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)

Human cytomegalovirus (HCMV) infection of low serum-arrested confluent whole human embryo (Flow 5000) cells markedly stimulated ornithine decarboxylase (ODC) activity. Increased ODC activity was apparent by 12 h post-infection. The capacity of HCMV to stimulate ODC was: (1) dependent upon multiplicity of infection; (2) eliminated when the virus was neutralized with specific antiserum; and (3) sensitive to ultraviolet irradiation. Virus-mediated induction, in contrast to high serum induction of ODC, was not subject to inhibition by polyamines added to the growth medium. Phosphonoacetic acid (PAA) which blocks HCMV replication by inhibiting the activity of HCMV-specific DNA polymerase and which does not prevent HCMV induced stimulation of cell DNA synthesis, reversibly inhibited HCMV-induced stimulation of ODC activity by 74%. Studies with PAA indicated that HCMV-induced stimulation of ODC activity is independent of cell DNA synthesis and that the mechanism regulating virus-induced stimulation may be related to the HCMV-specific DNA polymerase.
J Gen Virol 1979 Feb
PMID:Stimulation of ornithine decarboxylase by human cytomegalovirus. 21 56

A possible minor route of ornithine catabolism in Aspergillus nidulans might begin with the ornithine decarboxylase reaction and end with the succinic semialdehyde dehydrogenase reaction. It is therefore of interest that the putative structural genes for these two enzymes, puA and ssuA, respectively, are tightly linked group II. However, this linkage is unlikely to have regulatory significance because ileA, the structural gene for threonine dehydratase, separates them. The gene order in this region is ssuA-ileA-puA-mauB-anB. (mauB- mutations result in loss of monoamine oxidase whilst anB- mutations lead to aneurin auxotrophy.) 2. An auxotrophy for ornithine or putrescine in A. nidulans occurs in double mutants lacking arginase and blocked before ornithine in the arginine biosynthetic pathway. Some residual ornithine synthesis in such double mutants can be catalysed by ornithine delta-transaminase, especially if it is synthesised constitutively.
Mol Gen Genet 1977 Feb 28
PMID:Some genetical aspects of ornithine metabolism in Aspergillus nidulans. 32 61

The polyamine spermidine and the diamine putrescine have been detected in coliphages T5 and phiX174. Polyamines were identified by thin-layer chromatography and mass-spectrometry of dansyl derivatives, as well as by ion-exchange chromatography. In phiX174 phages, polyamines were sufficient to neutralize 0.5% of DNA phosphates. The polyamine content of T5 phages depended on growth media and purification procedures, but at least 1% of DNA phosphates were neutralized by polyamines. After infection, an increase in cellular polyamine was noticed. This increase paralleled variations in ornithine decarboxylase activity.
J Gen Virol 1975 Mar
PMID:Occurrence of polyamines in coliphages T5, phiX174 and in phage-infected bacteria. 109 18

We report the physical and genetic mapping of pheV, an Escherichia coli gene for phenylalanine tRNA, to 64 min on the chromosomal map in the near vicinity of speC coding for ornithine decarboxylase.
Mol Gen Genet 1990 Jan
PMID:Genetic mapping of pheV, an Escherichia coli gene for tRNA(Phe). 218 6

Hyphal development in Candida albicans was selectively blocked by the ornithine decarboxylase competitive inhibitor 1,4-diaminobutanone (DAB). Inhibition of hyphal development required DAB during both yeast inoculum growth and subsequent incubation at 37 degrees C to induce mycelial growth. This effect was not due to general growth inhibition since DAB did not inhibit yeast growth, and reduced protein synthesis by 30% at most. Moreover, protein synthesis was unaffected by DAB when cells were pre-grown in drug-containing media. Since DAB inhibited dimorphic transition at 37 degrees C, morphology- and temperature-dependent protein synthesis could be distinguished. DAB stimulated the synthesis of several yeast wall-proteins, irrespective of morphology or growth temperature, and two at 37 degrees C only, but it inhibited the synthesis of a single mycelial-specific glycoprotein species.
J Gen Microbiol 1990 Oct
PMID:Inhibition of the dimorphic transition of Candida albicans by the ornithine decarboxylase inhibitor 1,4-diaminobutanone: alterations in the glycoprotein composition of the cell wall. 226 70

