerner, E.W.4
  • 70
    • 84861677889 scopus 로고    scopus 로고
    • Recent advances in the molecular biology of metazoan polyamine transport
    • Poulin, R., Casero, R. A., and Soulet, D. (2012) Recent advances in the molecular biology of metazoan polyamine transport Amino Acids 42, 711-723
    • (2012) Amino Acids , vol.42 , pp. 711-723
    • Poulin, R.1    Casero, R.A.2    Soulet, D.3
  • 71
    • 0014908465 scopus 로고
    • Metabolism and function of spermine and related polyamines
    • Bachrach, U. (1970) Metabolism and function of spermine and related polyamines Annu. Rev. Microbiol. 24, 109-134
    • (1970) Annu. Rev. Microbiol. , vol.24 , pp. 109-134
    • Bachrach, U.1
  • 73
    • 0032416352 scopus 로고    scopus 로고
    • Polyamine oxidases-enzymes of unknown function?
    • Morgan, D. M. (1998) Polyamine oxidases-enzymes of unknown function? Biochem. Soc. Trans. 26, 586-591
    • (1998) Biochem. Soc. Trans. , vol.26 , pp. 586-591
    • Morgan, D.M.1
  • 74
    • 3042653176 scopus 로고    scopus 로고
    • Catabolism of polyamines
    • Seiler, N. (2004) Catabolism of polyamines Amino Acids 26, 217-233 (Pubitemid 38829785)
    • (2004) Amino Acids , vol.26 , Issue.3 , pp. 217-233
    • Seiler, N.1
  • 76
    • 79951950697 scopus 로고    scopus 로고
    • The structure of maize polyamine oxidase K300M mutant in complex with the natural substrates provides a snapshot of the catalytic mechanism of polyamine oxidation
    • Fiorillo, A., Federico, R., Polticelli, F., Boffi, A., Mazzei, F., Di Fusco, M., Ilari, A., and Tavladoraki, P. (2011) The structure of maize polyamine oxidase K300M mutant in complex with the natural substrates provides a snapshot of the catalytic mechanism of polyamine oxidation FEBS J. 278, 809-821
    • (2011) FEBS J. , vol.278 , pp. 809-821
    • Fiorillo, A.1    Federico, R.2    Polticelli, F.3    Boffi, A.4    Mazzei, F.5    Di Fusco, M.6    Ilari, A.7    Tavladoraki, P.8
  • 77
    • 84866518900 scopus 로고    scopus 로고
    • Mechanistic studies of the role of a conserved histidine in a mammalian polyamine oxidase
    • Tormos, J. R., Henderson Pozzi, M., and Fitzpatrick, P. F. (2012) Mechanistic studies of the role of a conserved histidine in a mammalian polyamine oxidase Arch. Biochem. Biophys. 528, 45-49
    • (2012) Arch. Biochem. Biophys. , vol.528 , pp. 45-49
    • Tormos, J.R.1    Henderson Pozzi, M.2    Fitzpatrick, P.F.3
  • 78
    • 84861662550 scopus 로고    scopus 로고
    • The members of Arabidopsis thaliana PAO gene family exhibit distinct tissue- and organ-specific expression pattern during seedling growth and flower development
    • Fincato, P., Moschou, P. N., Ahou, A., Angelini, R., Roubelakis- Angelakis, K. A., Federico, R., and Tavladoraki, P. (2012) The members of Arabidopsis thaliana PAO gene family exhibit distinct tissue- and organ-specific expression pattern during seedling growth and flower development Amino Acids 42, 831-841
    • (2012) Amino Acids , vol.42 , pp. 831-841
    • Fincato, P.1    Moschou, P.N.2    Ahou, A.3    Angelini, R.4    Roubelakis-Angelakis, K.A.5    Federico, R.6    Tavladoraki, P.7
  • 79
    • 84866883593 scopus 로고    scopus 로고
    • A mass spectrometric method to determine activities of enzymes involved in polyamine catabolism
    • Moriya, S., Iwasaki, K., Samejima, K., Takao, K., Kohda, K., Hiramatsu, K., and Kawakita, M. (2012) A mass spectrometric method to determine activities of enzymes involved in polyamine catabolism Anal. Chim. Acta 748, 45-52
    • (2012) Anal. Chim. Acta , vol.748 , pp. 45-52
    • Moriya, S.1    Iwasaki, K.2    Samejima, K.3    Takao, K.4    Kohda, K.5    Hiramatsu, K.6    Kawakita, M.7
  • 80
    • 84982334045 scopus 로고
    • Uber den enzymatischen abbau von histamin und diaminen
    • Zeller, E. A. (1938) Uber den enzymatischen abbau von histamin und diaminen Helv. Chim. Acta 21, 880-890
    • (1938) Helv. Chim. Acta , vol.21 , pp. 880-890
    • Zeller, E.A.1
  • 81
    • 0013979088 scopus 로고
    • Histaminase and related amine oxidases
    • Buffoni, F. (1966) Histaminase and related amine oxidases Pharmacol. Rev. 18, 1163-1199
    • (1966) Pharmacol. Rev. , vol.18 , pp. 1163-1199
    • Buffoni, F.1
  • 83
    • 0034126310 scopus 로고    scopus 로고
    • Oxidation of polyamines and brain injury
    • DOI 10.1023/A:1007508008731
    • Seiler, N. (2000) Oxidation of polyamines and brain injury Neurochem. Res. 2000, 471-490 (Pubitemid 30317680)
    • (2000) Neurochemical Research , vol.25 , Issue.4 , pp. 471-490
    • Seiler, N.1
  • 84
    • 0000590881 scopus 로고
    • Identification of the aminoaldehydes produced by the oxidation of spermine and spermidine with purified plasma amine oxidase
    • Tabor, C. W., Tabor, H., and Bachrach, U. (1964) Identification of the aminoaldehydes produced by the oxidation of spermine and spermidine with purified plasma amine oxidase J. Biol. Chem. 239, 2194-2203
    • (1964) J. Biol. Chem. , vol.239 , pp. 2194-2203
    • Tabor, C.W.1    Tabor, H.2    Bachrach, U.3
  • 85
    • 0041333378 scopus 로고
    • Observations on spermine oxidase of mammalian plasma
    • Blaschko, H. and Hawes, R. (1959) Observations on spermine oxidase of mammalian plasma J. Physiol. 145, 124-131
    • (1959) J. Physiol. , vol.145 , pp. 124-131
    • Blaschko, H.1    Hawes, R.2
  • 86
    • 0032584718 scopus 로고    scopus 로고
    • Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini
    • DOI 10.1074/jbc.273.31.19490
    • Lee, Y. and Sayre, L. M. (1998) Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini J. Biol. Chem. 273, 19490-19494 (Pubitemid 28366999)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.31 , pp. 19490-19494
    • Lee, Y.1    Sayre, L.M.2
  • 89
    • 0021920139 scopus 로고
    • The influence of catabolic reactions on polyamine excretion
    • Seiler, N., Bolkenius, F. N., and Knödgen, B. (1985) The influence of catabolic reactions on polyamine excretion Biochem. J. 225, 219-226 (Pubitemid 15151972)
    • (1985) Biochemical Journal , vol.225 , Issue.1 , pp. 219-226
    • Seiler, N.1    Bolkenius, F.N.2    Knodgen, B.3
  • 90
    • 0017623867 scopus 로고
    • Oxidation of spermidine and spermine in rat liver: Purification and properties of polyamine oxidase
