ArticleThe Biochemical journal2008
Human PDE4A8, a novel brain-expressed PDE4 cAMP-specific phosphodiesterase that has undergone rapid evolutionary change.
Article in The Biochemical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 29 citations in OpenAlex.
- Phosphodiesterase-4 Inhibitors in Chronic Obstructive Pulmonary Disease: Molecular Mechanisms, Current Therapeutics, and Future Perspectives.Cell biochemistry and biophysics · 2026Review
- Discovery of natural CdnP inhibitors through structure-based virtual screening and molecular dynamics simulations.Microbiology spectrum · 2025Article
- Phosphodiesterase 4B inhibition: a potential novel strategy for treating pulmonary fibrosis.European respiratory review : an official journal of the European Respiratory Society · 2023Review
- Clinical Implication of Phosphodiesterase-4-Inhibition.International journal of molecular sciences · 2022Review
- Phosphodiesterases and cAMP Pathway in Pituitary Diseases.Frontiers in endocrinology · 2019Review
- cAMP-specific PDE4 phosphodiesterases and AIP in the pathogenesis of pituitary tumors.Endocrine-related cancer · 2016Article
- mAKAP-a master scaffold for cardiac remodeling.Journal of cardiovascular pharmacology · 2015Review
- PDE4 as a target for cognition enhancement.Expert opinion on therapeutic targets · 2013Review
- β-Adrenergic receptor stimulation increases surface NKCC2 expression in rat thick ascending limbs in a process inhibited by phosphodiesterase 4.American journal of physiology. Renal physiology · 2012Article
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Authors and funding
14 authors at 4 institutions in 3 countries.
Funding
Abstract
We have isolated cDNAs encoding PDE4A8 (phosphodiesterase 4 isoform A8), a new human cAMP-specific PDE4 isoform encoded by the PDE4A gene. PDE4A8 has a novel N-terminal region of 85 amino acids that differs from those of the related 'long' PDE4A4, PDE4A10 and PDE4A11 isoforms. The human PDE4A8 N-terminal region has diverged substantially from the corresponding isoforms in the rat and other mammals, consistent with rapid evolutionary change in this region of the protein. When expressed in COS-7 cells, PDE4A8 localized predominantly in the cytosol, but approx. 20% of the enzyme was associated with membrane fractions. Cytosolic PDE4A8 was exquisitely sensitive to inhibition by the prototypical PDE4 inhibitor rolipram (IC(50) of 11+/-1 nM compared with 1600 nM for PDE4A4), but was less sensitive to inhibition by cilomilast (IC(50) of 101+/-7 nM compared with 61 nM for PDE4A4). PDE4A8 mRNA was found to be expressed predominantly in skeletal muscle and brain, a pattern that differs from the tissue expression of other human PDE4 isoforms and also from that of rat PDE4A8. Immunohistochemical analysis showed that PDE4A8 could be detected in discrete regions of human brain, including the cerebellum, spinal cord and cerebral cortex. The unique tissue distribution of PDE4A8, combined with the evolutionary divergence of its N-terminus, suggest that this isoform may have a specific function in regulating cAMP levels in human skeletal muscle and brain.
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