Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.1.17 (ornithine decarboxylase)
 6,351 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Single pharmacological doses of parathyroid hormone, calcitonin, vasopressin, d-aldosterone, or L-triiodothyronine produced a significant increase in the ornithine decarboxylase activity of rat kidney. The activity of kidney ornithine decarboxylase was also enhanced by other hormones, such as pentagastrin and serotonin, which, although they are not known to modify kidney physiology, are secreted by cells having close relationships to the calcitonin-secreting parafollicular cells. The induction of the enzyme was observed in hypophysectomized rats, with or without some other hormone-secreting glands remaining. However, the magnitude of the stimulation elicited by the hormones was somewhat diminished in animals still having the endocrine gland whose hormone was being tested. The maximal stimulation of kidney ornithine decarboxylase activity by parathyroid hormone, calcitonin, vasopressin, L-triiodothyronine, pentagastrin, and serotonin occurred at 4 h after the hormone injection. The enhancement in ornithine decarboxylase activity produced by d-aldosterone was maximal at 3 h after the injection of the hormone. The content of ornithine in the kidney was found to be virtually unchanged whatever the type of hormone treatment. No statistically significant increases in renal ornithine decarboxylase activity of hypophysectomized animals were observed after injection of melatonin or of vitamin D3. Since the stimulating hormones possess clearly different mechanisms of action, the role of cyclic AMP as a general mediator of ornithine decarboxylase induction is questioned.
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PMID:In vivo hormonal induction of ornithine decarboxylase in rat kidney. 18 46

The activity of ornithine decarboxylase (ODC) in rabbit costal chondrocytes in culture markedly increased after addition of parathyroid hormone (PTH), reaching a maximum 4 to 5 h after PTH addition. The effect of PTH was dose-dependent both in the presence and absence of fetal calf serum. Addition of cycloheximide or actinomycin D prevented the induction of ODC by PTH. Calcitonin, 1,25-dihydroxyvitamin D3, and vitamin A had no stimulatory effect on the activity of ODC, and did not inhibit the induction of ODC by PTH, when added with PTH.
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PMID:Induction by parathyroid hormone of ornithine decarboxylase in rabbit costal chondrocytes in culture. 76 50

As elastase is known to affect cell functions in various cell systems, its effects on the functions of control and 12-O-tetradecanoylphorbol 13-acetate (TPA)-treated chondrocytes in vitro were examined. Pretreatment of chondrocytes with TPA (10(-8) M) for 48 h significantly enhanced DNA synthesis, inhibited glycosaminoglycan (GAG) synthesis and inhibited the increase in ornithine decarboxylase (ODC) activity in response to parathyroid hormone (PTH) relative to values in control cultures. Addition of elastase (1, 10 and 50 ng/ml) for 24 h partially inhibited the de-differentiated phenotypes induced by TPA such as the decreased synthesis of GAG and decreased response of ODC activity to PTH without affecting the DNA synthesis. Moreover, elastase significantly increased both the basal level of cyclic AMP and that on PTH treatment of TPA-pretreated cells. These results suggested that elastase partially restored the differentiated phenotypes of de-differentiated chondrocytes probably through its effect in increasing the level of intracellular cyclic AMP.
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PMID:Effect of elastase in reversing the de-differentiation of rabbit costal chondrocytes in culture induced by the tumor promoter 12-O-tetradecanoylphorbol 13-acetate (TPA). 165 31