    • Hölttä, E. (1977) Oxidation of spermidine and spermine in rat liver: purification and properties of polyamine oxidase Biochemistry 16, 91-100
    • (1977) Biochemistry , vol.16 , pp. 91-100
    • Hölttä, E.1
  • 92
    • 61749094173 scopus 로고    scopus 로고
    • PH Dependence of a mammalian polyamine oxidase: Insights into substrate specificity and the role of lysine 315
    • Henderson Pozzi, M., Gawandi, V., and Fitzpatrick, P. F. (2009) pH Dependence of a mammalian polyamine oxidase: insights into substrate specificity and the role of lysine 315 Biochemistry 48, 1508-1516
    • (2009) Biochemistry , vol.48 , pp. 1508-1516
    • Henderson Pozzi, M.1    Gawandi, V.2    Fitzpatrick, P.F.3
  • 94
    • 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, P. M., Stewart, T. M., Hacker, A., and Casero, R. A., Jr. (2001) Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure Cancer Res. 61, 5370-5373 (Pubitemid 32694912)
    • (2001) Cancer Research , vol.61 , Issue.14 , 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
  • 96
    • 0036846756 scopus 로고    scopus 로고
    • Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin
    • DOI 10.1042/BJ20020720
    • Vujcic, S., Diegelman, P., Bacchi, C. J., Kramer, D. L., and Porter, C. W. (2002) Indentification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin Biochem. J. 367, 665-675 (Pubitemid 35305705)
    • (2002) Biochemical Journal , vol.367 , Issue.3 , pp. 665-675
    • Vujcic, S.1    Diegelman, P.2    Bacchi, C.J.3    Kramer, D.L.4    Porter, C.W.5
  • 98
    • 79956227428 scopus 로고    scopus 로고
    • A simple assay for mammalian spermine oxidase: A polyamine catabolic enzyme implicated in drug response and disease
    • Goodwin, A. C., Murray-Stewart, T. R., and Casero, R. A., Jr. (2011) A simple assay for mammalian spermine oxidase: a polyamine catabolic enzyme implicated in drug response and disease Methods Mol. Biol. 720, 173-181
    • (2011) Methods Mol. Biol. , vol.720 , pp. 173-181
    • Goodwin, A.C.1    Murray-Stewart, T.R.2    Casero Jr., R.A.3
  • 99
    • 75349100932 scopus 로고    scopus 로고
    • Mechanistic studies of human spermine oxidase: Kinetic mechanism and pH effects
    • Adachi, M. S., Juarez, P. R., and Fitzpatrick, P. F. (2010) Mechanistic studies of human spermine oxidase: kinetic mechanism and pH effects Biochemistry 49, 386-392
    • (2010) Biochemistry , vol.49 , pp. 386-392
    • Adachi, M.S.1    Juarez, P.R.2    Fitzpatrick, P.F.3
  • 100
    • 43549112141 scopus 로고    scopus 로고
    • Nuclear localization of human spermine oxidase isoforms - Possible implications in drug response and disease etiology
    • DOI 10.1111/j.1742-4658.2008.06419.x
    • Murray-Stewart, T., Wang, Y., Goodwin, A., Hacker, A., Meeker, A., and Casero, R. A., Jr. (2008) Nuclear localization of human spermine oxidase isoforms-possible implications in drug response and disease etiology FEBS J. 275, 2795-2806 (Pubitemid 351678666)
    • (2008) FEBS Journal , vol.275 , Issue.11 , pp. 2795-2806
    • Murray-Stewart, T.1    Wang, Y.2    Goodwin, A.3    Hacker, A.4    Meeker, A.5    Casero Jr., R.A.6
  • 104
    • 17444422874 scopus 로고    scopus 로고
    • Crystal structures of Fms1 and its complex with spermine reveal substrate specificity
    • DOI 10.1016/j.jmb.2005.03.008
    • Huang, Q., Liu, Q., and Hao, Q. (2005) Crystal structures of Fms1 and its complex with spermine reveal substrate specificity J. Mol. Biol. 348, 951-959 (Pubitemid 40544394)
    • (2005) Journal of Molecular Biology , vol.348 , Issue.4 , pp. 951-959
    • Huang, Q.1    Liu, Q.2    Hao, Q.3
  • 105
    • 84868093877 scopus 로고    scopus 로고
    • Mechanistic and structural analyses of the roles of active site residues in yeast polyamine oxidase Fms1: Characterization of the N195A and D94N enzymes
    • Adachi, M. S., Taylor, A. B., Hart, P. J., and Fitzpatrick, P. F. (2012) Mechanistic and structural analyses of the roles of active site residues in yeast polyamine oxidase Fms1: characterization of the N195A and D94N enzymes Biochemistry 51, 8690-8697
    • (2012) Biochemistry , vol.51 , pp. 8690-8697
    • Adachi, M.S.1    Taylor, A.B.2    Hart, P.J.3    Fitzpatrick, P.F.4
  • 106
    • 0021989550 scopus 로고
    • N-2,3-butadienyl-1,4-butanediamine derivatives: Potent irreversible inactivators of mammalian polyamine oxidase
    • DOI 10.1021/jm00379a001
    • Bey, P., Bolkenius, F. N., Seiler, N., and Casara, P. (1985) N -2,3-Butadienyl-1,4-butanediamine derivatives: potent irreversible inactivators of mammalian polyamine oxidase J. Med. Chem. 28, 1-2 (Pubitemid 15156285)
    • (1985) Journal of Medicinal Chemistry , vol.28 , Issue.1 , pp. 1-2
    • Bey, P.1    Bolkenius, F.N.2    Seiler, N.3    Casara, P.4
  • 107
    • 0021957073 scopus 로고
    • Specific inhibition of polyamine oxidase in vivo is a method for the elucidation of its physiological role
    • DOI 10.1016/0304-4165(85)90251-X
    • Bolkenius, F. N., Bey, P., and Seiler, N. (1985) Specific inhibition of polyamine oxidase in vivo is a method for the elucidation of its physiological role Biochim. Biophys. Acta 838, 69-76 (Pubitemid 15127950)
    • (1985) Biochimica et Biophysica Acta - General Subjects , vol.838 , Issue.1 , pp. 69-76
    • Bolkenius, F.N.1    Bey, P.2    Seiler, N.3
  • 108
    • 0036389837 scopus 로고    scopus 로고
    • The polyamine oxidase inactivator MDL 72527
    • Seiler, N., Duranton, B., and Raul, F. (2002) The polyamine oxidase inactivator MDL 72527 Prog. Drug Res. 59, 1-40
    • (2002) Prog. Drug Res. , vol.59 , pp. 1-40
    • Seiler, N.1    Duranton, B.2    Raul, F.3
  • 111
    • 33644785135 scopus 로고    scopus 로고
    • Inhibition of polyamine and spermine oxidases by polyamine analogues
    • DOI 10.1111/j.1742-4658.2006.05137.x
    • Bianchi, M., Polticelli, F., Ascenzi, P., Botta, M., Federico, R., Mariottini, P., and Cona, A. (2006) Inhibition of polyamine and spermine oxidases by polyamine analogues FEBS J. 273, 1115-1123 (Pubitemid 43345033)
    • (2006) FEBS Journal , vol.273 , Issue.6 , pp. 1115-1123
    • Bianchi, M.1    Polticelli, F.2    Ascenzi, P.3    Botta, M.4    Federico, R.5    Mariottini, P.6    Cona, A.7
