Studies on ornithine decarboxylase from the liver of thioacetamide-treated rats Purification and some properties

Ono, Masayoshi; Inoue, Hideo; Suzuki, Fujio; Takeda, Yoshiro

doi:10.1016/0005-2744(72)90067-8

Cited by 127 publications

(27 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is possible that there are isoenzymes of ornithine decarboxylase in various tissues, variably sensitive to inhibitors of protein synthesis. The finding of a single species of this enzyme in the liver of rats treated with thioacetamide (22) does not preclude the possibility that there are tissue-specific ornithine decarboxylase isoenzymes. Two distinct ornithine decarboxylases, one a biosynthetic enzyme and the other an inducible catabolic enzyme, have been identified in Escherichia coli (23).…”

Section: Resultsmentioning

confidence: 95%

Nature of the increase in renal ornithine decarboxylase activity after cycloheximide administration in the rat.

Levine¹,

Nicholson²,

Orth³

1975

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

View full text Add to dashboard Cite

The present study was designed to determine whether the increase in rat renal ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) activity after cycloheximide administration was a primary effect on the kidney or was a secondary effect of adrenal or pituitary hormones released in response to the drug. Renal ornithine decarboxylase activity was reduced approximately 70% 1 hr after intraperitoneal administration of doses of cycloheximide that also inhibited renal protein synthesis by 68-95% within 1 hr. Protein synthesis began to recover by the second hour, accompanied by a rise in decarboxylase activity that reached a peak about six times greater than pretreatment values at 8 hr, then gradually declined to preinjection levels by 16 hr. Peak ornitlhine decarboxylase activity was directly proportional to cycloheximide doses up to 250 Mg; larger doses, which almost abolished protein synthesis for 8 hr, were inhibitory. Plasma corticosterone rose rapidly after cycloheximide, reached a peak at 2 hr, then fell to baseline by 8 hr. Corticosterone response was also dose-dependent up to 250 Mg, but larger doses were inhibitory. Adrenalectomy did not reduce decarboxylase activity response to cycloheximide, nor did cortisol administration enhance it. Hypophysectomy greatly reduced baseline renal decarboxylase activity within 9 hr and all but abolished the increase in enzyme activity normally seen after cycloheximide administration to the intact rat. The hypophysectomized animal exhibited apparent increased sensitivity to cyclohieximide, since a smaller dose of the drug caused a reduction in renal protein synthesis similar to that seen with a larger dose in the intact rat. As protein synthesis was recovering in the hypophysectomized animals, renal decarboxylase activity responded adequately to the injection of a crude pituitary extract. These data suggest that renal ornithine decarboxylase turnover is rapid, that baseline activity is maintained by new protein synthesis, and that the increase in renal enzyme activity after cyclolieximide is in large part dependent upon pituitary hormone action.

show abstract

Section: Resultsmentioning

confidence: 95%

Nature of the increase in renal ornithine decarboxylase activity after cycloheximide administration in the rat.

Levine¹,

Nicholson²,

Orth³

1975

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

View full text Add to dashboard Cite

show abstract

“…It was purified about fifteen fold by acid treatment at pH 4.6, as described by Ono et al 31 . The protocol for rats was approved by Internal Committee for the Care and Use of Laboratory Animals, Escuela Superior de Medicina-IPN.…”

Section: Rat Liver Odcmentioning

confidence: 99%

N-ω-chloroacetyl-l-ornithine, a new competitive inhibitor of ornithine decarboxylase, induces selective growth inhibition and cytotoxicity on human cancer cells versus normal cells

Medina-Enríquez

Alcántara-Farfán

Aguilar-Faisal

et al. 2014

Journal of Enzyme Inhibition and Medicinal Chemistry

View full text Add to dashboard Cite

“…When a prostatic extract was subjected to precipitation at pH 4.6 by the method of Ono et al [14], the precipitate showed a 3-fold increase in the specific activity of ODC accompanied by a halving of the specific activity of ODC inactivating factor (table 2). The supernatant solution showed negligible ODC activity and nearly a doubling in its ODIF specific activity.…”

Section: Resultsmentioning

confidence: 99%

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

Icekson

Kaye

1976

FEBS Letters

View full text Add to dashboard Cite

Studies on ornithine decarboxylase from the liver of thioacetamide-treated rats Purification and some properties

Cited by 127 publications

References 28 publications

Nature of the increase in renal ornithine decarboxylase activity after cycloheximide administration in the rat.

Nature of the increase in renal ornithine decarboxylase activity after cycloheximide administration in the rat.

N-ω-chloroacetyl-l-ornithine, a new competitive inhibitor of ornithine decarboxylase, induces selective growth inhibition and cytotoxicity on human cancer cells versus normal cells

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

Contact Info

Product

Resources

About