Ornithine decarboxylase (ODC) is a rate-limiting enzyme of the biosynthesis of polyamines, which are important in cell growth and differentiation. Here, we studied whether parathyroid hormone (PTH) affects the induction of ODC and the proliferation of the human osteoblast-like cell line SaOS2, which is sensitive to PTH. In confluent cells, ODC activity was not detected, but activity was significantly induced by fresh medium, with maximum activity 6 h after the change. PTH potentiated this enzyme induction in a dose-dependent manner at 10(-9) and 10(-8) M at which range the intracellular cAMP level also rose. Dibutyryl cAMP, cholera toxin, and 3-isobutyl-1-methylxanthine each caused an increase in ODC activity similar to that with PTH. The half-life of enzyme activity was about 30 min and was not changed by the addition of PTH. mRNA coding for ODC was detected in the confluent cells and its concentration was increased two- to threefold by the fresh medium. No further increase in mRNA occurred when PTH was added. At 48 h after the change of medium, PTH inhibited the DNA synthesis induced by fresh medium. These results suggest that the increase in ODC activity caused by PTH was caused by enhancement of cAMP synthesis, and that this augmentation involves post-transcriptional regulation.
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PMID:Effects of parathyroid hormone on ornithine decarboxylase activity in human osteosarcoma cells. 165 84

In order to elucidate the possible role of polyamines in the mobilization of mineral from long-term bone cultures stimulated with parathyroid hormone we have measured the activity of ornithine decarboxylase in osteoblasts, the levels of polyamines in calvarial bone and determined the effect of added polyamines and inhibitors of polyamine biosynthesis on calcium mobilization. Parathyroid hormone (10 nmol l-1) stimulated omithine decarboxylase activity by approximately 50% in both cultured bone cells of osteoblastic phenotype, UMR 106 and in mouse calvarial osteoblast-like cells. In mouse calvaria the levels of putrescine and spermidine were increased by parathyroid hormone after 24 hours. The levels of spermine were very low and were unchanged by parathyroid hormone. The two polyamine synthesis inhibitors alpha-difluoromethylornithine (DFMO; 2 mmol l-1) and methylglyoxal-bis-guanylhydrazone (MGBG; 50 mu mol l-1) did not significantly affect the mobilization of 45Ca from parathyroid hormone-stimulated bones. All three polyamines, putrescine, spermidine and spermine, inhibited the mobilization of 45Ca induced by parathyroid hormone in a dose-dependent manner. The inhibition induced by putrescine was reversible. In summary, we have shown that parathyroid hormone increases the accumulation of polyamines in bone, but the effect is small. Furthermore, inhibition of polyamine biosynthesis does not reduce parathyroid hormone-induced mineral mobilization and the addition of polyamines leads to a reduced rather than a stimulated mineral mobilization. Thus, polyamines do not seem to be critically involved in the changes in bone resorption induced by parathyroid hormone.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:On the role of polyamines in bone resorption induced by parathyroid hormone. 187 75

We investigated the role of cAMP and Ca2+ as mediators in parathyroid hormone (PTH)-induced ornithine decarboxylase (ODC) activity in primary cultures of chicken osteoblasts. We present evidence that the induction of ODC activity by PTH is most likely a receptor-mediated process and that cAMP is a mediator. However, using three different approaches we have strong indications that cAMP is not the exclusive mediator of PTH-induced ODC activity. First, when the dose-response curve of PTH-induced ODC activity is compared with that of PTH-stimulated cAMP production, the ED50 for cAMP production is about five times as high as that for the induction of ODC activity. Second, 1 mM 9-(tetrahydro-2-furanyl) adenine (SQ 22.536) almost completely inhibited PTH-stimulated cAMP production whereas there was only a small inhibitory effect on PTH-induced ODC activity. Third, some PTH fragments unable to stimulate cAMP production were still able to induce ODC activity. We therefore propose that apart from cAMP, an additional messenger, most likely Ca2+, must be present. Evidence for this concept are the observations that substances affecting extracellular and intracellular Ca2+ levels (EGTA, A23187, CoCl2, verapamil) or antagonizing calmodulin (Trifluoroperazin, Compound 48/80) also strongly affect PTH-induced ODC activity. These effects could not be explained by a positive interaction of Ca2+ with the hormone-stimulated cAMP system as 2 mM EGTA strongly enhanced PTH-stimulated cAMP production but at the same time completely inhibited PTH-induced ODC activity. A similar dissociation between hormone-induced cAMP production and induction of ODC activity was found with the Ca2+ -ionophore A23187 (10(-7) M) which significantly inhibited PTH-stimulated cAMP production but strongly enhanced PTH-induced ODC activity. Our results suggest that intracellular Ca2+, and possibly calmodulin, in addition to cAMP, are involved in PTH-induced ODC activity in chicken osteoblasts. Most probably Ca2+ is the initial messenger and cAMP acts in a coordinate pattern as a synarchic messenger making the induction of ODC activity by PTH more sensitive to Ca2+. Furthermore, the present findings are in agreement with our concept of the existence of two receptors or two receptor-sites for PTH on osteoblasts. One receptor is coupled to the production of cAMP and is presumably activated when the first two aminoacids of the NH2-terminus of the hormone are present and the other, suggested to be responsible for the increase in intracellular Ca2+, is thought to be activated by a region of the hormone sequence between amino acid 3 and 34.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Induction of ornithine decarboxylase activity in isolated chicken osteoblasts by parathyroid hormone: the role of cAMP and calcium. 246 67

