Prostaglandin E1 as an Intercellular Regulator of Cyclic AMP Levels

Pathobiology ◽  
1976 ◽  
Vol 44 (3-6) ◽  
pp. 260-277 ◽  
Author(s):  
Vittorio Tomasi
Keyword(s):  
Cyclic Amp ◽  
Prostaglandin E

Interaction between parathyroid hormone and prostaglandin E1 on cyclic AMP metabolism in rat kidney

1980 ◽  
Vol 93 (3) ◽  
pp. 339-345 ◽  
Author(s):  
Naokazu Nagata ◽  
Yuriko Ono ◽  
Narimichi Kimura
Keyword(s):  
Parathyroid Hormone ◽  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Rat Kidney ◽  
Prostaglandin E ◽  
Cortical Tissue ◽  
Newborn Rat ◽  
Simultaneous Addition ◽  
Renal Cortical Tissue ◽  
Subsequent Addition

Abstract. The interaction between parathyroid hormone (PTH) and prostaglandin E1 (PGE1) in influencing cyclic AMP metabolism in rat renal cortical tissue was examined. PTH and PGE1 stimulated additively the adenylate cyclase activity in the homogenate of the tissue. Both PTH and PGE1 enhanced the level of cyclic AMP in the incubated renal cortical tissue, but the effect of their simultaneous addition did not exceed the effect induced by PTH alone. Cyclic AMP accumulated in the incubation medium by stimulation by PTH was decreased by the simultaneous addition of PGE1. When the tissue was pre-incubated for 30 min with 2 to 10 μg/ml of PGE1, the magnitude of the increase of cyclic AMP caused by PTH subsequently added was lessened. However, the response to PTH of adenylate cyclase preparation obtained from the homogenate of PGE1-pre-treated tissue was not decreased. When first PTH was added to the incubating renal cortical tissue, the subsequent addition of PGE1 accelerated the decrease of cyclic AMP content in the tissue and decreased the amount of cyclic AMP released from the tissue. The interaction of PTH and PGE1 on cyclic AMP metabolism in the renal cortical tissue was in contrast to that seen in newborn rat calvaria where PGE1 and PTH acted additively in enhancing the level of cyclic AMP.

Degradation of the Cyclic AMP Antagonist Prostaglandylinositol Cyclic Phosphate (Cyclic PIP) by Dephosphorylation

1999 ◽  
Vol 380 (1) ◽  
Author(s):  
A. Kassner ◽  
M. Lessmann ◽  
H.K. Wasner
Keyword(s):  
Cyclic Amp ◽  
Inositol Phosphate ◽  
Prostaglandin E ◽  
Rat Tissues ◽  
Degrading Enzyme ◽  
Cyclic Phosphate ◽  
The Difference ◽  
Synthesis And Degradation

AbstractThe cAMP antagonist, prostaglandylinositol cyclic phosphate (cyclic PIP), is synthesized from prostaglandin E and activated inositol phosphate. From various tissues only that amount of cyclic PIP can be isolated that constitutes the difference between synthesis and degradation. In order to overcome this drawback, the cyclic PIP degrading enzyme or enzymes had to be characterized prior to searching for inhibitors. Cyclic PIP degrading activities have been found in all rat tissues tested, and are lowest in brain (380 pmol × min

scholarly journals Phosphorylation of β-Catenin by Cyclic AMP-Dependent Protein Kinase Stabilizes β-Catenin through Inhibition of Its Ubiquitination

2005 ◽  
Vol 25 (20) ◽  
pp. 9063-9072 ◽  
Author(s):  
Shin-ichiro Hino ◽  
Chie Tanji ◽  
Keiichi I. Nakayama ◽  
Akira Kikuchi
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Wnt Signaling ◽  
Protein Level ◽  
Glycogen Synthase ◽  
Wnt Signaling Pathway ◽  
Prostaglandin E ◽  
Dependent Protein Kinase ◽  
Intact Cells ◽  
Dependent Protein

ABSTRACT The mechanism of cross talk between the Wnt signaling and cyclic AMP (cAMP)-dependent protein kinase (protein kinase A [PKA]) pathways was studied. Prostaglandin E1 (PGE1), isoproterenol, and dibutyryl cAMP (Bt2cAMP), all of which activate PKA, increased the cytoplasmic and nuclear β-catenin protein level, and these actions were suppressed by a PKA inhibitor and RNA interference for PKA. PGE1 and Bt2cAMP also increased T-cell factor (Tcf)-dependent transcription through β-catenin. Bt2cAMP suppressed degradation of β-catenin at the protein level. Although PKA did not affect the formation of a complex between glycogen synthase kinase 3β (GSK-3β), β-catenin, and Axin, phosphorylation of β-catenin by PKA inhibited ubiquitination of β-catenin in intact cells and in vitro. Ser675 was found to be a site for phosphorylation by PKA, and substitution of this serine residue with alanine in β-catenin attenuated inhibition of the ubiquitination of β-catenin by PKA, PKA-induced stabilization of β-catenin, and PKA-dependent activation of Tcf. These results indicate that PKA inhibits the ubiquitination of β-catenin by phosphorylating β-catenin, thereby causing β-catenin to accumulate and the Wnt signaling pathway to be activated.