  • 112
    • 0026092925 scopus 로고
    • On the degradation and elimination of spermine by the vertebrate organism
    • Sarhan, S., Quemener, V., Moulinoux, J. P., Knödgen, B., and Seiler, N. (1991) On the degradation and elimination of spermine by the vertebrate organism Int. J. Biochem. 23, 617-626
    • (1991) Int. J. Biochem. , vol.23 , pp. 617-626
    • Sarhan, S.1    Quemener, V.2    Moulinoux, J.P.3    Knödgen, B.4    Seiler, N.5
  • 113
    • 4344702219 scopus 로고    scopus 로고
    • Characterization of transgenic mice with widespread overexpression of spermine synthase
    • DOI 10.1042/BJ20040419
    • Ikeguchi, Y., Wang, X., McCloskey, D. E., Coleman, C. S., Nelson, P., Hu, G., Shantz, L. M., and Pegg, A. E. (2004) Characterization of transgenic mice with widespread overexpression of spermine synthase Biochem. J. 381, 701-707 (Pubitemid 39120479)
    • (2004) Biochemical Journal , vol.381 , Issue.3 , pp. 701-707
    • Ikeguchi, Y.1    Wang, X.2    McCloskey, D.E.3    Coleman, C.S.4    Nelson, P.5    Hu, G.6    Shantz, L.M.7    Pegg, A.E.8
  • 115
    • 0025785329 scopus 로고
    • Human aldehyde dehydrogenase: Activity with aldehyde metabolites of monoamines, diamines, and polyamines
    • Ambroziak, W. and Pietruszko, R. (1991) Human aldehyde dehydrogenase. Activity with aldehyde metabolites of monoamines, diamines, and polyamines J. Biol. Chem. 266, 13011-13018 (Pubitemid 21907301)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.20 , pp. 13011-13018
    • Ambroziak, W.1    Pietruszko, R.2
  • 116
    • 0009736856 scopus 로고
    • Isolation of acrolein from incubated mixtures of spermine with calf serum and its effects on mammalian cells
    • Alarcon, R. A. (1964) Isolation of acrolein from incubated mixtures of spermine with calf serum and its effects on mammalian cells Arch. Biochem. Biophys. 106, 240-242
    • (1964) Arch. Biochem. Biophys. , vol.106 , pp. 240-242
    • Alarcon, R.A.1
  • 117
    • 0014984818 scopus 로고
    • Preparation and stability of oxidized polyamines
    • Kimes, B. W. and Morris, D. R. (1971) Preparation and stability of oxidized polyamines Biochim. Biophys. Acta 228, 223-234
    • (1971) Biochim. Biophys. Acta , vol.228 , pp. 223-234
    • Kimes, B.W.1    Morris, D.R.2
  • 118
    • 0014981738 scopus 로고
    • Inhibition of nucleic acid and protein synthesis in Escherichia coli by oxidized polyamines and acrolein
    • Kimes, B. W. and Morris, D. R. (1971) Inhibition of nucleic acid and protein synthesis in Escherichia coli by oxidized polyamines and acrolein Biochim. Biophys. Acta 228, 235-244
    • (1971) Biochim. Biophys. Acta , vol.228 , pp. 235-244
    • Kimes, B.W.1    Morris, D.R.2
  • 119
    • 0015189502 scopus 로고
    • Antivirus action of acrolein, glutaraldehyde and oxidized spermine
    • Bachrach, U., Don, S., and Wiener, H. (1971) Antivirus action of acrolein, glutaraldehyde and oxidized spermine J. Gen. Virol. 13, 415-422
    • (1971) J. Gen. Virol. , vol.13 , pp. 415-422
    • Bachrach, U.1    Don, S.2    Wiener, H.3
  • 121
    • 0028137994 scopus 로고
    • HPLC and NMR investigation of the serum amine oxidase catalyzed oxidation of polyamines
    • Houen, G., Bock, K., and Jensen, A. L. (1994) HPLC and NMR investigation of the serum amine oxidase catalyzed oxidation of polyamines Acta Chem. Scand. 48, 52-60
    • (1994) Acta Chem. Scand. , vol.48 , pp. 52-60
    • Houen, G.1    Bock, K.2    Jensen, A.L.3
  • 122
    • 33947689120 scopus 로고    scopus 로고
    • The concept of "aldehyde load" in neurodegenerative mechanisms: Cytotoxicity of the polyamine degradation products hydrogen peroxide, acrolein, 3-aminopropanal, 3-acetamidopropanal and 4-aminobutanal in a retinal ganglion cell line
    • DOI 10.1016/j.brainres.2006.10.004, PII S000689930602943X
    • Wood, P. L., Khan, M. A., and Moskal, J. R. (2007) The concept of "aldehyde load" in neurodegenerative mechanisms: cytotoxicity of the polyamine degradation products hydrogen peroxide, acrolein, 3-aminopropanal, 3-acetamidopropanal and 4-aminobutanal in a retinal ganglion cell line Brain Res. 1145, 150-156 (Pubitemid 46497975)
    • (2007) Brain Research , vol.1145 , Issue.1 , pp. 150-156
    • Wood, P.L.1    Khan, M.A.2    Moskal, J.R.3
  • 124
    • 34547638065 scopus 로고    scopus 로고
    • Quantitation of acrolein-derived (3-hydroxypropyl)mercapturic acid in human urine by liquid chromatography-atmospheric pressure chemical ionization tandem mass spectrometry: Effects of cigarette smoking
    • DOI 10.1021/tx700075y
    • Carmella, S. G., Chen, M., Zhang, Y., Zhang, S., Hatsukami, D. K., and Hecht, S. S. (2007) Quantitation of acrolein-derived (3-hydroxypropyl) mercapturic acid in human urine by liquid chromatography-atmospheric pressure chemical ionization tandem mass spectrometry: effects of cigarette smoking Chem. Res. Toxicol. 20, 986-990 (Pubitemid 47204811)
    • (2007) Chemical Research in Toxicology , vol.20 , Issue.7 , pp. 986-990
    • Carmella, S.G.1    Chen, M.2    Zhang, Y.3    Zhang, S.4    Hatsukami, D.K.5    Hecht, S.S.6
  • 126
    • 0038578527 scopus 로고    scopus 로고
    • Induction of phase 2 enzymes by serum oxidized polyamines through activation of Nrf2: Effect of the polyamine metabolite acrolein
    • DOI 10.1016/S0006-291X(03)00834-9
    • Kwak, M. K., Kensler, T. W., and Casero, R. A., Jr. (2003) Induction of phase 2 enzymes by serum oxidized polyamines through activation of Nrf2: effect of the polyamine metabolite acrolein Biochem. Biophys. Res. Commun. 305, 662-670 (Pubitemid 36579282)
    • (2003) Biochemical and Biophysical Research Communications , vol.305 , Issue.3 , pp. 662-670
    • Kwak, M.-K.1    Kensler, T.W.2    Casero Jr., R.A.3
  • 130
    • 54049127788 scopus 로고    scopus 로고
    • Niemann-Pick C1 functions in regulating lysosomal amine content
    • Kaufmann, A. M. and Krise, J. P. (2008) Niemann-Pick C1 functions in regulating lysosomal amine content J. Biol. Chem. 283, 24584-24593
    • (2008) J. Biol. Chem. , vol.283 , pp. 24584-24593
    • Kaufmann, A.M.1    Krise, J.P.2
  • 131
    • 32944467076 scopus 로고    scopus 로고
    • Mammalian polyamine catabolism: A therapeutic target, a pathological problem, or both?
