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- W2323877568 abstract "Although enzymes of the phosphodiesterase 3 (PDE3) and PDE4 families each regulate the activities of both protein kinases A (PKAs) and exchange proteins activated by cAMP (EPACs) in human endothelial cells, the mechanisms that allow these PDEs to individually regulate the activities of these two effectors are ill understood. Our recent studies have identified and determined the composition and functionality of two separate signaling complexes “signalosomes” which coordinate individual actions of PDE3B and PDE4D on EPAC1-mediated actions in these cells. First, we showed that EPAC1 and PDE4D together integrate into a VE-Cadherin (VECAD)-based signaling complex that allowed cAMP to promote VECAD-based intercellular adhesions and permeability in human arterial VEC permeability. Second, we showed that PDE3B and EPAC1 bind directly through protein-protein interactions and that this signalosome tethers and regulated PI3Kγ activity and its effects on human endothelial cell adhesion, spreading, and tubule formation. Of potential translational importance, we mapped the distinct EPAC1 peptide motif involved in binding this cAMP effector to either PDE3B or PDE4D and showed that cell-permeable peptides that antagonized these interactions impacted relevant cellular functions." @default.
- W2323877568 created "2016-06-24" @default.
- W2323877568 creator A5088433204 @default.
- W2323877568 date "2012-09-04" @default.
- W2323877568 modified "2023-09-26" @default.
- W2323877568 title "PDEs and Endothelial Cell Function" @default.
- W2323877568 doi "https://doi.org/10.1055/s-0032-1304235" @default.
- W2323877568 hasPublicationYear "2012" @default.
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