PDE4B


Also found in: Acronyms.

PDE4B

A gene on chromosome 1q31 that encodes a cyclic AMP-specific nucleotide phosphodiesterase, which plays a critical role in signal transduction by hydrolysing the second messenger cAMP to AMP, thereby playing a role in regulating physiological processes.

Molecular pathology
PDE4B alterations have been anecdotally linked to schizophrenia and bipolar disorder.
References in periodicals archive ?
To investigate whether PDE4B regulates the expression of additional inflammatory mediators other than TNF-a and whether inhibition of PDE4B is sufficient to block these responses in macrophages, in this study we used two-dimensional (2D) gel electrophoresis to screen the secreted proteins that are modulated by the PDE4 inhibitor rolipram in LPS-stimulated Raw 264.7 cells.
The generation of mice deficient in PDE4A, PDE4B, and PDE4D has been described previously.
Contrarily, LPS-induced CCL3 production was significantly decreased in PDE4B[sup]−/− macrophages ( P < 0.01), exerting 62% decrease compared to the PDE4B [sup]+/+ macrophages.
[sup][5] To determine whether these signal pathways mediate the effect of PDE4 inhibitors or PDE4B ablation on CCL3 production, mouse peritoneal macrophages were stimulated with LPS in the presence of the cAMP analog dibutyryl-cAMP (db-cAMP), the Epac activator 8-pCPT-2′-O-Me-cAMP or the PKA activator 6-Bnz-cAMP.
Of the three proteins identified, TNF-a regulation by PDE4B has been studied extensively, [sup][12],[13],[14],[15],[16] whereas the information on CCL3 and IL-1Ra regulation by PDE4 subtypes remains largely unclear.
Using PDE4-deficient macrophages and their wild-type counterparts, we demonstrated that the pharmacological effect of rolipram on LPS-induced CCL3 production is exerted mainly through inhibition of PDE4B, one of the three PDE4 subtypes expressed in macrophages.
Like its impact on TNF-a production, ablation or inactivation of PDE4B also suppressed LPS-induced CCL3 production in macrophages.
Conti, "Induction of the cyclic nucleotide phosphodiesterase PDE4B is essential for LPS-activated TNFa responses," Proceedings of the National Academy of Sciences of the United States of America, vol.
Whole cell lysate proteins were then extracted and evaluated by immunoblotting for PDE4 isoforms (PDE4A, PDE4B, PDE4C, and PDE4D) with [beta]-actin utilized as a loading control.
The microarray analysis revealed significant differences in activity of NOR1, PDE4B, and PKC-beta between the two patient groups.