Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1985 Oct 15;231(2):285–289. doi: 10.1042/bj2310285

Induction of spermidine/spermine N1-acetyltransferase in rat tissues by polyamines.

A E Pegg, B G Erwin
PMCID: PMC1152743  PMID: 4062898

Abstract

Treatment of rats with spermidine, spermine or sym-norspermidine led to a substantial induction of spermidine/spermine N1-acetyltransferase activity in liver, kidney and lung. The increase in this enzyme, which was determined independently of other acetylases by using a specific antiserum, accounted for all of the increased acetylase activity in extracts from rats treated with these polyamines. Spermine was the most active inducer, and the greatest effect was seen in liver. Liver spermidine/spermine N1-acetyltransferase activity was increased about 300-fold within 6 h of treatment with 0.3 mmol/kg doses of spermine; activity in kidney increased 30-fold and activity in the lung 15-fold under these conditions. The increased spermidine/spermine N1-acetyltransferase activity led to a large increase in the liver putrescine content and a decline in spermidine. These changes are due to the oxidation by polyamine oxidase of the N1-acetylspermidine formed by the acetyltransferase. Our results indicated that spermidine was the preferred substrate in vivo of the acetylase/oxidase pathway for the conversion of the higher polyamines into putrescine. The induction of the spermidine/spermine N1-acetyltransferase by polyamines may provide a mechanism by which excess polyamines can be removed.

