In PDE10 the allosteric activator is cAMP whereas in all other mammalian PDEs of this sub-family cGMP serves as an activator. Mutational studies indicated that the PDE 10 GAF tandem domain signals via its GAF-B region like PDE2 whereas the GAF tandem of PDE5 signals via its GAF-A region. We generated hybrid chimeras between the GAF tandems of PDE 5, binding cGMP, and PDE 10, binding cAMP, in order to investigate whether we would obtain a GAF tandem capable of signalling by cGMP via GAF A and by cAMP via GAF B. This was not unequivocally accomplished. However, we demonstrate that the mode of signalling appears to be strongly affected by the source of the α-helix which connects the GAF-A and GAF-B regions. A hybrid construct comprised of the N-terminal and GAF-A from PDE5 and the linker and GAF-B from PDE10 could be stimulated by cAMP and, to a lesser extent, by cGMP. However, a similar construct in which the linker between GAF-A (from PDE5) and B (from PDE10) was from the PDE 5 was unresponsive ...

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RATIONALE: cAMP and cGMP are intracellular second messengers involved in heart pathophysiology. cGMP can potentially affect cAMP signals via cGMP-regulated phosphodiesterases (PDEs). OBJECTIVE: To study the effect of cGMP signals on the local cAMP response to catecholamines in specific subcellular compartments. METHODS AND RESULTS: We used real-time FRET imaging of living rat ventriculocytes expressing targeted cAMP and cGMP biosensors to detect cyclic nucleotides levels in specific locales. We found that the compartmentalized, but not the global, cAMP response to isoproterenol is profoundly affected by cGMP signals. The effect of cGMP is to increase cAMP levels in the compartment where the protein kinase (PK)A-RI isoforms reside but to decrease cAMP in the compartment where the PKA-RII isoforms reside. These opposing effects are determined by the cGMP-regulated PDEs, namely PDE2 and PDE3, with the local activity of these PDEs being critically important. The cGMP-mediated modulation of cAMP also affects

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To date, just one structural class of cyclic nucleotide receptors has been characterized, that comprises the bacterial CAP (McKay and Steitz, 1981), the cyclic nucleotide‐regulated protein kinases PKG and PKA (Weber et al., 1989; Su et al., 1995) and the cyclic nucleotide‐gated ion channels (Altenhofen et al., 1991; Kumar and Weber, 1992). This class has been referred to as the cNMP domain family (Schultz et al., 1998). The GAF domains of the cGMP‐regulated PDEs represented a potentially different class of cyclic nucleotide receptors, since they lacked any sequence homology to the cNMP motif. The structure of the YKG9 protein shows no similarity to the cNMP domain and thus establishes beyond any doubt that there are at least two entirely different structural classes of cyclic nucleotide receptors.. The YKG9 structure provides a three‐dimensional template for modeling other GAF domains, including those of the PDEs. The use of multiple threading alignment based on the solved structure ...

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Cyclic nucleotide phosphodiesterases (PDEs) are the only enzymes that degrade the cyclic nucleotides cAMP and cGMP, and play a key role in modulating the amplitude and duration of the signal delivered by these two key intracellular second messengers. Defects in cyclic nucleotide signalling are known to be involved in several pathologies. As a consequence, PDEs have long been recognized as potential drug targets, and they have been the focus of intense research for the development of therapeutic agents. A number of PDE inhibitors are currently available for the treatment of disease, including obstructive pulmonary disease, erectile dysfunction, and heart failure. However, the performance of these drugs is not always satisfactory, due to a lack of PDE-isoform specificity and their consequent adverse side effects. Recent advances in our understanding of compartmentalised cyclic nucleotide signalling and the role of PDEs in local regulation of cAMP and cGMP signals offers the opportunity for the development

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General Research Interests: Regulation and function of cyclic nucleotide phosphodiesterases in the cardiovascular system. Second messenger cyclic nucleotides (cAMP and cGMP) regulate many signaling pathways in the cardiovascular system. For example, the vascular tone, smooth muscle cell growth, and cardiac muscle contractility are all regulated by cyclic nucleotide signaling. We are interested in phosphodiesterases (PDEs), the enzymes that break down cyclic nucleotides and thus control the amplitude, duration, and compartmentalization of cyclic nucleotide signaling in the cell. It has become increasingly clear that cyclic nucleotide degradation by PDEs is not a constitutive function of the cell, but rather a highly regulated one controlled by different mechanisms in different physiological and pathological circumstances. PDE regulation and function is further complicated by the fact that there are more than 50 individual PDEs belonging to 11 different PDE families, yet our understanding of the ...

General Research Interests: Regulation and function of cyclic nucleotide phosphodiesterases in the cardiovascular system. Second messenger cyclic nucleotides (cAMP and cGMP) regulate many signaling pathways in the cardiovascular system. For example, the vascular tone, smooth muscle cell growth, and cardiac muscle contractility are all regulated by cyclic nucleotide signaling. We are interested in phosphodiesterases (PDEs), the enzymes that break down cyclic nucleotides and thus control the amplitude, duration, and compartmentalization of cyclic nucleotide signaling in the cell. It has become increasingly clear that cyclic nucleotide degradation by PDEs is not a constitutive function of the cell, but rather a highly regulated one controlled by different mechanisms in different physiological and pathological circumstances. PDE regulation and function is further complicated by the fact that there are more than 50 individual PDEs belonging to 11 different PDE families, yet our understanding of the ...