Follicle-stimulating hormone-induced prostaglandin E formation in isolated rat ovarian theca

1983 ◽  
Vol 97 (1) ◽  
pp. 43-49 ◽  
Author(s):  
U. Zor ◽  
B. Strulovici ◽  
R. Braw ◽  
H. R. Lindner ◽  
A. Tsafriri
Keyword(s):  
Cyclic Amp ◽  
Cyclic Gmp ◽  
Follicle Stimulating Hormone ◽  
Fold Increase ◽  
Prostaglandin E ◽  
Β Subunit ◽  
Biochemical Effects ◽  
Isolated Rat ◽  
Stimulating Hormone

The aim of this study was to search for direct biochemical effects of highly purified FSH on isolated ovarian follicular theca in vitro. Granulosa cells (GC; approximately 1 × 105 cells per follicle) were flushed from isolated follicles of pro-oestrous rats. The remaining theca layer and the isolated GC were incubated with highly purified ovine FSH. Prostaglandin E (PGE) accumulation was measured by radioimmunoassay. Follicle-stimulating hormone induced a 15-fold increase in PGE accumulation over the basal level in the follicular theca, the stimulated rate exceeding threefold that observed in the GC fraction derived from the same follicle. Follicle-stimulating hormone caused no significant increase in cyclic AMP level or steroidogenesis in the theca layer, but was active on these parameters in the GC. In contrast, LH increased the accumulation of cyclic AMP, progesterone and testosterone, as well as of PGE, in follicular theca. Exogenous 8-bromo cyclic AMP or cyclic GMP also stimulated PGE production in follicular theca or GC, but FSH was without any effect on the level of endogenous cyclic GMP in GC or follicular theca. Antibodies to FSH prevented the effect of FSH (but not that of LH) on PGE formation by follicular theca and GC, while antibodies to the β-subunit of LH blocked the effect of LH but not of FSH. We conclude that highly purified FSH has a stimulatory effect on PGE formation by the follicular theca.

Differences in prostaglandin E2, prostaglandin F2α and prostacyclin contents and their response to thyrotrophin stimulation and in prostaglandin-stimulated cyclic AMP response in normal and Graves's thyroid slices

1983 ◽  
Vol 98 (3) ◽  
pp. 357-363 ◽  
Author(s):  
Nobuyuki Takasu ◽  
Kazunori Takahashi ◽  
Tatsuro Ishigami ◽  
Takashi Yamada ◽  
Seiya Sato
Keyword(s):  
Cyclic Amp ◽  
Prostaglandin E2 ◽  
Prostaglandin F2α ◽  
Human Thyroid ◽  
Prostaglandin E ◽  
Normal Thyroid ◽  
Cyclic Amp Synthesis

The human thyroid contained prostaglandin (PG) E2, PGF2α and 6-oxo-PGF1α, an end-metabolite of prostacyclin (PGI2), the 6-oxo-PGF1α content being the highest of these prostaglandins. Graves's thyroid contained a significantly higher amount of PGF2α and lower amounts of PGE2 and 6-oxo-PGF1α than the normal thyroid. Thyrotrophin acutely augmented the thyroid contents of PGE2, PGF2α and 6-oxo-PGF1α. The TSH-stimulated increases in PGE2 and 6-oxo-PGF1α were lower but the TSH-stimulated increase in PGF2α was significantly higher in Graves's thyroid than in the normal thyroid. Prostaglandin E2 and PGI2 stimulated human thyroid cyclic AMP synthesis, with the magnitudes of PGE2-and PGI2-stimulated increases in cyclic AMP being equal in normal and Graves's thyroid. Prostaglandin E2α did not stimulate cyclic AMP synthesis significantly. These results provide evidence that prostaglandins play important roles in thyroid physiology and the pathophysiology of Graves's disease.

scholarly journals Effect of Ciprofloxacin-Induced Prostaglandin E2 on Interleukin-18-Treated Monocytes

2005 ◽  
Vol 49 (8) ◽  
pp. 3228-3233 ◽  
Author(s):  
Hideo Kohka Takahashi ◽  
Hiromi Iwagaki ◽  
Dong Xue ◽  
Goutarou Katsuno ◽  
Sachi Sugita ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Peripheral Blood Mononuclear Cells ◽  
Peripheral Blood ◽  
Mononuclear Cells ◽  
Cyclooxygenase 2 ◽  
Prostaglandin E ◽  
Dependent Manner ◽  
Interleukin 18 ◽  
Peripheral Blood Mononuclear ◽  
Blood Mononuclear Cells

ABSTRACT Ciprofloxacin, a fluorinated 4-quinolone, is useful for the clinical treatment of infections due to its antibacterial properties and also modulates the immune response of monocytes isolated from human peripheral blood mononuclear cells. In the present study, we found that ciprofloxacin induced the production of prostaglandin E2 in monocytes in a concentration-dependent manner regardless of the presence of interleukin-18 by enhancing the expression of cyclooxygenase-2 protein and that this in turn led to the elevation of intercellular cyclic AMP in monocytes via the stimulation of prostaglandin receptors. The prostaglandin E2 and cyclic AMP production increased by ciprofloxacin was inhibited by indomethacin, a nonselective cyclooxygenase-2 inhibitor, and NS398, a selective cyclooxygenase-2 inhibitor. In addition, ciprofloxacin suppressed the interleukin-18-induced production of tumor necrosis factor alpha, gamma interferon, and interleukin-12 in peripheral blood mononuclear cells by inhibiting the expression of intercellular adhesion molecule 1, B7.1, B7.2, and CD40 on monocytes, and this effect could be reversed by the addition of indomethacin or NS398. These results indicate that ciprofloxacin exerts immunomodulatory activity via the production of prostaglandin E2 and imply therapeutic potential of ciprofloxacin for the treatment of systemic inflammatory responses initiated by interleukin-18.

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