Reconstitution of alpha2D-adrenergic receptor coupling to phospholipase D in a PC12 cell lysate.

The Journal of Biological Chemistry
A Jinsi-Parimoo, Richard C Deth

Abstract

We have previously shown that alpha2-adrenergic receptor-mediated coupling to phospholipase D (PLD) in vascular tissues requires a tyrosine kinase activity (Jinsi, A., Paradise, J., and Deth, R. C. (1996) Eur. J. Pharmacol. 302, 183-190). To further clarify this mode of regulation we reconstituted alpha2A/D-adrenergic receptor-stimulated PLD activity in PC12 cells expressing the cloned receptor. [3H]Myristic acid-labeled cells were lysed by nitrogen cavitation, and aliquots of subnuclear fraction were utilized in the PLD assay. Agonist-stimulated PLD activity was measured in the presence of 0.4% butanol as [3H]phosphatidylbutanol formation. Both GTP and its non-hydrolyzable analog guanosine 5'-O-(thiotriphosphate) stimulated PLD activity in a concentration- and time-dependent manner that required co-activation of protein kinase C by phorbol dibutyrate. Addition of epinephrine produced a 3-fold stimulation of PLD activity in the presence of GTP and GDP. This agonist-stimulated PLD activity was completely blocked by the alpha2-adrenergic receptor antagonist rauwolscine and by Clostridium botulinum toxin as well as by antibodies directed against either pp60(src), RhoA, or Ras GTPase-activating protein. These results indicate that ...Continue Reading

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Citations

Nov 24, 1999·Journal of Cellular Physiology·T C Gibbs, K E Meier
Nov 8, 2003·Molecular and Cellular Endocrinology·Susan E Senogles
Apr 2, 2003·Biochimica Et Biophysica Acta·Sanjoy MehtaJoel Horwitz
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