scholarly journals Overexpression of arginine decarboxylase in transgenic plants

1997 ◽  
Vol 325 (2) ◽  
pp. 331-337 ◽  
Author(s):  
Daniel BURTIN ◽  
Anthony J. MICHAEL
Keyword(s):  
Transgenic Plants ◽  
Arginine Decarboxylase ◽  
Polyamine Metabolism ◽  
Morphological Development ◽  
Polyamine Biosynthesis ◽  
Adenosylmethionine Decarboxylase ◽  
Two Generations ◽  
Key Enzyme ◽  
Polyamine Conjugate ◽  
And Control

The activity of arginine decarboxylase (ADC), a key enzyme in plant polyamine biosynthesis, was manipulated in two generations of transgenic tobacco plants. Second-generation transgenic plants overexpressing an oat ADC cDNA contained high levels of oat ADC transcript relative to tobacco ADC, possessed elevated ADC enzyme activity and accumulated 10–20-fold more agmatine, the direct product of ADC. In the presence of high levels of the precursor agmatine, no increase in the levels of the polyamines putrescine, spermidine and spermine was detected in the transgenic plants. Similarly, the activities of ornithine decarboxylase and S-adenosylmethionine decarboxylase were unchanged. No diversion of polyamine metabolism into the hydroxycinnamic acid–polyamine conjugate pool or into the tobacco alkaloid nicotine was detected. Activity of the catabolic enzyme diamine oxidase was the same in transgenic and control plants. The elevated ADC activity and agmatine production were subjected to a metabolic/physical block preventing increased, i.e. deregulated, polyamine accumulation. Overaccumulation of agmatine in the transgenic plants did not affect morphological development.

Inhibitors Influencing Plant Enzymes of the Polyamine Biosynthetic Pathway

1989 ◽  
Vol 44 (1-2) ◽  
pp. 49-54 ◽  
Author(s):  
Marbeth Christ ◽  
Hansruedi Felix ◽  
Jost Harr
Keyword(s):  
Biosynthetic Pathway ◽  
Early Stage ◽  
Arginine Decarboxylase ◽  
Polyamine Biosynthesis ◽  
Polyamine Synthesis ◽  
Adenosylmethionine Decarboxylase ◽  
Stage Of Development ◽  
Decarboxylase Inhibitors ◽  
Plant Enzymes ◽  
To Come

Absract Several enzymes involved in polyamine biosynthesis namely ornithine, arginine and S-adenosylmethionine decarboxylase as well as spermidine synthase, were analyzed in partially purified wheat extracts. For all enzymes effective inhibitors were found. Among them the most interesting was l-aminooxy-3-aminopropane, which inhibited all three decarboxylases. Classical polyamine biosynthesis inhibitors like difluoromethylornithine, difluoromethylarginine. methyl glyoxal bis- (guanylhydrazone) and cyclohexylamine were also inhibitory on plant enzymes. A remarkable difference in the amount of arginine and ornithine decarboxylase existed in wheat. Arginine decarboxylase seems to be more important at least during the early stage of development. Influence of polyamine synthesis inhibitors on polyamine levels is more likely to come from arginine decarboxylase inhibitors. As inhibitors of all essential enzymes involved in plant polyamine biosynthesis were found, the study of the importance of polyamines in plant physiology will be considerably facilitated.

scholarly journals Polyamines Are Not Required for Aerobic Growth of Escherichia coli: Preparation of a Strain with Deletions in All of the Genes for Polyamine Biosynthesis

2009 ◽  
Vol 191 (17) ◽  
pp. 5549-5552 ◽  
Author(s):  
Manas K. Chattopadhyay ◽  
Celia White Tabor ◽  
Herbert Tabor
Keyword(s):  
Escherichia Coli ◽  
Ornithine Decarboxylase ◽  
Arginine Decarboxylase ◽  
Strictly Anaerobic ◽  
Lysine Decarboxylase ◽  
Free Medium ◽  
Aerobic Growth ◽  
Anaerobic Conditions ◽  
Polyamine Biosynthesis ◽  
Adenosylmethionine Decarboxylase

