ODCp, a brain- and testis-specific ornithine decarboxylase paralogue, functions as an antizyme inhibitor, although less efficiently than AzI1

2008 ◽  
Vol 410 (3) ◽  
pp. 613-619 ◽  
Author(s):  
Zohar Snapir ◽  
Alona Keren-Paz ◽  
Zippi Bercovich ◽  
Chaim Kahana
Keyword(s):  
Ornithine Decarboxylase ◽  
Antizyme Inhibitor

scholarly journals A macromolecular inhibitor of the antizyme to ornithine decarboxylase

1982 ◽  
Vol 204 (3) ◽  
pp. 647-652 ◽  
Author(s):  
K Fujita ◽  
Y Murakami ◽  
S Hayashi
Keyword(s):  
Ornithine Decarboxylase ◽  
Rat Liver ◽  
Molecular Size ◽  
Antizyme Inhibitor ◽  
Heat Labile

A macromolecular factor that inhibits the activity of the antizyme to ornithine decarboxylase (ODC) was found in rat liver extracts. The factor, ‘antizyme inhibitor’, was heat-labile, non diffusable and of similar molecular size to ODC. The antizyme inhibitor re-activated ODC that had been inactivated by antizyme, apparently by replacing ODC in a complex with antizyme. Therefore the antizyme inhibitor can be used to assay the amount of inactive ODC-antizyme complex formed in vitro. When assayed by this method, the complex was shown to be eluted before ODC from a Sephadex G-100 column. Significant increase in ODC activity was observed when the antizyme inhibitor was added to crude liver extracts from rats that had been injected with 1,3-diaminopropane to cause decay of ODC activity, suggesting the presence of inactive ODC-antizyme complex in the extracts.

scholarly journals Mouse Ornithine Decarboxylase-like Gene Encodes an Antizyme Inhibitor Devoid of Ornithine and Arginine Decarboxylating Activity

2006 ◽  
Vol 281 (41) ◽  
pp. 30896-30906 ◽  
Author(s):  
Andrés J. López-Contreras ◽  
Carlos López-Garcia ◽  
Celia Jiménez-Cervantes ◽  
Asunción Cremades ◽  
Rafael Peñafiel
Keyword(s):  
Ornithine Decarboxylase ◽  
Antizyme Inhibitor

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

1984 ◽  
Vol 218 (2) ◽  
pp. 557-562 ◽  
Author(s):  
K Fujita ◽  
S Matsufuji ◽  
Y Murakami ◽  
S Hayashi
Keyword(s):  
Molecular Weight ◽  
Ornithine Decarboxylase ◽  
Kinetic Properties ◽  
Average Amount ◽  
Physiological Conditions ◽  
Antizyme Inhibitor ◽  
Ad Libitum

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.

scholarly journals Structural and degradative aspects of ornithine decarboxylase antizyme inhibitor 2

FEBS Open Bio ◽  
2014 ◽  
Vol 4 (1) ◽  
pp. 510-521 ◽  
Author(s):  
Bruno Ramos-Molina ◽  
Ana Lambertos ◽  
Andrés J. Lopez-Contreras ◽  
Joanna M. Kasprzak ◽  
Anna Czerwoniec ◽  
...  
Keyword(s):  
Ornithine Decarboxylase ◽  
Antizyme Inhibitor ◽  
Antizyme Inhibitor 2

scholarly journals Cloning of Antizyme Inhibitor, a Highly Homologous Protein to Ornithine Decarboxylase

1996 ◽  
Vol 271 (7) ◽  
pp. 3340-3342 ◽  
Author(s):  
Yasuko Murakami ◽  
Tamotsu Ichiba ◽  
Senya Matsufuji ◽  
Shin-ichi Hayashi
Keyword(s):  
Ornithine Decarboxylase ◽  
Homologous Protein ◽  
Antizyme Inhibitor

Antizyme inhibitor: a defective ornithine decarboxylase or a physiological regulator of polyamine biosynthesis and cellular proliferation

2007 ◽  
Vol 35 (2) ◽  
pp. 311-313 ◽  
Author(s):  
A. Keren-Paz ◽  
Z. Bercovich ◽  
C. Kahana
Keyword(s):  
Ornithine Decarboxylase ◽  
Cellular Proliferation ◽  
Cellular Transformation ◽  
Polyamine Biosynthesis ◽  
Polyamine Synthesis ◽  
Homologous Protein ◽  
Antizyme Inhibitor ◽  
Physiological Regulator ◽  
Growth Promoting

ODC (ornithine decarboxylase) is a central regulator of cellular polyamine synthesis. ODC is a highly regulated enzyme stimulated by a variety of growth-promoting stimuli. ODC overexpression leads to cellular transformation. Cellular ODC levels are determined at transcriptional and translational levels and by regulation of its degradation. Here we review the mechanism of ODC degradation with particular emphasis on AzI (antizyme inhibitor), an ODC homologous protein that appears as a central regulator of ODC stability, cellular polyamine homoeostasis and cellular proliferation.

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