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Gene Review

SMOX  -  spermine oxidase

Homo sapiens

Synonyms: C20orf16, FLJ20746, MGC1010, PAO, PAO-1, ...
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Disease relevance of SMOX


High impact information on SMOX

  • Monoclonal antibody SMO, which blocks oxLDL binding to CD36, did not inhibit adhesion of macrophages to oxLDL-coated surfaces but markedly reduced H2O2 secretion by these cells [5].
  • This effect correlated with increased adherence of PAO1 to epithelial cells after exposure to PAO1 neuraminidase and was consistent with in vitro studies demonstrating Pseudomonas adherence to asialoganglioside receptors [6].
  • In this study, the properties of the PAO1 neuraminidase were examined to determine its potential role in facilitating Pseudomonas colonization of the respiratory epithelium [6].
  • For example, PAPI-1 carries a complete gene cluster predicted to encode a type IV group B pilus, a well known adhesin absent from strain PAO1 [7].
  • In contrast, in a non-CF strain, PAO1, an algT mutation did not affect its virulence on alfalfa [8].

Chemical compound and disease context of SMOX


Biological context of SMOX

  • Overall, the data indicate that the enzyme represents a novel mammalian oxidase which, on the basis of substrate specificity, we have designated spermine oxidase in order to distinguish it from the PAO involved in polyamine back-conversion [12].
  • Potentiation of apple procyanidin-triggered apoptosis by the polyamine oxidase inactivator MDL 72527 in human colon cancer-derived metastatic cells [13].
  • In this study, the specific contribution of polyamine oxidase (PAO), a hydrogen peroxide (H2O2)-producing enzyme, to the oxidative burst induced in maize mesocotyl by the phosphatase inhibitor cantharidin was examined [14].
  • However, induction of SMO/PAOh1 by inflammation or infectious agents has the potential to produce sufficient ROS in normal, non-tumour cells to lead to DNA damage, mutation and, potentially, carcinogenic transformation ('bad') [15].
  • The open reading frame predicts a 555-amino acid protein with a calculated M(r) of 61,852.30, which shows a 95.1% identity with PAOh1 [16].

Anatomical context of SMOX

  • The induction of PAOh1/SMO in response to multiple polyamine analogues was examined in representative lung tumor cell lines [1].
  • These studies demonstrate a new mechanism for pathogen-induced oxidative stress in macrophages in which activation of PAO1 leads to H(2)O(2) release and apoptosis by a mitochondrial-dependent cell death pathway, contributing to deficiencies in host defense in diseases such as H. pylori infection [4].
  • To address this issue, we tested wild-type strains PAO1, PA14, the mucoid cystic fibrosis isolate, FRD1 (mucA22+), and the respective isogenic mutants which lacked the ability to produce alginate, for their susceptibility to human leukocytes in the presence and absence of IFN-gamma [17].
  • We have shown that dendritic cells (DCs) genetically engineered with a recombinant adenovirus vector (Ad) to express CD40 ligand (CD40L) elicit specific humoral immunity against the Pseudomonas aeruginosa laboratory strain PAO1, without CD4(+) T cell help [18].
  • PAO1 supernatant altered wound repair by slowing the migration velocity in association with altered actin cytoskeleton polymerization in the lamellipodia of migrating airway epithelial cells and delaying or inhibiting the restoration of epithelial integrity after wound closure [10].

Associations of SMOX with chemical compounds

  • This ranking is identical to that reported for purified PAO and distinctly different from the recently identified spermine oxidase (SMO), which prefers spermine over N1-acetylspermine [19].
  • Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin [12].
  • Using a series of polyamine analogues, it was found that the most potent inducers of PAOh1/SMO possessed multiple three-carbon linkers between nitrogens, as typified by N1,N11-bis(ethyl)norspermine [1].
  • PAO-PR1, an avirulent exotoxin A mutant of PAO1, did not cause a decrease in the resistance [20].
  • One appears to be identical with the polyamine oxidase that was postulated to catalyse the conversion of spermidine to putrescine within the interconversion cycle [21].