ABSTRACT A strain of Escherichia coli was constructed in which all of the genes involved in polyamine biosynthesis—speA (arginine decarboxylase), speB (agmatine ureohydrolase), speC (ornithine decarboxylase), spe D (adenosylmethionine decarboxylase), speE (spermidine synthase), speF (inducible ornithine decarboxylase), cadA (lysine decarboxylase), and ldcC (lysine decarboxylase)—had been deleted. Despite the complete absence of all of the polyamines, the strain grew indefinitely in air in amine-free medium, albeit at a slightly (ca. 40 to 50%) reduced growth rate. Even though this strain grew well in the absence of the amines in air, it was still sensitive to oxygen stress in the absence of added spermidine. In contrast to the ability to grow in air in the absence of polyamines, this strain, surprisingly, showed a requirement for polyamines for growth under strictly anaerobic conditions.

scholarly journals DFMO Reduces Cortical Infarct Volume after Middle Cerebral Artery Occlusion in the Rat

1993 ◽  
Vol 13 (6) ◽  
pp. 1033-1037 ◽  
Author(s):  
Cheryl A. Muszynski ◽  
Claudia S. Robertson ◽  
J. Clay Goodman ◽  
Charles M. Henley
Keyword(s):  
Infarct Volume ◽  
Vasogenic Edema ◽  
Specific Inhibitor ◽  
Focal Ischemia ◽  
Artery Occlusion ◽  
Polyamine Metabolism ◽  
Polyamine Biosynthesis ◽  
Ischemic Tissue ◽  
Key Enzyme ◽  
Transient Focal Ischemia

Ornithine decarboxylase (ODC), a key enzyme in polyamine biosynthesis, is induced in ischemic tissue and may mediate vasogenic edema and delayed neuronal death. We determined the effects of α-difluoromethylornithine (DFMO), a specific inhibitor of ODC, on infarct size and ODC activity in a rat model of transient focal ischemia. DFMO blocked the ischemia-induced increase in ODC and significantly reduced infarct volumes by 57–45%, depending upon the treatment regimen. These studies suggest that polyamine metabolism plays a role in the development of cerebral infarction after focal ischemia and that DFMO may be useful in limiting injury after a stroke.

scholarly journals Polyamine homoeostasis as a drug target in pathogenic protozoa: peculiarities and possibilities

2011 ◽  
Vol 438 (2) ◽  
pp. 229-244 ◽  
Author(s):  
Lyn-Marie Birkholtz ◽  
Marni Williams ◽  
Jandeli Niemand ◽  
Abraham I. Louw ◽  
Lo Persson ◽  
...  
Keyword(s):  
Drug Targets ◽  
Current Knowledge ◽  
New Drugs ◽  
Polyamine Metabolism ◽  
Decarboxylase Activity ◽  
Polyamine Biosynthesis ◽  
Adenosylmethionine Decarboxylase ◽  
Thiol Metabolism ◽  
Potential Drug Targets ◽  
Unique Compound

New drugs are urgently needed for the treatment of tropical and subtropical parasitic diseases, such as African sleeping sickness, Chagas' disease, leishmaniasis and malaria. Enzymes in polyamine biosynthesis and thiol metabolism, as well as polyamine transporters, are potential drug targets within these organisms. In the present review, the current knowledge of unique properties of polyamine metabolism in these parasites is outlined. These properties include prozyme regulation of AdoMetDC (S-adenosylmethionine decarboxylase) activity in trypanosomatids, co-expression of ODC (ornithine decarboxylase) and AdoMetDC activities in a single protein in plasmodia, and formation of trypanothione, a unique compound linking polyamine and thiol metabolism in trypanosomatids. Particularly interesting features within polyamine metabolism in these parasites are highlighted for their potential in selective therapeutic strategies.

scholarly journals Altered polyamine metabolism in the PRO/Re strain of inbred mice

1976 ◽  
Vol 158 (3) ◽  
pp. 529-533 ◽  
Author(s):  
C A Manen ◽  
R L Blake ◽  
D H Russell
Keyword(s):  
Biosynthetic Pathway ◽  
Inbred Mice ◽  
Proline Accumulation ◽  
Polyamine Metabolism ◽  
Decarboxylase Activity ◽  
Polyamine Biosynthesis ◽  
Male And Female ◽  
Adenosylmethionine Decarboxylase ◽  
Significant Difference ◽  
High Concentrations

