Developmental Pattern of Ornithine Decarboxylase Activity, S-Adenosylmethionine Decarboxylase, and Polyamines of Rat Adrenal Glands

1. Polyamine concentrations were decreased in rats fed on a diet deficient in vitamin B-6. 2. Ornithine decarboxylase activity was decreased by vitamin B-6 deficiency when assayed in tissue extracts without addition of pyridoxal phosphate, but was greater than in control extracts when pyridoxal phosphate was present in saturating amounts. 3. In contrast, the activity of S-adenosylmethionine decarboxylase was not enhanced by pyridoxal phosphate addition even when dialysed extracts were prepared from tissues of young rats suckled by mothers fed on the vitamin B-6-deficient diet. 4. S-Adenosylmethionine decarboxylase activities were increased by administration of methylglyoxal bis(guanylhydrazone) (1,1′-[(methylethanediylidine)dinitrilo]diguanidine) to similar extents in both control and vitamin B-6-deficient animals. 5. The spectrum of highly purified liver S-adenosylmethionine decarboxylase did not indicate the presence of pyridoxal phosphate. After inactivation of the enzyme by reaction with NaB3H4, radioactivity was incorporated into the enzyme, but was not present as a reduced derivative of pyridoxal phosphate. 6. It is concluded that the decreased concentrations of polyamines in rats fed on a diet containing vitamin B-6 may be due to decreased activity or ornithine decarboxylase or may be caused by an unknown mechanism responding to growth retardation produced by the vitamin deficiency. In either case, measurements of S-adenosylmethionine decarboxylase and ornithine decarboxylase activity under optimum conditions in vitro do not correlate with the polyamine concentrations in vivo.

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Polyamines and their biosynthetic decarboxylases in various tissues of the young rat during recovery from undernutrition

Biochemical Journal ◽

10.1042/bj1620109 ◽

1977 ◽

Vol 162 (1) ◽

pp. 109-121 ◽

Cited By ~ 8

Author(s):

P A McAnulty ◽

J P G Williams

Keyword(s):

Ornithine Decarboxylase ◽

Liver Weight ◽

Female Rats ◽

Male Rats ◽

Decarboxylase Activity ◽

Adenosylmethionine Decarboxylase ◽

Ornithine Decarboxylase Activity ◽

Male And Female Rats ◽

Gastrocnemius Muscles ◽

Ad Libitum Feeding

1. Weanling male and female rats were undernourished for 4 weeks and then rehabilitated by allowing ad libitum feeding. 2. During rehabilitation polyamine-biosynthetic enzymes were examined in the liver, spleen and quadriceps and gastrocnemius muscles. 3. During the first few hours of rehabilitiation there was a marked increase in liver weight, accompanied by a very marked increase in ornithine decarboxylase activity. Increases in the activity of this enzyme in other tissues did not occur until between 2 and 7 days of rehabilitation, at which time there were further increases in enzyme activity in the liver. 4. S-Adenosylmethionine decarboxylase activity also showed marked fluctuations in activity in all the tissues examined. 5. Hepatic putrescine and spermidine concentrations also varied during rehabilitation, but permine concentration remained relatively constant. Both spermine and spermidine were at normal concentrations in the liver from the 10th days of rehabilitation onwards. 6. In all of the tissues examined there were marked sex differences in the parameters studied, particularly in splenic and muscular ornithine decarboxylase activity. 7. In the tissues of the male rats, changes in polyamine synthesis paralled changes in nucleic acid and protein synthesis.

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Differential effects of 2-difluoromethylornithine and methylglyoxal bis(guanylhydrazone) on the testosterone-induced growth of ventral prostate and seminal vesicles of castrated rats

Biochemical Journal ◽

10.1042/bj2190811 ◽

1984 ◽

Vol 219 (3) ◽

pp. 811-817 ◽

Cited By ~ 10

Author(s):

K Käpyaho ◽

A Kallio ◽

J Jänne

Keyword(s):

