Phosphorylation of cAMP hydrolyzing PDE (PDE3A) by cGMP-dependent protein kinase (PKG) in human platelets
✍ Scribed by Sergei D Rybalkin; Irina G Rybalkina; Joseph A Beavo
- Publisher
- BioMed Central
- Year
- 2007
- Tongue
- English
- Weight
- 186 KB
- Volume
- 7
- Category
- Article
- ISSN
- 1471-2210
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✦ Synopsis
Endogenous inhibitory mediators such as prostacyclin and nitric oxide keep platelet activation under tight control through the corresponding cGMP and cAMP signaling pathways. Intracellular levels of cAMP and cGMP are regulated by cyclic-nucleotide phosphodiesterases (PDEs). PDE3A (also known as cGMP-inhibited cAMP PDE) and PDE5 (cGMP specific PDE) are major cAMP-hydrolyzing and cGMP hydrolyzing PDEs expressed in platelets. Platelet PDE3A has been found to be phosphorylated and activated by PKA [1] and PDE5 by PKG [2]. Here we report that in human platelets PKG can also phosphorylate PDE3A, providing an additional cross-talk between cGMP and cAMP signaling.