The effect of activation of protein kinase C on stimulation of ornithine decarboxylase (ODC) activity and cAMP production was studied in fetal rat osteoblasts. Both phorbol 12-myristate, 13-acetate (PMA), an activator of protein kinase C, and 4 alpha-phorbol, ineffective in activating protein kinase C, failed to stimulate ODC activity and cAMP production. We tested the effect of protein kinase C on stimulation of ODC activity by parathyroid hormone (PTH) and forskolin. In contrast to PTH-stimulated ODC activity, which was not affected by PMA, forskolin-stimulated (1 and 10 microM) ODC activity was dose dependently reduced. PMA (400 nM) reduced both 1 and 10 microM forskolin-stimulated ODC activity to the same level, approximately 3 nmol CO2/mg protein, which suggests a controlling role of protein kinase C in forskolin-stimulated ODC activity. The study of the effect of protein kinase C on PTH- and forskolin-stimulated cAMP production also revealed differences between PTH and forskolin. When PMA was added simultaneously with PTH (4 and 20 nM) or forskolin (1 and 10 microM) the PTH-stimulated cAMP production was dose-dependently potentiated by PMA, whereas forskolin-stimulated cAMP production was not affected. However, both PTH- and forskolin-stimulated cAMP production was dose-dependently augmented when PMA was added 3 min prior to PTH or forskolin. With increasing preincubation periods (up to 24 h) with PMA instead of a potentiation an inhibition was observed. This inhibition is not due to PTH receptor desensitization, although, on basis of the present results desensitization can not completely be excluded. In all cases 4 alpha-phorbol was without effect. The present results show that protein kinase C modulates stimulation of ODC activity and cAMP production in fetal rat osteoblasts. The modulation of both ODC activity and cAMP production appears to be dependent on the nature of the stimulator. The present data suggest a role for protein kinase C in limiting the cAMP-mediated stimulation of ODC activity in these cells. Furthermore, it is suggested that protein kinase C can interfere at more than one site in the cAMP-generating system.
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PMID:Modulatory function of protein kinase C in the activation of ornithine decarboxylase and in cAMP production in rat osteoblasts. 253 85

