Protein kinase C-mediated phosphorylation and activation of PDE3A regulate cAMP levels in human platelets.

@article{Hunter2009ProteinKC,
  title={Protein kinase C-mediated phosphorylation and activation of PDE3A regulate cAMP levels in human platelets.},
  author={Roger W. Hunter and Carol MacKintosh and Ingeborg Hers},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 18},
  pages={12339-48}
}
The elevation of [cAMP](i) is an important mechanism of platelet inhibition and is regulated by the opposing activity of adenylyl cyclase and phosphodiesterase (PDE). In this study, we demonstrate that a variety of platelet agonists, including thrombin, significantly enhance the activity of PDE3A in a phosphorylation-dependent manner. Stimulation of platelets with the PAR-1 agonist SFLLRN resulted in rapid and transient phosphorylation of PDE3A on Ser(312), Ser(428), Ser(438), Ser(465), and Ser… CONTINUE READING

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