Treatment with α-difluoromethylornithine plus a spermidine analog leads to spermine depletion and growth inhibition in cultured L1210 leukemia cells

Robert A Casero, R. J. Bergeron, C. W. Porter

Research output: Contribution to journalArticle

Abstract

Of the three biological polyamines, putrescine (Put), spermidine (Spd), and spermine (Spm), the relevance of Spm to cell proliferation has yet to be defined because of our general inability to deplete it selectively in intact cells. In the present study, Spm depletion was accomplished by treating cultured L1210 cells for 96 hr with α-difluoromethylornithine (DFMO) and an analog of Spd such as aminopropylcadaverine, N4-methylSpd, N4-ethylSpd, or homoSpd. DFMO, a specific inhibitor of ornithine decarboxylase, halts continued polyamine biosynthesis and the Spd analog serves as a functional substitute for Spd. Thus, while the Spd analog fulfills the role(s) of Spd in cell proliferation, Spm becomes steadily depleted. In cells treated with DFMO plus the analog, aminopropylcadaverine, Spm pools decline steadily and growth inhibition occurs after 48 hr (when Spm pools decline to 60% of control). By 96 hr, Spm is ~15% of control and growth is

Original languageEnglish (US)
Pages (from-to)476-482
Number of pages7
JournalJournal of Cellular Physiology
Volume121
Issue number3
StatePublished - 1984
Externally publishedYes

Fingerprint

Eflornithine
Leukemia L1210
Spermidine
Spermine
Growth
Cell proliferation
Polyamines
Cell Proliferation
Putrescine
Biosynthesis
Cultured Cells

ASJC Scopus subject areas

  • Cell Biology
  • Clinical Biochemistry
  • Physiology

Cite this

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title = "Treatment with α-difluoromethylornithine plus a spermidine analog leads to spermine depletion and growth inhibition in cultured L1210 leukemia cells",
abstract = "Of the three biological polyamines, putrescine (Put), spermidine (Spd), and spermine (Spm), the relevance of Spm to cell proliferation has yet to be defined because of our general inability to deplete it selectively in intact cells. In the present study, Spm depletion was accomplished by treating cultured L1210 cells for 96 hr with α-difluoromethylornithine (DFMO) and an analog of Spd such as aminopropylcadaverine, N4-methylSpd, N4-ethylSpd, or homoSpd. DFMO, a specific inhibitor of ornithine decarboxylase, halts continued polyamine biosynthesis and the Spd analog serves as a functional substitute for Spd. Thus, while the Spd analog fulfills the role(s) of Spd in cell proliferation, Spm becomes steadily depleted. In cells treated with DFMO plus the analog, aminopropylcadaverine, Spm pools decline steadily and growth inhibition occurs after 48 hr (when Spm pools decline to 60{\%} of control). By 96 hr, Spm is ~15{\%} of control and growth is",
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AU - Casero, Robert A

AU - Bergeron, R. J.

AU - Porter, C. W.

PY - 1984

Y1 - 1984

N2 - Of the three biological polyamines, putrescine (Put), spermidine (Spd), and spermine (Spm), the relevance of Spm to cell proliferation has yet to be defined because of our general inability to deplete it selectively in intact cells. In the present study, Spm depletion was accomplished by treating cultured L1210 cells for 96 hr with α-difluoromethylornithine (DFMO) and an analog of Spd such as aminopropylcadaverine, N4-methylSpd, N4-ethylSpd, or homoSpd. DFMO, a specific inhibitor of ornithine decarboxylase, halts continued polyamine biosynthesis and the Spd analog serves as a functional substitute for Spd. Thus, while the Spd analog fulfills the role(s) of Spd in cell proliferation, Spm becomes steadily depleted. In cells treated with DFMO plus the analog, aminopropylcadaverine, Spm pools decline steadily and growth inhibition occurs after 48 hr (when Spm pools decline to 60% of control). By 96 hr, Spm is ~15% of control and growth is

AB - Of the three biological polyamines, putrescine (Put), spermidine (Spd), and spermine (Spm), the relevance of Spm to cell proliferation has yet to be defined because of our general inability to deplete it selectively in intact cells. In the present study, Spm depletion was accomplished by treating cultured L1210 cells for 96 hr with α-difluoromethylornithine (DFMO) and an analog of Spd such as aminopropylcadaverine, N4-methylSpd, N4-ethylSpd, or homoSpd. DFMO, a specific inhibitor of ornithine decarboxylase, halts continued polyamine biosynthesis and the Spd analog serves as a functional substitute for Spd. Thus, while the Spd analog fulfills the role(s) of Spd in cell proliferation, Spm becomes steadily depleted. In cells treated with DFMO plus the analog, aminopropylcadaverine, Spm pools decline steadily and growth inhibition occurs after 48 hr (when Spm pools decline to 60% of control). By 96 hr, Spm is ~15% of control and growth is

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