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Recurrent Acrodysostosis-Related PKA RIα Mutant Reveals a Novel Mechanism of Aberrant PKA Deactivation. [PDF]
J Mol BiolDella Libera L +5 more
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Lack of effect of cyclic adenosine monophosphate modulation during prematuration in vitro on development to the blastocyst stage and expression of specific genes associated with lineage commitment. [PDF]
JDS CommunDesenzi R +5 more
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Distribution and function of 3′,5′-Cyclic-AMP phosphodiesterases in the human ovary
Molecular and Cellular Endocrinology, 2015The concentration of the important second messenger cAMP is regulated by phosphodiesterases (PDEs) and hence an attractive drug target. However, limited human data are available about the PDEs in the ovary. The aim of the present study was to describe and characterise the PDEs in the human ovary.
T.S. Petersen +6 more
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3′, 5′-cyclic AMP phosphodiesterases in cytosol of uterine smooth muscle ; effects of angiotensin
Life Sciences, 1973Abstract The total 3′,5′-cyclic AMP phosphodiesterase activity measured in the 100,000 g supernatant of rat uterus homogenates appears to be the sum of the activities of two phosphodiesterases with different Vmax and Km. Vmax and Km for both enzymes are not affected by variations of calcium concentration.
G, Angles d'Auriac, P, Meyer
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Biochemical and Biophysical Research Communications, 1970
Abstract The phosphodiesterase activity extracted from frog bladder epithelial cells and rat kidney may be described as the sum of the activities of two phosphodiesterases (I and II). Phosphodiesterases I and II may be partially separated by gel filtration or by centrifugation in sucrose gradients.
S, Jard, M, Bernard
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Abstract The phosphodiesterase activity extracted from frog bladder epithelial cells and rat kidney may be described as the sum of the activities of two phosphodiesterases (I and II). Phosphodiesterases I and II may be partially separated by gel filtration or by centrifugation in sucrose gradients.
S, Jard, M, Bernard
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A modified assay of 3′:5′-cyclic-AMP phosphodiesterase
Analytical Biochemistry, 1975Abstract A modification of the assay of cyclic nucleotide phosphodiesterase involving batch use of Dowex 1 anion exchange resin is described which allows for quantitative recovery of adenosine, guanosine, and their metabolites from the resin slurry. The assay described is suitable for use in crude preparations containing purine catabolizing enzymes ...
R J, Boudreau, G I, Drummond
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Nicotinamide inhibition of 3′,5′- cyclic AMP phosphodiesterase in vitro
Biochemical and Biophysical Research Communications, 1972Abstract Nicotinamide was found to be potent inhibitor of 3′,5′- cyclic AMP phosphodiesterase, but nicotinamide adenine dinucleotide was found impotent. Therefore, it may be presumed that the induction of certain enzymes following the intraperitoneal injection of nicotinamide into rats would due to the elevation of the steady state level of 3′,5 ...
M, Shimoyama +3 more
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Physostigmine inhibition of 3',5'-cyclic AMP phosphodiesterase from cat sciatic nerve.
The Journal of Pharmacology and Experimental Therapeutics, 1984This study was designed to determine whether cholinergic drug interaction with cyclic (c) AMP phosphodiesterase (PDE) might account for part of the effects of this class of drugs at the neuromuscular junction. The activity levels of both high- and low-affinity forms of cAMP PDE from cat sciatic nerve were examined for drug inhibition or activation.
W H, Curley +2 more
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Biochemical and Biophysical Research Communications, 1980
Summary In this study we report two Ca 2+ dependent inhibitor proteins of 3′:5′-cyclic-AMP phosphodiesterase which were isolated from salivary glands of the ixodid tick, Amblyomma americanum . These inhibitors prevent the activation of 3′:5′-cyclic-AMP phosphodiesterase by its Ca 2+ -dependent activator protein.
H L, McMullen +3 more
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Summary In this study we report two Ca 2+ dependent inhibitor proteins of 3′:5′-cyclic-AMP phosphodiesterase which were isolated from salivary glands of the ixodid tick, Amblyomma americanum . These inhibitors prevent the activation of 3′:5′-cyclic-AMP phosphodiesterase by its Ca 2+ -dependent activator protein.
H L, McMullen +3 more
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An effect of glucagon on 3′,5′-cyclic AMP phosphodiesterase activity in isolated rat hepatocytes
Biochemical and Biophysical Research Communications, 1975Abstract Glucagon was found to activate the low Km form of 3′,5′-cyclic AMP phosphodiesterase in intact isolated rat hepatocytes while the high Km phosphodiesterase was unaltered. Activation was concentration dependent and occurred at the same concentration required to observe an increase in 3′,5′-cyclic AMP levels in the cell.
E H, Allan, J G, Sneyd
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