Subcellular localization of ornithine decarboxylase in liver of control and growth-hormone-treated rats

Murphy, Brian J.; Brosnan, Margaret E.

doi:10.1042/bj1570033

Cited by 44 publications

(20 citation statements)

References 27 publications

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“…Previous studies on the effect of GH on liver enzymes in intact animals have demonstrated increases in the activities of ornithine decarboxylase (22,23), alanine aminotransferase (24), and DNA polymerase (25) after the injection of a single dose of GH. In this study, the administration of a single dose of GH had no effect on liver alcohol dehydrogenase activity.…”

Section: Discussionmentioning

confidence: 99%

Rat Liver Alcohol Dehydrogenase Activity: Effects of Growth Hormone and Hypophysectomy*

Mezey

Potter

1979

Endocrinology

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Previously demonstrated increases in liver alcohol dehydrogenase in experimental uremia and after stress in the rat may be mediated by hormonal changes found in these conditions. In this study, the effects of corticosteroids, GH, adrenalectomy, and hypophysectomy on the activity of liver alcohol dehydrogenase in the rat were determined. Neither the daily administration of hydrocortisone, corticosterone, or corticotropin for 6 days nor adrenalectomy had any effect on the enzyme activity. Bovine GH, administered in doses of 0.02, 0.2, 1.0, and 4 mg/100 g BW-day for 6.5 days, resulted in increases in liver alcohol dehydrogenase. A maximum increase in the enzyme activity was found after the administration of the low dose of 0.02 mg/100 g BW-day. Plasma GH was found to be elevated in rats with increased liver alcohol dehydrogenase due to uremia or after repeated stress induced by immobilization; hence, GH may play a role in the elevation of the enzyme activity in these conditions. However, hypophysectomy was found also to increase the activity of the enzyme, and the administration of GH to the hypophysectomized animals suppressed the enhanced enzyme activity. Maximum suppression was obtained after the administration of a dose of 1.0 mg/100 g BW • day. These results indicate that liver alcohol dehydrogenase activity is affected by GH as well as by other unknown factors which are altered by hypophysectomy. (Endocrinology 104: 1667, 1979)

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Section: Discussionmentioning

confidence: 99%

Rat Liver Alcohol Dehydrogenase Activity: Effects of Growth Hormone and Hypophysectomy*

Mezey

Potter

1979

Endocrinology

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“…AOAA is an inhibitor of transaminases and at the concentration used, ornithine-2-oxo acid aminotransferase (EC 2.6.1.13) is virtually completely inhibited (14). The latter enzyme is on a pathway whereby the carboxyl group of ornithine is transformed by transamination to glutamic semialdehyde and thence to glutamate (15) mination and entry of 2-oxoglutarate into the tricarboxylic acid cycle.…”

Section: Resultsmentioning

confidence: 99%

Ornithine decarboxylase activity associated with a particulate fraction of brain

Bae

1986

Neurochem Res

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The enzymic decarboxylation of ornithine by adult rat brain largely occurs in the particulate fraction. The activity is primarily due to omithine decarboxylase (ODC) as evidenced by several criteria: i) the concurrent production of equimolar amounts of C0 2 and putrescine, ii) the sensitivity of the reaction to difluoromethylomithine (DFMO), a specific inhibitor of ODC, iii) the lack of major effect of two inhibitors of omithine-2-oxo-acid transaminase, upon the DFMO-sensitive component of decarboxylation, iv) the failure to profoundly reduce decarboxylation activity in the presence of a large excess of many aminoacids which could compete for non-specific decarboxylases. The insoluble ODC activity appears largely within synaptosomal and mitochondrial-enriched morphological fractions, yet cannot be attributed to trapped soluble ODC. Particulate ODC has a pH optimum and kinetic parameters that differ from those of soluble cerebral ODC.

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“…In some eucaryotic cells, such as normal rat liver (Murphy and Brosman, 1976;Bartholens, 1983), chick embryos (Snyder and Kreuz, 1970), and T. pyriformis (Sklaviadis et al, 1985) ODC has been found in the nucleus. In germinated barley, corn, pea and bean seeds ODC is located both in the cytosol and in the nucleus tightly bound to chromatin (Panagiotidis et al, 1982;Foudouli and Kyriakidis, 1989).…”

Section: Introductionmentioning

confidence: 98%

Ornithine decarboxylase inThermus thermophilus: An RNA-associated enzyme

Pantazaki

Liakopoulou-Kyriakides

Kyriakidis

1997

Amino Acids

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Summary.Ornithine decarboxylase (ODC) of Therrnus thermophilus is associated with the nucleoid protein fraction. Analysis of this fraction by agarose gel electrophoresis and immunostaining revealed that ODC was bound to two groups of RNA-protein complexes. These two complexes of 1.5 and 0.6kb in size disappeared from the gel by RNase A treatment or migrated to small molecular weight complexes by proteinase K treatment. Phenol extraction of either the nucleoid fraction or the eluted RNA-protein complexes from the agarose gel, shows that both contain the 0.56kb RNA. Both RNA-protein complexes contain the ODC protein (55 kDa) but their protein composition differs in at least six proteins. Extraction of the nucleoid fraction with H2SO4, indicates that ODC was present in the acid-soluble fraction, showing that it is a non-histone protein tightly bound to 0.56kb RNA. The purified ODC by various columns (-140-fold), is close to homogeneity and still carries the 0.56kb RNA further explaining all the difficulties in the purification of this enzyme.

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Subcellular localization of ornithine decarboxylase in liver of control and growth-hormone-treated rats

Cited by 44 publications

References 27 publications

Rat Liver Alcohol Dehydrogenase Activity: Effects of Growth Hormone and Hypophysectomy*

Rat Liver Alcohol Dehydrogenase Activity: Effects of Growth Hormone and Hypophysectomy*

Ornithine decarboxylase activity associated with a particulate fraction of brain

Ornithine decarboxylase inThermus thermophilus: An RNA-associated enzyme

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