scholarly journals Evidence against an involvement of cyclic nucleotides in the induction of βcyanin synthesis by cytokinins

1975 ◽  
Vol 146 (2) ◽  
pp. 333-337 ◽  
Author(s):  
D C Elliott ◽  
A W Murray
Keyword(s):  
Cyclic Amp ◽  
Cyclic Nucleotides ◽  
Red Light ◽  
Phosphodiesterase Activity ◽  
Dibutyryl Cyclic Amp ◽  
Purine Bases ◽  
Cyclic Amp Phosphodiesterase ◽  
Induction Process ◽  
Wide Range

1. A wide range of purine bases, nucleosides and cyclic nucleotides were shown to induce βcyanin synthesis in Amaranthus seedlings. 2. The induction of pigment by benzyladenine, dibutyryl cyclic AMP or cyclic AMP was not potentiated by aminophylline. Aminophylline was shown to inhibit Amaranthus cyclic AMP phosphodiesterase activity. 4. Incubation of seedlings with aminophylline inhibited the conversion of 6-[G-3H]benzyladenine into presumed 9- and 7-glucosylbenzyladenine. 5. Induction of βcyanin synthesis by 6-benzyladenine or by exposure to red light was not accompanied by changes in the total cyclic AMP content in seedlings. 6. It is concluded that the inducers tested act as cytokinin analogues; no evidence was obtained to support cyclic AMP as an intermediate in the induction process.

Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae

1987 ◽  
Vol 7 (10) ◽  
pp. 3629-3636
Author(s):  
J Nikawa ◽  
P Sass ◽  
M Wigler
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cyclic Amp ◽  
Copy Number ◽  
Growth Arrest ◽  
Yeast Cells ◽  
Phosphodiesterase Activity ◽  
Camp Phosphodiesterase ◽  
High Affinity ◽  
Cyclic Amp Phosphodiesterase

Saccharomyces cerevisiae contains two genes which encode cyclic AMP (cAMP) phosphodiesterase. We previously isolated and characterized PDE2, which encodes a high-affinity cAMP phosphodiesterase. We have now isolated the PDE1 gene of S. cerevisiae, which encodes a low-affinity cAMP phosphodiesterase. These two genes represent highly divergent branches in the evolution of phosphodiesterases. High-copy-number plasmids containing either PDE1 or PDE2 can reverse the growth arrest defects of yeast cells carrying the RAS2(Val-19) mutation. PDE1 and PDE2 appear to account for the aggregate cAMP phosphodiesterase activity of S. cerevisiae. Disruption of both PDE genes results in a phenotype which resembles that induced by the RAS2(Val-19) mutation. pde1- pde2- ras1- ras2- cells are viable.

scholarly journals In VitroEffect of Inhibin on Cyclic AMP-Phosphodiesterase Activity in Rat Testes

1982 ◽  
Vol 3 (1) ◽  
pp. 69-71
Author(s):  
ANIL R. SHETH ◽  
S. VIJAYALAKSHMI ◽  
PARUL R. SHETH ◽  
A. H. BANDIVDEKAR ◽  
SUDHIR B. MOODBIDRI
Keyword(s):  
Cyclic Amp ◽  
Phosphodiesterase Activity ◽  
Cyclic Amp Phosphodiesterase

scholarly journals Specific antibodies and the selective inhibitor ICI 118233 demonstrate that the hormonally stimulated ‘dense-vesicle’ and peripheral-plasma-membrane cyclic AMP phosphodiesterases display distinct tissue distributions in the rat

1987 ◽  
Vol 248 (3) ◽  
pp. 897-901 ◽  
Author(s):  
N J Pyne ◽  
N Anderson ◽  
B E Lavan ◽  
G Milligan ◽  
H G Nimmo ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Plasma Membrane ◽  
Cyclic Amp ◽  
Rat Liver ◽  
White Adipose Tissue ◽  
Tissue Homogenate ◽  
Phosphodiesterase Activity ◽  
Cyclic Amp Phosphodiesterase ◽  
Peripheral Plasma ◽  
Membrane Enzyme

