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PubMed1985

Distinct difference in the polyamine compositions of bryophyta and pteridophyta.

Polyamine contents of various species of plants and fungi including Bryophyta, Pteridophyta, Gymnospermae, Ascomycota, Basidiomycota, and Lichenobionta were determined by the combination of six chromatographic techniques. Polyamines examined included putrescine, spermidine, spermine, 1,3-diaminopropane (diaminopropane), sym-norspermidine (norspermidine), sym-norspermine (norspermine), thermospermine, caldopentamine, homocaldopentamine, cadaverine, aminopropylcadaverine, sym-homospermidine (homospermidine), agmatine, and canavalmine. In addition to the widely occurring polyamines (putrescine, spermidine, and spermine), the "unusual" polyamines norspermidine and norspermine were found to be widely distributed in Bryophyta and Lichenobionta. These two polyamines were not detected in any species of Pteridophyta, Gymnospermae, and fungi even though their possible precursor, diaminopropane, was found in some species. Homospermidine was one of the major polyamines in Bryophyta and Lichenobionta, and was detected in most species of Pteridophyta and sporadically in higher plants. Agmatine was detected in most species of Bryophyta and in certain species of Gymnospermae. These data suggest that norspermidine, norspermine, and homospermidine can serve as chemical phylogenic and taxonomic markers in Plantae and Fungi.

Fungi↗
PubMed1996

Polyamine levels in various tissues of rats treated with 3-hydroxy-4-methoxycinnamic acid and 3,4-dimethoxycinnamic acid.

The effects of 3-hydroxy-4-methoxycinnamic acid (3H4MCA) and 3,4-dimethoxycinnamic acid (3,4DMCA) on body weight, organ weight, and the contents of putrescine, spermidine and spermine in 15 different tissues were examined in rats that had been given these compounds for 5 days. In 3H4MCA-treated rats, the weight of the spleen was significantly increased, while none of the other organs showed any significant changes. A diet containing either 3H4MCA or 3,4DMCA should not be taken by patients bearing cancers in the seminal vesicles, spleen or liver, and a diet containing 3,4DMCA should not be taken by patients bearing cancers in the testis, kidney, muscle, small intestine or brain (cortex) because of the significant increases in polyamines, which are associated with a risk of cancer growth, in these tissues. However, a diet containing 3H4MCA is recommended for the management of cancers in the skeletal muscle (femoral), tongue, small intestine (jejunum), stomach, lung and brain based on reductions in polyamines which stimulate tumor growth. A diet containing 3,4DMCA is also recommended for cancer in the prostate, thymus and stomach for the same reason. In addition, a synergic therapeutic effect for the treatment of cancers in these tissues may be anticipated by a combination of such a diet with anti-cancer drugs which reduce polyamine levels. The metastasis of cancers in these tissues may also be inhibited by the reduction of polyamines by these acids. The ratio of spermidine to spermine was significantly higher in the lung of 3H4MCA-treated rats, and lower in the seminal vesicle, thymus, kidney, heart, tongue, stomach and lung of 3,4DMCA-treated rats, than in control rats. The present experiment indicated that cancer patients should pay careful attention to endogenous polyamines in tissues bearing tumors induced by chemicals in ingesta and anti-cancer drugs, in addition to exogenous polyamines.

Animals↗
PubMed1996

Estimation of 24-hour polyamine intake from mature human milk.

It has been suggested that milk polyamines stimulate GI tract proliferation and maturation in newborns. We determined human milk polyamine concentrations and estimated 24-h outputs on days 16 +/- 4 (n = 98), 44 +/- 3 (n = 97) and 91 +/- 6 (n = 25) after delivery. Median concentrations in micromolars were, respectively, putrescine 0.77, 0.63, and 0.63; spermidine 4.54, 3.07, and 2.73; spermine 3.76, 2.90, and 2.22; and total polyamines 9.82, 6.83, and 5.71. Concentrations of spermidine, spermine, and total polyamines decreased during the observation period. Putrescine, spermidine, and spermine milk/maternal plasma ratios were estimated to be 16-19, 14-24, and 44-75, respectively. It would appear that milk polyamines are derived from the high polyamine contents in the mammary gland and that they may be important in infant nutrition.

