Ras/mitogen-activated protein kinase mediates norepinephrine-induced phospholipase D activation in rabbit aortic smooth muscle cells by a phosphorylation-dependent mechanism.

@article{Muthalif2000RasmitogenactivatedPK,
  title={Ras/mitogen-activated protein kinase mediates norepinephrine-induced phospholipase D activation in rabbit aortic smooth muscle cells by a phosphorylation-dependent mechanism.},
  author={Mubarack M. Muthalif and J H Parmentier and Ibrahim Fadil Benter and Nour A. Karzoun and Aftab Ahmed and Zinat Khandekar and Mohammad Adl and Sylvain Bourgoin and Kafait U. Malik},
  journal={The Journal of pharmacology and experimental therapeutics},
  year={2000},
  volume={293 1},
  pages={268-74}
}
Phospholipase D (PLD) activity is regulated by phosphatidylinositol 4,5-biphosphate, protein kinase C (PKC), ADP-ribosylation factor, and Rho. The present study was designed to investigate the mechanism of norepinephrine (NE)-mediated PLD activation in rabbit aortic vascular smooth muscle cells (VSMC). NE (10 microM) caused activation of PLD, as measured by the production of phosphatidylethanol in [(3)H]oleic acid-labeled cells. NE also increased PKC activity in VSMC. However, treatment of… CONTINUE READING