The regulation of cyclic AMP-phosphodiesterase and its specific inhibitor by cyclic AMP in dictyostelium

The concentrations of cAMP, cAMP phosphodiesterase (PDE) activity, and the effect of theophylline in vitro on the forward motility (FM) of maturing goat epididymal sperm have been analyzed. cAMP levels increased slowly during transit of the cells from the caput to the proximal cauda, although they acquired a minimal degree of forward progression. The last phase of sperm transit (proximal to distal cauda) was associated with a concomitant sharp rise in the level of both c AMP as well as flagellar motility. PDE activity progressively decreased (approximately threefold) during epididymal maturation, being minimal in mature cauda sperm. Theophylline (30 mM), a specific inhibitor of PDE, markedly activated (10-fold or greater) motility of the sperm derived from proximal-corpus, mid-corpus, distal-corpus, and proximal-cauda epididymides. FM of the native mature caudal sperm was similar to that of the theophylline-treated proximal-cauda sperm. The terminal stage of sperm maturity (proximal to distal cauda) was associated with a markedly reduced level of theophylline-dependent motility activation (approximately 50%). The data are consistent with the view that PDE plays an important role in the initiation of motility during epididymal sperm maturation.Key words: epididymal sperm, cyclic AMP, cyclic AMP phosphodiesterase, flagellar motility, theophylline

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The Effect of Mitomycin C on Platelet Aggregation and Adenosine 3′, 5′-Monophosphate Metabolism

Thrombosis and Haemostasis ◽

10.1055/s-0038-1646667 ◽

1978 ◽

Vol 39 (01) ◽

pp. 177-185 ◽

Cited By ~ 3

Author(s):

Shuichi Hashimoto ◽

Sachiko Shibata ◽

Bonro Kobayashi

Keyword(s):

Platelet Aggregation ◽

Cyclic Amp ◽

Mitomycin C ◽

Blood Platelets ◽

Adenosine Diphosphate ◽

Cellular Membrane ◽

Adenyl Cyclase ◽

Cyclic Amp Phosphodiesterase ◽

Membrane Structure And Function ◽

And Function

SummaryThe effect of Mitomycin C on aggregation, adenosine 3′, 5′-monophosphate (cyclic AMP) metabolism and reactions induced by thrombin was studied in rabbit platelets. Mitomycin C inhibited the platelet aggregation induced by adenosine diphosphate or thrombin. The level of radioactive cyclic AMP derived from 8-14C adenine or 8-14C adenosine increased after incubating intact platelets with Mitomycin G. Formation of radioactive adenosine triphosphate also increased though mitochondrial oxidation was not stimulated. Similar effect was observed also in rabbit liver. Mitomycin C failed to stimulate platelet adenyl cyclase but inhibited cyclic AMP phosphodiesterase in the absence of theophylline. In the platelets preincubated with Mitomycin C, thrombin-induced inhibition of adenyl cyclase, stimulation of membrane-bound cyclic AMP phosphodiesterase, and release of 250,000 dalton protein from platelet membranes were prevented. These results suggest that Mitomycin C will affect cellular membrane structure and function, and this extranuclear effect of Mitomycin C will lead to inhibition of aggregation in blood platelets.

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Cyclic AMP phosphodiesterase in diabetes. Effect of glyburide

Diabetes ◽

10.2337/diabetes.35.11.1233 ◽

1986 ◽

Vol 35 (11) ◽

pp. 1233-1236 ◽

Cited By ~ 6

Author(s):

S. S. Solomon ◽

J. Deaton ◽

T. P. Shankar ◽

M. Palazzolo

Keyword(s):

Cyclic Amp ◽

Cyclic Amp Phosphodiesterase

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The Biological Effects of Forsythia Leaves Containing the Cyclic AMP Phosphodiesterase 4 Inhibitor Phillyrin

Molecules ◽

10.3390/molecules26082362 ◽

2021 ◽

Vol 26 (8) ◽

pp. 2362

Author(s):

Sansei Nishibe ◽

Kumiko Mitsui-Saitoh ◽

Junichi Sakai ◽

Takahiko Fujikawa

Keyword(s):

Cyclic Amp ◽

Influenza A ◽

Biological Effects ◽

Polyphenolic Compounds ◽

Pde4 Inhibitor ◽

Food Material ◽

Common Component ◽

Phosphodiesterase 4 ◽

Cyclic Amp Phosphodiesterase ◽

Forsythia Suspensa

Forsythia fruit (Forsythia suspensa Vahl (Oleaceae)) is a common component of Kampo medicines for treating the common cold, influenza, and allergies. The main polyphenolic compounds in the leaves of F. suspensa are pinoresinol β-d-glucoside, phillyrin and forsythiaside, and their levels are higher in the leaves of the plant than in the fruit. It is known that polyphenolic compounds stimulate lipid catabolism in the liver and suppress dyslipidemia, thereby attenuating diet-induced obesity and polyphenolic anti-oxidants might attenuate obesity in animals consuming high-fat diets. Recently, phillyrin was reported as a novel cyclic AMP phosphodiesterase 4 (PDE4) inhibitor derived from forsythia fruit. It was expected that the leaves of F. suspensa might display anti-obesity effects and serve as a health food material. In this review, we summarized our studies on the biological effects of forsythia leaves containing phillyrin and other polyphenolic compounds, particularly against obesity, atopic dermatitis, and influenza A virus infection, and its potential as a phytoestrogen.

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A GENETICALLY DISTINCT FORM OF CYCLIC AMP PHOSPHODIESTERASE ASSOCIATED WITH CHROMOMERE 3D4 IN DROSOPHILA MELANOGASTER

Genetics ◽

10.1093/genetics/91.3.521 ◽

1979 ◽

Vol 91 (3) ◽

pp. 521-535

Author(s):

John A Kiger ◽

Eric Golanty

Keyword(s):

Drosophila Melanogaster ◽

Cyclic Amp ◽

Structural Gene ◽

Regulatory Gene ◽

Heat Stability ◽

Normal Female ◽

Dependent Manner ◽

Cyclic Amp Phosphodiesterase ◽

Heat Stable ◽

Camp Levels

ABSTRACT Two cyclic AMP phosphodiesterase enzymes (E.C.3.1.4.17) are present in homogenates of adult Drosophila melanogaster. The two enzymes differ from one another in heat stability, affinity for Mg++, Ca++ activation and molecular weight. They do not differ markedly in their affinities for cyclic AMP, and both exhibit anomalous Michaelis-Menten kinetics. The more heatlabile enzyme is controlled in a dosage-dependent manner by chromomere 3D4 of the X chromosome and is absent in flies that are deficient for chromomere 3D4. Chromomere 3D4 is also necessary for the maintenance of normal cAMP levels, for male fertility, and for normal female fertility and oogenesis. The structural gene(s) for the more heat-stable enzyme is located outside of chromomeres 3C12-3D4. Whether 3D4 contains a structural gene, or a regulatory gene necessary for the presence of the labile enzyme, remains to be determined.

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