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Gene Review

Smox  -  spermine oxidase

Mus musculus

Synonyms: B130066H01Rik, PAO, PAO-1, PAOh1, Polyamine oxidase 1, ...
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Disease relevance of Smox

  • The over-expression of the active isoforms mSMOalpha and mSMOmu, and the inactive mSMOdelta and mSMOgamma in mouse neuroblastoma cells, demonstrated the first evidence of the direct oxidative DNA damage by the SMO activities, either alone or, in a higher extent, when associated with radiation exposure, thus working as radio sensitizer [1].
  • There was no appreciable increase in the virulence of Pseudomonas aeruginosa PAO-1 after six passes through infections in mice [2].
  • METHODS: A murine model of P. aeruginosa keratitis was used to compare the response to ofloxacin, tobramycin, prednisolone acetate, and non-preserved saline treatment, as well as combination antibiotic-corticosteroid therapy for infection caused by a cytotoxic strain (6206) and an invasive strain (PAO1) [3].
  • A single intraperitoneal injection of Lactobacillus casei YIT 0003 into normal or dexamethasone-treated mice led to nonspecific resistance against intraperitoneal challenge with lethal doses of Pseudomonas aeruginosa PAO 3047 [4].

High impact information on Smox


Chemical compound and disease context of Smox

  • To investigate the contribution of the TonB protein to high-affinity iron acquisition in Pseudomonas aeruginosa, we constructed tonB-inactivated mutants from strain PAO1 and its derivative deficient in producing the siderophores pyoverdin and pyochelin [10].
  • Two phospholipase C fractions were detected in culture supernatants from Pseudomonas aeruginosa ATCC 19660, PAO1, and D10C by preparative polyacrylamide gel electrophoresis [11].
  • Pseudomonas aeruginosa PAO leucine-, isoleucine-, valine-binding protein (LIVAT-BP) encoded by the braC gene was used as a model antigen [12].
  • Role of exotoxin A and elastase in the pathogenicity of Pseudomonas aeruginosa strain PAO experimental mouse burn infection [13].

Biological context of Smox

  • Two short protein domains are responsible for the nuclear localization of the mouse spermine oxidase mu isoform [14].
  • The nonpiliated strain PA1244-NP was as virulent as the piliated strain PAO1, suggesting that expression of other virulence factors are also important in the development of acute pneumonia [15].
  • We studied galU mutants of strain PAO1, of its cytotoxic variant expressing ExoU from a plasmid, and of the inherently cytotoxic strain PA103 [16].
  • Quantitative bacteriology of blood and tissue homogenates revealed that P. aeruginosa PAO could multiply in the skin and could also be cultured from the blood, livers, and spleens of infected mice [17].
  • Putreanine is not only derived from spermidine, but can also be formed from N8-(2-carboxyethyl)spermidine by oxidative deamination, catalysed by serum spermine oxidase, and subsequent spontaneous elimination of acrolein [18].

Anatomical context of Smox

  • Mouse amniotic fluid was found to contain high levels of a spermine oxidase having a somewhat different specificity than that in FCS, and this enzyme produced a noncytotoxic immune inhibitor from cadaverine, spermidine and spermine [19].
  • Mice were anesthetized, and their corneas were scratched and inoculated with virulent P. aeruginosa 6294 or PAO1, along with either 50 microg of oligosaccharide derived from LPS from P. aeruginosa PAC557 (complete outer core but no O side chains) or oligosaccharide derived from LPS of P. aeruginosa PAC1RalgC::tet (incomplete-core oligosaccharide) [20].
  • A cross-reactivity was observed between pili from two strains of P. aeruginosa, namely, PAK and PAO, at the T-cell level [21].
  • MPT was induced more readily by ouabain, PAO, or TMRM in DKO myocytes than in WT [22].
  • The purpose of the present study was to further delineate the role of natural killer (NK) cells in the early stages of resistance to infection by Pseudomonas aeruginosa, strain PAO1 [23].

