Increased content of mRNA for a precursor of S-adenosylmethionine decarboxylase in rat prostate after treatment with 2-difluoromethylornithine

A. Shirahata, A. E. Pegg

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Abstract

Total poly(A)-containing mRNA was isolated from rat ventral prostate and translated in a reticulocyte lysate system. The proteins corresponding to S-adenosylmethionine decarboxylase were precipitated with a specific antiserum to this protein. Two proteins were found; one having an M(r) of 32,000, which corresponded to the subunit of this enzyme, and a larger protein of M(r) 37,000. Immunopurification of polysomes with the antiserum to S-adenosylmethionine decarboxylase followed by mRNA extraction yielded an mRNA preparation which was 10-30% pure mRNA for S-adenosylmethionine decarboxylase. The translation of this mRNA showed clearly that the protein of M(r) 37,000 was a precursor of the M(r) 32,000 S-adenosylmethionine decarboxylase subunit. Treatment with 2-difluoromethylornithine, which depletes cellular spermidine and is known to increase the content of S-adenosylmethionine decarboxylase protein, led to a 9-fold increase in the content of its mRNA, but treatment with methylglyoxal bis(guanylhydrazone) did not change the mRNA content.

Original languageEnglish (US)
Pages (from-to)13833-13837
Number of pages5
JournalJournal of Biological Chemistry
Volume261
Issue number29
StatePublished - Dec 1 1986

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Adenosylmethionine Decarboxylase
Eflornithine
RNA Precursors
Rats
Prostate
Messenger RNA
Proteins
Immune Sera
Mitoguazone
Spermidine
Polyribosomes
Reticulocytes
Protein Biosynthesis
Poly A
Enzymes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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title = "Increased content of mRNA for a precursor of S-adenosylmethionine decarboxylase in rat prostate after treatment with 2-difluoromethylornithine",
abstract = "Total poly(A)-containing mRNA was isolated from rat ventral prostate and translated in a reticulocyte lysate system. The proteins corresponding to S-adenosylmethionine decarboxylase were precipitated with a specific antiserum to this protein. Two proteins were found; one having an M(r) of 32,000, which corresponded to the subunit of this enzyme, and a larger protein of M(r) 37,000. Immunopurification of polysomes with the antiserum to S-adenosylmethionine decarboxylase followed by mRNA extraction yielded an mRNA preparation which was 10-30{\%} pure mRNA for S-adenosylmethionine decarboxylase. The translation of this mRNA showed clearly that the protein of M(r) 37,000 was a precursor of the M(r) 32,000 S-adenosylmethionine decarboxylase subunit. Treatment with 2-difluoromethylornithine, which depletes cellular spermidine and is known to increase the content of S-adenosylmethionine decarboxylase protein, led to a 9-fold increase in the content of its mRNA, but treatment with methylglyoxal bis(guanylhydrazone) did not change the mRNA content.",
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AU - Shirahata, A.

AU - Pegg, A. E.

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N2 - Total poly(A)-containing mRNA was isolated from rat ventral prostate and translated in a reticulocyte lysate system. The proteins corresponding to S-adenosylmethionine decarboxylase were precipitated with a specific antiserum to this protein. Two proteins were found; one having an M(r) of 32,000, which corresponded to the subunit of this enzyme, and a larger protein of M(r) 37,000. Immunopurification of polysomes with the antiserum to S-adenosylmethionine decarboxylase followed by mRNA extraction yielded an mRNA preparation which was 10-30% pure mRNA for S-adenosylmethionine decarboxylase. The translation of this mRNA showed clearly that the protein of M(r) 37,000 was a precursor of the M(r) 32,000 S-adenosylmethionine decarboxylase subunit. Treatment with 2-difluoromethylornithine, which depletes cellular spermidine and is known to increase the content of S-adenosylmethionine decarboxylase protein, led to a 9-fold increase in the content of its mRNA, but treatment with methylglyoxal bis(guanylhydrazone) did not change the mRNA content.

AB - Total poly(A)-containing mRNA was isolated from rat ventral prostate and translated in a reticulocyte lysate system. The proteins corresponding to S-adenosylmethionine decarboxylase were precipitated with a specific antiserum to this protein. Two proteins were found; one having an M(r) of 32,000, which corresponded to the subunit of this enzyme, and a larger protein of M(r) 37,000. Immunopurification of polysomes with the antiserum to S-adenosylmethionine decarboxylase followed by mRNA extraction yielded an mRNA preparation which was 10-30% pure mRNA for S-adenosylmethionine decarboxylase. The translation of this mRNA showed clearly that the protein of M(r) 37,000 was a precursor of the M(r) 32,000 S-adenosylmethionine decarboxylase subunit. Treatment with 2-difluoromethylornithine, which depletes cellular spermidine and is known to increase the content of S-adenosylmethionine decarboxylase protein, led to a 9-fold increase in the content of its mRNA, but treatment with methylglyoxal bis(guanylhydrazone) did not change the mRNA content.

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