    • DOI 10.1093/jb/mvj021
    • Wang, Y. and Casero, R. A., Jr. (2006) Mammalian polyamine catabolism: a therapeutic target, a pathological problem, or both? J. Biochem. (Tokyo) 139, 17-25 (Pubitemid 43258842)
    • (2006) Journal of Biochemistry , vol.139 , Issue.1 , pp. 17-25
    • Wang, Y.1    Casero Jr., R.A.2
  • 132
    • 84896314770 scopus 로고    scopus 로고
    • Polyamine catabolism in carcinogenesis: Potential targets for chemotherapy and chemoprevention
    • in press
    • Battaglia, V., Destefano Shields, C., Murray-Stewart, T., and Casero, R. A. Polyamine catabolism in carcinogenesis: potential targets for chemotherapy and chemoprevention. Amino Acids 2013, in press
    • (2013) Amino Acids
    • Battaglia, V.1    Destefano Shields, C.2    Murray-Stewart, T.3    Casero, R.A.4
  • 133
    • 0026445548 scopus 로고
    • A proposed function for spermine and spermidine: Protection of replicating DNA against damage by singlet oxygen
    • Khan, A. U., Mei, Y. H., and Wilson, T. (1992) A proposed function for spermine and spermidine: protection of replicating DNA against damage by singlet oxygen Proc. Natl. Acad. Sci. U.S.A. 89, 11426-11427
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 11426-11427
    • Khan, A.U.1    Mei, Y.H.2    Wilson, T.3
  • 134
    • 0026446108 scopus 로고
    • Spermine and spermidine protection of plasmid DNA against single-strand breaks induced by singlet oxygen
    • Khan, A. U., Di Mascio, P., Medeiros, M. H., and Wilson, T. (1992) Spermine and spermidine protection of plasmid DNA against single-strand breaks induced by singlet oxygen Proc. Natl. Acad. Sci. U.S.A. 89, 11428-11430
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 11428-11430
    • Khan, A.U.1    Di Mascio, P.2    Medeiros, M.H.3    Wilson, T.4
  • 135
    • 0001019256 scopus 로고    scopus 로고
    • Structural specificity of polyamines and polyamine analogues in the protection of DNA from strand breaks induced by reactive oxygen species
    • DOI 10.1006/bbrc.1998.8258
    • Ha, H. C., Yager, J. D., Woster, P. A., and Casero, R. A., Jr. (1998) Structural specificity of polyamines and polyamine analogues in the protection of DNA from strand breaks induced by reactive oxygen species Biochem. Biophys. Res. Commun. 244, 298-303 (Pubitemid 28419942)
    • (1998) Biochemical and Biophysical Research Communications , vol.244 , Issue.1 , pp. 298-303
    • Ha, H.C.1    Yager, J.D.2    Woster, P.A.3    Casero Jr., R.A.4
  • 137
    • 0034923283 scopus 로고    scopus 로고
    • The role of the natural polyamine putrescine in defense against oxidative stress in Escherichia coli
    • DOI 10.1007/s002030100301
    • Tkachenko, A., Nesterova, L., and Pshenichnov, M. (2001) The role of the natural polyamine putrescine in defense against oxidative stress in Escherichia coli Arch. Microbiol. 176, 155-157 (Pubitemid 32692657)
    • (2001) Archives of Microbiology , vol.176 , Issue.1-2 , pp. 155-157
    • Tkachenko, A.1    Nesterova, L.2    Pshenichnov, M.3
  • 138
    • 3543078259 scopus 로고    scopus 로고
    • Mechanisms of protective functions of Escherichia coli polyamines against toxic effect of paraquat, which causes superoxide stress
    • Tkachenko, A. G. (2004) Mechanisms of protective functions of Escherichia coli polyamines against toxic effect of paraquat, which causes superoxide stress Biochemistry (Moscow) 69, 188-194
    • (2004) Biochemistry (Moscow) , vol.69 , pp. 188-194
    • Tkachenko, A.G.1
  • 139
    • 0025305215 scopus 로고
    • Paraquat toxicity is increased in Escherichia coli defective in the synthesis of polyamines
    • Minton, K. W., Tabor, H., and Tabor, C. W. (1990) Paraquat toxicity is increased in Escherichia coli defective in the synthesis of polyamines Proc. Natl. Acad. Sci. U.S.A. 87, 2851-2855
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 2851-2855
    • Minton, K.W.1    Tabor, H.2    Tabor, C.W.3
  • 140
    • 33846878034 scopus 로고    scopus 로고
    • Dependence of protective functions of Escherichia coli polyamines on strength of stress caused by superoxide radicals
    • DOI 10.1134/S0006297907010130
    • Tkachenko, A. G. and Fedotova, M. V. (2007) Dependence of protective functions of Escherichia coli polyamines on strength of stress caused by superoxide radicals Biochemistry (Moscow) 72, 109-116 (Pubitemid 46219194)
    • (2007) Biochemistry (Moscow) , vol.72 , Issue.1 , pp. 109-116
    • Tkachenko, A.G.1    Fedotova, M.V.2
  • 141
    • 84858004545 scopus 로고    scopus 로고
    • Polyamines reduce oxidative stress in Escherichia coli cells exposed to bactericidal antibiotics
    • Tkachenko, A. G., Akhova, A. V., Shumkov, M. S., and Nesterova, L. Y. (2012) Polyamines reduce oxidative stress in Escherichia coli cells exposed to bactericidal antibiotics Res. Microbiol. 163, 83-91
    • (2012) Res. Microbiol. , vol.163 , pp. 83-91
    • Tkachenko, A.G.1    Akhova, A.V.2    Shumkov, M.S.3    Nesterova, L.Y.4
  • 142
    • 0242335090 scopus 로고    scopus 로고
    • Polyamines as modulators of gene expression under oxidative stress in Escherichia coli
    • Tkachenko, A. G. and Nesterova, L. Y. (2003) Polyamines as modulators of gene expression under oxidative stress in Escherichia coli Biochemistry (Moscow) 68, 850-856
    • (2003) Biochemistry (Moscow) , vol.68 , pp. 850-856
    • Tkachenko, A.G.1    Nesterova, L.Y.2
  • 144
    • 33747777126 scopus 로고    scopus 로고
    • Polyamine deficiency leads to accumulation of reactive oxygen species in a spe2Δ mutant of Saccharomyces cerevisiae
    • DOI 10.1002/yea.1393
    • Chattopadhyay, M. K., Tabor, C. W., and Tabor, H. (2006) Polyamine deficiency leads to accumulation of reactive oxygen species in a spe2Delta mutant of Saccharomyces cerevisiae Yeast 23, 751-761 (Pubitemid 44275560)
    • (2006) Yeast , vol.23 , Issue.10 , pp. 751-761
    • Chattopadhyay, M.K.1    Tabor, C.W.2    Tabor, H.3
  • 145
    • 84859712406 scopus 로고    scopus 로고
    • Selenium and spermine alleviate cadmium induced toxicity in the red seaweed Gracilaria dura by regulating antioxidants and DNA methylation
