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

Infection of primary cultures of mouse kidney cells with polyoma virus causes a biphasic increase in the activities of L-ornithine decarboxylase (ODC; L-ornithine carboxy-lyase; EC 4.1.1.17) and S-adenosyl-L-methionine decarboxylase (SAMD; S-adenoxyl-L-methionine carboxy-lyase; EC 4.1.50), as well as in the level of the polyamines putrescine, spermidine, and spermine. An early peak occurs during the period when early viral mRNA is synthesized and prior to the onset of virus-induced synthesis of host cell DNA. A late peak coincides in time with the maximum rate of virus-induced synthesis of cellular DNA. A similar biphasic stimulation of polyamine synthesis is induced even when DNA synthesis is prevented by 5-fluorodeoxyuridine. Actinomycin D (AMD) in a dose that inhibits rRNA synthesis causes no inhibition of ODC or SAMD. In a dose that inhibits mRNA synthesis as well, short-term AMD treatment causes "superinduction" of ODC but inhibition of SAMD. Prolonged treatment with the high dose of AMD inhibits ODC as well, indicating that late ODC activity may be dependent on mRNA synthesized during early infection. Cycloheximide effectively obliterates the ODC and SAMD activities during the entire infectious cycle. Uncoupling from DNA and rRNA synthesis suggests that polyamine synthesis is regulated independently of these events. The experiments with AMD and cycloheximide suggest that the formation of ODC is subject to post-transcriptional control, whereas that of SAMD is regulated primarily at the transcriptional level.
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PMID:Biphasic stimulation of polyamine biosynthesis in primary mouse kidney cells by infection with polyoma virus:uncoupling from DNA and rRNA synthesis. 18 74

Two effectors of ornithine decarboxylase (ODC; L-ornithine carboxy-lyase, EC 4.1.1.17) have been extracted from an ODC- (speC-) mutant, Escherichia coli MA 255. One of these is an ODC inhibitor (Mr 15,000 +/- 2000) that is labile to trypsin; its activity increases 20-fold in response to increased polyamine levels in the growth medium. It has additional characteristics similar to those of the ODC antizyme of eukaryote cells: it is a noncompetitive inhibitor of ODC; the complex formed between ODC and the ODC inhibitor can be dissociated with salt to provide active ODC and active ODC inhibitor; furthermore, this E. coli ODC inhibitor is inhibitory to eukaryote ODC. A thermostable nondialyzable factor that activates ODC in vitro has also been extracted from MA255; increased polyamine levels in the growth medium caused a 1.6-fold increase in the activity of this ODC activator. Effectors with comparable activities have also been identified in the parent ODC+ (speC+) strain MA197. The fluctuations of the intracellular levels of these two ODC effectors during the growth of E. coli MA255 have been related to the temporal changes of the activity of ODC in the parent ODC+ MA197 strain. The mode of interaction of these three macromolecules, as reflected in the changes of the activity of ODC, appears to be complex. The results suggest that ODC activity may be controlled post-translationally by macromolecules that act as positive and negative effectors and whose levels fluctuate in response to the concentration of the end products of the reaction.
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PMID:Modulation of ornithine decarboxylase activity in Escherichia coli by positive and negative effectors. 36 95

Pregnant albino rats were placed on a complete liquid diet (Ensure) containing either 9% ethanol or an isocaloric amount of sucrose between the third and twentieth day of gestation. The pups born to these rats were sacrificed either day 11 or day 14 postnatum and morphometrical, histological and biochemical analyses were done on their cerebellums and cerebrums. Pups that were exposed to ethanol in utero had significantly smaller body weights, cerebrums and cerebellums than pair-fed controls. The cerebellar mass was reduced by 10% and the cerebral weight by 3% in the pups exposed to alcohol when body weights were normalized to that of pair-fed controls. Cerebellar aspartyl aminotransferase (EC 2.6.1.1) activity was reduced at day 11 and 14 in ethanol treated pups compared with controls. Serum T4 levels were also reduced in the ethanol treated group. Histological analyses revealed that the external granule cell (EGC) layer of ethanol treated pups was significantly thicker at 11 and 14 days postnatum than that of pair-fed control pups. Cerebellar ornithine decarboxylase (ODC, EC 4.1.1.17) activity was higher at day 11 in the ethanol treated pups than in controls. The reduced mass, AAT activity, T4 serum levels and the increased thickness of the ECG layer indicate a delayed or impeded maturation of cerebellum in ethanol treated pups. These data are considered from the viewpoint that ethanol, other drugs such as methadone and prenatal stress (malnutrition) may cause delayed cerebellar maturation by reducing serum T4 levels in the early postnatal period (day 5-14).
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PMID:Impeded cerebellar development and reduced serum thyroxine levels associated with fetal alcohol intoxication. 49 36