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The hydrolysis of cyclic nucleotide second messengers takes place through multiple cyclic nucleotide phosphodiesterases (PDEs). The significance of this diversification is not fully understood. Here we report the differential regulation of low K(m) Ca2+-activated (PDE1C) and Ca2+-independent, rolipr …

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We isolated a human cAMP-specific phosphodiesterase (PDE7B) cDNA from human caudate nucleus. The human PDE7B was composed of 450 amino acid residues with a molecular mass of 51,835 Da. The deduced amino acid sequence of human PDE7B was 64.1% identical to that of human PDE7A (67.1% identity in the ca …

In mammals, adenosine 3, 5-cyclic monophosphate (cAMP) is known to play highly important roles in sperm motility and acrosomal exocytosis. It is known to act through protein phosphorylation via PRKA and through the activation of guanine nucleotide exchange factors like EPAC. Sperm intracellular cAMP levels depend on the activity of adenylyl cyclases, mostly SACY, though transmembrane-containing adenylyl cyclases are also present, and on the activity of cyclic nucleotide phosphodiesterases (PDE) whose role is to degrade cAMP into 5-AMP. The PDE superfamily is subdivided into 11 families (PDE1 to 11), which act on either cAMP or cGMP, or on both cAMP and cGMP although with different enzymatic properties. PDE10, which is more effective on cAMP than cGMP, has been known for almost 15 years and is mostly studied in the brain where it is associated with neurological disorders. Although a high level of PDE10A gene expression is observed in the testis, information on the identity of the isoforms or ...

At this time it is expected that isooctanol will not be a reproductive toxicant. A one-generation study in rats (Hansen, 1992) was performed with the analog substance 1-dodecanol (CAS RN 112-53-8) using the Combined Repeat Dose and Reproductive/Developmental Toxicity Screening Test protoc ol. Male and female rats were administered 1-dodecanol orally via the feed at doses of 100, 500 and 2000 mg/kg/day for a period of 14 days. No effects were seen on reproductive or developmental parameters up to doses of 2000 mg/kg/day. 1-Dodecanol at the dose administered had no influence on body weight, weight gain, food consumption and reproductive efficiency in the parental generation. Pregnancy rates were not statistically altered and there were no differences in the lengths of the gestation periods. No organ toxicity was observed in the females, and there was no effect on the number of pups per litter, weight, sex ratio, or mortality rate from Days 1 to 5 after birth. Test data that will be collected as ...

EHNA is a selective inhibitor of the cGMP-specific phosphodiesterase (PDE2) (IC₅₀s = 0.8 and 2 μM from human and porcine myocardium, respectively, 3.5 μM in rat hepatocyte, and 5.5 μM in human platelet).

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MacPherson, M., Broderick, K., Graham, S., Day, J., Houslay, M., Dow, J. and Davies, S. (2004) The dg2 (for) gene confers a renal phenotype in Drosophila by modulation of cGMP-specific phosphodiesterase. Journal of Experimental Biology, 207, pp. 2769-2776. (doi:10.1242/jeb.01086) ...

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NMDA and nitric oxide act through the cGMP signal transduction pathway to repress hypothalamic gonadotropin-releasing hormone gene expression.s profile, publications, research topics, and co-authors

Definition of 2,3-cyclic-nucleotide phosphodiesterases in the Definitions.net dictionary. Meaning of 2,3-cyclic-nucleotide phosphodiesterases. What does 2,3-cyclic-nucleotide phosphodiesterases mean? Information and translations of 2,3-cyclic-nucleotide phosphodiesterases in the most comprehensive dictionary definitions resource on the web.

Andrea Carter, Susan Spiller, Eve Isabelle Charbonneau, Paulina Delgado, Stephanie Kwong, Thomas Huser, Nathan Rockwell, and Clark Lagarias. We are currently studying a family of cyanobacteriochromes through the use of a bacterium called Thermosynechococcus elongatus, which is a member of a family of thermophilic bacteria that contain cyanobacteriochromes. Cyanobacteriochromes contain GAF domains related to phytochromes. We are currently working with five genes from the genome of T. elongatus with class II GAF domains. GAF domains are blue/green photoreversible. This means that the organism can absorb green and blue photons, and once it is excited above a certain threshold in either color, it will reverse back to absorbing the opposite color, blue or green respectively. The genes we worked with include tlr0924, tll0569, tll0899, tlr0911, and tlr1999. All of these genes have been successfully truncated to GAF domain only and some have been expressed. I specifically worked with tlr1999 gene. Our ...

Increases of cAMP are controlled by the enzyme adenylate cyclase (sAC). This enzyme produces cAMP molecules from the cellular energy reservoir adenosyne triphosphate (ATP). In order for the enzyme to assume this catalytic function, it itself has to be activated, e.g. by bicarbonate.. • The opposite process, e.g. the reduction of cAMP levels, is initiated by another enzyme. The protein involved here originates from the family of phosphodiesterases (PDE); to be precise, an isoform of PDE2A. This enzyme must also be activated so that it may reduce the amount of cAMP contained in the mitochondria. This process is performed by molecules which aggregate along an area at the end of the protein, the N-terminus of the PDE2A molecules.. In this manner, the messenger cAMP acts as an enzyme controlled switch which strengthens or weakens the energy metabolism. The position of the switch is determined by which of the two enzymes dominates: Adenylate cyclase (sAC) increases the amount of cAMP, ...

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HormoneStimuli for ReleaseMechanism of Synthesis/ReleaseTarget Tissue(s)Effects and MOAFeedback RegulationACTHCorticotrophs (CRH)Exocytosis; increase cAMP, which activates PKAAdrenal GlandStimulates production of glucocor...