Effects of streptozotocin-induced diabetes on calmodulin and cyclic AMP phosphodiesterase activity in rat lungs

Lung ◽  
1982 ◽  
Vol 160 (1) ◽  
pp. 303-310 ◽  
Author(s):  
A. F. Ofulue ◽  
M. S. Nijjar
Keyword(s):  
Cyclic Amp ◽  
Phosphodiesterase Activity ◽  
Cyclic Amp Phosphodiesterase ◽  
Rat Lungs ◽  
Streptozotocin Induced Diabetes

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

Growth of S49 wild type cells in 3 nM epinephrine increases cyclic AMP phosphodiesterase activity

Life Sciences ◽  
1994 ◽  
Vol 54 (13) ◽  
pp. 863-875 ◽  
Author(s):  
Mark D. Richardson ◽  
Thomas J. Goka ◽  
Roger Barber ◽  
R.W. Butcher
Keyword(s):  
Cyclic Amp ◽  
Phosphodiesterase Activity ◽  
Wild Type ◽  
Cyclic Amp Phosphodiesterase

Calmodulin and Ca2+-dependent cyclic AMP phosphodiesterase activity in Trypanosoma cruzi

1985 ◽  
Vol 17 (2) ◽  
pp. 143-153 ◽  
Author(s):  
María T. Téllez-iñón ◽  
Rita M. Ulloa ◽  
Mónica Torruella ◽  
Héctor N. Torres
Keyword(s):  
Cyclic Amp ◽  
Trypanosoma Cruzi ◽  
Phosphodiesterase Activity ◽  
Cyclic Amp Phosphodiesterase

scholarly journals Cross-talk between glucagon- and adenosine-mediated signalling systems in rat hepatocytes: effects on cyclic AMP-phosphodiesterase activity

1995 ◽  
Vol 312 (3) ◽  
pp. 763-767 ◽  
Author(s):  
M Robles-Flores ◽  
G Allende ◽  
E Piña ◽  
J A García-Sáinz
Keyword(s):  
Cyclic Amp ◽  
Pertussis Toxin ◽  
Plasma Membranes ◽  
Rat Hepatocytes ◽  
Dependent Manner ◽  
Phosphodiesterase Activity ◽  
Cyclic Amp Phosphodiesterase ◽  
Cyclic Amp Accumulation ◽  
A1 Adenosine Receptors ◽  
Dose Dependent

The effect of adenosine analogues on glucagon-stimulated cyclic AMP accumulation in rat hepatocytes was explored. N6-Cyclopentyladenosine (CPA), 5′-N-ethylcarboxamidoadenosine and N6-(R-phenylisopropyl)adenosine inhibited in a dose-dependent manner the cyclic AMP accumulation induced by glucagon. This effect seems to be mediated through A1 adenosine receptors. Pertussis toxin completely abolished the effect of CPA on glucagon-stimulated cyclic AMP accumulation in whole cells which suggested that a pertussis-toxin-sensitive G-protein was involved. On the other hand, this action of adenosine analogues on glucagon-induced cyclic AMP accumulation was reverted by the selective low-Km cyclic AMP-phosphodiesterase inhibitor Ro 20-1724. Analysis of cyclic AMP-phosphodiesterase activity in purified hepatocyte plasma membranes showed that glucagon in the presence of GTP inhibited basal PDE activity by 45% and that CPA reverted this inhibition in dose-dependent manner. In membranes derived from pertussis-toxin-treated rats, we observed no inhibition of cyclic AMP-phosphodiesterase activity by glucagon in the absence or presence of CPA. Our results indicate that in hepatocyte plasma membranes, stimulation of adenylate cyclase activity and inhibition of a low-Km cyclic AMP phosphodiesterase activity are co-ordinately regulated by glucagon, and that A1 adenosine receptors can inhibit glucagon-stimulated cyclic AMP accumulation by blocking glucagon's effect on phosphodiesterase activity.

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