Phosphorylation of ornithine decarboxylase by a polyamine-dependent protein kinase.

Atmar, Valerie J.; Kuehn, Glenn D.

doi:10.1073/pnas.78.9.5518

Cited by 80 publications

(35 citation statements)

References 22 publications

(40 reference statements)

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“…The mechanisms controlling ornithine decarboxylase activity seem to be complex and partially understood. Several modified forms of the enzyme have been reported, including phosphorylated [7] and transamidated forms [6], and the existence of an equilibrium between active and cryptic forms of ODC has also been suggested [lo]. Moreover, different investigators have observed multiple &forms of ODC after fractionation by gel permeation chromatography [13,17], but the physiological significance of these forms remains unknown.…”

Section: Resultsmentioning

confidence: 99%

“…This enzyme, which is considered to play an important role in the control of cell growth, proliferation and differentiation [4], exhibits an extremely short half-life [5] and its activity is affected by a great variety of agents. To account for the rapid changes in its activity, several in vivo regulatory mechanisms have been reported, such as post-translational modifications [6,7] and regulatory proteins [8,9]. The existence of cryptic or latent forms of the enzyme has also been suggested [lo].…”

Section: Introductionmentioning

confidence: 99%

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Equilibrium between active and inactive forms of rat liver ornithine decarboxylase mediated by L‐ornithine and salts

Solano¹,

Peñafiel²,

Solano³

et al. 1985

FEBS Letters

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The mechanisms controlling the activity of ornithine decarboxylase (ODC) are complex and only partly understood. This study shows that ODC can exist as two different aggregation states, that differ in catalytic activity, the dimeric form being active and the monomeric form inactive. While L-ornithine shifts the association-dissociation equilibrium to the dimeric form, salts produce an opposite effect leading to subunit dissociation. a-DFMO, an enzyme-activated irreversible inhibitor of ODC, does not react with the monomeric form and therefore the influence of substrate and salts on the aggregation equilibrium must be taken into account in titration experiments with a-DFMO of the total amount of ODC in tissue preparations.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Equilibrium between active and inactive forms of rat liver ornithine decarboxylase mediated by L‐ornithine and salts

Solano¹,

Peñafiel²,

Solano³

et al. 1985

FEBS Letters

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“…An ORNdc antizyme has been identified to be responsible for the control of ORNdc by polyamines by a specific degradation mechanism (Li and Coffino, 1994). Phosphorylation may also play a role in the regulation of ORNdc by polyamines (Atmar and Kuehn, 1981;Kanamoto et al, 1993). The regulation of ORNdc has not been well characterized in plants.…”

Section: Discussionmentioning

confidence: 99%

Regulation of Arabidopsis thaliana (L.) Heynh Arginine Decarboxylase by Potassium Deficiency Stress

1996

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Arginine decarboxylase (ARCdc) is the first enzyme in one of the two pathways to putrescine in plants. ARCdc enzyme activity has been shown to be induced by many environmental factors, including potassium deficiency stress. W e investigated the mechanism for induction of ARGdc activity during potassium deficiency stress in Arabidopsis fhaliana (1.) Heynh. W e show that A. fhaliana responds to potassium deficiency stress by increasing ARCdc activity by up to 1 O-fold over unstressed plants with a corresponding increase in putrescine levels of up to 20-fold. Spermidine and spermine levels do not increase proportionately. Northern analysis showed no increase in ARCdc mRNA levels correlated with the increase in ARCdc enzyme activity. Western analysis revealed that there was no difference between ARCdc protein levels in stressed plants compared with controls. The increase in ARCdc enzyme activity due to potassium deficiency stress does not appear to involve changes in mRNA or protein abundance.ARGdc is the first enzyme in one of two pathways to putrescine, the other being ORNdc. The relative functions of the two pathways is one of the important problems in polyamine synthesis. ARGdc activity levels have been correlated with many abiotic stresses in plants. An early report showed that plants subjected to potassium deficiency stress accumulated putrescine to higher than normal concentrations (Coleman and Richards, 1956). Since this observation, many other stresses have been shown to stimulate putrescine accumulation. These include, but are not limited to, osmotic (Flores and Galston, 1982;Basu and Ghosh, 1991), pH (Young and Galston, 1983), nutrient (Basso and Smith, 1974), UV light (Kramer et al., 1991), and pollutant (Priebe et al., 1978) stress. Basso and Smith (1974) demonstrated that potassium deficiency resulted in increased putrescine levels in a wide variety of plants. This stress has been shown to increase ARGdc activity in many monocots (Young and Galston, 1984). The effects on dicots have been less well studied. Putrescine accumulation during environmental stress is correlated with increased ARGdc enzyme activity in oats. Schroder and Schroder, 1995).We have examined the effect of potassium deficiency stress on the model genetic organism Arabidopsis thaliana (L.) Heyhn. In this report, we show that A. thaliana responds to potassium deficiency stress in a manner similar to that described for monocots, and we use molecular probes to look for the mechanism of induction. MATERIALS A N D M E T H O D S Plant MaterialArabidopsis thaliana (L.) Heynh. ecotype Columbia seeds were surface-sterilized by washing for 2 min in 70% ethanol, followed by 20 min in 30% Clorox plus 0.5% Triton X-100 (Sigma). Seeds were then washed three times with sterile distilled water and dispersed onto sterile sand (Fisher Scientific). The sea sand had been washed with five changes of 3 volumes of deionized distilled water per volume of sand, dried, autoclaved, and dispensed into sterile 100-X 20-mm plastic Petri dishes (Falcon, Becton D...

