Paradoxical enhancement of S-adenosylmethionine decarboxylase in rat tissues following administration of the specific inhibitor methyl glyoxal bis(guanylhydrazone)

A. E. Pegg, A. Corti, H. G. Williams-Ashman

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Abstract

Treatment of rats with large but sublethal doses of methyl glyoxal bis(guanylhydrazone), a potent in vitro inhibitor of animal S-adenosylmethionine decarboxylases, causes marked increases in the enzyme activity of extracts of kidney, ventral prostate, and testis which had been extensively dialyzed to remove any remaining drug. One day after administration of the inhibitor to female rats, the renal S-adenosylmethionine decarboxylase activity was 12 times the normal level and remained greatly enhanced for a further 24 hr. As indicated by decline in decarboxylase activity following depression of protein biosynthesis by injection of cycloheximide, the apparent half-life of the kidney enzyme in normal female rats is roughly 2 hr; in contrast, the apparent half-life of the enzyme is elevated to a value of more than 20 hr in animals that were previously treated with methyl glyoxal bis(guanylhydrazone). The increased renal S-adenosylmethionine decarboxylase activity following administration of the specific enzyme inhibitor in vivo may thus be due, at least in part, to stabilization of the enzyme against intracellular inactivation as a result either of direct combination of the enzyme protein with the inhibitor, or with substance(s) in the tissue whose levels are influenced by treatment with methyl glyoxal bis(guanylhydrazone).

Original languageEnglish (US)
Pages (from-to)696-701
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume52
Issue number2
DOIs
StatePublished - May 15 1973

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Adenosylmethionine Decarboxylase
Rats
Tissue
Kidney
Enzymes
Animals
Half-Life
Carboxy-Lyases
Biosynthesis
Enzyme activity
Enzyme Inhibitors
Cycloheximide
Protein Biosynthesis
Proteins
Stabilization
Testis
Prostate
glyoxal bis(guanylhydrazone)
Injections
Pharmaceutical Preparations

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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title = "Paradoxical enhancement of S-adenosylmethionine decarboxylase in rat tissues following administration of the specific inhibitor methyl glyoxal bis(guanylhydrazone)",
abstract = "Treatment of rats with large but sublethal doses of methyl glyoxal bis(guanylhydrazone), a potent in vitro inhibitor of animal S-adenosylmethionine decarboxylases, causes marked increases in the enzyme activity of extracts of kidney, ventral prostate, and testis which had been extensively dialyzed to remove any remaining drug. One day after administration of the inhibitor to female rats, the renal S-adenosylmethionine decarboxylase activity was 12 times the normal level and remained greatly enhanced for a further 24 hr. As indicated by decline in decarboxylase activity following depression of protein biosynthesis by injection of cycloheximide, the apparent half-life of the kidney enzyme in normal female rats is roughly 2 hr; in contrast, the apparent half-life of the enzyme is elevated to a value of more than 20 hr in animals that were previously treated with methyl glyoxal bis(guanylhydrazone). The increased renal S-adenosylmethionine decarboxylase activity following administration of the specific enzyme inhibitor in vivo may thus be due, at least in part, to stabilization of the enzyme against intracellular inactivation as a result either of direct combination of the enzyme protein with the inhibitor, or with substance(s) in the tissue whose levels are influenced by treatment with methyl glyoxal bis(guanylhydrazone).",
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AB - Treatment of rats with large but sublethal doses of methyl glyoxal bis(guanylhydrazone), a potent in vitro inhibitor of animal S-adenosylmethionine decarboxylases, causes marked increases in the enzyme activity of extracts of kidney, ventral prostate, and testis which had been extensively dialyzed to remove any remaining drug. One day after administration of the inhibitor to female rats, the renal S-adenosylmethionine decarboxylase activity was 12 times the normal level and remained greatly enhanced for a further 24 hr. As indicated by decline in decarboxylase activity following depression of protein biosynthesis by injection of cycloheximide, the apparent half-life of the kidney enzyme in normal female rats is roughly 2 hr; in contrast, the apparent half-life of the enzyme is elevated to a value of more than 20 hr in animals that were previously treated with methyl glyoxal bis(guanylhydrazone). The increased renal S-adenosylmethionine decarboxylase activity following administration of the specific enzyme inhibitor in vivo may thus be due, at least in part, to stabilization of the enzyme against intracellular inactivation as a result either of direct combination of the enzyme protein with the inhibitor, or with substance(s) in the tissue whose levels are influenced by treatment with methyl glyoxal bis(guanylhydrazone).

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