Growth signal transduction: rapid activation of covalently bound ornithine decarboxylase during phosphatidylinositol breakdown.
We have previously shown that treatment of T lymphocytes with mitogenic ligands induces a rapid activation of ornithine decarboxylase (ODC) through a mechanism that is independent of protein synthesis but requires energy and an intact cytoskeleton. Here we show by immunoprecipitation experiments and by chemical analyses that ODC is covalently linked to the cell membrane by inositol. Treatment of sonicated cells with a phosphatidylinositol-specific phospholipase C from B. thuringiensis caused a rapid 3-fold increase in ODC activity. Similar treatment of intact cells had no effect, suggesting that the ODC is attached to the cytoplasmic surface of the membrane. We conclude that ODC release and activation occur by a novel mechanism involving phosphatidylinositol breakdown following ligand-receptor interaction.
D000818:Animals; D002453:Cell Cycle; D002462:Cell Membrane / Q000201:enzymology; D004789:Enzyme Activation; D007295:Inositol Phosphates / Q000378:metabolism; D007700:Kinetics; D008213:Lymphocyte Activation; D051379:Mice; D009955:Ornithine Decarboxylase / Q000378:metabolism*; D010716:Phosphatidylinositols / Q000378:metabolism*; D011975:Receptors, Mitogen / Q000502:physiology; D013601:T-Lymphocytes / Q000166:cytology* / Q000201:enzymology; D010738:Type C Phospholipases / Q000378:metabolism
D007295:Inositol Phosphates; D010716:Phosphatidylinositols; D011975:Receptors, Mitogen; D010738:Type C Phospholipases; D009955:Ornithine Decarboxylase