scholarly journals Calmodulin activation of cyclic AMP phosphodiesterase in the B16 mouse melanoma

1984 ◽  
Vol 219 (3) ◽  
pp. 941-946 ◽  
Author(s):  
S W Walker ◽  
S Mac Neil ◽  
H J Senior ◽  
S S Bleehen ◽  
S Tomlinson
Keyword(s):  
Cyclic Amp ◽  
Cultured Cells ◽  
Soluble Fraction ◽  
Inhibitory Effect ◽  
Tumour Tissue ◽  
Phosphodiesterase Activity ◽  
Calmodulin Antagonist ◽  
Mouse Melanoma ◽  
Cyclic Amp Phosphodiesterase ◽  
B16 Mouse Melanoma

Mouse B16 melanoma extracts of both cultured cells and tumour tissue contain cyclic AMP phosphodiesterase activity, with 95% present in the soluble fraction. Although activation of the enzyme by added calmodulin did not occur, it was found that endogenous calmodulin was present at a level sufficient to activate fully the enzyme. The ability of Ca-calmodulin to stimulate cyclic AMP phosphodiesterase in this tissue was shown by the inhibitory effect of N-(6-aminohexyl)-5-chloronaphthalenesulphonamide (W7), a known calmodulin antagonist; by the activation of the enzyme with exogenous calmodulin observed in supernatants depleted of endogenous calmodulin by passage over fluphenazine-Sepharose 6B in the presence of Ca2+; by the Ca-dependent binding of the enzyme to calmodulin-agarose and its activation by Ca-calmodulin after elution from the column with EGTA-containing buffer. It was calculated that about 50% of the total cyclic AMP phosphodiesterase activity was calmodulin-activated in this tissue.

Inhibitory effect of thyroid hormones on pituitary cyclic AMP phosphodiesterase activity in vitro

1984 ◽  
Vol 9 (7) ◽  
pp. 1011-1018 ◽  
Author(s):  
Akio Nagasaka ◽  
Hiroyoshi Hidaka ◽  
Kunitaka Kataoka ◽  
Katsumi Iwase ◽  
Hifumi Nakagawa ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Thyroid Hormones ◽  
Inhibitory Effect ◽  
Phosphodiesterase Activity ◽  
Cyclic Amp Phosphodiesterase

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.

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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