Induction of ornithine decarboxylase (ODC, E.C. 4.1.1.17) activity by parathyroid hormone (PTH) in cultured fetal rat osteoblasts was studied. PTH induced ODC activity and stimulated cAMP production in a dose-dependent manner, the ED50 for cAMP being five times as high as that for ODC. Induction of ODC activity by PTH was partly inhibited by actinomycin D and cycloheximide, with 40 and 55% inhibition, respectively. PTH increased the intracellular ionized calcium concentration ([Ca2+]i), which was absent in a Ca2+-free medium. Blocking calcium influx, lowering the extracellular calcium concentration, and adding trifluoperazine inhibited both induction of ODC activity and stimulation of cAMP production by PTH. A23187 (100 nM and 1 microM), combined with a low dose of PTH (4 nM), resulted in a synergistic induction of ODC activity and an inhibition of cAMP production. A23187 inhibited induction of ODC activity as well as stimulation of cAMP production by the dose of PTH (20 nM) maximally effective in inducing ODC activity. Forskolin together with this maximal dose of PTH resulted in an additive effect on ODC activity and a synergistic stimulation of cAMP production. The current results show similarities and differences with respect to results obtained with osteoblasts from other species and osteoblast cell lines. The present data indicate that (1) PTH stimulates ODC activity and this is partly due to new enzyme synthesis; (2) calcium is involved in induction of ODC activity and stimulation of cAMP production by PTH; furthermore, it is suggestive that calmodulin and/or protein kinase C are involved; and (3) stimulation of cAMP production by PTH depends on an optimal intracellular calcium concentration range.
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PMID:Parathyroid hormone-induced ornithine decarboxylase activity in fetal rat osteoblasts. 255 85

The effects of insulin and parathyroid hormone (PTH) on the proliferation of developing bovine dental pulp in an explant culture system were studied. Dental pulp explants were cultured on siliconized lens paper floating on the serum-free medium for up to 72 h. Ornithine decarboxylase (ODC) activity increased and reached a peak after 24 h. DNA synthesis increased continuously after a lag period of 24 h. Insulin (10 milliunits per ml) stimulated ODC activity 1.3-fold and DNA synthesis 1.5-fold. PTH alone (1 unit per ml) stimulated ODC activity in 1.7-fold, but did not affect DNA synthesis. PTH plus insulin caused greater increases in ODC activity and DNA synthesis in dental pulp explants than insulin alone (ODC, 2.6-fold; DNA, 3.7-fold). These results suggest that insulin and PTH are involved in the regulation of growth of dentinogenically active bovine dental pulp.
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PMID:Effects of insulin and parathyroid hormone on DNA synthesis and ornithine decarboxylase activity in cultured bovine dental pulp. 269 23

Pulsed electromagnetic fields promote healing of delayed united and ununited fractures by triggering a series of events in fibrocartilage. We examined the effects of a pulsed electromagnetic field (recurrent bursts, 15.4 Hz, of shorter pulses of an average of 2 gauss) on rabbit costal chondrocytes in culture. A pulsed electromagnetic field slightly reduced the intracellular cyclic adenosine 3',5'-monophosphate (cAMP) level in the culture. However, it significantly enhanced cAMP accumulation in response to parathyroid hormone (PTH) to 140% of that induced by PTH in its absence, while it did not affect cAMP accumulation in response to prostaglandin E1 or prostaglandin I2. The effect on cAMP accumulation in response to PTH became evident after exposure of the cultures to the pulsed electromagnetic field for 48 h, and was dependent upon the field strength. cAMP accumulation in response to PTH is followed by induction of ornithine decarboxylase, a good marker of differentiated chondrocytes, after PTH treatment for 4 h. Consistent with the enhanced cAMP accumulation, ornithine decarboxylase activity induced by PTH was also increased by the pulsed electromagnetic field to 170% of that in cells not exposed to a pulsed electromagnetic field. Furthermore, stimulation of glycosaminoglycan synthesis, a differentiated phenotype, in response to PTH was significantly enhanced by a pulsed electromagnetic field. Thus, a pulsed electromagnetic field enhanced a series of events in rabbit costal chondrocytes in response to PTH. These findings show that exposure of chondrocytes to a pulsed electromagnetic field resulted in functional differentiation of the cells.
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PMID:Enhanced responsiveness to parathyroid hormone and induction of functional differentiation of cultured rabbit costal chondrocytes by a pulsed electromagnetic field. 282 May 12


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