Associations of Smox with chemical compounds

  • In mouse, at least two catalytically active splice variants (mSMOalpha and mSMOmicro) of the flavin-containing spermine oxidase enzyme are present [14].
  • Oxidation was inhibited by the spermine oxidase inhibitors hydroxylamine and isonicotinic acid hydrazide, and inhibition of the immune response was no longer evident suggesting that the inhibitory material was a product of the action of the enzyme on spermic and spermidine [19].
  • The flavoprotein SMO is the most recently characterized catabolic enzyme, preferentially oxidizing SPM to SPD, 3-aminopropanal and H(2)O(2) [1].
  • PAO blocks turnover of the phosphoryl group of pp15, causing its accumulation, and thereby appears to interrupt signal transmission from the receptor to the glucose-transport system [9].
  • One monoclonal antitoxin displayed specificity for PA103-derived exotoxin yet failed to react with exotoxin purified from PAO-PR1 or PAO1, suggesting that structural differences exist between these exotoxins [24].

Other interactions of Smox


Analytical, diagnostic and therapeutic context of Smox

  • Dealing with the unbalanced tissue specific SMO activities, these results could indicate a new direction to tailor chemotherapy-associated radiotherapy, improving dose-rate protocol and allowing the modulation of deleterious side effects on healthy tissues [1].
  • However, passive immunization did prevent mortality from pneumonia due to the cytotoxic PAO1 variant at low-challenge doses [26].
  • After active immunization, high levels of protection were achieved against an ExoU-expressing cytotoxic variant of the parental strain PAO1 at doses up to 1,000-fold greater than the 50% lethal dose [26].
  • METHODS: Scarified corneas were placed in organ culture and inoculated with P. aeruginosa cell suspensions containing either ATCC 19660 or PAO1 bacterial strains classed as cytotoxic or invasive, respectively [27].


