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Volume 146, Issue 10

Dependence of upon polyamine backconversion Free

Abstract

grown for 16 h in the presence of [C]spermine formed a high intracellular pool of [C]spermidine and a small but detectable pool of [C]putrescine. When [H]putrescine was added to the growth medium, a large intracellular pool of [H]putrescine was found, but it was not further metabolized, confirming previous studies suggesting the absence of a forward-directed polyamine synthetic pathway in . Spermidine:spermine -acetyltransferase (SSAT) and polyamine oxidase enzyme activities were detected which collectively converted spermine to spermidine. Polyamine oxidase was localized in the hydrogenosome-enriched fraction, whereas SSAT was found predominantly in the cytosolic fraction. In the presence of saturating substrate, the trichomonad SSAT had an activity of 039±009 nmol min (mg protein) (the mean of five analyses) and an apparent for spermine of 17 μM. The enzyme was competitively inhibited by di(ethyl)spermine with a of 28 μM. Growth studies indicated that 50 μM di(ethyl)spermine caused a 68% and 84% reduction in the intracellular concentrations of spermidine and spermine, respectively. The trichomonad polyamine oxidase required FAD as a cofactor and had an apparent of 60 μM for -acetylspermine. The potential of bis(alkyl) polyamine analogues as antitrichomonad agents is discussed.

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  • Accepted:
  • Revised:
  • Published Online:
Keyword(s): acetylated polyamines , DENSpm, di(ethyl)norspermine , ODC, ornithine decarboxylase , polyamine oxidation , Polyamines , SSAT, spermidine:spermine N1-acetyltransferase and Trichomonas
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2000-10-01
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References