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“…In that system, an increase in enzyme half-life augmented the inductive effect of increased OrnDCase mRNA levels. Posttranslational modification of OrnDCase and of inducible proteins that modulate its activity have also been proposed to participate in the regulation of OrnDCase activity (43)(44)(45)(46). Although biochemical data support the existence of such mechanisms, their biological role, if any, remains to be determined.…”

Section: Discussionmentioning

confidence: 99%

Nerve growth factor rapidly induces ornithine decarboxylase mRNA in PC12 rat pheochromocytoma cells.

Feinstein¹,

Dana²,

McConlogue³

et al. 1985

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

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The mechanism by which nerve growth factor (NGF) stimulates ornithine decarboxylase (OrnDCase; EC 4.1.1.17) activity in the rat pheochromocytoma cell line PC12 was investigated. As demonstrated previously, NGF rapidly induces OrnDCase activity in a dose-dependent manner, with maximal enzymatic activity at 4-6 hr after exposure to NGF. Activity subsequently returns to near basal levels. A cloned OrnDCase cDNA was used to analyze the levels of OrnDCase RNA. In response to NGF administration, OrnDCase RNA levels were induced. The time course of the OrnDCase RNA induction paralleled that of the enzyme activity induction, and the magnitude of both inductions was quantitatively the same. Increased concentration of OrnDCase RNA was clearly detected at the earliest time point examined, 2 hr. No change was observed in the size of OrnDCase RNA. The dose-response curves for both RNA and enzyme activity inductions were also similar. Thus, increased OrnDCase RNA levels fully account for, and are responsible for, the induction of activity. Further, one-third of the OrnDCase RNA induction was unaffected by cycloheximide treatment but was fully blocked by actinomycin D treatment, suggesting that NGF acts through at least two mechanisms to mediate the OrnDCase induction. The first mechanism is cycloheximide insensitive and the second is mediated through an event requiring ongoing protein synthesis. Both mechanisms require ongoing transcription, as evidenced by the complete sensitivity of the induction process to actinomycin D.

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Phosphorylation of ornithine decarboxylase by a polyamine-dependent protein kinase.

Abstract: This paper presents evidence that a polyaminedependent protein idnase (EC 2.7A 1.37) purified from nuclei ofthe slime mold Physarum polycephalum catalyzes phosphorylation of ornithine decarboxylase (OrnDCase; L-ornithine carboxy-lyase, EC 4.1.

Cited by 80 publications

References 22 publications

Equilibrium between active and inactive forms of rat liver ornithine decarboxylase mediated by L‐ornithine and salts

Equilibrium between active and inactive forms of rat liver ornithine decarboxylase mediated by L‐ornithine and salts

Regulation of Arabidopsis thaliana (L.) Heynh Arginine Decarboxylase by Potassium Deficiency Stress

Nerve growth factor rapidly induces ornithine decarboxylase mRNA in PC12 rat pheochromocytoma cells.

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