Differential inhibition of mammalian aminopropyltransferase activities

Hiroshige Hibasami, Anthony Pegg

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Rat ventral prostate spermine synthetase was inhibited by 5′-methylthioadenosine and by S-adenosylhomocysteine at concentrations which did not inhibit spermidine synthetase from the same tissue. S-Adenosylethionine inhibited both enzymes to an equal extent. These aminopropyltransferases were also inhibited by diamines not normally present in mammalian cells. All the α,ω-diamines with 3 to 12 C atoms had inhibitory activity, but 1,3-diaminopropane and 1,5-diaminopentane were most active. Spermine synthetase was more sensitive than spermidine synthetase to the effects of these diamines. These results suggest that the relative rates of spermidine and spermine formation in,vivo might be affected by the intracellular concentration of nucleosides such as S-adenosylhomocysteine. They also raise the possibility that these rates of synthesis could be selectively affected by administration of one or the other of these inhibitors.

Original languageEnglish (US)
Pages (from-to)1398-1405
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume81
Issue number4
DOIs
StatePublished - Apr 28 1978

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Spermidine Synthase
Diamines
Spermine Synthase
S-Adenosylhomocysteine
Spermidine
Spermine
Nucleosides
Rats
Prostate
Cells
Tissue
Atoms
Enzymes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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title = "Differential inhibition of mammalian aminopropyltransferase activities",
abstract = "Rat ventral prostate spermine synthetase was inhibited by 5′-methylthioadenosine and by S-adenosylhomocysteine at concentrations which did not inhibit spermidine synthetase from the same tissue. S-Adenosylethionine inhibited both enzymes to an equal extent. These aminopropyltransferases were also inhibited by diamines not normally present in mammalian cells. All the α,ω-diamines with 3 to 12 C atoms had inhibitory activity, but 1,3-diaminopropane and 1,5-diaminopentane were most active. Spermine synthetase was more sensitive than spermidine synthetase to the effects of these diamines. These results suggest that the relative rates of spermidine and spermine formation in,vivo might be affected by the intracellular concentration of nucleosides such as S-adenosylhomocysteine. They also raise the possibility that these rates of synthesis could be selectively affected by administration of one or the other of these inhibitors.",
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Differential inhibition of mammalian aminopropyltransferase activities. / Hibasami, Hiroshige; Pegg, Anthony.

In: Biochemical and Biophysical Research Communications, Vol. 81, No. 4, 28.04.1978, p. 1398-1405.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Differential inhibition of mammalian aminopropyltransferase activities

AU - Hibasami, Hiroshige

AU - Pegg, Anthony

PY - 1978/4/28

Y1 - 1978/4/28

N2 - Rat ventral prostate spermine synthetase was inhibited by 5′-methylthioadenosine and by S-adenosylhomocysteine at concentrations which did not inhibit spermidine synthetase from the same tissue. S-Adenosylethionine inhibited both enzymes to an equal extent. These aminopropyltransferases were also inhibited by diamines not normally present in mammalian cells. All the α,ω-diamines with 3 to 12 C atoms had inhibitory activity, but 1,3-diaminopropane and 1,5-diaminopentane were most active. Spermine synthetase was more sensitive than spermidine synthetase to the effects of these diamines. These results suggest that the relative rates of spermidine and spermine formation in,vivo might be affected by the intracellular concentration of nucleosides such as S-adenosylhomocysteine. They also raise the possibility that these rates of synthesis could be selectively affected by administration of one or the other of these inhibitors.

AB - Rat ventral prostate spermine synthetase was inhibited by 5′-methylthioadenosine and by S-adenosylhomocysteine at concentrations which did not inhibit spermidine synthetase from the same tissue. S-Adenosylethionine inhibited both enzymes to an equal extent. These aminopropyltransferases were also inhibited by diamines not normally present in mammalian cells. All the α,ω-diamines with 3 to 12 C atoms had inhibitory activity, but 1,3-diaminopropane and 1,5-diaminopentane were most active. Spermine synthetase was more sensitive than spermidine synthetase to the effects of these diamines. These results suggest that the relative rates of spermidine and spermine formation in,vivo might be affected by the intracellular concentration of nucleosides such as S-adenosylhomocysteine. They also raise the possibility that these rates of synthesis could be selectively affected by administration of one or the other of these inhibitors.

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