Polyclonal-antibody preparations DV1 and PM1, raised against purified preparations of rat liver insulin-stimulated ‘dense-vesicle’ and peripheral-plasma-membrane cyclic AMP phosphodiesterases, were used to analyse rat liver homogenates by Western-blotting techniques. The antibody DV1 identified only the 63 kDa native subunit of the ‘dense-vesicle’ enzyme, and the antibody PM1 only the 52 kDa subunit of the plasma-membrane enzyme. These antibodies also detected the subunits of these two enzymes in homogenates of kidney, heart and white adipose tissue from rat. Quantitative immunoblotting demonstrated that the amount of these enzymes (by wt.) varied in these different tissues, as did the expression of these two enzymes, relative to each other, by a factor of as much as 7-fold. The ratio of the dense-vesicle enzyme to the peripheral-plasma-membrane enzyme was lowest in liver and kidney and highest in heart and white adipose tissue. ICI 118233 was shown to inhibit selectively the ‘dense-vesicle’ cyclic AMP phosphodiesterase in liver. It did this in a competitive fashion, with a Ki value of 3.5 microM. Inhibition of tissue-homogenate cyclic AMP phosphodiesterase activity by ICI 118233 was used as an index of the contribution to activity by the ‘dense-vesicle’ enzyme. By this method, a tissue distribution of the ‘dense-vesicle’ enzyme was obtained which was similar to that found by using the immunoblotting technique. The differential expression of isoenzymes of cyclic AMP phosphodiesterase activity in various tissues might reflect a functional adaptation, and may provide the basis for the different physiological actions of compounds which act as selective inhibitors.

scholarly journals Prostacyclin and beta-adrenergic catecholamines inhibit arachidonate release and PGI2 synthesis by vascular endothelium

Blood ◽  
1981 ◽  
Vol 58 (3) ◽  
pp. 514-517 ◽  
Author(s):  
B Adler ◽  
MA Jr Gimbrone ◽  
AI Schafer ◽  
RI Handin
Keyword(s):  
Endothelial Cells ◽  
Cyclic Amp ◽  
Vascular Endothelium ◽  
Calcium Ionophore ◽  
Phosphodiesterase Activity ◽  
Dibutyryl Cyclic Amp ◽  
Membrane Phospholipids ◽  
Aortic Endothelial Cells ◽  
Bovine Aortic Endothelial Cells ◽  
Arachidonate Release

Abstract We have investigated the mechanism by which cyclic AMP inhibits PGI2 synthesis in cultured bovine aortic endothelial cells. Inhibition of cyclic AMP phosphodiesterase activity by 3-isobutyl-1-methylxanthine (IBMX) blocks calcium ionophore-induced PGI2 production by 62%. The addition of 3 mM dibutyryl cyclic AMP, alone with IBMX, increases the inhibition to 96%. Release o 3H-arachidonate from membrane phospholipids was inhibited 25% by dibutyryl cyclic AMP, 48% by IBMX, and 76% by isoproterenol plus IBMX. Inhibition by isoproterenol was reversed by 10 micro M propranolol. Release of 3H-arachidonate was also reduced 75% by a combination of 10 micro M PGI2 and 3 mM IBMX. We conclude that hormones like isoproterenol and PGI2 may regulate endothelial cell PGI2 biosynthesis by increasing intracellular cyclic AMP, which then inhibits release of endogenous arachidonate from membrane phospholipids.

Effect of indomethacin on cyclic AMP phosphodiesterase activity in myometrium from pregnant rhesus monkeys

1976 ◽  
Vol 11 (4) ◽  
pp. 713-725 ◽  
Author(s):  
Clarissa H. Beattyc ◽  
Rose Mary Bocek ◽  
Martha K. Young ◽  
Miles J. Novy
Keyword(s):  
Cyclic Amp ◽  
Rhesus Monkeys ◽  
Phosphodiesterase Activity ◽  
Cyclic Amp Phosphodiesterase

A new allele with abnormal cyclic-AMP phosphodiesterase activity in Phycomyces

1985 ◽  
Vol 201 (1) ◽  
pp. 124-125 ◽  
Author(s):  
Vishwanath M. Reddy ◽  
Paul Galland ◽  
Edward D. Lipson
Keyword(s):  
Cyclic Amp ◽  
Phosphodiesterase Activity ◽  
Cyclic Amp Phosphodiesterase
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