Seminal Vesicle ◽

Ornithine Decarboxylase ◽

Seminal Vesicles ◽

Ventral Prostate ◽

Decarboxylase Activity ◽

Adenosylmethionine Decarboxylase ◽

Ornithine Decarboxylase Activity ◽

Combined Use ◽

Sexual Glands ◽

Stimulation Of

2-Difluoromethylornithine totally prevented any increases in putrescine and spermidine concentrations in the ventral prostate of castrated rats during a 6-day testosterone treatment. Prostatic ornithine decarboxylase activity was inhibited by 80%, whereas S-adenosylmethionine decarboxylase was stimulated by more than 9-fold. In seminal vesicle, the inhibition of putrescine and spermidine accumulation, as well as of ornithine decarboxylase activity, was only minimal, and no stimulation of S-adenosylmethionine decarboxylase was observed. Administration of methylglyoxal bis(guanylhydrazone) to castrated androgen-treated rats resulted in a marked increase in concentrations of all prostatic polyamines. Prostatic ornithine decarboxylase activity was nearly 2 times and adenosylmethionine decarboxylase activity 9 times higher than that of the testosterone-treated animals. In contrast with ventral prostate, methylglyoxal bis(guanylhydrazone) treatment inhibited moderately the accumulation of spermidine and spermine in seminal vesicle, although both ornithine decarboxylase and S-adenosylmethionine decarboxylase activities were stimulated. Difluoromethylornithine inhibited significantly the weight gain of ventral prostate, but methylglyoxal bis(guanylhydrazone) produced a substantial increase in prostatic weight. These changes were largely due to the fact that the volume of prostatic secretion was greatly decreased by difluoromethylornithine, whereas methylglyoxal bis(guanylhydrazone) increased the amount of secretion. Treatment with difluoromethylornithine strikingly increased the methylglyoxal bis(guanylhydrazone) content of both ventral prostate and seminal vesicle, but even under these conditions the drug concentration remained low in comparison with other tissues. The results indicate that a combined use of these two polyamine anti-metabolites does not necessarily result in a synergistic growth inhibition of the androgen-induced growth of male accessory sexual glands.

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Polyamine and amino acid content, and activity of polyamine-synthesizing decarboxylases, in liver of streptozotocin-induced diabetic and insulin-treated diabetic rats

Biochemical Journal ◽

10.1042/bj1900395 ◽

1980 ◽

Vol 190 (2) ◽

pp. 395-403 ◽

Cited By ~ 11

Author(s):

Margaret E. Brosnan ◽

Barbara V. Roebothan ◽

Douglas E. Hall

Keyword(s):

Amino Acids ◽

Ornithine Decarboxylase ◽

Insulin Treatment ◽

Amino Acid Content ◽

Diabetic Rats ◽

Diabetic Rat ◽

Decarboxylase Activity ◽

Adenosylmethionine Decarboxylase ◽

Ornithine Decarboxylase Activity ◽

Total Dna

1. Concentrations of polyamines, amino acids, glycogen, nucleic acids and protein, and activities of ornithine decarboxylase and S-adenosylmethionine decarboxylase, were measured in livers from control, streptozotocin-diabetic and insulin-treated diabetic rats. 2. Total DNA per liver and protein per mg of DNA were unaffected by diabetes, whereas RNA per mg of DNA and glycogen per g of liver were decreased. Insulin treatment of diabetic rats induced both hypertrophy and hyperplasia, as indicated by an increase in all four of these constituents to or above control values. 3. Spermidine content was increased in the livers of diabetic rats, despite the decrease in RNA, but it was further increased by insulin treatment. Spermine content was decreased by diabetes, but was unchanged by insulin treatment. Thus the ratio spermidine/spermine in the adult diabetic rat was more typical of that seen in younger rats, whereas insulin treatment resulted in a ratio similar to that seen in rapidly growing tissues. 4. Ornithine decarboxylase activity was variable in the diabetic rat, showing a positive correlation with endogenous ornithine concentrations. This correlation was not seen in control or insulin-treated rats. Insulin caused a significant increase in ornithine decarboxylase activity relative to control or diabetic rats. 5. S-Adenosylmethionine decarboxylase activity was increased approx. 2-fold by diabetes and was not further affected by insulin. 6. Hepatic concentrations of the glucogenic amino acids, alanine, glutamine and glycine were decreased by diabetes. Their concentrations and that of glutamate were increased by injection of insulin. Concentrations of ornithine, proline, leucine, isoleucine and valine were increased in livers of diabetic rats and were decreased by insulin. Diabetes caused a decrease in hepatic concentration of serine, threonine, lysine and histidine. Insulin had no effect on serine, lysine and histidine, but caused a further fall in the concentration of threonine.

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Polyamine and ornithine metabolism during the germination of conidia of Aspergillus nidulans

Biochemical Journal ◽

10.1042/bj1580235 ◽

1976 ◽

Vol 158 (2) ◽

pp. 235-241 ◽

Cited By ~ 21

Author(s):

L Stevens ◽

I M McKinnon ◽

M Winther

Keyword(s):

Aspergillus Nidulans ◽

Ornithine Decarboxylase ◽

Growth Medium ◽

Germ Tube ◽

Decarboxylase Activity ◽

Aminotransferase Activity ◽

Adenosylmethionine Decarboxylase ◽

Ornithine Decarboxylase Activity ◽

Low Concentrations ◽

Enzyme Changes

1. The activities of ornithine decarboxylase, S-adenosylmethionine decarboxylase and ornithine-2-oxoglutarate aminotransferase were studied during the first 24 h of conidial germination in Aspergillus nidulans. 2. Increases (over 100-fold) in the activities of ornithine decarboxylase and S-adenosylmethionine decarboxylase occurred during the emergence of the germ-tube and before the doubling of DNA and this was followed by a sharp fall in the activities of both enzymes by 16h. 3. The increase in ornithine decarboxylase could be largely suppressed if 0.6 mM-putrescine was added to the growth medium. 4. Low concentrations of cycloheximide, which delayed germination by 2h, caused a corresponding delay in the changes in ornithine decarboxylase activity. 5. Ornithine-2-oxoglutarate aminotransferase activity increased steadily during the first 24h of germination. 6. Ornithine or arginine in the growth medium induced higher activity of ornithine-2-oxoglutarate aminotransferase, but did not affect ornithine decarboxylase activity. 7. The significance of these enzyme changes during germination is discussed.

