scholarly journals The influence of nerve section on the metabolism of polyamines in rat diaphragm muscle

1981 ◽  
Vol 196 (2) ◽  
pp. 603-610 ◽  
Author(s):  
D Hopkins ◽  
K L Manchester
Keyword(s):  
Ornithine Decarboxylase ◽  
Normal Values ◽  
Methionine Adenosyltransferase ◽  
Diaphragm Muscle ◽  
Regulatory Mechanisms ◽  
Polyamine Metabolism ◽  
Decarboxylase Activity ◽  
Rat Diaphragm ◽  
Nerve Section ◽  
Adenosylmethionine Decarboxylase

Concentrations of spermidine, spermine and putrescine have been measured in rat diaphragm muscle after unilateral nerve section. The concentration of putrescine increased approx. 10-fold 2 days after nerve section, that of spermidine about 3-fold by day 3, whereas an increase in the concentration of spermine was only observed after 7-10 days. It was not possible to show enhanced uptake of either exogenous putrescine or spermidine by the isolated tissue during the hypertrophy. Consistent with the accumulation of putrescine, activity of ornithine decarboxylase increased within 1 day of nerve section, was maximally elevated by the second day and then declined. Synthesis of spermidine from [14C]putrescine and either methionine or S-adenosylmethionine bt diaphragm cytosol rose within 1 day of nerve section, but by day 3 had returned to normal or below normal values. Activity of adenosylmethionine decarboxylase similarly increased within 1 day of nerve section, but by day 3 had declined to below normal values. Activity of methionine adenosyltransferase was elevated throughout the period studied. The concentration of S-adenosylmethionine was likewise enhanced during hypertrophy. Administration of methylglyoxal bis(guanylhydrazone) produced a marked increase in adenosylmethionine decarboxylase activity and a large increase in putrescine concentration, but did not prevent the rise in spermidine concentration produced by denervation. Possible regulatory mechanisms of polyamine metabolism consistent with the observations are discussed.

scholarly journals Effect on prostatic growth of 2-difluoromethylornithine, an effective inhibitor of ornithine decarboxylase

1982 ◽  
Vol 202 (1) ◽  
pp. 175-181 ◽  
Author(s):  
C Danzin ◽  
N Claverie ◽  
J Wagner ◽  
J Grove ◽  
J Koch-Weser
Keyword(s):  
Ornithine Decarboxylase ◽  
Ventral Prostate ◽  
Polyamine Metabolism ◽  
Decarboxylase Activity ◽  
Irreversible Inhibitor ◽  
Adult Rats ◽  
Adenosylmethionine Decarboxylase ◽  
Dna Contents ◽  
Wet Weight ◽  
Rna And Dna

2-Difluoromethylornithine (DFMO), an enzyme-activated irreversible inhibitor of ornithine decarboxylase, causes marked changes in the polyamine metabolism of ventral prostate when given to adult rats in drinking water (20 g/l) for 3 consecutive days. A 90% inhibition of ornithine decarboxylase activity is accompanied by approx. 80% decreases of the concentrations of putrescine and spermidine and by a 36% decrease in spermine. Concomitantly, S-adenosylmethionine decarboxylase activity increases 7-fold and the concentration of decarboxylated S-adenosylmethionine 450-fold. When DFMO is given to immature rats for 12 consecutive days the above described changes are accompanied by a marked reduction in the age-dependent increases of the wet weight and RNA and DNA contents of the ventral prostate. In adult rats DFMO decreases the weight and RNA content of the ventral prostate within 4 days by 32% and 24% respectively and maintains them constant for the next 19 days. After 23 days of treatment, the prostatic weight is 46% of that of control animals of the same age, whereas the weights of other organs are only slightly decreased. Cytological studies carried out at this time show that DFMO reduces the size of both prostatic acini and the epithelial cells lining the acini.

Hormonal regulation of postprandial induction of gastrointestinal ornithine decarboxylase activity

1986 ◽  
Vol 251 (4) ◽  
pp. G460-G466
Author(s):  
E. R. Seidel
Keyword(s):  
Ornithine Decarboxylase ◽  
Hormonal Regulation ◽  
Polyamine Metabolism ◽  
Decarboxylase Activity ◽  
Growth Activity ◽  
Epidermal Growth ◽  
Elemental Diets ◽  
Mucosal Growth ◽  
Glyceryl Trioleate ◽  
Fasted Rats

