Regulation of cAMP and cGMP signaling: new phosphodiesterases and new functions

Soderling, Scott H.; Beavo, Joseph A.

doi:10.1016/s0955-0674(99)00073-3

Cited by 673 publications

(451 citation statements)

References 40 publications

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“…Highly conserved PDEs are tissue specific and differentially distributed in cells and cellular compartments. They form a large group of enzymes consisting of eleven families (PDE1-11), characterized by different substrate affinities, biochemical and physical properties, different mechanisms whereby they are regulated, and different sensitivities to inhibitors [6,7]. Adipocytes express mainly PDE3B and PDE4s.…”

Section: Introductionmentioning

confidence: 99%

Novel mechanisms of the regulation of Protein kinase B in adipocytes; implications for Protein kinase A, Epac, Phosphodiesterases 3 and 4

Zmuda-Trzebiatowska

Manganiello

Degerman

2007

Cellular Signalling

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Crosstalk between insulin and cAMP signalling pathways has a great impact on adipocyte metabolism. Whilst Protein kinase B (PKB) is a pivotal mediator of insulin action, in some cells regulation of PKB by cAMP has also been demonstrated. Here we provide evidence that, in a phosphatidyl inositol 3-kinase dependent manner, β3-adrenergic stimulation (using CL316243) in adipocytes induces PKB phosphorylation in the absence of insulin and also potentiates insulin-induced phosphorylation of PKB. Interestingly, insulin-and CL316243-induced PKB phosphorylation was found to be inhibited by pools of cAMP controlled by PDE3B and PDE4 (mainly in the context of insulin), whereas a cAMP pool controlling protein kinase A appeared to mediate stimulation of PKB phosphorylation (mainly in the context of CL316243).

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Section: Introductionmentioning

confidence: 99%

Novel mechanisms of the regulation of Protein kinase B in adipocytes; implications for Protein kinase A, Epac, Phosphodiesterases 3 and 4

Zmuda-Trzebiatowska

Manganiello

Degerman

2007

Cellular Signalling

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“…Eleven PDE families (PDE1-11) have been identified based on their substrate affinities, biochemical and physical properties, mechanisms whereby they are regulated and different sensitivities to inhibitors [1,2]. Adipocytes express membrane-bound PDE3B and membrane bound as well as cytosolic PDE4s [3].…”

Section: Introductionmentioning

confidence: 99%

Long-term regulation of cyclic nucleotide phosphodiesterase type 3B and 4 in 3T3-L1 adipocytes

Oknianska¹,

Zmuda-Trzebiatowska²,

Manganiello³

et al. 2007

Biochemical and Biophysical Research Communications

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Phosphodiesterase 3B (PDE3B), known to play an important role in acute insulin and cAMP-mediated regulation of lipid metabolism, and PDE4 are the main PDE types expressed in adipocytes. Here we show that members of all PDE4 isoforms are expressed in 3T3-L1 and primary mouse adipocytes. Long-term treatment of 3T3-L1 adipocytes with insulin induced up-regulation of PDE3B and PDE4D in a phosphatidylinositol 3-kinase-dependent manner whereas long-term treatment with β-adrenergic agonists induced down-regulation of PDE3B and up-regulation of PDE4D. Thus, PDE3B and PDE4D can be added to the list of genes regulated by insulin and cAMP-increasing hormones. Altered expression of PDE3B and PDE4D in response to long-term treatment with insulin and catecholamines may contribute to altered regulation of metabolism in diabetes.

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“…The accumulation of cAMP is tightly and dynamically regulated by two major enzymes, adenylyl cyclase (AC) and phosphodiesterase (PDE), which catalyze the synthesis or degradation of cAMP, respectively. PDE are a large group of isoenzymes encoded by at least 21 different genes and organized into 10 families depending on their biochemical and pharmacological properties, such as substrate affinity (cAMP or cGMP) or sensitivity to specific inhibitors [1][2][3]. In the ovaries, granulosa cells are known to express the type 4 cAMP-specific PDE (PDE4D) gene, a mammalian homologue of the Drosophila dunce [4,5].…”

Section: Introductionmentioning

confidence: 99%

Role of phosphodiesterase in cyclic AMP signaling in cultured rat granulosa cells

et al. 2006

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-Inactivation of the cyclic nucleotide signal in granulosa cells depends on a complex array of cyclic nucleotide phosphodiesterases (PDE). In order to examine the role of PDE in cyclic AMP (cAMP) signaling in granulosa cells, the present study examined the expression of PDE4D proteins and regulation of cAMP-PDE activities in cultured rat granulosa cells. The results of immunoblot analyses showed that two predominant PDE4D subtypes of approximately 80 and 70 kDa appeared when immature rat granulosa cells were treated with FSH. However, these two new subtypes presumed to be PDE4D proteins were not influenced by treatments of DETA/NO, cGMP and PKB inhibitor, LY294002. Immature rat granulosa cells treated with medium alone displayed low cAMP-PDE activity throughout 48 h of culture while those treated with FSH (2 ng·mL -1 ) showed a marked increase in cAMP-PDE activity between 6 and 12 h of culture, followed by a decline. The findings from the present study indicate that the increased cAMP-PDE activity by FSH is mainly related to the changes of PDE4D protein levels. However, the inhibitory effects of NO on cAMP accumulation in rat granulosa cells are not via the increased cAMP-PDE activity.phosphodiesterase / cyclic AMP / granulosa cell / nitric oxide / rat

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Regulation of cAMP and cGMP signaling: new phosphodiesterases and new functions

Cited by 673 publications

References 40 publications

Novel mechanisms of the regulation of Protein kinase B in adipocytes; implications for Protein kinase A, Epac, Phosphodiesterases 3 and 4

Novel mechanisms of the regulation of Protein kinase B in adipocytes; implications for Protein kinase A, Epac, Phosphodiesterases 3 and 4

Long-term regulation of cyclic nucleotide phosphodiesterase type 3B and 4 in 3T3-L1 adipocytes

Role of phosphodiesterase in cyclic AMP signaling in cultured rat granulosa cells

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