Cellular control of ornithine decarboxylase activity by its antizyme

Heller, J; Canellakis, E.S.

doi:10.1002/jcp.1041070206

Cited by 72 publications

(40 citation statements)

References 30 publications

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“…A similar role for antizyme in the regulation of polyamine biosynthesis in eukaryotic cells has been indicated by the inverse relationship that we have found to exist between the activity of ornithine decarboxylase and antizyme in neuroblastoma cells; enhancement of the activity of one leads to the decrease in the activity of the other (18).…”

Section: Resultssupporting

confidence: 79%

“…The concentration of substrate used in the enzyme assays and the reference describing the assay are indicated after each enzyme: biosynthetic ornithine decarboxylase (0.55 mM) (18); biosynthetic arginine decarboxylase (0.075 mM) (3); biodegradative ornithine decarboxylase (0.55 mM) (19); biodegradative arginine decarboxylase (0.075 mM) (16); lysine decarboxylase (0.4 mM) (20); and S-adenosylmethionine decarboxylase (0.022 mM) (17).…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Regulation of polyamine biosynthesis in Escherichia coli by basic proteins.

Heller¹,

Rostomily²,

Kyriakidis³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

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Section: Resultssupporting

confidence: 79%

Section: Methodsmentioning

confidence: 99%

Regulation of polyamine biosynthesis in Escherichia coli by basic proteins.

Heller¹,

Rostomily²,

Kyriakidis³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

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“…[1][2][3][4]. Several studies (1)(2)(3)(4)(5)(6) have suggested that regulation of OrnDCase activity occurs through modulation of the amount of the enzyme protein, although other factors such as inhibitors (7)(8)(9)(10) or activators (11) of OrnDCase and post-translational enzyme modifications (12, 13) also may be involved. A major reason for difficulties in studying the regulation of this enzyme is that it represents only 0.01-0.05% of the total cellular protein, even when maximally induced.…”

mentioning

confidence: 99%

Androgen induction of ornithine decarboxylase mRNA in mouse kidney as studied by complementary DNA.

Kontula¹,

Torkkeli²,

Bardin³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

162

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To investigate the mechanisms by which androgens regulate ornithine decarboxylase (OrnDCase; L-ornithine carboxy-lyase, EC 4.1.1.17) in mouse kidney, a cDNA clone encoding OrnDCase mRNA was prepared. Purification of OrnDCase mRNA from kidneys of androgen-treated mice was accomplished by immunoadsorption of renal polysomes to a protein A-Sepharose column and enrichment for poly(A)-containing RNA by oligo(dT)-cellulose. Double-stranded cDNA synthesized from this mRNA was inserted into the Pst I site of plasmid pBR322 by using oligo(dGdC)-tailing and was propagated in Escherichia coli. Plasmids containing cDNA sequences coding for OrnDCase were identified by differential colony hybridization, by radioimmunological detection of OrnDCase-like antigens in bacterial cultures, and by cell-free translation of hybrid-selected mRNA followed by imununoprecipitation with monospecific OrnDCase antiserun%. A restriction endonuclease fragment of the selected plasmid DNA (pODCS4) was labeled by nick-translation and used to study changes in OrnDCase mRNA concentration. After a single dose of testosterone, renal OrnDCase mRNA concentration increased as soon as 6 hr and peaked 24 hr after steroid injection, as measured by RNA blot hybridization. Continuous androgen treatment for 4 days resulted in a 10-to 20-fold increase in OrnDCase mRNA concentration in normal animals, but no induction of this mRNA was detected in mice that have an inherent defect of the androgen receptor (testicular feminization). These results indicate that androgens regulate OrnDCase synthesis in mouse kidney, at least in part, by increasing OrnDCase mRNA accumulation.Ornithine decarboxylase (OrnDCase; L-ornithine carboxylyase, EC 4.1.1.17) catalyzes the conversion of ornithine to putrescine and is the first and apparently rate-limiting enzyme in polyamine biosynthesis. A striking feature of this enzyme is that it has extremely rapid induction kinetics and a high turnover rate (for review, see refs. 1-4). Several studies (1-6) have suggested that regulation of OrnDCase activity occurs through modulation of the amount of the enzyme protein, although other factors such as inhibitors (7-10) or activators (11) of OrnDCase and post-translational enzyme modifications (12, 13) also may be involved. A major reason for difficulties in studying the regulation of this enzyme is that it represents only 0.01-0.05% of the total cellular protein, even when maximally induced. Nonetheless, purification of the enzyme to apparent homogeneity (5,(14)(15)(16)(17) and development of radioimmunoassays (5, 6) have permitted studies on OrnDCase turnover.We reasoned that further understanding of the factors that regulate OrnDCase would be facilitated if a probe were available that would allow direct measurement of OrnDCase mRNA sequences. Kidneys of testosterone-treated mice were chosen as a source for isolation of OrnDCase mRNA because androgen administration increases enzyme protein in this organ to a higher concentration than is known in most tissues (2, 5, 6). In the presen...

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“…Indeed, high putrescine con centrations strongly reduce ODC levels through the inhibition of the enzyme synthe sis. There is a great deal of evidence that putrescine and other polyamines are also able to induce the synthesis of an inhibitory protein, the antizyme, which binds to the enzyme and inhibits its activity [11][12][13].…”

mentioning

confidence: 99%

Regulation of Diamine Oxidase Expression by Ornithine Decarboxylase in Isolated Rat Small Bowel Enterocytes

D’Agostino¹,

Pignata

Daniele

et al. 1990

Digestion

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Ornithine decarboxylase (ODC) and diamine oxidase (DAO), enzymes involved in polyamine metabolism, are highly expressed by small bowel enterocytes. Modulation of ODC expression is mediated through cellular concentration of polyamines that inhibits the enzyme synthesis and also induces the synthesis of an inhibitory protein, the antizyme, which in turn binds to ODC and inhibits its activity. DAO is an important regulator of intracellular concentration of polyamines because it catalyzes the degradation of putrescine into n-aminobutyraldehyde. Change in intracellular polyamine concentration has been suggested to represent a regulatory factor for DAO expression. In order to investigate a possible regulation of DAO expression by ODC, we studied the effect of difluoromethylornithine (DFMO), a selective, irreversible inhibitor of ODC, on DAO activity in isolated rat small bowel enterocytes. Our data demonstrate that in isolated small bowel enterocytes ODC inhibition by 10 mM DFMO reduced DAO activity by 53%, suggesting that, in our experimental conditions, ODC plays a regulatory role on DAO expression.

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Cellular control of ornithine decarboxylase activity by its antizyme

Cited by 72 publications

References 30 publications

Regulation of polyamine biosynthesis in Escherichia coli by basic proteins.

Regulation of polyamine biosynthesis in Escherichia coli by basic proteins.

Androgen induction of ornithine decarboxylase mRNA in mouse kidney as studied by complementary DNA.

Regulation of Diamine Oxidase Expression by Ornithine Decarboxylase in Isolated Rat Small Bowel Enterocytes

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