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

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 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

scholarly journals Initiation of meiosis and sporulation in Saccharomyces cerevisiae does not require a decrease in cyclic AMP.

1987 ◽  
Vol 7 (6) ◽  
pp. 2141-2147 ◽  
Author(s):  
Z Olempska-Beer ◽  
E Freese
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Carbon Source ◽  
Cyclic Amp ◽  
Phosphodiesterase Inhibitor ◽  
Intracellular Camp ◽  
Glucose Medium ◽  
Camp Concentration ◽  
Ishikawa Cell ◽  
Camp Phosphodiesterase ◽  
Low Level

Meiosis and sporulation of Saccharomyces cerevisiae are initiated in a guanine auxotroph by guanine deprivation (E. Bautz Freese, Z. Olempska-Beer, A. Hartig, and E. Freese, Dev. Biol. 102:438-451, 1984). We used this condition to examine a hypothesis (K. Matsumoto, I. Uno, and T. Ishikawa, Cell 32:417-423, 1983) that initiation of meiosis requires a low level of cAMP. We found that, after guanine deprivation, the intracellular concentration of cAMP transiently decreased not more than 20% and not at all if the cAMP phosphodiesterase inhibitor 3-isobutyl-1-methylxanthine (IBMX) was added to the medium. Under these conditions, at least 76% of the cells sporulated in the absence of IBMX, and almost 100% sporulated in its presence. The sporulating cells continually excreted cAMP and utilized the gluconeogenic carbon source. The cells failed to sporulate efficiently and to form four-spored asci if simultaneously deprived of guanine and carbon. After guanine deprivation in glucose medium, sporulation remained suppressed and intracellular cAMP was unchanged. We conclude that, under conditions of guanine starvation, cAMP deficiency is not required for initiation of meiosis and sporulation, cAMP is produced in excess and excreted to the medium, the cells sporulate better if the cAMP concentration is increased by addition of IBMX, the cells require a gluconeogenic carbon source for complete and efficient sporulation, and suppression of sporulation by glucose is not mediated by cAMP.

Initiation of meiosis and sporulation in Saccharomyces cerevisiae does not require a decrease in cyclic AMP

1987 ◽  
Vol 7 (6) ◽  
pp. 2141-2147
Author(s):  
Z Olempska-Beer ◽  
E Freese
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Carbon Source ◽  
Cyclic Amp ◽  
Phosphodiesterase Inhibitor ◽  
Intracellular Camp ◽  
Glucose Medium ◽  
Camp Concentration ◽  
Ishikawa Cell ◽  
Camp Phosphodiesterase ◽  
Low Level

Meiosis and sporulation of Saccharomyces cerevisiae are initiated in a guanine auxotroph by guanine deprivation (E. Bautz Freese, Z. Olempska-Beer, A. Hartig, and E. Freese, Dev. Biol. 102:438-451, 1984). We used this condition to examine a hypothesis (K. Matsumoto, I. Uno, and T. Ishikawa, Cell 32:417-423, 1983) that initiation of meiosis requires a low level of cAMP. We found that, after guanine deprivation, the intracellular concentration of cAMP transiently decreased not more than 20% and not at all if the cAMP phosphodiesterase inhibitor 3-isobutyl-1-methylxanthine (IBMX) was added to the medium. Under these conditions, at least 76% of the cells sporulated in the absence of IBMX, and almost 100% sporulated in its presence. The sporulating cells continually excreted cAMP and utilized the gluconeogenic carbon source. The cells failed to sporulate efficiently and to form four-spored asci if simultaneously deprived of guanine and carbon. After guanine deprivation in glucose medium, sporulation remained suppressed and intracellular cAMP was unchanged. We conclude that, under conditions of guanine starvation, cAMP deficiency is not required for initiation of meiosis and sporulation, cAMP is produced in excess and excreted to the medium, the cells sporulate better if the cAMP concentration is increased by addition of IBMX, the cells require a gluconeogenic carbon source for complete and efficient sporulation, and suppression of sporulation by glucose is not mediated by cAMP.