  1. Direct oxidative DNA damage, apoptosis and radio sensitivity by spermine oxidase activities in mouse neuroblastoma cells. Amendola, R., Bellini, A., Cervelli, M., Degan, P., Marcocci, L., Martini, F., Mariottini, P. Biochim. Biophys. Acta (2005) [Pubmed]
  2. Passage of Pseudomonas aeruginosa in compromised mice. Cox, C.D. Infect. Immun. (1979) [Pubmed]
  3. A comparison of invasive and cytotoxic Pseudomonas aeruginosa strain-induced corneal disease responses to therapeutics. Lee, E.J., Truong, T.N., Mendoza, M.N., Fleiszig, S.M. Curr. Eye Res. (2003) [Pubmed]
  4. Effects of Lactobacillus casei on Pseudomonas aeruginosa infection in normal and dexamethasone-treated mice. Saito, H., Watanabe, T., Horikawa, Y. Microbiol. Immunol. (1986) [Pubmed]
  5. Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase. Wu, T., Yankovskaya, V., McIntire, W.S. J. Biol. Chem. (2003) [Pubmed]
  6. Targeted disruption of spermidine/spermine N1-acetyltransferase gene in mouse embryonic stem cells. Effects on polyamine homeostasis and sensitivity to polyamine analogues. Niiranen, K., Pietilä, M., Pirttilä, T.J., Järvinen, A., Halmekytö, M., Korhonen, V.P., Keinänen, T.A., Alhonen, L., Jänne, J. J. Biol. Chem. (2002) [Pubmed]
  7. Rac1 and Cdc42 are required for phagocytosis, but not NF-kappaB-dependent gene expression, in macrophages challenged with Pseudomonas aeruginosa. Lee, D.J., Cox, D., Li, J., Greenberg, S. J. Biol. Chem. (2000) [Pubmed]
  8. Correlation of polyamine and growth responses to N1,N11-diethylnorspermine in primary fetal fibroblasts derived from transgenic mice overexpressing spermidine/spermine N1-acetyltransferase. Alhonen, L., Karppinen, A., Uusi-Oukari, M., Vujcic, S., Korhonen, V.P., Halmekytö, M., Kramer, D.L., Hines, R., Jänne, J., Porter, C.W. J. Biol. Chem. (1998) [Pubmed]
  9. Insulin-receptor tyrosine kinase and glucose transport. Lane, M.D., Flores-Riveros, J.R., Hresko, R.C., Kaestner, K.H., Liao, K., Janicot, M., Hoffman, R.D., McLenithan, J.C., Kastelic, T., Christy, R.J. Diabetes Care (1990) [Pubmed]
  10. Requirement of the Pseudomonas aeruginosa tonB gene for high-affinity iron acquisition and infection. Takase, H., Nitanai, H., Hoshino, K., Otani, T. Infect. Immun. (2000) [Pubmed]
  11. In vivo studies with two phospholipase C fractions from Pseudomonas aeruginosa. Berk, R.S., Brown, D., Coutinho, I., Meyers, D. Infect. Immun. (1987) [Pubmed]
  12. Epitope selection in major histocompatibility complex class I-mediated pathway is affected by the intracellular localization of an antigen. Yamazaki, H., Tanaka, M., Nagoya, M., Fujimaki, H., Sato, K., Yago, T., Nagata, T., Minami, M. Eur. J. Immunol. (1997) [Pubmed]
  13. Role of exotoxin A and elastase in the pathogenicity of Pseudomonas aeruginosa strain PAO experimental mouse burn infection. Wretlind, B., Björklind, A., Pavlovskis, O.R. Microb. Pathog. (1987) [Pubmed]
  14. Two short protein domains are responsible for the nuclear localization of the mouse spermine oxidase mu isoform. Bianchi, M., Amendola, R., Federico, R., Polticelli, F., Mariottini, P. FEBS J. (2005) [Pubmed]
  15. Role of Pseudomonas aeruginosa pili in acute pulmonary infection. Tang, H., Kays, M., Prince, A. Infect. Immun. (1995) [Pubmed]
  16. The galU Gene of Pseudomonas aeruginosa is required for corneal infection and efficient systemic spread following pneumonia but not for infection confined to the lung. Priebe, G.P., Dean, C.R., Zaidi, T., Meluleni, G.J., Coleman, F.T., Coutinho, Y.S., Noto, M.J., Urban, T.A., Pier, G.B., Goldberg, J.B. Infect. Immun. (2004) [Pubmed]
  17. Surface expression of ferripyochelin-binding protein is required for virulence of Pseudomonas aeruginosa. Sokol, P.A. Infect. Immun. (1987) [Pubmed]
  18. On the formation of amino acids deriving from spermidine and spermine. Seiler, N., Knödgen, B., Gittos, M.W., Chan, W.Y., Griesmann, G., Rennert, O.M. Biochem. J. (1981) [Pubmed]
  19. Enzymatic oxidation of polyamines. Relationship to immunosuppressive properties. Labib, R.S., Tomasi, T.B. Eur. J. Immunol. (1981) [Pubmed]
  20. Inhibition of bacterial adherence to host tissue does not markedly affect disease in the murine model of Pseudomonas aeruginosa corneal infection. Zaidi, T.S., Preston, M.J., Pier, G.B. Infect. Immun. (1997) [Pubmed]
  21. Mapping of the T-cell recognition sites of Pseudomonas aeruginosa PAK polar pili. Smart, W., Sastry, P.A., Paranchych, W., Singh, B. Infect. Immun. (1988) [Pubmed]
  22. CRYAB and HSPB2 deficiency increases myocyte mitochondrial permeability transition and mitochondrial calcium uptake. Kadono, T., Zhang, X.Q., Srinivasan, S., Ishida, H., Barry, W.H., Benjamin, I.J. J. Mol. Cell. Cardiol. (2006) [Pubmed]
  23. Enhanced splenic bacterial clearance and neutrophilia in anti-NK1.1-treated mice infected with Pseudomonas aeruginosa. Newton, D.W., Runnels, H.A., Kearns, R.J. Nat. Immun. (1992) [Pubmed]
  24. Production and characterization of monoclonal antibodies to exotoxin A from Pseudomonas aeruginosa. Galloway, D.R., Hedstrom, R.C., Pavlovskis, O.R. Infect. Immun. (1984) [Pubmed]
  25. Chain-fluorinated polyamines as tumor markers. II. Metabolic aspects in normal tissues. Seiler, N., Sarhan, S., Knödgen, B., Gerhart, F. J. Cancer Res. Clin. Oncol. (1988) [Pubmed]
  26. Protection against fatal Pseudomonas aeruginosa pneumonia in mice after nasal immunization with a live, attenuated aroA deletion mutant. Priebe, G.P., Meluleni, G.J., Coleman, F.T., Goldberg, J.B., Pier, G.B. Infect. Immun. (2003) [Pubmed]
  27. Environmental factors influence P. aeruginosa binding to the wounded mouse cornea. Chen, L., Hobden, J.A., Masinick, S.A., Hazlett, L.D. Curr. Eye Res. (1998) [Pubmed]
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