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Phosphorylation and Activation of a cAMP-specific Phosphodiesterase by the cAMP-dependent Protein Kinase
  • C. Sette, M. Conti
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 7 October 1995
A cAMP-specific phosphodiesterase (PDE4D3) is activated in rat thyroid cells by TSH through a cAMP-dependent phosphorylation (Sette, C., Iona, S., and Conti, M. (1994) J. Biol. Chem. 269, 9245-9252).Expand
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Recent progress in understanding the hormonal regulation of phosphodiesterases.
I. Introduction LAYER after layer of novel regulatory circuits have been added to the map charting the signal transduction pathways that transport information throughout the cell. New components ofExpand
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Peptide-mediated Interference of TIR Domain Dimerization in MyD88 Inhibits Interleukin-1-dependent Activation of NF-κB*
Myeloid differentiation factor 88 (MyD88) plays a crucial role in the signaling pathways triggered by interleukin (IL)-1 and Toll-like receptors in several steps of innate host defense. A crucialExpand
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The short-term activation of a rolipram-sensitive, cAMP-specific phosphodiesterase by thyroid-stimulating hormone in thyroid FRTL-5 cells is mediated by a cAMP-dependent phosphorylation.
To elucidate the mechanism causing the transient accumulation of intracellular cAMP in the FRTL-5 thyroid cell line, the short-term effect of thyroid-stimulating hormone (TSH) on phosphodiesteraseExpand
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Pivotal Advance: Inhibition of MyD88 dimerization and recruitment of IRAK1 and IRAK4 by a novel peptidomimetic compound
MyD88 is an adaptor protein, which plays an essential role in the intracellular signaling elicited by IL‐1R and several TLRs. Central to its function is the ability of its Toll/IL‐1R translationExpand
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Activation and selective inhibition of a cyclic AMP-specific phosphodiesterase, PDE-4D3.
Prostaglandin E2 produces a transient increase in the intracellular concentration of cAMP in a human promonocytic cell line (U937). The temporal pattern consists of a rapid increase followed by aExpand
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The cAMP-specific Phosphodiesterase PDE4D3 Is Regulated by Phosphatidic Acid Binding
Hormones and growth factors induce in many cell types the production of phosphatidic acid (PA), which has been proposed to play a role as a second messenger. We have previously shown in an acellularExpand
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The ratPDE3/IVd phosphodiesterase gene codes for multiple proteins differentially activated by cAMP-dependent protein kinase.
Several mRNAs coding for a cAMP-specific phosphodiesterase (ratPDE3/IVd) with divergent 5' regions have been detected in mammalian cells. To determine the physiological significance of theseExpand
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The Mechanism of Docosahexaenoic Acid-induced Phospholipase D Activation in Human Lymphocytes Involves Exclusion of the Enzyme from Lipid Rafts*
Docosahexaenoic acid (DHA), ann-3 polyunsaturated fatty acid that inhibits T lymphocyte activation, has been shown to stimulate phospholipase D (PLD) activity in stimulated human peripheral bloodExpand
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Selective activation of rolipram-sensitive, cAMP-specific phosphodiesterase isoforms by phosphatidic acid.
In rat thymic lymphocytes, accumulation of phosphatidic acid (PA) occurs at the same time as decrease in cAMP levels and activation of a cAMP-specific phosphodiesterase (PDE) [type 4, EC 3.1.4.17Expand
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