Control of ornithine decarboxylase activity by cyclic nucleotides in the phytohemagglutinin induced lymphocyte transformation

doi:10.1016/S0006-291X(75)80332-9

Biochemical and Biophysical Research Communications

Volume 66, Issue 1, 2 September 1975, Pages 328-335

https://doi.org/10.1016/S0006-291X(75)80332-9 Get rights and content

Summary

N²,O^2′-Dibutyryl guanosine 3′:5′-cyclic monophosphate enhanced the ornithine decarboxylase activity which was induced during lymphocyte transformation by phytohemagglutinin, while N⁶,O^2′-dibutyryl adenosine 3′:5′-cyclic monophosphate tended to inhibit it. The increased ornithine decarboxylase activity was not observed when N²,O^2′-dibutyryl guanosine 3′:5′-cyclic monophosphate alone was added to the non-stimulated lymphocytes. In contrast to the dibutyryl derivative, guanosine 3′:5′-cyclic monophosphate did not show any effect on enzyme induction following phytohemagglutinin stimulation.

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Induction of ornithine decarboxylase in guinea-pig lymphocytes and its relation to phospholipid metabolism
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Treatment of lymphocytes with exogenous phospholipase C (phosphatidylcholine cholinephosphohydrolase, EC 3.1.4.3.) derived from Clostridium perfringens at concentrations similar to those which induced ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) activity produced diacylglycerol and phosphatidate. A divalent cation ionophore, A23187, and phytohemagglutinin induced not only diacylglycerol formation, but also ornithine decarboxylase activity. Dibutyryl cAMP inhibited both diacylglycerol formation and ornithine decarboxylase induction to a similar extent in phytohemagglutinin-stimulated lymphocytes, but stimulated them somewhat in ionophore A23187-activated lymphocytes. This suggests that the activation of intracellular phospholipase C and the formation of diacylglycerol is involved in ornithine decarboxylase induction in lymphocytes.
Induction of ornithine decarboxylase by treatment of guinea pig lymphocytes with phospholipase C
1983, FEBS Letters
Treatment of guinea pig lymphocytes with Clostridium perfringens phospholipase C but not with Naja naja snake venom phospholipase A₂ increased ornithine decarboxylase activity. The increase in ornithine decarboxylase activity was suppressed by actinomycin D or cycloheximide, suggesting that de novo syntheses of RNA and protein are necessary for the increase in the enzyme activity. These results suggest that the activation of phospholipase C rather than that of phospholipase A₂ is responsible for induction of ornithine decarboxylase during lymphocyte transformation.
Polyamines in Mammalian Tumors Part I
1981, Advances in Cancer Research
This chapter reviews selectively and in detail the extensive literature on the connections between the polyamines and cancer in mammals and judges whether these connections are coincidental or characteristic of the neoplastic disease process. A customary and widely accepted definition of a tumor is that it is a mass of abnormal cells with altered phenotypes. Its many differences from normal cells, in both morphological and biochemical features, lead to excessive growth of the tumorous cells. The aliphatic polyamines are nonprotein, polycationic substances that are widely distributed in living organisms and in biological fluids. Four enzymes are known to be involved in the biosynthesis of polyamines in eukaryotic organisms: two decarboxylases and two synthases. Oncogenic viruses are not only of great importance in the etiology of some animal tumors, but some human tumors are also associated with and actually strongly suspected to be caused by viruses. A normal cell population is transformed by infection with an oncogenic virus, followed by isolation of colonies of cells with altered properties. RNA tumor viruses possess attractive features for study of mechanisms involved in cell transformation.
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Induction of ornithine decarboxylase by biliverdin in rat liver
1979, Life Sciences
The administration of biliverdin (0.1mg/g of body weight) into the peritoneal cavity of rats resulted in the induction of ornithine decarboxylase in the liver. When the temporal relationships between the changes in intracellular adenosine 3', 5'-cyclic monophosphate (cyclic AMP) level, cyclic AMP-dependent protein kinase activity and the induction of ornithine decarboxylase were investigated, the concentration of cyclic AMP increased significantly 2 h after the administration of biliverdin, while cyclic AMP-dependent protein kinase was activated after 2–4 h. The hepatic ornithine decarboxylase activity began to increase 4 h after biliverdin injection. These results suggest that there is some sequential relationship between the increase of cyclic AMP, the activation of cyclic AMP-dependent protein kinase and the induction of ornithine decarboxylase although the direct correlation of these three events remains to be elucidated.
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1979, Advances in Enzyme Regulation
- 1.
  (1) Ornithine decarboxylase induction in response to a variety of trophic stimuli, including trophic hormones, appears to occur via a transcriptional mechanism mediated by the activation of cyclic AMP-dependent protein kinase.
- 2.
  (2) Evidence from cell cycle progression studies suggests that ornithine decarboxylase induction is a universal marker of G₁ phase of the cell cycle and is a mandatory event for cells to traverse G₁ phase and enter S phase.
- 3.
  (3) Specific activation of type I cyclic AMP-dependent protein kinase has been implicated in ornithine decarboxylase induction in cell cycle, lymphocyte mitogenesis, and cardiac hypertrophy.
- 4.
  (4) Studies of protein kinase alterations and ornithine decarboxylase activity in the intact prostate after castration link steroid action to the ability of steroid-responsive tissues to maintain substantial concentrations of type I cyclic AMP-dependent protein kinase.

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Control of ornithine decarboxylase activity by cyclic nucleotides in the phytohemagglutinin induced lymphocyte transformation

Summary

Biochem. Biophys. Res. Commun.

J. Biol. Chem.

FEBS Letters

Exp. Cell. Res.

Biochem. Biophys. Res. Commun.

Biochem. Biophys. Res. Commun.

FEBS Letters

J. Cell Physiol.

Nature

Nature

J. Natl. Cancer Inst.

Nature New Biology