Signaling pathways regulating ornithine decarboxylase activity in the embryonic chicken.
The pathways regulating ornithine decarboxylase (ODC) activity in the chick embryo were studied to determine which kinase-signaling pathways regulate ODC activity levels during development. Insulin-dependent tyrosine kinase, protein kinase C and cAMP-dependent protein kinase were activated by the addition of insulin, tetradecanoylphorbol-12,13-acetate, and forskolin, respectively. All three drugs increased ODC activity and forskolin combined with insulin increased ODC activity above the increase caused by either drug alone. These results suggest that all three signaling pathways regulate ODC activity during development and that common intermediates exist among the pathways downstream of the kinases.
Shibley
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Department of Biochemistry, East Carolina University School of Medicine, Greenville 27834, USA.
Pennington
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D000818:Animals; D002642:Chick Embryo; D017868:Cyclic AMP-Dependent Protein Kinases / Q000494:pharmacology*; D007328:Insulin / Q000494:pharmacology*; D009955:Ornithine Decarboxylase / Q000187:drug effects / Q000378:metabolism*; D011493:Protein Kinase C / Q000494:pharmacology*; D011505:Protein-Tyrosine Kinases / Q000494:pharmacology*; D015398:Signal Transduction / Q000502:physiology*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D007328:Insulin; D011505:Protein-Tyrosine Kinases; D017868:Cyclic AMP-Dependent Protein Kinases; D011493:Protein Kinase C; D009955:Ornithine Decarboxylase; D013755:Tetradecanoylphorbol Acetate