Regulations of thyroid decarboxylase by the polyamines Induction of a protein inhibitor of ornithine decarboxylase by the end-products of the reaction

Friedman, Yochanan; Park, S.; Levasseur, Steven; Burke, Gerald

doi:10.1016/0304-4165(77)90021-6

Cited by 31 publications

(13 citation statements)

References 17 publications

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“…Several of these individual results have been confirmed and extended by other laboratories (McCann et al, 1977;Friedman et al, 1977;Jefferson and Pegg, 1977;Poso et al, 1978;Kallio et al, 1979). McCann et al, (1977) have also demonstrated the in vivo existence of the "ODC-antizyme" complex in HTC cells.…”

supporting

confidence: 58%

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Cellular control of ornithine decarboxylase activity by its antizyme

Heller

Canellakis

1981

Journal Cellular Physiology

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Conditions have been established under which the antizyme of ornithine decarboxylase (E.C. 4.1.1.17, L-ornithine carboxy-lyase, ODC) a non-competitive protein inhibitor of ODC, can be detected in cells in response to as little as 10(-7) M putrescine. The maintenance of intracellular antizyme activity depends upon the continued presence of putrescine in the medium. Removal of putrescine results in a rapid decline of antizyme activity. These phenomena are unaffected by the presence of cycloheximide and are comparable to the requirement of L-asparagine for the maintenance of ODC activity. The extent to which the antizyme level is increased is inversely related to the preexisting level of intracellular ODC at the time of addition of putrescine. The time of appearance of free antizyme is delayed in cells that have high levels of ODC; the amount of free antizyme that can be assayed for in these cells, at any particular time is correspondingly less. The converse is also true. In cells that have high levels of antizyme, the delay in appearance of ODC is greater and the amount of ODC that can be assayed for is correspondingly less than in cells with low levels of antizyme. These experiments, as well as others, indicate that the ODC antizyme and ODC interact in vivo with each other to modify their respective activities.

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confidence: 58%

“…All other details are as described in Figure 1 and Methods. tained in growth media , as well as in bovine thyroid slices maintained in salts-glucose solution (Friedman et al, 1977).…”

Section: The Effect Of Putrescine On the Appearance Of Antizymementioning

confidence: 99%

Cellular control of ornithine decarboxylase activity by its antizyme

Heller

Canellakis

1981

Journal Cellular Physiology

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“…The production of antizyme can be induced in different experimental conditions by introducing pol yamines or diamines into a system where ODC activity is first stimulated, as in mouse leukemia, neuroblastoma, and H-35 cells, in dexamethasone acetate-treated rat liver , HTC-cell extract (McCann et al, 1977), and in thyroid (Friedman et al, 1977). In 3T3 cells (Clark and Fuller, 1976) and in regenerating rat liver (Kallio et al, 1977c), corresponding experimental arrangements did not result in antizyme production, suggesting that it may be limited to certain physiological conditions or cell types.…”

Section: Detection Of Ornithine Decarboxylase Antizyme In Mouse Brainmentioning

confidence: 99%

Detection of Ornithine Decarboxylase Antizyme in Mouse Brain

Hietala¹

1983

Journal of Neurochemistry

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Ornithine decarboxylase, the rate-limiting enzyme in polyamine synthesis, is known to be regulated by a macromolecular inhibitor, termed antizyme, in a number of cellular systems. The present results show that the antizyme is also a functional component of polyamine metabolism in the brain. It could be demonstrated both in normal randomly selected mice and in animals which had been subjected either to intracerebroventricular injection of saline, which is known to cause a transient activation of ornithine decarboxylase, or to 1,3-diamino-2-propanol, an antizyme-inducing agent. When compared to tissues or cell systems studied so far, the cytosol fraction from mouse brain homogenate appeared to contain an exceptionally high amount of antizyme, that was bound to some material other than active ornithine decarboxylase. This feature was seen in all the animal groups studied, being most prominent after saline injection, when the amount of dissociable antizyme exceeded 14-fold the corresponding released ornithine decarboxylase activity. In untreated animals the excess was about eightfold and after 1,3-diamino-2-propanol about fivefold.

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“…Diamines such as diaminopropane, putrescine and cadaverine decrease ODC activity very rapidly in the tissues and cells (Hayashi & Murakami 1995). Diaminopropane, which is reported to act as an antigoitrogenic agent by suppressing polyamine biosynthesis in the thyroid (Friedman et al 1977), did not suppress PTU-induced ODC activity. This discrep¬ ancy can be explained by the fact that diaminopropane had not accumulated in the thyroid within 1 h after its injection.…”

Section: Discussionmentioning

confidence: 95%

Acute inhibitory effect of excess iodide on ornithine decarboxylase in the thyroid of propylthiouracil-treated rats

H.T.

Reuse²,

Koibuchi³

et al. 1996

Journal of Endocrinology

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Polyamines such as putrescine, spermidine and spermine have been thought to play an important role in thyroid growth induced by goitrogens. Reduced biosynthesis of these polyamines might play a role in the antigoitrogenic effects of excess iodide. This study was designed to examine the effect of potassium iodide (KI) on ornithine decarboxylase (ODC), a rate-limiting enzyme in the biosynthesis of polyamines. Thyroidal ODC activity, protein content and mRNA were increased in rats made hypothyroid by 10 days of propylthiouracil treatment. The increase in ODC activity was suppressed after subcutaneous injection of KI (13mg/kg body weight); the apparent half-life of ODC activity after the treatment was estimated to be 19 min and the maximum suppression (90%) was seen 60 min after the treatment. On the other hand, administration of iodine-containing compounds including L-thyroxine, L-di-iodotyrosine,amiodarone, iopanoic acid and erythrosine showed no significant effect on ODC activity. The inhibitory effect of excess iodide was not reversed by pretreatment with dibutyryl cAMP and theophylline. The amount of immunoreactive ODC protein was reduced by iodide treatment (40%). However, the decrease was not as great as the decrease in ODC activity (90%). No significant change in thyroidal ODC mRNA content was seen 1 and 3 h following KI treatment. These results suggest that excess iodide reduces ODC activity in the rat thyroid gland by a post-transcriptional mechanism.

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Regulations of thyroid decarboxylase by the polyamines Induction of a protein inhibitor of ornithine decarboxylase by the end-products of the reaction

Cited by 31 publications

References 17 publications

Cellular control of ornithine decarboxylase activity by its antizyme

Cellular control of ornithine decarboxylase activity by its antizyme

Detection of Ornithine Decarboxylase Antizyme in Mouse Brain

Acute inhibitory effect of excess iodide on ornithine decarboxylase in the thyroid of propylthiouracil-treated rats

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