Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.4.1 (phosphodiesterase)
 18,767 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The role of cAMP as a mediator of gonadotropin stimulation of ovarian ornithine decarboxylase (ODC) activity was studied in granulosa cells isolated from small (1--2 mm) porcine ovarian follicles. These cells responded to both FSH and LH with significant increases in intracellular concentration of cAMP. At concentrations of gonadotropins which were saturating for the induction of ODC activity, FSH was a more potent stimulator of both cAMP production and ODC activity than LH. N,O'-Dibutyryl cAMP (1.0--10.0 mM) caused a dose-dependent stimulation of ODC activity which equaled the maximal effect of LH but was significantly less effective than the saturating dose of FSH. 8-Bromo-cAMP was more potent than N,O'-dibutyryl cAMP and as effective as FSH as an inducer of ODC activity. Addition of theophylline, a phosphodiesterase inhibitor, to the incubation medium resulted in a dose-dependent inhibition of ODC activity in both control and gonadotropin-stimulated cells. In contrast, 1-methyl,3-isobutyl xanthine, another phosphodiesterase inhibitor, potentiated effects of both submaximal and maximal effective doses of gonadotropins while producing no effect on basal ODC activity of these cells. The results of this study are consistent with the concept that cAMP can mediate gonadotropin stimulation of ODC in porcine granulosa cells. In addition, this study shows the importance of proper selection of cAMP analogs and phosphodiesterase inhibitors, and their concentration in studying such effects.
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PMID:Gonadotropin stimulation of porcine ovarian ornithine decarboxylase in vitro: the role of 3',5'-adenosine monophosphate. 8 47

After partial hepatectomy in rats, the following changes in enzymic activities were observed in the remnant liver during the prereplicative period. In the initial period of the prereplicative process, soon after removal of part of the liver, ornithine decarboxylase [EC 4.1.1.17] and IMP dehydrogenase [EC 1.2.1.14] increase. Subsequently, for entry into the S period, thymidine kinase [EC 2.7.1.75] increases simultaneously with increase in the intracellular cyclic AMP level and decrease in its phosphodiesterase [EC 3.1.4.17].
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PMID:Prereplicative enzymic changes in regenerating rat liver. 16 85

The activity of ornithine decarboxylase (EC 4.1.1.17; L-ornithine carboxy-lyase) of C6-BU-1 glioma and N115 neuroblastoma cells increases significantly when confluent cultures are treated with compounds that increase cellular cAMP levels. These include norepinephrine or isoproterenol, and prostaglandin E1 or adenosine, which stimulate ornithine decarboxylase activity in C6-BU-1 glioma and N115 neuroblastoma cells, respectively. Ornithine decarboxylase activity is also elevated in confluent C6-BU-1 glioma cells treated with dibutyrylcAMP and theophylline, or after the glioma cells are fed with a serum-depleted medium in the presence of catecholamines and inhibitors of cyclic nucleotide phosphodiesterase. The activity of the enzyme increases 500- to 1000-fold, 2-6 hr after stationary-phase N115 neuroblastoma cells are fed with a serum-free medium, supplemented with phosphodiesterase inhibitors, adenosine, or prostaglandin E1. This stimulation is antagonized by carbamoyl choline and is blocked by actinomycin D or cycloheximide. These results suggest that the synthesis of ornithine decarboxylase of C6-BU-1 glioma and N115 neuroblastoma cells is controlled by cAMP.
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PMID:Cyclic AMP-mediated induction of ornithine decarboxylase of glioma and neuroblastoma cells. 17 52

