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Thsese findings provide insight into the existence of distinct "pools" of PDE5A in human arterial smooth muscle cells and support the idea that these discrete compartments regulate distinct cGMP-dependent events.
The analogues showed a relative narrow range of Ki values for PDE5A inhibition (1.2-14 nm).
Data indicate that high type 5 phosphodiesterase (PDE5) expression in glioblastoma multiforme (GBM) cells significantly correlated with longer overall survival of patients.
the relationship between PDE5A polymorphisms, diabetes, and the efficacy of sildenafil treatment.The response to sildenafil treatment depends on polymorphisms in the PDE5A gene and the glycemic status of the patients.
Study showed that past attempts to quantify PDE5 mRNA were flawed due to the use of incorrect primers, and that when correct primers are used, PDE5 mRNA is detectable in human brain tissue; that PDE5 protein exists in human brain by western blot and ELISA; and performed immunohistochemistry and demonstrate that PDE5 is present in human neurons.
Our data showed a significant and previously undocumented upregulation of PDE5 in both rat and human BPH.
Overexpression of PDE5 in papillary thyroid carcinomas.
cGMP PDE isozymes, PDE5 and 10, are elevated in colon tumor cells compared with normal colonocytes, and inhibitors and siRNAs can selectively suppress colon tumor cell growth
Results show that Ser102 and Ser104 may influence the conformational flexibility of PDE5A, which may in turn influence phosphorylation status, allosteric regulation by cGMP or other as yet unknown regulatory mechanisms for PDE5A.
PDE5A appears to jointly influence amygdala volume and emotion recognition performance.
inhibition of PDE5 can counteract apoptosis during aging by modulating proand antiapoptotic molecules and the APP pathway.
Myocardial PDE5 expression is increased in the hearts of humans and mice with chronic pressure overload.
it is concluded that assessment of PDE5 and PDE9 expression may be useful in the differential diagnosis of benign and malignant breast disease and successful treatment of breast cancer
analysis of amino acid residues responsible for the selectivity of tadalafil binding to two closely related phosphodiesterases, PDE5 and PDE6
PDE5 is highly expressed and increases ( approximately 130%) during growth whereas ABCC5 exhibited low to moderate expression, with a moderate increase ( approximately 40%) during growth
PDE9 is widely distributed in the urothelial epithelium of the human lower urinary tract and its potential roles may be different from those of PDE5.
Treatment of L-1236 with PDE5A-inhibitor sildenafil or with siRNA directed against PDE5A and concomitant stimulation with cyclic guanosine monophosphate (cGMP) resulted in enhanced apoptosis, indicating PDE5A as an oncogene.
found in smooth muscle wall of blood vessels transversing the clitoral supepithelial and stromal space
PDE5 inhibition by sulindac sulfide selectively induces apoptosis and attenuates oncogenic Wnt/beta-catenin-mediated transcription in human breast tumor cells
the spatial localization of PDE5A at the level of caveolin-rich lipid rafts allows for a feedback loop between endothelial PDE5A and nitric oxide synthase (NOS3)
ectopic expression of bovine phosphodiesterase 5 in Drosophila has shown that it has a critical role in Malpighian (renal) tubule function in vivo and that function is conserved across evolution
Phosphodiesterase-5 activity exerts a vasoconstrictor influence on coronary resistance vessels that is mediated, in part, via an increase in endothelial endothelin production.
PDE5 inhibition and increase in cGMP produce pulmonary vasodilation that is mediated in part through inhibition of the ET pathway, thereby precluding an additional vasodilator effect of ETA/ETB receptor blockade in the presence of PDE5 inhibition.
Endothelial dysfunction enhances the pulmonary and systemic vasodilator effects of phosphodiesterase-5 inhibition in awake swine at rest and during treadmill exercise
PDE5 is a key regulator of NO-induced vasodilation in the postnatal pulmonary arteries.
This gene encodes a cGMP-binding, cGMP-specific phosphodiesterase, a member of the cyclic nucleotide phosphodiesterase family. This phosphodiesterase specifically hydrolyzes cGMP to 5'-GMP. It is involved in the regulation of intracellular concentrations of cyclic nucleotides and is important for smooth muscle relaxation in the cardiovascular system. Alternative splicing of this gene results in three transcript variants encoding distinct isoforms.
cGMP-binding cGMP-specific 3',5'-cyclic nucleotide phosphodiesterase
, cGMP-specific 3',5'-cyclic phosphodiesterase
, cGMP-specific phosphodiesterase PDE5A2
, cGMP-specific phosphodiesterase type 5A
, phosphodiesterase isozyme 5
, cGMP-binding cGMP specific phosphodiesterase 5A2
, cGMP-binding cGMP-specific phosphodiesterase
, phosphodiesterase type 5
, cGMP-binding/cGMP-specific phosphodiesterase
, 3',5'-Cyclic GMP Phosphodiesterase
, phosphodiesterase 5A, cGMP-specific
, phosphodiesterase 5a, cGMP-specific
, phosphodiesterase 5a
, cGMP-specific 3',5'-cyclic phosphodiesterase-like
, cyclic nucleotide phosphodiesterase 5a