Other interactions of SMOX


Analytical, diagnostic and therapeutic context of SMOX

  • In Northern blot analysis, PAO mRNA was much less abundant in HEK-293 cells than SMO or SSAT mRNA, and all three were differentially induced in a similar manner by selected polyamine analogues [19].
  • METHODS: The activity of AcPAO and SMO and the level of protein-conjugated acrolein in plasma of the stroke patients and normal subjects were measured by high-performance liquid chromatography and ELISA, respectively [2].
  • After patients with chronic renal failure had undergone hemodialysis, their levels of plasma polyamines, spermine oxidase and acrolein returned towards normal [3].
  • In addition, the relative transcription levels of the gene splicing variants were evaluated by RT-PCR analysis to verify a relationship with the SMO enzyme activity in various murine organs [24].
  • The results obtained by both flow cytometry and a microplate adhesion assay indicate that the FliD protein of strain PAO1 is involved in the binding of glycoconjugates bearing Le(x) or sialyl-Le(x) determinants, while the binding of flagellin is restricted to the glycoconjugate bearing Le(x) glycotope [25].


  1. Induction of the PAOh1/SMO polyamine oxidase by polyamine analogues in human lung carcinoma cells. Devereux, W., Wang, Y., Stewart, T.M., Hacker, A., Smith, R., Frydman, B., Valasinas, A.L., Reddy, V.K., Marton, L.J., Ward, T.D., Woster, P.M., Casero, R.A. Cancer Chemother. Pharmacol. (2003) [Pubmed]
  2. 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., Igarashi, K. Stroke (2005) [Pubmed]
  3. Polyamines in renal failure. Igarashi, K., Ueda, S., Yoshida, K., Kashiwagi, K. Amino Acids (2006) [Pubmed]
  4. Induction of polyamine oxidase 1 by Helicobacter pylori causes macrophage apoptosis by hydrogen peroxide release and mitochondrial membrane depolarization. Chaturvedi, R., Cheng, Y., Asim, M., Bussière, F.I., Xu, H., Gobert, A.P., Hacker, A., Casero, R.A., Wilson, K.T. J. Biol. Chem. (2004) [Pubmed]
  5. Complementary roles for scavenger receptor A and CD36 of human monocyte-derived macrophages in adhesion to surfaces coated with oxidized low-density lipoproteins and in secretion of H2O2. Maxeiner, H., Husemann, J., Thomas, C.A., Loike, J.D., El Khoury, J., Silverstein, S.C. J. Exp. Med. (1998) [Pubmed]
  6. Production of the Pseudomonas aeruginosa neuraminidase is increased under hyperosmolar conditions and is regulated by genes involved in alginate expression. Cacalano, G., Kays, M., Saiman, L., Prince, A. J. Clin. Invest. (1992) [Pubmed]
  7. The broad host range pathogen Pseudomonas aeruginosa strain PA14 carries two pathogenicity islands harboring plant and animal virulence genes. He, J., Baldini, R.L., Déziel, E., Saucier, M., Zhang, Q., Liberati, N.T., Lee, D., Urbach, J., Goodman, H.M., Rahme, L.G. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  8. A simple alfalfa seedling infection model for Pseudomonas aeruginosa strains associated with cystic fibrosis shows AlgT (sigma-22) and RhlR contribute to pathogenesis. Silo-Suh, L., Suh, S.J., Sokol, P.A., Ohman, D.E. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  9. Toll-like receptor 5-mediated corneal epithelial inflammatory responses to Pseudomonas aeruginosa flagellin. Zhang, J., Xu, K., Ambati, B., Yu, F.S. Invest. Ophthalmol. Vis. Sci. (2003) [Pubmed]