Protein synthesis is shown to be very heat-sensitive in Chinese hamster cells. It is shut off completely following 15-20 min at 42 degrees C whereas RNA and DNA syntheses are affected only after much longer exposure times. Cells recover from inhibition of protein synthesis upon transfer to 37 degrees C. The degree of recovery is inversely related to the duration of heat exposure and it fits cell survival quantitatively. Cells which become temporarily heat-resistant by prior heat-treatment, are able to recover translational capacity even after a very long exposure to heat (4 h at 42 degrees C). Spermine, which enhances heat-induced cell killing, does not increase the response to heat of protein, RNA and DNA synthesis. Ornithine decarboxylase (ODC, EC 4.1.1.17) activity is lost exponentially following a 20 min lag period during exposure at 42 degrees C. The half-life observed (12 min) is in agreement with the reported values of half-life of decay of ODC in other systems. It is concluded that the loss of activity is due to the shut-off of translation. The activity of ODC is recovered upon transfer to 37 degrees C. The presence of spermine during heating does not affect the loss of enzyme activity but delays its recovery by about 3 h upon transfer to 37 degrees C.
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PMID:Enhancement of thermal killing by polyamines. IV. Effects of heat and spermine on protein synthesis and ornithine decarboxylase activity. 49 61

Ornithine decarboxylase (ODC; E.C.4.1.1.17) activities can be stimulated 2-10 fold in rat epidermis and dermis by hair plucking. Stimulation does not involve the removal of a soluble ODC inhibitor. ODC activity in the dermis and whole skin decreased with aging, while the epidermis showed little change. The apparent Km for ornithine and the heat stability of ODC in plucked and unplucked skin were similar. ODC was assayed in plucked and unplucked skin of rats fed diets containing between 2 and 24% protein. Activities in both plucked and unplucked skin were higher in the animals fed diets with higher protein contents. ODC levels were positively correlated with the weight changes undergone by rats on controlled-protein diets. In animals restricted to 2% protein diets and rehabilitated with 16% protein diets, enzyme levels were increased after 2 days rehabilitation and peaked after 5 days rehabilitation. The responsiveness of ODC to changes in dietary protein may be useful in the diagnosis of protein malnutrition.
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PMID:Ornithine decarboxylase in rat skin. 64 76

1. Male weanling rats were maintained at a constant body-weight by feeding them reduced amounts of the normal diet for various periods up to 4 weeks. Control male rats were allowed free access to the normal diet and some were killed at the beginning of the experiment and others at the same ages as the experimental rats. 2. After killing by cervical dislocation the rats had their liver, quadriceps muscles and spleen removed. The tissues were weighed and the activities of the enzymes ornithine decarboxylase (ODC; EC 4.1.1.17) and S-adenosylmethionine decarboxylase (SAMD; EC 4.1.1.50) assayed in each tissue. In the liver the content of the polyamines (spermidine and spermine) and putrescine was also measured. 3. The liver and quadriceps muscles showed an over-all maintenance of weight during undernutrition, but the spleen lost weight during the first 7 d of undernutrition and then remained constant. The weight of the liver increased by approximately 50% following the daily maintenance feed, but returned to its prefeeding value by 24 h after feeding. 4. During the first 7 d of undernutrition ODC activity decreased in all three tissues, and remained fairly constant thereafter. In the liver there were marked increases in the activity of ODC during the first 4 h after the daily feed, but the activity then decreased to prefeeding values. SAMD activity tended to remain normal in the liver, decreased initially and then returned to normal in the quadriceps muscles, and remained normal initially and then decreased in the spleen. Hepatic SAMD activity showed no consistent response to the daily feed, but quadriceps SAMD activity increased significantly between 1 and 8 h after feeding. 5. Hepatic putrescine content remained constant during undernutrition whilst spermine increased slightly and was then maintained above normal for liver size. Hepatic spermidine content decreased initially and then remained constant. Putrescine increased slightly in response to the daily feed and spermidine increased considerably. Spermine content was unaffected by the daily feed. 6. It is suggested that the response of polyamine synthesis in the various tissues is primarily dependent upon the way in which nutrients are made available to the tissues. The maintenance of spermine content in the liver at the expense of spermidine may be related to differential changes in the nucleic acids.
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PMID:Polyamines and their biosynthetic decarboxylases in various tissues of the young rat during undernutrition. 88 74

Putrescine, the end-product of ornithine decarboxylase (ODC: L-ornithine carboxylyase, EC; 4.1.1.17) action, induces the synthesis of a protein(s), in L1210, neuroblastoma, and H-35 cells as well as in rat liver, which inhibits ODC activity. Spermidine and spermine, distal products of ODC activity, also induce the synthesis of a similar protein in H-35 cells. These ODC-inhibitors are heat-labile, trypsin-sensitive, and their induction is dependent upon protein synthesis. They have short half-lives which range from 18 to 66 min; these half-lives are similar to those of the ODC derived from the same source. They are noncompetitive inhibitors of ODC activity with an apparent molecular weight of 26,500. Each inhibitor crossreacts with the ODC's of the other cells and forms an enzyme-inhibitor complex which is stable during Sephadex chromatography; however, after treatment with ammonium sulfate, enzyme and inhibitor activities can be dissociated and recovered intact from the same column. We propose the name antizyme for proteins whose synthesis is induced by the proximal or distal products of the enzyme they inhibit.
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PMID:Induction of a protein inhibitor to ornithine decarboxylase by the end products of its reaction. 106 59

Ornithine decarboxylase may be a useful biomarker for risk of neoplasia in colorectal tissues. Investigators have reported enzyme activities varying by as much as 10- to 20-fold using variations of the usual 14CO2 release assay. We have examined the effect of different methodologic factors on calculated ornithine decarboxylase activity. Major effects on the assay result (greater than 20% change) were produced by: (1) use of Tris vs. phosphate buffer, the former yielding 1.5- to 4-fold greater activity; (2) protein content of the reaction mixture with significant error if less than 50 micrograms; (3) use of alpha-difluoro-methylornithine-inhibited blank versus buffer-only blank. Other changes in assay conditions, including addition of sucrose, detergent, protease inhibitors, specific activity of 14C-ornithine, the nature of the trapping agent used, and incorporation of a sonication step, did not have a significant effect on ODC quantification (less than or equal to 20%). Thus, seemingly minor variations in assay conditions can greatly affect the results, which may provide a partial explanation for the variability of ODC activities reported in the literature. Strict quality control measures are mandatory in the interpretation of clinical observations utilizing this marker as an endpoint.
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PMID:Ornithine decarboxylase assay in human colorectal mucosa. Methodologic issues of importance to quality control. 139 10

The effects of butylated hydroxyanisole (BHA), a representative phenolic antioxidant, on the activity of ornithine decarboxylase (ODC, an indicator of tumor promotion and epidermal hyperproliferation) induced by ultraviolet-B (UVB) or PUVA in mouse skin were investigated. By topical application of BHA (55 mumol), PUVA-induced ODC activity was suppressed by about 60% at both 12 h and 24 h after treatment. In contrast, BHA failed to suppress UVB-induced ODC activity in mouse skin. These results suggest that the induction of ODC activity by UVB or PUVA is mediated by different pathways.
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PMID:Effects of butylated hydroxyanisole on ornithine decarboxylase activity induced by ultraviolet-B and PUVA in mouse skin. 140 95

The influence of the anti-inflammatory drug ibuprofen on the activity of ornithine decarboxylase (ODC, EC 4.1.1.17), the key enzyme of polyamine synthesis, was studied using a 20,000 g supernatant of rat testis and regenerating liver homogenates as sources of the enzyme. Ibuprofen, in all concentrations studied (10(-6) to 2 x 10(-3) M), did not influence either testicular or hepatic ODC activity in vitro. The role of ODC in inflammatory processes and the lack of ODC inhibition by ibuprofen are discussed in view of the controversial findings of other authors.
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PMID:Lack of inhibition of ornithine decarboxylase activity by ibuprofen. 140 47


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