The PRO/Re strain of inbred mice are characterized by abnormally high concentrations of proline in both blood (hyperprolinaemia) and urine (prolinuria). They excrete increased amounts of polyamines in their urine. Male PRO/Re mice excreted putrescine at 175% and spermidine at 300% the amount of male C57BL/6J controls. Female PRO/Re mice excreted putrescine at 115% and spermidine at 150% of the amount in the urine of female controls. Examination of the enzymes involved in polyamine biosynthesis revealed that ornithine decarboxylase, the initial enzyme in the polyamine-biosynthetic pathway, was increased by 150% in the kidneys and by 100% in the liver of male PRO/Re mice. There was no significant difference between PRO/Re and C57BL/6J male mice for either putrescine- or spermidine-stimulated S-adenosylmethionine decarboxylase activity. Female PRO/Re mice showed no significant difference from female C57BL/6J mice for any of the enzymes examined. When the concentrations of the polyamines in the tissues of the PRO/Re mice were determined, spermidine and spermine concentrations in the kidneys of the male PRO/Re mice were twice those of the controls. Spermidine concentration in the livers of both male and female PRO/Re mice was approx. 130% that of the controls. Polyamine concentrations in the brains were similar in controls and mutants. The increased polyamine biosynthesis and excretion in the PRO/Re mutant mice may be a mechanism to decrease the extent of proline accumulation.

scholarly journals Modulation of polyamine metabolism in Arabidopsis thaliana by salicylic acid

2020 ◽  
Author(s):  
Franco R. Rossi ◽  
Andrés Gárriz ◽  
María Marina ◽  
Fernando L. Pieckenstain
Keyword(s):  
Salicylic Acid ◽  
Pseudomonas Syringae ◽  
Amine Oxidase ◽  
Regulatory Protein ◽  
Arginine Decarboxylase ◽  
Polyamine Metabolism ◽  
Polyamine Biosynthesis ◽  
Whole Plant ◽  
Regulatory Effects ◽  
Plant Pathogen Interactions

AbstractPolyamines (PAs) play important roles in plant defense against pathogens, but the regulation of PA metabolism by hormone-mediated defense signaling pathways has not been studied in depth. In this study, the modulation of PA metabolism in Arabidopsis by salicylic acid (SA) was analyzed, by combining the exogenous application of this hormone with the use of PA biosynthesis and SA synthesis/signaling mutants. SA induced notable modifications of polyamine metabolism, mainly consisting in putrescine accumulation both in whole-plant extracts and apoplastic fluids. Put was accumulated at the expense of increased biosynthesis by arginine decarboxylase 2 and decreased oxidation by copper amine oxidase. Enhancement of Put levels by SA was independent of the regulatory protein Non-Expressor of Pathogenesis Related 1 (NPR1) and the signaling kinases MKK4 and MPK3, but depended on MPK6. On its part, plant infection by Pseudomonas syringae pv. tomato DC3000 elicited Put accumulation in a SA-dependent way. The present study demonstrates a clear connection between SA signaling and plant PA metabolism in Arabidopsis and contributes to understand the mechanisms by which SA modulates PA levels during plant-pathogen interactions.HighlightSalicylic acid modulates polyamine biosynthesis and catabolism in Arabidopsis. Regulatory effects of salicylic acid are independent of the master regulator NPR1 and are mediated by the MPK6 kinase.

scholarly journals Gibberellin and spermidine synergistically regulate polyamine metabolism during Rhododendron flower development

2021 ◽  
Author(s):  
Qian Xu ◽  
Huaxiong Li ◽  
Shiliang Liu ◽  
Wenpei Huang ◽  
Xiaolin Xian ◽  
...  
Keyword(s):  
Structural Equation ◽  
Early Stage ◽  
Arginine Decarboxylase ◽  
Equation Model ◽  
Flower Senescence ◽  
Polyamine Metabolism ◽  
Flower Bud ◽  
Adenosylmethionine Decarboxylase ◽  
Flower Bud Formation ◽  
Positive Effect