The activity of ornithine decarboxylase increases markedly in a biphasic manner during the hormone-dependent development of mouse mammary epithelium in vitro. The first peak of activity occurring at 3 to 4 hours of culture was elicited by incubating mammary explants in a culture medium without any added hormones, although addition of insulin or prolactin, or both, caused a greater increase. The emergence of the second peak of activity at about 12 hours depended on the actions of both insulin and prolactin. A second increase in activity could also be effected postmitotically by the delayed addition of prolactin. Studies with actinomycin D and cycloheximide suggest that the first increase in enzyme activity may be effected at a post-transcriptional level, whereas a second increase may be at both transcriptional and translational levels. During the first 3 hours of incubation, there was a rapid, transient increase in cyclic AMP concentration in mammary epithelium. The presence of insulin or prolactin in culture did not affect the change in epithelial cyclic AMP concentration. Addition of several derivatives of cyclic AMP, 0.1 to 0.5 mM, as well as prostaglandin E1, a stimulator of adenylate cyclase, resulted in enhancement of the first increase in enzyme activity. The effect of cyclic nucleotide was additive to that of insulin and prolactin and appears to be mediated at a post-transcriptional level. The stimulatory effect of a lower concentration of both the cyclic nucleotide and prostaglandin E1 was augmented by theophylline, an inhibitor of phosphodiesterase. These results may suggest possible involvement of cyclic AMP in the first increase in enzyme activity that occurs in the absence of any added hormones.
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PMID:Studies on regulatory factors of ornithine decarboxylase activity during development of mouse mammary epithelium in vitro. 17 59

Thyrotropin (TSH) stimulation of ornithine decarboxylase (ODC) activity and polyamine levels was studied in vitro in rat thyroids. The elevation in ODC activity was related to the concentration of TSH in the incubation medium with peak activity at a concentration of 25mU/ml. ODC activity with 50 mU/ml of TSH was 3 to 5-fold higher than control activity at 5 h of incubation; this stimulation was enhanced by the addition of 0.5 mM 3-isobutyl-l-methyl xanthine (MIX), a phosphodiesterase inhibitor. Dibutyryl cyclic AMP (DbcAMP) also stimulated ODC activity with a dose response up to 2.0 mm. The increase in ODC activity with TSH and MIX was prevented by incubation with actinomycin D (10 microgram/ml) or puromycin (0.2 mM). Putrescine concentrations in rat thyroids rose to three times basal levels after 6 h of incubation with TSH and MIX; no significant elevation in spermidine or spermine was observed after up to 7 h incubation. The increase in tissue putrescine preceded a rise in [3H]uridine incorporation into acid-soluble material that occurred at 7 h. The results suggest that stimulation of thyroid ODC activity by TSH is mediated by a cyclic AMP; the data further are consistent with a role for polyamines in the control of RNA synthesis in the thyroid.
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PMID:In vitro stimulation of thyroid ornithine decarboxylase activity and polyamines by thyrotropin. 19 94

The effect of different phorbol esters and of mechanical treatment on the activity of ornithine decarboxylase in mouse epidermis in vivo was investigated. The strong promoter 12-O-tetradecanoylphorbol-13-acetate as well as the weak promoters phorbol dibenzoate and the 12-O-tetradecanoylphorbol-13-acetate analog 12-O-tetradeca-2-cis, 4-trans-6,8-tetraenoylphorobol-13-acetate strongly increased the activity of the enzyme and the intraepidermal level of putrescine, with a maximum at 5 hr after application, when applied in doses which evoke comparable proliferative and irritant responses in skin. The hyperplasiogenic but nonirritant and almost nonpromoting 4-O-methyl ether of 12-O-tetradecanoylphorbol-13-acetate did not show such effects. Mechanical removal of the uppermost horny layer led to a considerable increase of ornithine decarboxylase activity after 4 to 8 hr, while skin massage showed only a minute effect under conditions in which both treatments exhibit about the same mitogenic efficiency. Neither manipulation promotes tumor development. After skin massage, the induction of ornithine decarboxylase was influenced neither by treatments which alter the cyclic adenosine 3',5'-monophosphate level in epidermis (inhibition of phosphodiesterase, beta-adrenergic stimulation, and injection of dibutyryl cyclic adenosine 3',5'-monophosphate) nor by injection of epidermal G1 chalone. The results indicate that no clear-cut correlation exists between epithelial cell proliferation, development of hyperplasia, and tumor promotion on the one hand and an activation of epidermal ornithine decarboxylase on the other.
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PMID:Ornithine decarboxylase activity, cell proliferation, and tumor promotion in mouse epidermis in vivo. 22 17