  10. Pseudomonas aeruginosa virulence factors delay airway epithelial wound repair by altering the actin cytoskeleton and inducing overactivation of epithelial matrix metalloproteinase-2. de Bentzmann, S., Polette, M., Zahm, J.M., Hinnrasky, J., Kileztky, C., Bajolet, O., Klossek, J.M., Filloux, A., Lazdunski, A., Puchelle, E. Lab. Invest. (2000) [Pubmed]
  11. Partial genetic characterization of FIZ15 bacteriophage of Pseudomonas aeruginosa. Vaca, S., Pérez, S., Martínez, G., Enriquez, F. Rev. Latinoam. Microbiol. (1993) [Pubmed]
  12. Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin. Vujcic, S., Diegelman, P., Bacchi, C.J., Kramer, D.L., Porter, C.W. Biochem. J. (2002) [Pubmed]
  13. Potentiation of apple procyanidin-triggered apoptosis by the polyamine oxidase inactivator MDL 72527 in human colon cancer-derived metastatic cells. Gossé, F., Roussi, S., Guyot, S., Schoenfelder, A., Mann, A., Bergerat, J.P., Seiler, N., Raul, F. Int. J. Oncol. (2006) [Pubmed]
  14. Flavin-containing polyamine oxidase is a hydrogen peroxide source in the oxidative response to the protein phosphatase inhibitor cantharidin in Zea mays L. Cona, A., Rea, G., Botta, M., Corelli, F., Federico, R., Angelini, R. J. Exp. Bot. (2006) [Pubmed]
  15. Inflammation and polyamine catabolism: the good, the bad and the ugly. Babbar, N., Murray-Stewart, T., Casero, R.A. Biochem. Soc. Trans. (2007) [Pubmed]
  16. Heterologous expression and characterization of mouse spermine oxidase. Cervelli, M., Polticelli, F., Federico, R., Mariottini, P. J. Biol. Chem. (2003) [Pubmed]
  17. The exopolysaccharide alginate protects Pseudomonas aeruginosa biofilm bacteria from IFN-gamma-mediated macrophage killing. Leid, J.G., Willson, C.J., Shirtliff, M.E., Hassett, D.J., Parsek, M.R., Jeffers, A.K. J. Immunol. (2005) [Pubmed]
  18. Cross-strain protection against clinical and laboratory strains of Pseudomonas aeruginosa mediated by dendritic cells genetically modified to express CD40 ligand and pulsed with specific strains of Pseudomonas aeruginosa. Kikuchi, T., Hackett, N.R., Crystal, R.G. Hum. Gene Ther. (2001) [Pubmed]
  19. Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion. Vujcic, S., Liang, P., Diegelman, P., Kramer, D.L., Porter, C.W. Biochem. J. (2003) [Pubmed]
  20. Adherence to and penetration of human intestinal Caco-2 epithelial cell monolayers by Pseudomonas aeruginosa. Hirakata, Y., Izumikawa, K., Yamaguchi, T., Igimi, S., Furuya, N., Maesaki, S., Tomono, K., Yamada, Y., Kohno, S., Yamaguchi, K., Kamihira, S. Infect. Immun. (1998) [Pubmed]
  21. Catabolism of polyamines. Seiler, N. Amino Acids (2004) [Pubmed]
  22. Up-regulation of Fas expression by Pseudomonas aeruginosa-infected endothelial cells depends on modulation of iNOS and enhanced production of NO induced by bacterial type III secreted proteins. Assis, M.C., Freitas, C., Saliba, A.M., D'A Carvalho, A.P., Simao, T.A., Albano, R.M., Plotkowski, M.C. Int. J. Mol. Med. (2006) [Pubmed]
  23. Biochemical aspects and functional role of the copper-containing amine oxidases. Buffoni, F., Ignesti, G. Inflammopharmacology. (2003) [Pubmed]
  24. Mouse spermine oxidase gene splice variants. Nuclear subcellular localization of a novel active isoform. Cervelli, M., Bellini, A., Bianchi, M., Marcocci, L., Nocera, S., Polticelli, F., Federico, R., Amendola, R., Mariottini, P. Eur. J. Biochem. (2004) [Pubmed]
  25. Recognition of Lewis x derivatives present on mucins by flagellar components of Pseudomonas aeruginosa. Scharfman, A., Arora, S.K., Delmotte, P., Van Brussel, E., Mazurier, J., Ramphal, R., Roussel, P. Infect. Immun. (2001) [Pubmed]
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