scholarly journals Cyclic AMP compartmentation due to increased cAMP‐phosphodiesterase activity in transgenic mice with a cardiac‐directed expression of the human adenylyl cyclase type 8 (AC8)

2003 ◽  
Vol 17 (11) ◽  
pp. 1380-1391 ◽  
Author(s):  
Marie Georget ◽  
Philippe Mateo ◽  
Grégoire Vandecasteele ◽  
Larissa Lipskaia ◽  
Nicole Defer ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Transgenic Mice ◽  
Adenylyl Cyclase ◽  
Phosphodiesterase Activity ◽  
Camp 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.

Thyrotrophin and prostaglandin E2 increase calmodulin levels and cyclic AMP phosphodiesterase activity in cultured porcine thyroid cells

1988 ◽  
Vol 117 (1) ◽  
pp. 109-114 ◽  
Author(s):  
N. Takasu ◽  
T. Yamada ◽  
Y. Shimizu
Keyword(s):  
Cyclic Amp ◽  
Prostaglandin E2 ◽  
Prostaglandin E ◽  
Maximal Velocity ◽  
Phosphodiesterase Activity ◽  
Dibutyryl Camp ◽  
Camp Phosphodiesterase ◽  
Thyroid Cells ◽  
Michaelis Constants ◽  
Camp Hydrolysis

ABSTRACT Thyrotrophin (TSH) and prostaglandin E2 (PGE2) increased cellular cyclic AMP (cAMP), calmodulin levels and cAMP phosphodiesterase activity in cultured porcine thyroid cells. Dibutyryl cAMP (dbcAMP), a stable analogue of cAMP, increased calmodulin levels and cAMP phosphodiesterase activity. These results indicate that TSH- and PGE2-stimulated increases in calmodulin are mediated by cAMP. This increased concentration of calmodulin in turn stimulates cAMP phosphodiesterase. Double reciprocal plots of cAMP hydrolysis yielded two apparent Michaelis constants (Km); the lower in the 1 μmol/l and the higher in the 10 μmol/l range. Thyrotrophin, PGE2 and dbcAMP increased the values of maximal velocity without changing the Km values. J. Endocr. (1988) 117, 109–114

scholarly journals THE CONSEQUENCES OF NULLOSOMY FOR A CHROMOSOMAL REGION AFFECTING CYCLIC AMP PHOSPHODIESTERASE ACTIVITY IN DROSOPHILA

Genetics ◽  
1977 ◽  
Vol 85 (4) ◽  
pp. 623-628
Author(s):  
John A Kiger
Keyword(s):  
Cyclic Amp ◽  
Male Fertility ◽  
Chromosomal Region ◽  
Maternal Influence ◽  
Normal Female ◽  
Physiological Effects ◽  
Motile Sperm ◽  
Phosphodiesterase Activity ◽  
Camp Phosphodiesterase ◽  
Camp Metabolism

ABSTRACT A study of Drosophila nullosomic for chromomere 3D4 shows that this region of the genome is necessary for male fertility, normal female fertility and normal oogenesis. Males nullosomic for 3D4 lack normal, motile sperm. Females nullosomic for this region exert a maternal influence on their progeny which results in a diversity of imaginal defects. The observation that chromomere 3D4 is the most probable locus for a chromosomal region which affects cAMP phosphodiesterase activity, and which may contain a structural gene for the enzyme, prompts the hypothesis that the diverse physiological effects caused by nullosomy for 3D4 are the result of an aberrant cAMP metabolism.

scholarly journals SRA5 encodes the low-Km cyclic AMP phosphodiesterase of Saccharomyces cerevisiae.