The growth of gastrointestinal mucosa can be related to ingestion and digestion of diet, with fasting producing mucosal hypoplasia and hyperphagia producing mucosal hyperplasia. Experiments were designed to determine whether induction of polyamine metabolism following ingestion of a meal was related to mucosal growth. Activity of the enzyme ornithine decarboxylase (ODC) in both jejunum and ileum but not in duodenum was dependent on the presence of food in the gut; ODC activity was more than 200-fold greater in mucosa of fed rats than in fasted rats. Inhibition of ODC with difluoromethylornithine lead to mucosal atrophy in ileum but not in duodenum. Refeeding of fasted rats resulted in significant induction of ODC in duodenal, ileal, and colonic, but not fundic, mucosa. In addition, two hormones, epidermal growth factor and glucagon, were effective inducers of ileal ODC activity. Direct evidence for hormonal involvement in the postprandial rise in mucosal ODC activity was provided by experiments in rats that had undergone ileal bypass surgery. After refeeding of fasted rats mucosal ODC activity was induced in both ileum left in continuity and in the bypassed segment. Refeeding of elemental diets demonstrated that ingestion of carbohydrate alone was sufficient for maximal enzyme induction. Mixed amino acids or glyceryl trioleate were no more effective inducers than nonnutritive solutions of cellulose or saccharin. These data demonstrate that hormones which are released during ingestion and digestion of a meal are the stimuli for induction of mucosal polyamine metabolism, suggesting that food-induced mucosal growth is hormonally mediated.

scholarly journals Role of pyridoxal phosphate in mammalian polyamine biosynthesis. Lack of requirement for mammalian S-adenosylmethionine decarboxylase activity

1977 ◽  
Vol 166 (1) ◽  
pp. 81-88 ◽  
Author(s):  
A E Pegg
Keyword(s):  
Ornithine Decarboxylase ◽  
Pyridoxal Phosphate ◽  
Vitamin B ◽  
Decarboxylase Activity ◽  
Deficient Diet ◽  
Polyamine Biosynthesis ◽  
Adenosylmethionine Decarboxylase ◽  
Ornithine Decarboxylase Activity

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.

Ornithine decarboxylase in rat small intestine: stimulation with food or insulin

1976 ◽  
Vol 231 (5) ◽  
pp. 1557-1561 ◽  
Author(s):  
DV Maudsley ◽  
J Leif ◽  
Y Kobayashi
Keyword(s):  
Enzyme Activity ◽  
Small Intestine ◽  
Ornithine Decarboxylase ◽  
Diamine Oxidase ◽  
Actinomycin D ◽  
Histidine Decarboxylase ◽  
Decarboxylase Activity ◽  
Adenosylmethionine Decarboxylase ◽  
Diamine Oxidase Activity ◽  
Similarities And Differences

Ornithine decarboxylase in the small intestine of starved rats was stimulated 3- to 10-fold by refeeding or administration of insulin. A peak is observed 3-5 h following treatment after which the enzyme activity rapidly declines. The rise in ornithine decarboxylase is reduced by actinomycin D or cycloheximide. The increase in enzyme activity occurs mainly in the duodenum and jejunum with less than a twofold change being observed in the ileum. A small (twofold) increase in S-adenosylmethionine decarboxylase activity in the small intestine was observed after food, but there was no change in diamine oxidase activity. Whereas pentagastrin and metiamide administration markedly stimulated histidine decarbosylase in the gastric mucosa, no consistent effect of these agents on ornithine decarboxylase in the small intestine was observed. The similarities and differences between histidine decarboxylase and ornithine decarboxylase are discussed.

Polyamine synthesis in liver and kidney of flounder in response to methylmercury

1976 ◽  
Vol 231 (2) ◽  
pp. 560-564 ◽  
Author(s):  
CA Manen ◽  
B Schmidt-Nielsen ◽  
DH Russell
Keyword(s):  
Ornithine Decarboxylase ◽  
Single Injection ◽  
Recovery Phase ◽  
Winter Flounder ◽  
Decarboxylase Activity ◽  
Pseudopleuronectes Americanus ◽  
Toxic Dose ◽  
Polyamine Synthesis ◽  
Adenosylmethionine Decarboxylase ◽  
Liver And Kidney

The effect of methylmercury administration on polyamine synthesis was studied in the liver and kidney of the winter flounder (Pseudopleuronectes americanus). A single injection of methylmercury resulted in five- and sevenfold elevations of ornithine decarboxylase activity in the liver and kidney within 15 and 45 h, respectively. There were elevations of both putrescine- and spermidine-stimulated S-adenosylmethionine decarboxylase activities (approximately 1.5-fold) in both tissues. Evaluation of the polyamine accumulation patterns in these tissues indicated that in the liver all three polyamines increased in concentration until 48 h and then decline. In the kidney, the concentration of putrescine increased steadily until it was 200% of control at 72 h and then declined. Spermidine concentration decreased throughout the time studied and was 17% of control at 1 wk. There was no significant change in the concentration of spermine throughout the period studied. The changes in the polyamine pools and in the activities of the polyamine biosynthetic enzymes after methylmercury administration are consistent with an involvement of the polyamines in the recovery phase to a toxic dose of methylmercury.

scholarly journals Response of enzymes involved in the metabolism of polyamines to phytohaemagglutinin-induced activation of human lymphocytes