    • Kumar, M., Bijo, A. J., Baghel, R. S., Reddy, C. R., and Jha, B. (2012) Selenium and spermine alleviate cadmium induced toxicity in the red seaweed Gracilaria dura by regulating antioxidants and DNA methylation Plant Physiol. Biochem. 51, 129-138
    • (2012) Plant Physiol. Biochem. , vol.51 , pp. 129-138
    • Kumar, M.1    Bijo, A.J.2    Baghel, R.S.3    Reddy, C.R.4    Jha, B.5
  • 146
    • 0024382725 scopus 로고
    • Influence of polyamines on membrane functions
    • Schuber, F. (1989) Influence of polyamines on membrane functions Biochem. J. 260, 1-10 (Pubitemid 19139892)
    • (1989) Biochemical Journal , vol.260 , Issue.1 , pp. 1-10
    • Schuber, F.1
  • 147
    • 84857089163 scopus 로고    scopus 로고
    • Surface-localized spermidine protects the Pseudomonas aeruginosa outer membrane from antibiotic treatment and oxidative stress
    • Johnson, L., Mulcahy, H., Kanevets, U., Shi, Y., and Lewenza, S. (2012) Surface-localized spermidine protects the Pseudomonas aeruginosa outer membrane from antibiotic treatment and oxidative stress J. Bacteriol. 194, 813-826
    • (2012) J. Bacteriol. , vol.194 , pp. 813-826
    • Johnson, L.1    Mulcahy, H.2    Kanevets, U.3    Shi, Y.4    Lewenza, S.5
  • 148
    • 0034536576 scopus 로고    scopus 로고
    • Skin fibroblasts from spermine synthase-deficient hemizygous gyro male (Gy/Y) mice overproduce spermidine and exhibit increased resistance to oxidative stress but decreased resistance to UV irradiation
    • DOI 10.1042/0264-6021:3520381
    • Nilsson, J., Gritli-Linde, A., and Heby, O. (2000) Skin fibroblasts from spermine synthase-deficient hemizygous gryo male (Gy/Y) mice overproduce spermidine and exhibit increased resistance to oxidative stress but decreased resistance to UV irradiation Biochem. J. 352, 381-387 (Pubitemid 32011432)
    • (2000) Biochemical Journal , vol.352 , Issue.2 , pp. 381-387
    • Nilsson, J.1    Gritli-Linde, A.2    Heby, O.3
  • 149
    • 34547702823 scopus 로고    scopus 로고
    • Spermine and spermidine mediate protection against oxidative damage caused by hydrogen peroxide
    • DOI 10.1007/s00726-007-0513-4, Special Issue: Polyamines and their Analogs in Cancer and other Diseases
    • Rider, J. E., Hacker, A., Mackintosh, C. A., Pegg, A. E., Woster, P. M., and Casero, R. A., Jr. (2007) Spermine and spermidine mediate protection against oxidative damage caused by hydrogen peroxide Amino Acids 33, 231-240 (Pubitemid 47222959)
    • (2007) Amino Acids , vol.33 , Issue.2 , pp. 231-240
    • Rider, J.E.1    Hacker, A.2    Mackintosh, C.A.3    Pegg, A.E.4    Woster, P.M.5    Casero Jr., R.A.6
  • 150
    • 84872033494 scopus 로고    scopus 로고
    • Change in lipoperoxidation but not in scavenging enzymes activity during polyamine embryoprotection in rat embryo cultured in hyperglycemic media
    • Chirino-Galindo, G., Mejia-Zepeda, R., and Palomar-Morales, M. (2012) Change in lipoperoxidation but not in scavenging enzymes activity during polyamine embryoprotection in rat embryo cultured in hyperglycemic media In Vitro Cell Dev. Biol. Anim. 48, 570-576
    • (2012) In Vitro Cell Dev. Biol. Anim. , vol.48 , pp. 570-576
    • Chirino-Galindo, G.1    Mejia-Zepeda, R.2    Palomar-Morales, M.3
  • 151
    • 84863782665 scopus 로고    scopus 로고
    • Polyamines detoxify the anticoagulant effect of acetaldehyde on prothrombin time
    • Brecher, A. S. and Riaz, A. H. (2012) Polyamines detoxify the anticoagulant effect of acetaldehyde on prothrombin time J. Cardiovasc. Pharmacol. 60, 1-7
    • (2012) J. Cardiovasc. Pharmacol. , vol.60 , pp. 1-7
    • Brecher, A.S.1    Riaz, A.H.2
  • 152
    • 0033276656 scopus 로고    scopus 로고
    • Spermine inhibition of monocyte activation and inflammation
    • Zhang, M., Borovikova, L. V., Wang, H., Metz, C., and Tracey, K. J. (1999) Spermine inhibition of monocyte activation and inflammation Mol. Med. 5, 595-605 (Pubitemid 32936950)
    • (1999) Molecular Medicine , vol.5 , Issue.9 , pp. 595-605
    • Zhang, M.1    Borovikova, L.V.2    Wang, H.3    Metz, C.4    Tracey, K.J.5
  • 153
    • 0033073345 scopus 로고    scopus 로고
    • Oral spermidine administration inhibits nitric oxide-mediated intestinal damage and levels of systemic inflammatory mediators in a mouse endotoxin model
    • ter Steege, J. C. A., Forget, P. P., and Buurman, W. A. (1999) Oral spermidine administration inhibits nitric oxide-mediated intestinal damage and levels of systemic inflammatory mediators in a mouse endotoxin model Shock 11, 115-119
    • (1999) Shock , vol.11 , pp. 115-119
    • Ter Steege, J.C.A.1    Forget, P.P.2    Buurman, W.A.3
  • 154
    • 84862796333 scopus 로고    scopus 로고
    • Anti-inflammatory effects of spermidine in lipopolysaccharide-stimulated BV2 microglial cells
    • Choi, Y. H. and Park, H. Y. (2012) Anti-inflammatory effects of spermidine in lipopolysaccharide-stimulated BV2 microglial cells J. Biomed. Sci. 19, 31
    • (2012) J. Biomed. Sci. , vol.19 , pp. 31
    • Choi, Y.H.1    Park, H.Y.2
  • 155
    • 84879241308 scopus 로고    scopus 로고
    • Natural polyamine inhibits mouse skin inflammation and macrophage activation
    • Paul, S. and Kang, S. C. (2013) Natural polyamine inhibits mouse skin inflammation and macrophage activation Inflammation Res. 62, 681-688
    • (2013) Inflammation Res. , vol.62 , pp. 681-688
    • Paul, S.1    Kang, S.C.2
  • 156
    • 0037733975 scopus 로고    scopus 로고
    • The importance of glutathione in human disease
    • DOI 10.1016/S0753-3322(03)00043-X
    • Townsend, D. M., Tew, K. D., and Tapiero, H. (2003) The importance of glutathione in human disease Biomed. Pharmacother. 57, 145-155 (Pubitemid 36740460)
    • (2003) Biomedicine and Pharmacotherapy , vol.57 , Issue.3 , pp. 145-155
    • Townsend, D.M.1    Tew, K.D.2    Tapiero, H.3
  • 158
    • 0014938381 scopus 로고
    • The complete conversion of spermidine to a peptide derivative in Escherichia coli
    • Tabor, C. W. and Tabor, H. (1970) The complete conversion of spermidine to a peptide derivative in Escherichia coli Biochem. Biophys. Res. Commun. 41, 232-238
    • (1970) Biochem. Biophys. Res. Commun. , vol.41 , pp. 232-238
    • Tabor, C.W.1    Tabor, H.2
  • 159
    • 0016788549 scopus 로고
    • Isolation, characterization, and turnover of glutathionylspermidine from Escherichia coli