Full text

PDF
285

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Blankenship J. Deacetylation of N8-acetylspermidine by subcellular fractions of rat tissue. Arch Biochem Biophys. 1978 Jul;189(1):20–27. doi: 10.1016/0003-9861(78)90109-1. [DOI] [PubMed] [Google Scholar]
  2. Blankenship J. Metabolic conversion of N1-acetylspermidine to putrescine by a subcellular fraction of rat liver. Proc West Pharmacol Soc. 1979;22:115–118. [PubMed] [Google Scholar]
  3. Bolkenius F. N., Bey P., Seiler N. Specific inhibition of polyamine oxidase in vivo is a method for the elucidation of its physiological role. Biochim Biophys Acta. 1985 Jan 28;838(1):69–76. doi: 10.1016/0304-4165(85)90251-x. [DOI] [PubMed] [Google Scholar]
  4. Bolkenius F. N., Seiler N. Acetylderivatives as intermediates in polyamine catabolism. Int J Biochem. 1981;13(3):287–292. doi: 10.1016/0020-711x(81)90080-x. [DOI] [PubMed] [Google Scholar]
  5. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  6. Canellakis E. S., Viceps-Madore D., Kyriakidis D. A., Heller J. S. The regulation and function of ornithine decarboxylase and of the polyamines. Curr Top Cell Regul. 1979;15:155–202. [PubMed] [Google Scholar]
  7. Della Ragione F., Pegg A. E. Studies of the specificity and kinetics of rat liver spermidine/spermine N1-acetyltransferase. Biochem J. 1983 Sep 1;213(3):701–706. doi: 10.1042/bj2130701. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Erwin B. G., Persson L., Pegg A. E. Differential inhibition of histone and polyamine acetylases by multisubstrate analogues. Biochemistry. 1984 Aug 28;23(18):4250–4255. doi: 10.1021/bi00313a036. [DOI] [PubMed] [Google Scholar]
  9. Jänne J., Pösö H., Raina A. Polyamines in rapid growth and cancer. Biochim Biophys Acta. 1978 Apr 6;473(3-4):241–293. doi: 10.1016/0304-419x(78)90015-x. [DOI] [PubMed] [Google Scholar]
  10. Libby P. R. Acetylspermidine deacetylase (rat liver). Methods Enzymol. 1983;94:329–331. doi: 10.1016/s0076-6879(83)94059-4. [DOI] [PubMed] [Google Scholar]
  11. Libby P. R. Properties of an acetylspermidine deacetylase from rat liver. Arch Biochem Biophys. 1978 Jun;188(2):360–363. doi: 10.1016/s0003-9861(78)80020-4. [DOI] [PubMed] [Google Scholar]
  12. Matsui I., Pösö H., Pegg A. E. Conversion of exogenous spermidine into putrescine after administration to rats. Biochim Biophys Acta. 1982 Nov 24;719(2):199–207. doi: 10.1016/0304-4165(82)90089-7. [DOI] [PubMed] [Google Scholar]
  13. Matsui I., Wiegand L., Pegg A. E. 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. 1981 Mar 10;256(5):2454–2459. [PubMed] [Google Scholar]
  14. Pegg A. E., Matsui I., Seely J. E., Pritchard M. L., Pösö H. Formation of putrescine in rat liver. Med Biol. 1981 Dec;59(5-6):327–333. [PubMed] [Google Scholar]
  15. Pegg A. E., McCann P. P. Polyamine metabolism and function. Am J Physiol. 1982 Nov;243(5):C212–C221. doi: 10.1152/ajpcell.1982.243.5.C212. [DOI] [PubMed] [Google Scholar]
  16. Pegg A. E., Seely J. E., Pösö H., della Ragione F., Zagon I. A. Polyamine biosynthesis and interconversion in rodent tissues. Fed Proc. 1982 Dec;41(14):3065–3072. [PubMed] [Google Scholar]
  17. Persson L., Pegg A. E. Studies of the induction of spermidine/spermine N1-acetyltransferase using a specific antiserum. J Biol Chem. 1984 Oct 25;259(20):12364–12367. [PubMed] [Google Scholar]
  18. Pösö H., Pegg A. E. Effect of carbon tetrachloride on polyamine metabolism in rodent liver. Arch Biochem Biophys. 1982 Sep;217(2):730–737. doi: 10.1016/0003-9861(82)90554-9. [DOI] [PubMed] [Google Scholar]
  19. Santacroce M. J., Blankenship J. Inhibition of acetylspermidine deacetylating activity from rat liver. Proc West Pharmacol Soc. 1982;25:113–118. [PubMed] [Google Scholar]
  20. Seely J. E., Pegg A. E. Effect of 1,3-diaminopropane on ornithine decarboxylase enzyme protein in thioacetamide-treated rat liver. Biochem J. 1983 Dec 15;216(3):701–707. doi: 10.1042/bj2160701. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Seiler N., Bolkenius F. N., Knödgen B. The influence of catabolic reactions on polyamine excretion. Biochem J. 1985 Jan 1;225(1):219–226. doi: 10.1042/bj2250219. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Seiler N., Bolkenius F. N., Rennert O. M. Interconversion, catabolism and elimination of the polyamines. Med Biol. 1981 Dec;59(5-6):334–346. [PubMed] [Google Scholar]
  23. Seiler N., Knödgen B., Haegele K. N-(3-aminopropyl)pyrrolidin-2-one, a product of spermidine catabolism in vivo. Biochem J. 1982 Oct 15;208(1):189–197. doi: 10.1042/bj2080189. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Sjoerdsma A., Schechter P. J. Chemotherapeutic implications of polyamine biosynthesis inhibition. Clin Pharmacol Ther. 1984 Mar;35(3):287–300. doi: 10.1038/clpt.1984.33. [DOI] [PubMed] [Google Scholar]
  25. Sjoerdsma A. Suicide enzyme inhibitors as potential drugs. Clin Pharmacol Ther. 1981 Jul;30(1):3–22. doi: 10.1038/clpt.1981.121. [DOI] [PubMed] [Google Scholar]
  26. Tabor C. W., Tabor H. 1,4-Diaminobutane (putrescine), spermidine, and spermine. Annu Rev Biochem. 1976;45:285–306. doi: 10.1146/annurev.bi.45.070176.001441. [DOI] [PubMed] [Google Scholar]
  27. Tabor C. W., Tabor H. Polyamines. Annu Rev Biochem. 1984;53:749–790. doi: 10.1146/annurev.bi.53.070184.003533. [DOI] [PubMed] [Google Scholar]
  28. Van den Berg G. A., Elzinga H., Nagel G. T., Kingma A. W., Muskiet F. A. Catabolism of polyamines in the rat. Polyamines and their non-alpha-amino acid metabolites. Biochim Biophys Acta. 1984 Nov 28;802(2):175–187. doi: 10.1016/0304-4165(84)90159-4. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES