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)

The time required to induce two inducible hepatic enzymes, ornithine decarboxylase (ODC) and tyrosine aminotransferase (TAT), by growth hormone and dexamethasone, respectively, increases with age. Specific activity at the peak of induction is the same for all ages. On the other hand, for basal TAT the specific activity per unit of TAT antigen was found to decrease considerably with age. The half-life of ODC was determined after cycloheximide administration. The apparent half-life at the peak of ODC induction increases from 15 minutes in 3-4-month-old mice to 30 minutes in 24-month-old animals. Loss of efficiency in the protein degradation system is implicated in this phenomenon as no apparent differences could be observed in the susceptibility of ODC and TAT from young or old mice to chymotrypsin. ODC and TAT are activated by temperatures of up to 37 degrees C and 50 degrees C, respectively. ODC is inactivated at 50 degrees C while TAT is inactivated at 76 degrees C. "Young" ODC and TAT are more readily activated or inactivated by heating than the "old" enzymes.
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PMID:Age-related changes in inducible mouse liver enzymes: ornithine decarboxylase and tyrosine aminotransferase. 610 55

The effect of ethanol on the activity of ornithine decarboxylase (ODC), tyrosine aminotransferase (TAT), alanine aminotransferase (ALAT) and lactate dehydrogenase (LD), as well as on protein concentration, was studied in regenerating rat liver after partial hepatectomy. It was found that administration of an ethanol-containing liquid diet for 5 days after partial hepatectomy caused a significant accumulation of proteins in the liver. The activities of ODC and TAT were stimulated by ethanol treatment in the beginning of the regeneration. In control livers, partial hepatectomy decreased the activity of ALAT, but ethanol prevented this decrease. No differences in the activity of LD was found between ethanol and control groups after partial hepatectomy. When the half-lives of ODC and TAT were measured 24 hr after partial hepatectomy by using cycloheximide, it appeared that ethanol caused a significant stabilization of both enzymes. It is concluded that ethanol caused inhibition of degradation of ODC and TAT and it is suggested that this could be a general phenomenon, and could markedly contribute to the pathological accumulation of proteins in the liver after chronic ethanol consumption.
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PMID:Inhibition of protein degradation in regenerating rat liver by ethanol treatment. 611 5

Vitamin B6 metabolism has been investigated in several highly and well-differentiated Morris hepatomas. Comparisons have been made with two poorly differentiated Morris hepatomas, with host livers obtained from tumor-bearing animals, and with fetal, neonatal, and adult rat liver. The pyridoxal phosphate content and the activities of pyridoxine kinase and pyridoxine phosphate oxidase of all Morris hepatomas examined were significantly less than those in adult host or control livers and generally fell in the range determined for fetal and neonatal liver. A similar pattern was not evident for the activity of pyridoxine phosphate phosphatase. Relative to control and host livers, the activity in hepatomas of the pyridoxal phosphate (PLP)-dependent enzyme, ornithine decarboxylase, was generally elevated. Dexamethasone, at a dose which caused an elevation in the activity of PLP-dependent tumor tyrosine aminotransferase, had no effect on PLP metabolism. The data indicate that tumor progression in the Morris hepatoma spectrum in relation to vitamin b6 metabolism falls into an onco-developmental pattern characterized by a diminished amount of tissue PLP and a diminished capability to metabolize precursor vitamer forms to PLP.
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PMID:Vitamin B6 metabolism in liver and liver-derived tumors. 612 59

Dietary induction of ornithine decarboxylase (ODC) in rat liver depended on the quality of protein in the diet. Zein did not induce ODC unless it was supplemented with the deficient amino acids, tryptophan and lysine. Similar phenomena were observed with gelatin (tryptophan and methionine) and hemoglobin (isoleucine). However, ODC was found to be significantly induced by an amino acid mixture simulating zein. The difference between amino acid diet and protein diet effects could not be explained by digestibility of zein. Unphysiologically rapid influx of amino acids appeared to induce ODC by a mechanism different from that by which dietary protein induced ODC. After ingestion of zein, the concentration of tryptophan and lysine decreased markedly in plasma and liver. However, it was confirmed that their supply from intracellular protein degradation continued even after feeding. In contrast to ODC, tyrosine aminotransferase was induced by zein as well as by casein, indicating that the requirement of tryptophan and lysine as precursor amino acids for enzyme synthesis was satisfied by reutilization of the amino acids liberated by intracellular protein degradation. Therefore, it was concluded that good quality protein was required for ODC induction mainly as a signal but not as a source of precursor amino acids.
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PMID:Effect of protein quality on dietary induction of hepatic ornithine decarboxylase. 613 24

The effect of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) on [3H]thymidine incorporation into hepatic DNA was studied in rats. In non-hepatectomized male and female animals, incorporation measured at the peak of the first round of liver DNA synthesis after TCDD treatment (10 micrograms/kg) was similar to that of control animals. In contrast, the first round of [3H]thymidine incorporation after a 1/3 hepatectomy was enhanced 3-fold in TCDD-treated rats. The enhanced response to 1/3 hepatectomy was produced by doses of TCDD ranging from 1 to 30 micrograms/kg with an apparent ED50 of 5 micrograms/kg. Enhanced incorporation was observed when the 1/3 hepatectomy was performed 5-10 days after an ED50 dose and it returned to the control level after 20 days. This enhanced response was not preceded by changes in food consumption or hepatic activities of ornithine decarboxylase (ODC), tyrosine aminotransferase (TAT) or gamma glutamyl transpeptidase (GGT) when compared to respective control values. Also, the enhanced incorporation was not necessarily due to removal of 1/3 of the liver because it was also seen in TCDD-treated rats that were laparotomized. The mechanism of enhancement in laparotomized animals does not appear to involve a diminished response of the liver to the inhibitory effects of adrenal hormones on liver DNA synthesis. This was suggested by the finding that an adrenalectomy prior to the laparotomy did not block the enhanced incorporation of [3H]thymidine into hepatic DNA. The mechanism by which TCDD enhances the first round of liver DNA synthesis after a 1/3 hepatectomy or laparotomy remains to be determined.
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PMID:Effects of 2,3,7,8-tetrachlorodibenzo-p-dioxin on [3H]thymidine incorporation into rat liver deoxyribonucleic acid. 613 85

Rats having a protein-free diet available ad libitum were fed a daily casein meal at the beginning of either the light- or the dark-phase of the day. A control group received a mixed-diet ad libitum. In all three groups, daily food ingestion was the same and casein corresponded to 12% of total intake. Liver activities of alanine, aspartate, ornithine and tyrosine aminotransferase, ornithine decarboxylase and serine dehydratase were assessed. In mixed-fed controls, all activities were low. Tyrosine aminotransferase and ornithine decarboxylase exhibited clear circadian rhythms of low amplitude. Feeding casein as a concentrated meal had no effect on aspartate aminotransferase. It depressed alanine aminotransferase and serine dehydratase activities. Tyrosine aminotransferase and ornithine decarboxylase exhibited rapid and strong stimulatory responses but, within 12 hours, returned to levels similar to those observed in mixed-fed controls. Ornithine aminotransferase was increased in the group receiving the casein meal during the light phase. It is concluded that the capacity for amino acid catabolism remains low in separately-fed animals, and that only tyrosine and especially ornithine, which may become limiting for urea synthesis, are actively metabolized. Thus, when high fluxes of amino acids reach the liver following the absorption of the casein meal, more amino acids are available for incorporation into newly synthesized proteins.
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PMID:Activity of several enzymes of amino acid catabolism in the liver of rats fed protein as a meal. 613 52

IP injection in rats of 2-acetylaminofluorene (AAF) or N-hydroxy-2-acetylaminofluorene (N-OH-AAF) resulted in a transient increase of hepatic ornithine decarboxylase (ODC) and tyrosine aminotransferase (TAT) activity. Maximal activity of ODC was observed 4 hr and of TAT 3 hr after administration of either AAF or N-OH-AAF. A lag-time of 2 hr preceded the increase of ODC and TAT activity. N-OH-AAF dependent ODC induction displayed an almost linear dose-response in the dose range up to 94.1 mumol/kg bw (body weight) when the ODC activity was measured at its maximum 4 hr after administration. Elevation of the dose N-OH-AAF to 126 mol/kg bw resulted in a lower ODC induction. Administration of doses AAF to 31.4 mumol did not change ODC activity. At doses up to 126 mumol/kg bw ODC induction increased linear. TAT induction increased linear in the dose range 15.7-94.1 mumol N-OH-AAF and 31.4-94.1 mumol AAF/kg. Lowering the dose of AAF did not result in a lower ODC or TAT activity. Judged by the effects of actinomycin D or cycloheximide administered 1 hr prior to AAF or N-OH-AAF, the in vivo induction of rat liver ODC activity by AAF and N-OH-AAF appeared to be under transcriptional control, whereas augmentation of TAT activity under influence of AAF or N-OH-AAF appeared the result of (post) translational events. Induction of ODC by AAF or N-OH-AAF was not significantly changed by indomethacin, was slightly increased by pentachlorophenol (PCP) and was synergistically enhanced by retinylacetate (RA). The increase of TAT activity was stimulated by PCP and RA. The effect of PCP indicates that N-sulfonoxy-2-acetylaminofluorene is most probably not involved in the induction of ODC. AAF appeared more effective hepatic ODC inducer in females than males and moreover more effective than N-OH-AAF in females. N-OH-AAF had stronger ODC inducing capacity in males than females. Similar observations were made with respect to TAT activity. When induction of ODC is indicative for a tumor promoting property then the data presented here suggest that tumor promotion of the complete carcinogens AAF and N-OH-AAF is not mediated by N-O-sulfation; this might be due to other metabolic conversions.
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PMID:Induction of ornithine decarboxylase and augmentation of tyrosine aminotransferase activity by N-hydroxy-2-acetylaminofluorene and 2-acetylaminofluorene in rat liver. Influence of sex, retinylacetate, indomethacin, and pentachlorophenol. 614 83

Rats given an LD50 dose of Be2+ showed reduced activities of ornithine decarboxylase and tyrosine aminotransferase in liver in response to dexamethasone induction. Control fed animals showed 'superinduction'. Be2+ also inhibited the uptake of [3H]orotic acid into rapidly labelled RNA of ribonucleoprotein particles extracted from liver nuclei in isomolar solutions at pH 8.0. Consistent with inhibition of cytoplasmic protein kinase reported previously (Kaser et al., 1980), the uptake of [32P]Pi into proteins in the ribonucleoprotein particles was also diminished.
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PMID:Enzyme induction in rat liver: the effects of Be2+ in vivo. 617 Mar 54

Liver ornithine decarboxylase (ODC) and tyrosine aminotransferase (TAT) activities were assessed at 2200 h (prandial phase) and at 1000 h (postprandial phase) in virgin and in pregnant (day 13-20) rats fed on different levels of casein and carbohydrate. In virgin rats, ODC levels were higher at 2200 h after resumption of eating than at 1000 hours, the inductive effect being greater with the high-casein than with the low-casein diet. Rapid deinduction followed termination of eating, resulting in equally low enzyme levels at 1000 h with both diets. On the contrary, prandial and postprandial levels of TAT were always greater with the high-protein diet. In pregnant rats, there was a progressive stimulation of ODC that reached a maximum on day 19. However, the inductive capacity of the high-protein diet was lower than that of the low-casein diet. Prandial rest was not followed by enzyme deinduction at 1000 h. In contrast, TAT stimulation remained dependent on overall casein ingestion. At constant casein but restricted carbohydrate intake, pregnant females exhibited a reduction in ODC stimulation. Thus, whereas in virgin females proteins are determinant in the regulation of ODC, during pregnancy there determinant in the regulation of ODC, during pregnancy there is a shift toward modulation by carbohydrates. Levels of liver urea and ornithine were found to vary in inverse proportion with the magnitude of ODC stimulation.
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PMID:Liver ornithine decarboxylase in pregnant rats fed two levels of casein. 619 Apr 8

Previously we reported that intermittent intraperitoneal administration of ornithine decarboxylase-inducing factor (ODC factor), interleukin 1alpha (IL-1alpha), and tumor-necrosis factor-alpha (TNF-alpha) to normal mice induced biological changes in the hosts which included changes in the pattern of expression of pyruvate kinase (PK) isozymes in the liver and hypertrophy of the spleen. In the study reported here, we investigated the chronic and combined effects of these factors on hepatic enzymes using alzet microosmotic pumps implanted in the subcutis of the backs or abdominal cavities of mice. Continuous administration of ODC factor and recombinant human IL-1alpha (rhIL-1alpha) reduced the activity of L-type PK, which is a glycolysis-related enzyme in the liver, and induced the activity of M2-type PK, a known marker of liver dedifferentiation. Serine dehydratase (SDH) and tyrosine aminotransferase (TAT), enzymes associated with amino acid metabolism, were not significantly influenced at the examined concentration. The simultaneous continuous infusion of ODC factor and rhIL-1alpha or rhTNF-alpha caused alterations in the patterns of expression of PK isozyme activity profiles and reduced overall PK activity. SDH and TAT activities were also significantly induced. Moreover, mice treated with these combined factors displayed many other metabolic changes normally associated with cancer cachexia. These findings suggest that the tumor-derived ODC factor and cytokines such as IL-1alpha and TNF-alpha might function synergistically in the metabolic perturbations observed in Ehrlich ascites tumor bearers.
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PMID:Mechanisms mediating metabolic abnormalities in the livers of Ehrlich ascites tumor-bearing mice. 1266 85


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