    • Tabor, H. and Tabor, C. W. (1975) Isolation, characterization, and turnover of glutathionylspermidine from Escherichia coli J. Biol. Chem. 250, 2648-2654
    • (1975) J. Biol. Chem. , vol.250 , pp. 2648-2654
    • Tabor, H.1    Tabor, C.W.2
  • 160
    • 84871715452 scopus 로고    scopus 로고
    • Escherichia coli glutathionylspermidine synthetase/amidase: Phylogeny and effect on regulation of gene expression
    • Chattopadhyay, M. K., Chen, W., and Tabor, H. (2013) Escherichia coli glutathionylspermidine synthetase/amidase: phylogeny and effect on regulation of gene expression FEMS Microbiol. Lett. 338, 132-140
    • (2013) FEMS Microbiol. Lett. , vol.338 , pp. 132-140
    • Chattopadhyay, M.K.1    Chen, W.2    Tabor, H.3
  • 161
    • 0022002912 scopus 로고
    • Trypanothione: A novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids
    • Fairlamb, A. H., Blackburn, P., Ulrich, P., Chait, B. T., and Cerami, A. (1985) Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids Science (Washington, DC, U.S.) 227, 1485-1487 (Pubitemid 15146992)
    • (1985) Science , vol.227 , Issue.4693 , pp. 1485-1487
    • Fairlamb, A.H.1    Blackburn, P.2    Ulrich, P.3
  • 165
    • 84861909705 scopus 로고    scopus 로고
    • Update on field use of the available drugs for the chemotherapy of human African trypanosomiasis
    • Simarro, P. P., Franco, J., Diarra, A., Postigo, J. A., and Jannin, J. (2012) Update on field use of the available drugs for the chemotherapy of human African trypanosomiasis Parasitology 139, 842-846
    • (2012) Parasitology , vol.139 , pp. 842-846
    • Simarro, P.P.1    Franco, J.2    Diarra, A.3    Postigo, J.A.4    Jannin, J.5
  • 166
    • 77958502639 scopus 로고    scopus 로고
    • Chemotherapy of human African trypanosomiasis
    • Bacchi, C. J. (2009) Chemotherapy of human African trypanosomiasis Interdiscip. Perspect. Infect. Dis. 2009, 195040
    • (2009) Interdiscip. Perspect. Infect. Dis. , vol.2009 , pp. 195040
    • Bacchi, C.J.1
  • 167
    • 84872373862 scopus 로고    scopus 로고
    • Clinical features, diagnosis, and treatment of human African trypanosomiasis (sleeping sickness)
    • Kennedy, P. G. (2013) Clinical features, diagnosis, and treatment of human African trypanosomiasis (sleeping sickness) Lancet Neurol. 12, 186-194
    • (2013) Lancet Neurol. , vol.12 , pp. 186-194
    • Kennedy, P.G.1
  • 168
    • 84882298171 scopus 로고    scopus 로고
    • Dissecting the catalytic mechanism of Trypanosoma bruce i trypanothione synthetase by kinetic analysis and computational modelling
    • Leroux, A. E., Haanstra, J. R., Bakker, B. M., and Krauth-Siegel, R. L. (2013) Dissecting the catalytic mechanism of Trypanosoma bruce i trypanothione synthetase by kinetic analysis and computational modelling J..Biol. Chem. 288, 23751-23764
    • (2013) J.Biol. Chem. , vol.288 , pp. 23751-23764
    • Leroux, A.E.1    Haanstra, J.R.2    Bakker, B.M.3    Krauth-Siegel, R.L.4
  • 170
    • 84880292189 scopus 로고    scopus 로고
    • Trypanosomatidae diseases: From the current therapy to the efficacious role of trypanothione reductase in drug discovery
    • Bernardes, L. S., Zani, C. L., and Carvalho, I. (2013) Trypanosomatidae diseases: from the current therapy to the efficacious role of trypanothione reductase in drug discovery Curr. Med. Chem. 20, 2673-2696
    • (2013) Curr. Med. Chem. , vol.20 , pp. 2673-2696
    • Bernardes, L.S.1    Zani, C.L.2    Carvalho, I.3
  • 173
    • 79956209746 scopus 로고    scopus 로고
    • Use of polyamine metabolites as markers for stroke and renal failure
    • Igarashi, K. and Kashiwagi, K. (2011) Use of polyamine metabolites as markers for stroke and renal failure Methods Mol. Biol. 720, 395-408
    • (2011) Methods Mol. Biol. , vol.720 , pp. 395-408
    • Igarashi, K.1    Kashiwagi, K.2
  • 174
    • 0345291173 scopus 로고    scopus 로고
    • Effects of MDL 72527, a specific inhibitor of polyamine oxidase, on brain edema, ischemic injury volume, and tissue polyamine levels in rats after temporary middle cerebral artery occlusion
    • DOI 10.1046/j.1471-4159.1999.0720765.x
    • Dogan, A., Rao, A. M., Hatcher, J., Rao, V. L. R., Baskaya, M. K., and Dempsey, R. J. (1999) Effects of MDL 72527, a specific inhibitor of polyamine oxidase, on brain edema, ischemic injury volume, and tissue polyamine levels in rats after temporary middle cerebral artery occlusion J. Neurochem. 72, 765-770 (Pubitemid 29055241)
    • (1999) Journal of Neurochemistry , vol.72 , Issue.2 , pp. 765-770
    • Dogan, A.1    Rao, A.M.2    Hatcher, J.3    Rao, V.L.R.4    Baskaya, M.K.5    Dempsey, R.J.6
  • 179
    • 0038641715 scopus 로고    scopus 로고
    • 3-Aminopropanal, formed during cerebral ischaemia, is a potent lysosomotropic neurotoxin
    • DOI 10.1042/BJ20021520
    • Li, W., Yuan, X. M., Ivanova, S., Tracey, K. J., Eaton, J. W., and Brunk, U. T. (2003) 3-Aminopropanal, formed during cerebral ischaemia, is a potent lysosomotropic neurotoxin Biochem. J. 371, 429-436 (Pubitemid 36547626)
    • (2003) Biochemical Journal , vol.371 , Issue.2 , 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
  • 181
    • 33644694678 scopus 로고    scopus 로고
    • Polyamine oxidase and acrolein as novel biochemical markers for diagnosis of cerebral stroke
    • Tomitori, H., Usui, T., Saeki, N., Ueda, S., Kase, H., Nishimura, K., Kashiwagi, K., and Igarashi, K. (2005) Polyamine oxidase and acrolein as novel biochemical markers for diagnosis of cerebral stroke Stroke 36, 2609-2613
    • (2005) Stroke , vol.36 , pp. 2609-2613
    • Tomitori, H.1    Usui, T.2    Saeki, N.3    Ueda, S.4    Kase, H.5    Nishimura, K.6    Kashiwagi, K.7    Igarashi, K.8
  • 182
    • 80052525814 scopus 로고    scopus 로고
    • Protein-conjugated acrolein as a biochemical marker of brain infarction
    • Igarashi, K. and Kashiwagi, K. (2011) Protein-conjugated acrolein as a biochemical marker of brain infarction Mol. Nutr. Food Res. 55, 1332-1341
    • (2011) Mol. Nutr. Food Res. , vol.55 , pp. 1332-1341
    • Igarashi, K.1    Kashiwagi, K.2
  • 186
  • 188
    • 0018383504 scopus 로고
    • Polyamines: An unrecognised cardiovascular risk factor in chronic dialysis?