Abstract Polyamines (PAs) are involved in various plants developmental processes, especially in flowering. Their significant influence has been established, but the exact mechanisms by which PAs modulate flowering are not yet understood. To understand the PA metabolism during flowering/senescence in Rhododendron simsii ‘Zichendian’ plants, exogenous gibberellin (GA3, 0-2400 mg L− 1) and spermidine (Spd, 0–1 mM) were applied separately or in combination during the early stage of flower bud formation. The application of GA3 alone advanced the initial flowering by promoting the free Put (F) fraction and decreasing the Spd/Put ratio at the squaring stage, whereas Spd alone delayed the initial flowering by increasing the soluble conjugated (C) form, insoluble bound Put (B) fraction and Spd/Put ratio. When GA3 plus Spd was applied, the initial flowering advanced by 2 days. Furthermore, endogenous PA levels as well as the C and B fractions of PAs and key enzymes (diamine oxidase, PA oxidase, arginine decarboxylase, ornithine decarboxylase and S-adenosylmethionine decarboxylase) of PA metabolism increased, while the Spd/Spm ratio decreased by GA3 and Spd applications during flowering, resulting in delayed flower senescence. In addition, the structural equation model (SEM) showed that Spd directly participated in PA metabolism, while GA3 regulated flowering by modulating PA metabolism via Spd (c.f. 0.27). Taken together, our study provides comprehensive evidence regarding the clear relationships between GA3, Spd and flowering time, supporting the positive effect of PA metabolism on delaying flower senescence, and helps to provide a thorough understanding of the PA interconversions, biosynthesis and catabolism during flowering and senescence.

scholarly journals Forced expression of antizyme abolishes ornithine decarboxylase activity, suppresses cellular levels of polyamines and inhibits cell growth

1994 ◽  
Vol 304 (1) ◽  
pp. 183-187 ◽  
Author(s):  
Y Murakami ◽  
S Matsufuji ◽  
Y Miyazaki ◽  
S Hayashi
Keyword(s):  
Cell Growth ◽  
Ornithine Decarboxylase ◽  
Polyamine Metabolism ◽  
Decarboxylase Activity ◽  
Inhibitory Protein ◽  
Polyamine Biosynthesis ◽  
Rapid Degradation ◽  
Physiological Importance ◽  
Key Enzyme

Ornithine decarboxylase (ODC) is a key enzyme in polyamine biosynthesis. It is a short-lived protein and negatively regulated by its products, polyamines. Its degradation is accelerated by the binding of antizyme, an ODC-inhibitory protein induced by polyamines. To evaluate the physiological importance of antizyme we examined the effect of forced expression of antizyme on cellular ODC and polyamine levels and cell growth. Antizyme almost completely abolished the induction of ODC by growth stimuli. This may have been caused by antizyme-induced rapid degradation of newly synthesized ODC, since the half-life of ODC complexes with antizyme was less than 5 min. Forced expression of antizyme caused reductions of cellular putrescine and spermidine levels, and inhibited cell growth, which was partially restored by the addition of putrescine. These observations suggested a critically important role of antizyme in polyamine metabolism.

Translational regulation of the plant S-adenosylmethionine decarboxylase

2003 ◽  
Vol 31 (2) ◽  
pp. 424-427 ◽  
Author(s):  
C. Hanfrey ◽  
M. Franceschetti ◽  
M.J. Mayer ◽  
C. Illingworth ◽  
K. Elliott ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Rna Secondary Structure ◽  
Translational Regulation ◽  
Mrna Translation ◽  
Open Reading Frames ◽  
Polyamine Biosynthesis ◽  
Adenosylmethionine Decarboxylase ◽  
Key Enzyme ◽  
Upstream Open Reading Frames ◽  
Reading Frames

It is becoming apparent that control of protein synthesis by metabolites is more common than previously thought. Much of that control is exerted at the level of initiation of mRNA translation, orchestrated by upstream open reading frames (uORFs) and RNA secondary structure. S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in polyamine biosynthesis and both mammalian and plant AdoMetDCs are translationally regulated by uORFs in response to polyamine levels by distinct mechanisms.

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