Chicken growth hormone (cGH) was purified from frozen pituitary glands obtained from recently sacrificed broilers. Glands were homogenized in a protease inhibitor solution (0.5 mM PMSF, 50 KIU/ml aprotinin, pH 7.2); extract was taken to pH 9.0 with calcium hydroxide and the supernatant was differentially precipitated with 20% (fraction A) and 50% (fraction B) ammonium sulfate. cGH (fraction B-DE-1) was obtained in pure form from fraction B after DEAE-cellulose chromatography at pH 8.6, with a yield of 2.9 mg/g tissue. Three charge variants of cGH (Rf = 0.23, 0.30, and 0.35) could be isolated by electroelution after semipreparative nondenaturing polyacrylamide gel electrophoresis of fraction B-DE-1. These charge variants showed the same apparent molecular weight (26,300 Da) by sodium dodecyl sulfate polyacrylamide gel electrophoresis under reducing conditions. Isoelectric focusing of fraction B-DE-1 revealed two major components (pI = 7.2 and 7.4) and four minor bands (pI = 6.2, 6.7, 7.1, and 7.5). It was found that fraction B-DE-1 contained a significant amount of esterified phosphate (1 nmol PO4/3.5 nmol protein) similar to that reported previously for ovine GH. The functional integrity of the cGH obtained here was characterized by two heterologous and one homologous bioassays. High activity was shown by fraction B-DE-1 in the tibia assay (1.76 UI/mg) and in the liver ornithine decarboxylase assay (sixfold over control), both made in hypophysectomized rats; and it also stimulated lipolysis (138 and 215% at 10 and 100 ng/ml, respectively) on chicken abdominal adipose tissue explants.
Gen Comp Endocrinol 1989 Nov
PMID:Partial biochemical and biological characterization of purified chicken growth hormone (cGH). Isolation of cGH charge variants and evidence that cGH is phosphorylated. 259 23

Heart ornithine decarboxylase (ODC) from isoproterenol treated rats was compared to heart ODC from control rats. Isoproterenol administration did not significantly change Km for ornithine, but it induced a marked increase of Vmax, X Km for pyridoxal phosphate (PLP) was somewhat reduced. Both Kornm and Vmax were a function of the dithiothreitol (DTT) concentration, in a similar way for control and stimulated enzyme. Two ODC forms were detected by ion exchange chromatography in both control and isoproterenol treated hearts. In control heart, ODC specific activity was high in cytosol and nucleoli. Isoproterenol administration induced a remarkable increase of the cytosolic enzyme only.
Gen Pharmacol 1986
PMID:Heart ornithine decarboxylase from control and isoproterenol-treated rats: kinetic properties, multiple forms and subcellular distribution. 308 2

Prolactin has been shown to increase the activity of ornithine decarboxylase in a variety of mammalian tissues and in the pigeon crop sac. This study demonstrates a similar effect of ovine prolactin on ornithine decarboxylase activity in liver slices taken from larval tiger salamanders (Ambystoma tigrinum). An evaluation of potential mediators of prolactin action in liver slices revealed that the effect of the hormone on enzyme activity was not blocked by ouabain, an inhibitor of the sodium pump reported to block other actions of prolactin. Oxytocin, which inhibits prolactin actions in A. tigrinum, blocked the increase in ornithine decarboxylase activity induced by prolactin. Since previous results had implicated inositol phospholipid turnover in oxytocin action, the effects of the calcium ionophore, A 23187, and of synthetic diacylglycerol were examined. Both agents blocked the increase in enzyme activity when they were combined with prolactin treatment. Verapamil, a calcium channel blocker, had a prolactin-like effect on the activity of ornithine decarboxylase, and the combination of prolactin and verapamil produced a stimulation of the enzyme that was no greater than that observed with either the drug or prolactin alone, suggesting that both agents might be acting via a common cellular pathway. The tentative hypothesis that prolactin acts via a mechanism which lowers intracellular calcium is suggested.
Gen Comp Endocrinol 1988 Oct
PMID:Enhancement of ornithine decarboxylase activity in Ambystoma liver slices by ovine prolactin: an evaluation of possible mediators. 314 Dec 45

The biochemical properties of 39 strains of Haemophilus avium from chickens were determined. All the strains produced acid from fructose, galactose, glucose and mannose but not from lactose. Variable reactions were found for arabinose, maltose, mannitol, sorbitol, trehalose and xylose. No strains showed urease activity or produced indole, while beta-galactosidase and/or ornithine decarboxylase activity was present in some strains. This variability allowed the recognition of 15 biochemical biovars including some not previously recognized in H. avium. Only 25 (64%) of the H. avium strains could be assigned to the three species (Pasteurella avium, P. volantium and Pasteurella species A) recently proposed to replace H. avium.
J Gen Microbiol 1988 Oct
PMID:Biochemical properties of catalase-positive avian haemophili. 315 Dec 6

The effect of a single administration of catecholamines on ornithine decarboxylase activity and polyamine biosynthesis in the rat spleen was investigated. Isoproterenol elicited a dose-dependent increase in spleen ODC activity which reached a maximum 4 hr after the administration of the drug. Putrescine content was also found to increase within a few hours, whereas S-adenosylmethionine decarboxylase activity and spermidine and spermine levels did not change significantly. Adrenaline and noradrenaline proved to be even more effective in increasing splenic ODC activity than isoproterenol. alpha- and beta-adrenergic antagonists prevented the ODC increase by catecholamines to a different extent.
Gen Pharmacol 1986
PMID:Effect of adrenergic stimulation on ornithine decarboxylase activity in the rat spleen. 372 Nov 90


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