    • Bagdade, J. D., Subbaiah, P. V., Bartos, D., Bartos, F., and Campbell, R. A. (1979) Polyamines: an unrecognised cardiovascular risk factor in chronic dialysis? Lancet 1, 412-413 (Pubitemid 9121130)
    • (1979) Lancet , vol.1 , Issue.8113 , pp. 412-413
    • Bagdade, J.D.1    Bartos, D.2    Subbaiah, P.V.3
  • 189
  • 192
    • 33845208407 scopus 로고    scopus 로고
    • Polyamines in renal failure
    • DOI 10.1007/s00726-006-0264-7, Special Issue: Focus on Postnatal CNS PLasticity
    • Igarashi, K., Ueda, S., Yoshida, K., and Kashiwagi, K. (2006) Polyamines in renal failure Amino Acids 31, 477-483 (Pubitemid 44853470)
    • (2006) Amino Acids , vol.31 , Issue.4 , pp. 477-483
    • Igarashi, K.1    Ueda, S.2    Yoshida, K.3    Kashiwagi, K.4
  • 200
    • 34247122250 scopus 로고    scopus 로고
    • Inflammation and polyamine catabolism: The good, the bad and the ugly
    • DOI 10.1042/BST0350300
    • Babbar, N., Murray-Stewart, T., and Casero, R. A., Jr. (2007) Inflammation and polyamine catabolism: the good, the bad and the ugly Biochem. Soc. Trans. 35, 300-304 (Pubitemid 46596495)
    • (2007) Biochemical Society Transactions , vol.35 , Issue.2 , pp. 300-304
    • Babbar, N.1    Murray-Stewart, T.2    Casero Jr., R.A.3
  • 201
    • 33845730779 scopus 로고    scopus 로고
    • Tumor necrosis factor-α increases reactive oxygen species by inducing spermine oxidase in human lung epithelial cells: A potential mechanism for inflammation-induced carcinogenesis
    • DOI 10.1158/0008-5472.CAN-06-3174
    • Babbar, N. and Casero, R. A., Jr. (2006) Tumor necrosis factora increases reactive oxygen species by inducing spermine oxidase in human lung epithelial cells: a potential mechanism for inflammation-induced carcinogenesis Cancer Res. 66, 11125-11130 (Pubitemid 46009938)
    • (2006) Cancer Research , vol.66 , Issue.23 , pp. 11125-11130
    • Babbar, N.1    Casero Jr., R.A.2
  • 202
    • 33747666168 scopus 로고    scopus 로고
    • 1-acetyltransferase through nuclear factor κB in non-small cell lung cancer cells
    • DOI 10.1074/jbc.M601871200
    • 1- acetyltransferase through nuclear factor κB in non-small cell lung cancer cells J. Biol. Chem. 281, 24182-24192 (Pubitemid 44274192)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.34 , pp. 24182-24192
    • Babbar, N.1    Hacker, A.2    Huang, Y.3    Casero Jr., R.A.4
  • 203
    • 84889096256 scopus 로고    scopus 로고
    • Inhibition of polyamine oxidase prevented cyclin-dependent kinase inhibitor-induced apoptosis in HCT 116 colon carcinoma cells
    • Gurkan, A. C., Arisan, E. D., Obakan, P., and Palavan-Unsal, N. (2013) Inhibition of polyamine oxidase prevented cyclin-dependent kinase inhibitor-induced apoptosis in HCT 116 colon carcinoma cells Apoptosis 18, 1536-1547
    • (2013) Apoptosis , vol.18 , pp. 1536-1547
    • Gurkan, A.C.1    Arisan, E.D.2    Obakan, P.3    Palavan-Unsal, N.4
  • 206
    • 0028884169 scopus 로고
    • Identification of an endogenous inhibitor of prostatic carcinoma cell growth
    • Smith, R. C., Litwin, M. S., Lu, Y., and Zetter, B. R. (1995) Identification of an endogenous inhibitor of prostatic carcinoma cell growth Nature Med. 1, 1040-1045
    • (1995) Nature Med. , vol.1 , pp. 1040-1045
    • Smith, R.C.1    Litwin, M.S.2    Lu, Y.3    Zetter, B.R.4
  • 207
    • 0033572568 scopus 로고    scopus 로고
    • Sensitivity to polyamine-induced growth arrest correlates with antizyme induction in prostate carcinoma cells
    • Koike, C., Chao, D. T., and Zetter, B. R. (1999) Sensitivity to polyamine-induced growth arrest correlated with antizyme induction in prostate carcinoma cells Cancer Res. 59, 6109-6112 (Pubitemid 30035629)
    • (1999) Cancer Research , vol.59 , Issue.24 , pp. 6109-6112
    • Koike, C.1    Chao, D.T.2    Zetter, B.R.3
  • 208
    • 84861713664 scopus 로고    scopus 로고
    • Inducible expression of antizyme 1 in prostate cancer cell lines after lentivirus mediated gene transfer
    • Pietila, M., Lampinen, A., Pellinen, R., and Alhonen, L. (2012) Inducible expression of antizyme 1 in prostate cancer cell lines after lentivirus mediated gene transfer Amino Acids 42, 559-564
    • (2012) Amino Acids , vol.42 , pp. 559-564
    • Pietila, M.1    Lampinen, A.2    Pellinen, R.3    Alhonen, L.4
  • 210
    • 3042553345 scopus 로고    scopus 로고
    • Metabolic and antiproliferative consequences of activated polyamine catabolism in LNCaP prostate carcinoma cells
    • DOI 10.1074/jbc.M403323200
    • Kee, K., Vujcic, S., Merali, S., Diegelman, P., Kisiel, N., Powell, C. T., Kramer, D. L., and Porter, C. W. (2004) Metabolic and antiproliferative consequences of activated polyamine catabolism in LNCaP prostate carcinoma cells J. Biol. Chem. 279, 27050-27058 (Pubitemid 38812541)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 27050-27058
    • Kee, K.1    Vujcic, S.2    Meralis, S.3    Diegelman, P.4    Kisiel, N.5    Powell, C.T.6    Kramer, D.L.7    Porter, C.W.8
  • 211
    • 20444491996 scopus 로고    scopus 로고
    • Helicobacter pylori-induced macrophage apoptosis requires activation of ornithine decarboxylase by c-Myc
    • DOI 10.1074/jbc.C500122200
    • Cheng, Y., Chaturvedi, R., Asim, M., Bussiere, F. I., Scholz, A., Xu, H., Casero, R. A., Jr., and Wilson, K. T. (2005) Helicobacter pylori -induced macrophage apoptosis requires activation of ornithine decarboxylase by c-Myc J. Biol. Chem. 280, 22492-22496 (Pubitemid 40827905)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.23 , pp. 22492-22496
    • Cheng, Y.1    Chaturvedi, R.2    Asim, M.3    Bussiere, F.I.4    Xu, H.5    Casero Jr., R.A.6    Wilson, K.T.7
  • 213
    • 84896315732 scopus 로고    scopus 로고
    • Spermine oxidase is a regulator of macrophage host response to Helicobacter pylori: Enhancement of antimicrobial nitric oxide generation by depletion of spermine
    • in press
    • Chaturvedi, R., Asim, M., Barry, D. P., Frye, J. W., Casero, R. A., and Wilson, K. T. Spermine oxidase is a regulator of macrophage host response to Helicobacter pylori: enhancement of antimicrobial nitric oxide generation by depletion of spermine. Amino Acids 2013, in press
    • (2013) Amino Acids
    • Chaturvedi, R.1    Asim, M.2    Barry, D.P.3    Frye, J.W.4    Casero, R.A.5    Wilson, K.T.6
  • 214
    • 4544249197 scopus 로고    scopus 로고
    • Induction of polyamine oxidase 1 by Helicobacter pylori causes macrophage apoptosis by hydrogen peroxide release and mitochondrial membrane depolarization
    • DOI 10.1074/jbc.M401370200
    • Chaturvedi, R., Cheng, Y., Asim, M., Bussiere, F. I., Xu, H., Gobert, A. P., Hacker, A., Casero, R. A., Jr., and Wilson, K. T. (2004) Induction of polyamine oxidase 1 by Helicobacter pylori causes macrophage apoptosis by hydrogen peroxide release and mitochondrial membrane depolarization J. Biol. Chem. 279, 40161-40173 (Pubitemid 39258292)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.38 , pp. 40161-40173
    • Chaturvedi, R.1    Cheng, Y.2    Asim, M.3    Bussiere, F.I.4    Xu, H.5    Gobert, A.P.6    Hacker, A.7    Casero, R.A.8    Wilson Jr., K.T.9
  • 216
    • 79956220790 scopus 로고    scopus 로고
    • Methods to evaluate alterations in polyamine metabolism caused by Helicobacter pylori infection
    • Gobert, A. P., Chaturvedi, R., and Wilson, K. T. (2011) Methods to evaluate alterations in polyamine metabolism caused by Helicobacter pylori infection Methods Mol. Biol. 720, 409-425
    • (2011) Methods Mol. Biol. , vol.720 , pp. 409-425
    • Gobert, A.P.1    Chaturvedi, R.2    Wilson, K.T.3
  • 217
    • 84883399007 scopus 로고    scopus 로고
    • Chronic inflammation and oxidative stress: The smoking gun for Helicobacter pylori- induced gastric cancer?