  1. Ariyanayagan M. R., Fairlamb A. H. 1997; Diamine auxotrophy may be a universal feature of Trypanosoma cruzi epimastigotes. . Mol Biochem Parasitol 84:111–121 [CrossRef]
     [Google Scholar]
  2. Bergeron R. J., Hawthorne T. R., Vinson J. R. T., Beck D. E. Jr, Ingeno M. J. 1989; Role of the methylene backbone in the antiproliferative activity of polyamine analogues on L1210 cells. Cancer Res 49:2959–2964
     [Google Scholar]
  3. Casero R. A. Jr, Pegg A. E. 1993; Spermidine/spermine N 1-acetyltransferase - the turning point in polyamine metabolism. FASEB J 7:653–661
     [Google Scholar]
  4. Casero R. A. Jr, Celano P., Ervin S. J., Porter C. W., Bergeron R. J., Libby P. R. 1989; Differential induction of spermidine/spermine N 1-acetyltransferase in human lung cancer cells by the bis(ethyl) polyamine analogues. Cancer Res 49:3829–3833
     [Google Scholar]
  5. Chapman A., Linstead D. J., Lloyd D., Williams J. 1985; 13C-NMR reveals glycerol as an unexpected major metabolite of the protozoan parasite Trichomonas vaginalis. FEBS Lett 191:287–292 [CrossRef]
     [Google Scholar]
  6. Cohen S. 1998; Polyamine oxidases and dehydrogenases. In A Guide to the Polyamines pp. 69–93 New York: Oxford University Press;
     [Google Scholar]
  7. Diamond L. 1957; The establishment of various trichomonads of animals and man in axenic cultures. J Parasitol 43:488–490
     [Google Scholar]
  8. Erwin B. G., Pegg A. E. 1986; Regulation of spermidine/spermine N 1-acetyltransferase in L6 cells by polyamines and related compounds. Biochem J 238:581–587
     [Google Scholar]
  9. Federico R., Ercolini L., Laurenzi M., Angelini R. 1996; Oxidation of acetylpolyamines by maize polyamine oxidase. Phytochemistry 43:339–341 [CrossRef]
     [Google Scholar]
  10. Feurstein B. G., Pattabiraman N., Marton L. J. 1990; Molecular mechanisms of the interactions of spermine with DNA:DNA bending as a result of ligand binding. Nucleic Acids Res 18:1271–1277 [CrossRef]
     [Google Scholar]
  11. Ha H. C., Woster P. M., Yager J. D., Casero R. A. Jr 1997; The role of polyamine catabolism in polyamine analogue-induced programmed cell death. Proc Natl Acad Sci U S A 94:11557–11562 [CrossRef]
     [Google Scholar]
  12. Holta E. 1977; Oxidation of spermidine and spermine in rat liver: purification and properties of polyamine oxidase. Biochemistry 16:91–100 [CrossRef]
     [Google Scholar]
  13. Kim B. G., Sobota A., Bitonti A. J., McCann P. P., Byers T. J. 1987; Polyamine metabolism in Acanthamoeba: polyamine content and synthesis of ornithine, putrescine, and diaminopropane. J Protozool 34:278–284 [CrossRef]
     [Google Scholar]
  14. Knodler L. A., Edwards M. R., Schofield P. J. 1994; The intracellular amino acid pools of Giardia intestinalis, Trichomonas vaginalis, and Crithidia luciliae. Exp Parasitol 79:117–125 [CrossRef]
     [Google Scholar]
  15. Libby P. R., Henderson M., Bergeron R. J., Porter C. W. 1989; Major increases in spermidine/spermine N 1-acetyltransferase activity by spermine analogues and their relationship to polyamine depletion and growth inhibition in L1210 cells. Cancer Res 49:6226–6231
     [Google Scholar]
  16. Lindmark D. G., Müller M. 1974; Biochemical cytology of trichomonad flagellates. II. Subcellular distributions of oxidoreductases and hydrolases in Monocercomonas sp. J Protozool 21:374–378 [CrossRef]
     [Google Scholar]
  17. Linstead D., Cranshaw M. A. 1983; The pathway of arginine catabolism in the parasitic flagellate Trichomonas vaginalis. Mol Biochem Parasitol 8:241–252 [CrossRef]
     [Google Scholar]
  18. Marton L. J., Pegg A. E. 1995; Polyamines as targets for therapeutic intervention. Annu Rev Pharmacol Toxicol 35:55–91 [CrossRef]
     [Google Scholar]
  19. Mondovi B., Avigliano L., Morpurgo L. 1988; In vitro specificity of Cu-amine oxidase inhibitors. Pharmacol Res Commun 20:39–43
     [Google Scholar]
  20. Müller M. 1989; Biochemistry of Trichomonas vaginalis. In Trichomonads Parasitic in Humans pp. 53–83Edited by Honigberg B. M. New York: Springer;
     [Google Scholar]
  21. Pavlov V., Nikolov I., Damjanov D., Dimitrov O. 1991; Distribution of polyamine oxidase activity in rat tissues and subcellular fractions. Experientia 47:1209–1211 [CrossRef]
     [Google Scholar]
  22. Pegg A. E., Wechter R., Pakala R., Bergeron R. J. 1989; Effect of N 1, N 2- bis(ethyl)spermine and related compounds on growth and polyamine acetylation, content, and excretion in human colon tumour cells. J Biol Chem 264:11744–11749
     [Google Scholar]
  23. Porter C. W., Ganis B., Libby P. R., Bergeron R. J. 1991; Correlations between polyamine analog-induced increases in spermidine/spermine N 1-acetyltransferase activity, polyamine pool depletion, and growth inhibition in human melanoma cells lines. Cancer Res 51:3715–3720
     [Google Scholar]
  24. Reis I. A., Martinez M. P., Yarlett N., Johnson P. J., Silva-Filho F. C., Vannier-Santos M. A. 1999; Inhibition of polyamine synthesis arrests trichomonad growth and induces destruction of hydrogenosomes. Antimicrob Agents Chemother 43:1919–1923
     [Google Scholar]
  25. Santoro G. F., Yarlett N., Vannier-Santos M. A. 1999; Effects of polyamine analogues on Trichomonas vaginalis. Acta Microscop 8:645
     [Google Scholar]
  26. Segal I. H. 1976 Biochemical Calculations New York: Wiley;
     [Google Scholar]
  27. Seiler N. 1987; Function of polyamine acetylation. . Can J Physiol Pharmacol 65:2024–2035 [CrossRef]
     [Google Scholar]
  28. Tabor C. W., Tabor H. 1984; Polyamines. Annu Rev Biochem 53:749–790 [CrossRef]
     [Google Scholar]
  29. Wallace H. M. 1987; Polyamine catabolism in mammalian cells: excretion and acetylation. Med Sci Res 15:1437–1440
     [Google Scholar]
  30. Woster P. M. 1993; Spermidine/spermine N 1-acetyltransferase (SSAT) – an emerging target for the design of anti-tumour agents. Curr Opin Invest Drugs 2:1291–1299
     [Google Scholar]
  31. Yarlett N. 1988; Polyamine biosynthesis and inhibition in Trichomonas vaginalis. Parasitol Today 4:357–360 [CrossRef]
     [Google Scholar]
  32. Yarlett N., Bacchi C. J. 1988; Effect of dl-α-difluoromethylornithine on polyamine synthesis and interconversion in Trichomonas vaginalis grown in a semi-defined medium. Mol Biochem Parasitol 31:1–10 [CrossRef]
     [Google Scholar]
  33. Yarlett N., Bacchi C. J. 1994; Parasite polyamine metabolism: targets for chemotherapy. Biochem Soc Trans 22:875–880
     [Google Scholar]
  34. Yarlett N., Goldberg B., Moharrami M. A., Bacchi C. J. 1993; Trichomonas vaginalis: characterization of ornithine decarboxylase. Biochem J 293:487–493
     [Google Scholar]
  35. Yarlett N., Lindmark D. G., Goldberg B., Moharrami M. A., Bacchi C. J. 1994; Subcellular localization of the enzymes of the arginine dihydrolase pathway in Trichomonas vaginalis and Tritrichomonas foetus. . J Euk Microbiol 41:554–559 [CrossRef]
     [Google Scholar]
  36. Yarlett N., Martinez M. P., Moharrami M. A., Tachezy J. 1996; The contribution of arginine dihydrolase pathway to energy metabolism by Trichomonas vaginalis. Mol Biochem Parasitol 78:117–125 [CrossRef]
     [Google Scholar]
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Dependence of Trichomonas vaginalis upon polyamine backconversion
Microbiology 146, 2715 (2000); https://doi.org/10.1099/00221287-146-10-2715
/content/journal/micro/10.1099/00221287-146-10-2715
/content/journal/micro/10.1099/00221287-146-10-2715
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