In vitro inactivation of ornithine decarboxylase by a heat‐labile factor from rat ventral prostate

Icekson, Isaac; Kaye, Alvin M.

doi:10.1016/0014-5793(76)80170-6

Cited by 14 publications

(6 citation statements)

References 19 publications

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“…This study firmly demonstrated the presence of a small amount of antizyme and ODC-antizyme complex in liver cytosols of starved rats. Great care should be taken before identifying an ODC inhibitor as antizyme, since ODC activity could be affected by various macromolecular inhibitors, such as proteinases, phosphatases and ODC-in-activating factor (Icekson & Kaye, 1976), as well as by several low-molecular-weight compounds such as NaCl and KCI (Obenrader & Prouty, 1977), ornithine and arginine, which may be easily converted into ornithine in liver extracts . In the present study the identification was based on the following evidence.…”

Section: Discussionmentioning

confidence: 99%

Antizyme to ornithine decarboxylase is present in the liver of starved rats

Fujita¹,

Matsufuji²,

Murakami³

et al. 1984

Biochemical Journal

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Antizyme to ornithine decarboxylase (ODC) and ODC-antizyme complex were both present in liver cytosols of starved rats. The antizyme was identified by its molecular weight, kinetic properties, formation of a complex with ODC, and reversal of its inhibition by antizyme inhibitor. The average amount of antizyme in liver cytosols of starved rats was 0.1 unit/mg of protein, roughly corresponding to basal hepatic ODC activity in rats fed ad libitum. The presence of ODC-antizyme complex was detected by using antizyme inhibitor. These results indicate that antizyme participates in the regulation of ODC activity in vivo under physiological conditions.

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Section: Discussionmentioning

confidence: 99%

Antizyme to ornithine decarboxylase is present in the liver of starved rats

Fujita¹,

Matsufuji²,

Murakami³

et al. 1984

Biochemical Journal

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“…The selective proteolytic machinery, however, appears to be more fragile than the protein synthesis system, and establishment of a cell-free ODC degradation system took a long time. Although several in vitro ODC inactivation systems have been reported, these are probably not related to physiological ODC degradation in cells [90][91][92]. Several years ago, Kahana and co-workers developed an in vitro ODC degradation system [93].…”

Section: In Vitro Odc Degradation Systemsmentioning

confidence: 99%

Rapid and regulated degradation of ornithine decarboxylase

Hayashi

Murakami

1995

Biochemical Journal

194

131

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“…Assay ofornithine decarboxylase activity Ornithine decarboxylase activity was measured by a modified version of the method described previously (Kaye et al, 1973;Icekson & Kaye, 1976). The reaction mixture (final volume 100,l) consisted of an enzyme preparation (0.04-1.Omg of protein), 0.5 mM-DL-[l1-'4Clornithine, 0.05 mM-pyridoxal 5'-phosphate and 5 mM-dithiothreitol in 50mM-Tris/HCl buffer, pH 7.8.…”

Section: Effects Of Cholecalciferol and Its Metabolites On Ornithine mentioning

confidence: 99%

The effects of 24R,25-dihydroxycholecalciferol and of 1 α,25-dihydroxycholecalciferol on ornithine decarboxylase activity and on DNA synthesis in the epiphysis and diaphysis of rat bone and in the duodenum

Sömjen¹,

Binderman²,

Weisman³

1983

Biochemical Journal

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The effect of cholecalciferol metabolites on ornithine decarboxylase activity and on DNA synthesis in developing long bones was investigated in vitamin D-depleted rats. In the epiphysis there was a 6.4-fold increase in ornithine decarboxylase activity 5 h after a single injection of 24R,25-dihydroxycholecalciferol but not of 24S,25-dihydroxycholecalciferol or other vitamin D metabolites. In comparison, in the diaphysis and duodenum, 1 alpha,25-dihydroxycholecalciferol, but not other vitamin D metabolites, caused a 3-3.5-fold increase in the enzyme activity. The enzyme activity in the tissues examined attained a maximal value at 5 h after the injection of the metabolites. The activity of ornithine decarboxylase in the epiphysial region increased dose-dependently as the result of a single injection of 24R,25-dihydroxycholecalciferol and attained a maximal value at a dose between 30 and 3000 ng. In addition, administration of 24R,25-dihydroxycholecalciferol, but not 24S,25-dihydroxycholecalciferol or other metabolites, caused within 24 h a 1.7-2.0-fold increase in [3H]thymidine incorporation into DNA of the epiphyses of tibial bones. In comparison, 1 alpha,25-dihydroxycholecalciferol caused a 1.5-fold increase in [3H]thymidine incorporation into DNA of the diaphyses and of the duodenum. The present data indicate that 24R,25-dihydroxycholecalciferol is involved in the regulation of epiphyseal growth, whereas 1 alpha,25,dihydroxycholecalciferol stimulates the proliferation of cells in the diaphysis of long bones and in the intestinal mucosa.

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In vitro inactivation of ornithine decarboxylase by a heat‐labile factor from rat ventral prostate

Cited by 14 publications

References 19 publications

Antizyme to ornithine decarboxylase is present in the liver of starved rats

Antizyme to ornithine decarboxylase is present in the liver of starved rats

Rapid and regulated degradation of ornithine decarboxylase

The effects of 24R,25-dihydroxycholecalciferol and of 1 α,25-dihydroxycholecalciferol on ornithine decarboxylase activity and on DNA synthesis in the epiphysis and diaphysis of rat bone and in the duodenum

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