    • in press
    • Hardbower, D. M., de Sablet, T., Chaturvedi, R., and Wilson, K. T. Chronic inflammation and oxidative stress: The smoking gun for Helicobacter pylori- induced gastric cancer?. Gut Microbes 2013, in press
    • (2013) Gut Microbes
    • Hardbower, D.M.1    De Sablet, T.2    Chaturvedi, R.3    Wilson, K.T.4
  • 219
    • 85046980953 scopus 로고    scopus 로고
    • Spermine oxidase, a polyamine catabolic enzyme that links Helicobacter pylori CagA and gastric cancer risk
    • Chaturvedi, R., de Sablet, T., Peek, R. M., and Wilson, K. T. (2012) Spermine oxidase, a polyamine catabolic enzyme that links Helicobacter pylori CagA and gastric cancer risk Gut Microbes 3, 48-56
    • (2012) Gut Microbes , vol.3 , pp. 48-56
    • Chaturvedi, R.1    De Sablet, T.2    Peek, R.M.3    Wilson, K.T.4
  • 225
    • 68549101792 scopus 로고    scopus 로고
    • Recent advances in the development of polyamine analogues as antitumor agents
    • Casero, R. A., Jr. and Woster, P. M. (2009) Recent advances in the development of polyamine analogues as antitumor agents J. Med. Chem. 52, 4551-4573
    • (2009) J. Med. Chem. , vol.52 , pp. 4551-4573
    • Casero Jr., R.A.1    Woster, P.M.2
  • 226
    • 77449090884 scopus 로고    scopus 로고
    • Polyamine analogues targeting epigenetic gene regulation
    • Huang, Y., Marton, L. J., Woster, P. M., and Casero, R. A. (2009) Polyamine analogues targeting epigenetic gene regulation Essays Biochem. 46, 95-110
    • (2009) Essays Biochem. , vol.46 , pp. 95-110
    • Huang, Y.1    Marton, L.J.2    Woster, P.M.3    Casero, R.A.4
  • 230
    • 73149102982 scopus 로고    scopus 로고
    • Mechanistic studies of para-substituted N, N ′-dibenzyl-1,4- diaminobutanes as substrates for a mammalian polyamine oxidase
    • Pozzi, M. H., Gawandi, V., and Fitzpatrick, P. F. (2009) Mechanistic studies of para-substituted N, N ′-dibenzyl-1,4-diaminobutanes as substrates for a mammalian polyamine oxidase Biochemistry 48, 12305-12313
    • (2009) Biochemistry , vol.48 , pp. 12305-12313
    • Pozzi, M.H.1    Gawandi, V.2    Fitzpatrick, P.F.3
  • 231
    • 67049173035 scopus 로고    scopus 로고
    • Metabolism of an alkyl polyamine analog by a polyamine oxidase from themicrosporidian Encephalitozoon cuniculi
    • Bacchi, C. J., Yarlett, N., Faciane, E., Bi, X., Rattendi, D., Weiss, L. M., and Woster, P. M. (2009) Metabolism of an alkyl polyamine analog by a polyamine oxidase from themicrosporidian Encephalitozoon cuniculi Antimicrob. Agents Chemother. 53, 2599-2604
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 2599-2604
    • Bacchi, C.J.1    Yarlett, N.2    Faciane, E.3    Bi, X.4    Rattendi, D.5    Weiss, L.M.6    Woster, P.M.7
  • 233
    • 34547662510 scopus 로고    scopus 로고
    • Antiviral activity of oxidized polyamines
    • DOI 10.1007/s00726-007-0535-y, Special Issue: Polyamines and their Analogs in Cancer and other Diseases
    • Bachrach, U. (2007) Antiviral activity of oxidized polyamines Amino Acids 33, 267-272 (Pubitemid 47222981)
    • (2007) Amino Acids , vol.33 , Issue.2 , pp. 267-272
    • Bachrach, U.1
  • 234
    • 33749543605 scopus 로고    scopus 로고
    • Non-irradiation-derived reactive oxygen species (ROS) and cancer: Therapeutic implications
    • DOI 10.1007/s00726-005-0271-8, Special issue: Focus on Neuropeptides in Anxiety and Depression
    • Agostinelli, E. and Seiler, N. (2006) Non-irradiation-derived reactive oxygen species (ROS) and cancer: therapeutic implications Amino Acids 31, 341-355 (Pubitemid 44537062)
    • (2006) Amino Acids , vol.31 , Issue.3 , pp. 341-355
    • Agostinelli, E.1    Seiler, N.2
  • 237
    • 70349132707 scopus 로고    scopus 로고
    • Cytotoxicity of spermine oxidation products to multidrug resistant melanoma M14 ADR2 cells: Sensitization by the MDL 72527 lysosomotropic compound
    • Agostinelli, E., Condello, M., Molinari, A., Tempera, G., Viceconte, N., and Arancia, G. (2009) Cytotoxicity of spermine oxidation products to multidrug resistant melanoma M14 ADR2 cells: sensitization by the MDL 72527 lysosomotropic compound Int. J. Oncol. 35, 485-498
    • (2009) Int. J. Oncol. , vol.35 , pp. 485-498
    • Agostinelli, E.1    Condello, M.2    Molinari, A.3    Tempera, G.4    Viceconte, N.5    Arancia, G.6
  • 238
    • 84880634377 scopus 로고    scopus 로고
    • Reactive oxygen species spermine metabolites generated from amine oxidases and radiation represent a therapeutic gain in cancer treatments
    • Amendola, R., Cervelli, M., Fratini, E., Sallustio, D. E., Tempera, G., Ueshima, T., Mariottini, P., and Agostinelli, E. (2013) Reactive oxygen species spermine metabolites generated from amine oxidases and radiation represent a therapeutic gain in cancer treatments Int. J. Oncol. 43, 813-820
    • (2013) Int. J. Oncol. , vol.43 , pp. 813-820
    • Amendola, R.1    Cervelli, M.2    Fratini, E.3    Sallustio, D.E.4    Tempera, G.5    Ueshima, T.6    Mariottini, P.7    Agostinelli, E.8
  • 239
    • 33747113715 scopus 로고    scopus 로고
    • Hyperthermia enhances cytotoxicity of amine oxidase and spermine on drug-resistant LoVo colon adenocarcinoma cells
    • Agostinelli, E., Belli, F., Dalla Vedova, L., Marra, M., Crateri, P., and Arancia, G. (2006) 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
  • 243
    • 0027252891 scopus 로고
    • The implications of a unified theory of programmed cell death, polyamines, oxyradicals and histogenesis in the embryo
    • Parchment, R. E. (1993) The implications of a unified theory of programmed cell death, polyamines, oxyradicals and histogenesis in the embryo Int. J. Dev. Biol. 37, 75-83 (Pubitemid 23145241)
    • (1993) International Journal of Developmental Biology , vol.37 , Issue.1 , pp. 75-83
    • Parchment, R.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.