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Keynote review: phosphodiesterase-4 as a therapeutic target
findings identify PC2 and PDE4C as unique components of an AKAP complex in primary cilia and reveal a common mechanism for dysregulation of cAMP signaling in cystic kidney diseases arising from different gene mutations
Data show that PDE4C is downregulated through promoter hypermethylation in glioma.
PDE4A and PDE4C work in redundant fashion to mediate the loss of inhibitory PGE2 signaling in lung fibroblasts.
The protein encoded by this gene belongs to the cyclic nucleotide phosphodiesterase (PDE) family, and PDE4 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 described for this gene.
cAMP-specific 3',5'-cyclic phosphodiesterase 4C
, phosphodiesterase 4C, cAMP-specific (phosphodiesterase E1 dunce homolog, Drosophila)
, phosphodiesterase 4C, cAMP-specific (phosphodiesterase E1 dunce homolog)
, phosphodiesterase E1 dunce homolog
, cAMP-specific 35-cyclic phosphodiesterase 4C