Cyclic AMP (cAMP) causes growth arrest in G1 and induction of cAMP phosphodiesterase and decrease of ornithine decarboxylase in S49 mouse lymphoma cells. Dibutyryl cAMP treatment of partially synchronized cells causes similar changes in activities of both enzymes, regardless of position in the cell cycle. This suggests that cAMP regulation of these enzymes is not mediated by growth perturbation.
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PMID:Regulation of phosphodiesterase and ornithine decarboxylase by cAMP is cell cycle independent. 23 Oct 36

A study was made of the activity of adenylate cyclase and cAMP-phosphodiesterase in rat thymus and liver various time intervals following nonlethal fractionated gamma-irradiation (2 Gy three times at a week interval). There was a positive correlation between the activity of cAMP metabolism enzymes and the radiation modification of ornithine decarboxylase (ODC) observed before. It is suggested that cAMP system is involved in ODC activity regulation in the exposed tissue.
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PMID:[The possible participation of the cAMP system in the activation of ornithine decarboxylase in rat tissues following nonlethal fractionated gamma-irradiation]. 165 39

The early biochemical responses to concanavalin A (Con A) of thymocytes from rats fed a saturated (coconut oil), (n-6) (sunflower oil) or (n-3) (fish oil) fatty acid-enriched diet for 3 wk were investigated. Fish oil feeding resulted in greater (n-3) polyunsaturated fatty acid level (PUFA) at the expense of (n-6) PUFA in total and individual thymocyte phospholipids. Such alterations of the fatty acid composition did not affect basal ornithine decarboxylase (ODC), cyclic nucleotide phosphodiesterase (PDE) or gamma-glutamyl transferase activities. However, the fish oil-enriched diet impaired some of the early thymocyte responses to Con A, such as the rapid induction (30 min) of soluble ODC and PDE activities. Synthesis of [3H]20:4(n-6) oxygenated metabolites was not different between the dietary groups; however, the uptake of [3H]20:4(n-6) into phospholipid classes was significantly lower in phosphatidylcholine and greater in phosphatidylethanolamine and phosphatidylinositol after fish oil feeding. Similarly, the Con A-induced remodeling of the [3H]20:4(n-6) esterification in phospholipids differed in sunflower oil- vs. fish oil-fed rats, suggesting a modulation of acyl CoA synthase and/or acyl CoA transferase activities. Thus, the modulation of Con A-induced ODC and PDE stimulation upon in vivo changes of membrane phospholipid fatty acid composition is not related to eicosanoid formation, but rather to the modification of the fatty acid acylation processes, altering phospholipid composition and signal transduction.
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PMID:Dietary polyunsaturated fatty acids modulate fatty acid composition and early activation steps of concanavalin A-stimulated rat thymocytes. 168 29

Treatment of PC12 cells with nerve growth factor (NGF), epidermal growth factor (EGF), or agents that raise intracellular cyclic AMP (cAMP) levels (e.g., forskolin) reduces the activity of calmodulin-dependent protein kinase III (CaM-PK III) over a period of 8 h. The mechanism of this effect of NGF has now been examined in more detail, making use of a mutant PC12 cell line (A126-1B2) that is deficient in cAMP-dependent protein kinase activity. Control experiments showed that A126-1B2 cells retain other NGF-mediated responses (e.g., the induction of ornithine decarboxylase, a cAMP-independent event) and contain a complement of CaM-PK III and its substrate, elongation factor-2, comparable to that of wild-type cells. The ability of NGF or forskolin, but not of EGF, to down-regulate CaM-PK III was markedly attenuated in A126-1B2 compared to wild-type cells. Treatment of wild-type cells with the cAMP phosphodiesterase inhibitor, isobutylmethylxanthine, enhanced the effects of NGF, but not of EGF. The possibility that NGF led to a stimulation of cAMP-dependent protein kinase activity in wild-type cells was assessed by measurement of the "activation ratio" (-cAMP/+cAMP) of this enzyme before and at various times after NGF addition. A small, but significant, increase in the activation ratio from 0.3 to 0.48 was observed, reaching a peak 5 min after NGF treatment. EGF had no effect on the activation ratio in wild-type cells.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Nerve growth factor-induced down-regulation of calmodulin-dependent protein kinase III in PC12 cells involves cyclic AMP-dependent protein kinase. 168 74


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