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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Phosphodiesterase 8A

The protein encoded by this gene belongs to the cyclic nucleotide phosphodiesterase (PDE) family, and PDE8 subfamily. This PDE hydrolyzes the second messenger, cAMP, which is a regulator and mediator of a number of cellular responses to extracellular signals. Thus, by regulating the cellular concentration of cAMP, this protein plays a key role in many important physiological processes. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Jul 2011] (from NCBI)
Papers on PDE8A
Cyclic AMP-specific phosphodiesterase, PDE8A1, is activated by protein kinase A-mediated phosphorylation.
Baillie et al., Glasgow, United Kingdom. In Febs Lett, 2012
PDE8 activity can be modulated by a kinase
cAMP-specific phosphodiesterases 8A and 8B, essential regulators of Leydig cell steroidogenesis.
Beavo et al., Seattle, United States. In Mol Pharmacol, 2012
findings suggest that both PDE8A and PDE8B play essential roles to maintain low cAMP levels, thereby suppressing resting steroidogenesis by keeping CEH/HSL inactive and StAR protein expression low
Polymorphism in HIV-1 dependency factor PDE8A affects mRNA level and HIV-1 replication in primary macrophages.
van 't Wout et al., Amsterdam, Netherlands. In Virology, 2011
Polymorphism in PDE8A affects HIV-1 replication in primary macrophages.
Phosphodiesterase 8A (PDE8A) regulates excitation-contraction coupling in ventricular myocytes.
Beavo et al., Seattle, United States. In J Mol Cell Cardiol, 2010
PDE8A plays a critical role in the modulation of at least one compartment of cAMP and hence PKA activity during beta-adrenergic receptor (betaAR) activation in ventricular myocytes.
PDE8 regulates rapid Teff cell adhesion and proliferation independent of ICER.
Brocke et al., Farmington, United States. In Plos One, 2009
PDE8 as a novel target for suppression of Teff cell functions, including adhesion to endothelial cells
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