1981 ◽  
Vol 196 (3) ◽  
pp. 733-738 ◽  
Author(s):  
H Korpela ◽  
E Hölttä ◽  
T Hovi ◽  
J Jänne
Keyword(s):  
Ornithine Decarboxylase ◽  
Human Lymphocytes ◽  
Lymphocyte Activation ◽  
Decarboxylase Activity ◽  
Spermidine Synthase ◽  
Irreversible Inhibitor ◽  
Adenosylmethionine Decarboxylase ◽  
Spermine Synthase ◽  
Diamine Oxidase Activity ◽  
Stimulation Of

The stimulation of lymphocyte ornithine decarboxylase and adenosylmethionine decarboxylase produced by phytohaemagglutinin was accompanied by an equally marked, but delayed, stimulation of spermidine synthase, which is not commonly considered as an inducible enzyme. In contrast with the marked stimulation of these biosynthetic enzymes, less marked changes were observed in the biodegradative enzymes of polyamines in response to phytohaemagglutinin. Diamine oxidase activity was undetectable during all stages of the transformation. The activity of polyamine oxidase remained either constant or was slightly decreased several days after addition of the mitogen. The activity of polyamine acetylase (employing all the natural polyamines as substrates) distinctly increased both in the cytosolic and crude nuclear preparations of the cells during later stages of mitogen activation. Difluoromethylornithine, an irreversible inhibitor of ornithine decarboxylase, although powerfully inhibiting ornithine decarboxylase, produced a gradual enhancement of adenosylmethionine decarboxylase activity during lymphocyte activation, without influencing the activities of the two propylamine transferases (spermidine synthase and spermine synthase).

Ileal mucosal growth during intraluminal infusion of ethylamine or putrescine

1985 ◽  
Vol 249 (4) ◽  
pp. G434-G438 ◽  
Author(s):  
E. R. Seidel ◽  
M. K. Haddox ◽  
L. R. Johnson
Keyword(s):  
Protein Content ◽  
Ornithine Decarboxylase ◽  
Serum Gastrin ◽  
Decarboxylase Activity ◽  
Ileal Mucosa ◽  
Adenosylmethionine Decarboxylase ◽  
Serum Gastrin Concentration ◽  
Catheter Tip ◽  
Mucosal Growth ◽  
Do So

Either ethylamine or the diamine putrescine was infused at the rate of 1 mumol/h for 66 h into the ileal lumen of rats. Total mucosal RNA, DNA, and protein content was greater in amine-treated rats than in rats receiving 0.9% NaCl. Growth was greatest in the mucosa surrounding the tip of the infusion catheter but was also observed 9 cm proximal and distal to the catheter tip. Infusion of these amines induced the activity of the enzymes ornithine and S-adenosylmethionine decarboxylase. Ornithine decarboxylase activity was increased 2- and 6-fold and S-adenosylmethionine decarboxylase activity 10- and 5-fold by putrescine and ethylamine, respectively. Induction of the polyamine biosynthetic enzymes was not accompanied by increases in the tissue content of polyamines. Putrescine, spermidine, and spermine content of the ileal mucosa surrounding the catheter tip was the same in 0.9% NaCl-, ethylamine-, and putrescine-treated animals. Finally, ethylamine was without effect on serum gastrin concentration in these experiments. The results suggest that amines regulate mucosal growth and may do so by modulating the activity of the enzymes involved in the synthesis of the polyamines.

INFLUENCE OF DIETARY ORNITHINE AND METHIONINE ON GROWTH, CARCASS COMPOSITION, AND POLYAMINE METABOLISM IN THE CHICK

1981 ◽  
Vol 61 (4) ◽  
pp. 1005-1012 ◽  
Author(s):  
T. K. SMITH
Keyword(s):  
Soy Protein ◽  
Control Diet ◽  
Carcass Composition ◽  
Polyamine Metabolism ◽  
Decarboxylase Activity ◽  
Chick Growth ◽  
Polyamine Synthesis ◽  
Adenosylmethionine Decarboxylase ◽  
Regulatory Enzymes ◽  
Increased Activity

Experiments were conducted to determine the effects of factorial combinations of dietary ornithine and methionine on chick growth, carcass composition, and the regulatory enzymes of polyamine synthesis. Week-old leghorn cockerel chicks were fed 12 soy protein-based semipurified diets containing 0.00, 0.50, 0.85 or 1.25% ornithine plus 0.55, 0.75 or 1.00% methionine for 2 wk. Weight gains were depressed as dietary methionine increased but only when ornithine was fed at less than 0.85%. Ornithine supplements depressed growth regardless of methionine levels. Carcass protein decreased with supplemental ornithine when methionine was fed at 0.55% but not at higher levels. Methionine supplements decreased carcass protein only in the absence of ornithine. Feeding 0.85% ornithine plus 0.55% methionine resulted in increased activity of S-adenosylmethionine decarboxylase in heart, pancreas, and muscle when compared to the control diet containing 0.00% ornithine plus 0.55% methionine. Dietary ornithine supplements lowered ornithine decarboxylase activities in heart, pancreas, and liver regardless of methionine level. It can be concluded that there is a nutritional interrelationship between ornithine and methionine as indicated by their cumulative effects on growth, carcass composition, and S-adenosylmethionine decarboxylase activity.

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