1988 ◽  
Vol 8 (1) ◽  
pp. 505-510 ◽  
Author(s):  
R B Wilson ◽  
K Tatchell
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cyclic Amp ◽  
Nitrogen Starvation ◽  
Carbon Sources ◽  
Its Sequence ◽  
Phosphodiesterase Activity ◽  
Camp Phosphodiesterase ◽  
Rich Media ◽  
Minimal Media ◽  
The Right

sra5 mutations in Saccharomyces cerevisiae were previously shown to suppress the inefficient growth of ras2 strains on nonfermentable carbon sources and to result in deficient low-Km cyclic AMP (cAMP) phosphodiesterase activity. We have cloned SRA5 by complementation. It maps to the right arm of chromosome XV, tightly linked to PRT1, and its sequence matches the sequence of PDE2, encoding the low-Km cAMP phosphodiesterase. Disruptions of SRA5 allowed ras1 ras2 strains to grow either on rich media supplemented with cAMP or on minimal media without exogenous cAMP. sra5 strains failed to survive prolonged nitrogen starvation in the presence of exogenous cAMP.

scholarly journals 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.

SRA5 encodes the low-Km cyclic AMP phosphodiesterase of Saccharomyces cerevisiae

1988 ◽  
Vol 8 (1) ◽  
pp. 505-510
Author(s):  
R B Wilson ◽  
K Tatchell
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cyclic Amp ◽  
Nitrogen Starvation ◽  
Carbon Sources ◽  
Its Sequence ◽  
Phosphodiesterase Activity ◽  
Camp Phosphodiesterase ◽  
Rich Media ◽  
Minimal Media ◽  
The Right

sra5 mutations in Saccharomyces cerevisiae were previously shown to suppress the inefficient growth of ras2 strains on nonfermentable carbon sources and to result in deficient low-Km cyclic AMP (cAMP) phosphodiesterase activity. We have cloned SRA5 by complementation. It maps to the right arm of chromosome XV, tightly linked to PRT1, and its sequence matches the sequence of PDE2, encoding the low-Km cAMP phosphodiesterase. Disruptions of SRA5 allowed ras1 ras2 strains to grow either on rich media supplemented with cAMP or on minimal media without exogenous cAMP. sra5 strains failed to survive prolonged nitrogen starvation in the presence of exogenous cAMP.

Changes of calmodulin concentration and cyclic 3′, 5′-nucleotide phosphodiesterase activities in cardiac muscle of hyper- and hypothyroid rats

1994 ◽  
Vol 143 (3) ◽  
pp. 515-520 ◽  
Author(s):  
T Mano ◽  
K Iwase ◽  
Y Sawai ◽  
N Oda ◽  
Y Nishida ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Cardiac Muscle ◽  
Soluble Fraction ◽  
Nucleotide Metabolism ◽  
Muscle Dysfunction ◽  
Phosphodiesterase Activity ◽  
High Concentration ◽  
Camp Concentration ◽  
Camp Phosphodiesterase ◽  
Cardiac Muscles

Abstract To investigate the effect of thyroid hormone on cardiac muscle dysfunction in hyper- and hypothyroid states, we evaluated cyclic 3′, 5′-nucleotide metabolism by measuring cyclic 3′, 5′-nucleotide phosphodiesterase activity and calmodulin concentrations in the cardiac muscles of hyper- and hypothyroid rats. Cyclic AMP (cAMP) concentration was significantly high in the cardiac muscle of hyperthyroid rats and low in that from hypothyroid rats compared with control rats. Cyclic AMP and cyclic GMP phosphodiesterase activities were significantly decreased in the soluble fraction of cardiac muscle from hyperthyroid rats and markedly increased in this fraction in hypothyroid rats compared with normal animals. Calmodulin concentration was high in hyperthyroid and low in hypothyroid rats. It was concluded from these findings that low cAMP-phosphodiesterase activity might, in part, bring about the high concentration of cAMP. Calmodulin was sigificantly high in the cardiac muscle of hyperthyroid rats and the reverse was the case in hypothyroid rats compared with normal rats. The implication is that, in hyper- and hypothyroid states, these changes may play an important role in cardiac function via their effect on cyclic nucleotide and Ca2+ metabolism. Journal of Endocrinology (1994) 143, 515–520

scholarly journals Cyclic AMP responses are suppressed in mammalian cells expressing the yeast low Km cAMP-phosphodiesterase gene.

1990 ◽  
Vol 265 (10) ◽  
pp. 5840-5846
Author(s):  
M M Van Lookeren Campagne ◽  
E Wu ◽  
R D Fleischmann ◽  
M M Gottesman ◽  
K W Chason ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Mammalian Cells ◽  
Camp Phosphodiesterase
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