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Regulation of the activity of ornithine decarboxylase and S-adenosylmethionine decarboxylase in mammary gland and liver of lactating rats. Effects of starvation, prolactin and insulin deficiency

Biochemical Journal ◽

10.1042/bj2020693 ◽

1982 ◽

Vol 202 (3) ◽

pp. 693-698 ◽

Cited By ~ 5

Author(s):

M E Brosnan ◽

V Ilic ◽

D H Williamson

Keyword(s):

Mammary Gland ◽

Ornithine Decarboxylase ◽

Milk Production ◽

Marked Decrease ◽

Decarboxylase Activity ◽

Insulin Deficiency ◽

Fed State ◽

Simultaneous Injection ◽

Adenosylmethionine Decarboxylase ◽

Ornithine Decarboxylase Activity

1. Starvation caused a marked decrease in the activity of ornithine decarboxylase in mammary gland, together with a lesser decrease in the activity of S-adenosylmethionine decarboxylase and a marked fall in milk production. Liver ornithine decarboxylase and S-adenosylmethionine decarboxylase activities were unaffected. 2. Refeeding for 2.5 h was without effect on ornithine decarboxylase in mammary gland, but it returned the S-adenosylmethionine decarboxylase activity in mammary gland to control values and elevated both ornithine decarboxylase and S-adenosylmethionine decarboxylase in liver. 3. Refeeding for 5 h returned the activity of ornithine decarboxylase in mammary gland to fed-state values and resulted in further increases in S-adenosylmethionine decarboxylase in mammary gland and liver and in ornithine decarboxylase in liver. 4. Prolactin deficiency in fed rats resulted in decreased milk production and decreased activity of ornithine decarboxylase in mammary gland. The increase in ornithine decarboxylase activity normally seen after refeeding starved rats for 5 h was completely blocked by prolactin deficiency. 5. In fed rats, injection of streptozotocin 2.5 h before death caused a decrease in the activities of ornithine decarboxylase and S-adenosylmethionine decarboxylase in mammary gland, which could be reversed by simultaneous injection of insulin. Insulin deficiency also prevented the increase in S-adenosylmethionine decarboxylase in liver and mammary gland normally observed after refeeding starved rats for 2.5 h.

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PPAR-γ ligands induce G1 cell cycle arrest and reduce ornithine decarboxylase activity of human Barrett's adenocarcinoma cells

Gastroenterology ◽

10.1016/s0016-5085(01)82062-x ◽

2001 ◽

Vol 120 (5) ◽

pp. A415-A415

Author(s):

T TAKASHIMA ◽

Y FUJIWARA ◽

K HIGUCHI ◽

T ARAKAWA ◽

Y YANO ◽

...

Keyword(s):

Cell Cycle ◽

Cell Cycle Arrest ◽

Ornithine Decarboxylase ◽

Decarboxylase Activity ◽

Ornithine Decarboxylase Activity ◽

Ppar Γ ◽

Cycle Arrest ◽

Adenocarcinoma Cells ◽

Barrett’S Adenocarcinoma ◽

G1 Cell Cycle Arrest

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Ornithine Decarboxylase Activity in Cultured Endothelial Cells Stimulated by Serum, Thrombin and Serotonin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1646709 ◽

1978 ◽

Vol 39 (02) ◽

pp. 496-503 ◽

Cited By ~ 8

Author(s):

P A D’Amore ◽

H B Hechtman ◽

D Shepro

Keyword(s):

Endothelial Cells ◽

Ornithine Decarboxylase ◽

Decarboxylase Activity ◽

Aortic Endothelial Cells ◽

Ornithine Decarboxylase Activity ◽

Rate Limiting Step ◽

Bovine Aortic Endothelial Cells ◽

Limiting Step ◽

Rate Limiting ◽

Serum Serotonin

SummaryOrnithine decarboxylase (ODC) activity, the rate-limiting step in the synthesis of polyamines, can be demonstrated in cultured, bovine, aortic endothelial cells (EC). Serum, serotonin and thrombin produce a rise in ODC activity. The serotonin-induced ODC activity is significantly blocked by imipramine (10-5 M) or Lilly 11 0140 (10-6M). Preincubation of EC with these blockers together almost completely depresses the 5-HT-stimulated ODC activity. These observations suggest a manner by which platelets may maintain EC structural and metabolic soundness.

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