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

Regulation Of Adenylate Cyclase-Phosphodiesterase By Testosterone In Cultured Endothelium

1981 ◽  
Author(s):  
S S Ahmed ◽  
G J Stewart
Keyword(s):  
Enzyme Activity ◽  
Adenylate Cyclase ◽  
Cell Function ◽  
Control Level ◽  
Major Change ◽  
Experimental Period ◽  
Nucleotide Metabolism ◽  
High Concentration ◽  
Camp Phosphodiesterase ◽  
Bovine Endothelial Cell

The effects of testosterone on the activities of the enzymes involved in cyclic adenosine 3’:5’-monophosphate (cyclic AMP) metabolism in primary bovine endothelial cell cultures were examined. Adenylate cyclase was measured under basal and 10 mM NaF stimulated conditions. In control cultures, the enzyme activity remained essentially unchanged for 48 hours and then showed a significant increase (p<0.05) through 96 hours. Addition of testosterone (1 × 10-7M) six hours after plating stimulated the enzyme activity causing a significant increase (p<0.05) at 72 hours of incubation. Addition of 10 mM NaF enhanced basal activity as well as testosterone stimulated activity of adenylate cyclase throughout the experimental period. Low and high affinity forms of cAMP phosphodiesterase were measured independently by varying the substrate concentration. At 250 μM substrate the low Km enzyme contributed very little (about 8%) to the activity whereas at 0.1 μM substrate the contribution of the high Km form was about 26%. The activity of both forms fell rapidly during growth phase of control endothelial cells. The addition of 1 × 10-7M testosterone at the time of plating caused little change from the control level for the first 48 hours, i.e. the activity of phosphodiesterase fell at the same rate in control and treated cultures. Further incubation resulted in marked inhibition of both forms of phosphodiesterase by testosterone. Testosterone added to subconfluent cultures at low concentration (1 × 10-9M) failed to stimulate adenylate cyclase but did inhibit low Km phosphodiesterase (p<0.05). A high concentration (1 × 10-7M) of testosterone stimulated adenylate cyclase activity and markedly decreased activities of high and low Km phosphodiesterase. This study showed that testosterone induced a major change in cyclic nucleotide metabolism, an important factor in regulating cell function (cell adhesion in this case).

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.

STUDIES ON THE MECHANISMS OF SOMATOSTATIN ACTION ON INSULIN RELEASE

1977 ◽  
Vol 85 (2) ◽  
pp. 379-388 ◽  
Author(s):  
A Claro ◽  
V. Grill ◽  
S. Efendić ◽  
R. Luft
Keyword(s):  
Cyclic Amp ◽  
Insulin Release ◽  
Competitive Inhibition ◽  
Phosphodiesterase Inhibitor ◽  
Adenyl Cyclase ◽  
Phosphodiesterase Activity ◽  
High Concentration ◽  
Isolated Islets Of Langerhans ◽  
Cyclic Amp Accumulation ◽  
Effect Of Glucose

ABSTRACT The effects of somatostatin on insulin release and cyclic AMP metabolism were studied in collagenase-isolated islets of Langerhans from the rat. Concentrations from 500 to 2000 ng/ml significantly inhibited glucose stimulated insulin release, while 100 and 200 ng/ml were ineffective. Somatostatin (2000 ng/ml) inhibited insulin release and [3H]-cyclic AMP accumulation induced by 16.7 mm glucose after 10 and 30 min of incubation. In dose-response studies, the inhibition by somatostatin of the effect of glucose on [3H] cyclic AMP and insulin release could be overcome by a high concentration of the hexose (44.9 mM), suggesting competitive inhibition. In the absence of glucose, somatostatin inhibited [3H] cyclic AMP accumulation induced by the phosphodiesterase inhibitor, IBMX, while no inhibition was seen, again in the absence of hexose, when the [3H] cyclic AMP levels had been raised by the adenyl cyclase stimulator, cholera toxin. Somatostatin did not affect phosphodiesterase activity when added to islet homogenates, but preincubation of the islets with the peptide before homogenization decreased the activity by about 30 %. It is suggested that somatostatin-induced inhibition of insulin release is, at least partially, mediated by cyclic AMP, probably through an action on islet adenyl cyclase.

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.

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