Female↗
PubMed1997

Fecal polyamine concentration in children with and without nutrient malabsorption.

BACKGROUND: Fermentation products of malabsorbed nutrients are thought to be responsible for intestinal adaptation following small bowel resection in rats. It has been suggested that either short-chain fatty acids or polyamines (mainly putrescine and cadaverine) could be the fermentation products involved. There are no data available on fecal polyamine content in humans. The present study compared the fecal polyamine concentrations in children with and without malabsorption. METHODS: Sixteen (8 girls, 8 boys) malabsorption patients (cystic fibrosis: 13, short bowel syndrome: 2, biliary atresia: 1) with a mean age of 8 years were compared to 17 (9 girls, 8 boys) sick children without malabsorption (mean age 5.7 years). Three-day fecal collections were performed and analyzed for fat and polyamine concentrations. High-performance liquid chromatography (HPLC) was used for the measurement of polyamine concentrations. RESULTS: Mean and SEM for fecal fat excretion was 13.4 +/- 2.5 g/day and 1.5 +/- 0.3 g/day in the malabsorption and control group respectively. Median fecal cadaverine and putrescine concentrations were 3723 mumol.kg-1 feces and 4737 mumol.kg-1 feces for the malabsorption group and 114 mumol.kg-1 feces and 306 mumol.kg-1 feces for the control group (p < 0.007 and < 0.00001 respectively). No significant differences were found for fecal spermine and spermidine concentrations between the two groups. CONCLUSIONS: Children with malabsorption show very high fecal putrescine and cadaverine concentrations. Our results support the hypothesis that fecal polyamines could be important.

Adolescent↗
PubMed2001

Polyamine metabolism revisited.

The natural polyamines putrescine, spermidine and spermine play an essential role in cell growth and differentiation. Cellular polyamine depletion results in inhibition of growth, whereas its accumulation appears to be toxic. Intracellular levels of polyamines are regulated by a multitude of mechanisms affecting their synthesis, degradation, uptake and excretion. The three key enzymes in the regulation of polyamine metabolism have short half-lives and are inducible. Ornithine and S-adenosylmethionine decarboxylases regulate polyamine biosynthesis whereas spermidine/spermine acetyltransferase regulates polyamine interconvertion and degradation.

Digestive System↗
PubMed2001

Polyamines and colon cancer.

Colorectal cancer is a major health problem in the western world and is associated with significant morbidity and mortality. Diet makes a significant contribution to the disease, with high fat, low fibre diets correlating positively with a high incidence of colorectal cancer. Intracellular polyamine concentrations and ornithine decarboxylase activity are both increased in colorectal cancer tissue and in premalignant polyps. Measurement of the polyamine content of serum and urine of individuals has been proposed as a diagnostic marker of malignancy but a number of false positives make this idea untenable. There may, however, still be a role for the measurement of urinary polyamine content as a means of monitoring the efficacy of therapy. Inhibition of polyamine metabolism by polyamine analogues or by non-steroidal anti-inflammatory drugs may be useful in the chemotherapy and/or chemoprevention of colorectal cancer. Preliminary results suggest that a low polyamine diet might be helpful as part of a health care plan for cancer patients.

Biomarkers, Tumor↗
PubMed2003

Polyamines contribute to ethanol withdrawal-induced neurotoxicity in rat hippocampal slice cultures through interactions with the NMDA receptor.

BACKGROUND: Several reports demonstrate that withdrawal from long-term ethanol exposure is associated with significant central nervous system neurotoxicity, produced at least in part by increased activity of N-methyl-d-aspartate receptors (NMDARs). Recent evidence suggests that elevations in the synthesis and release of the polyamines spermidine and spermine, which are known modulators of NMDARs, contribute to the increased activity of the receptor during ethanol withdrawal. Therefore, the goal of this investigation was to examine what role, if any, spermidine and spermine have in the generation of ethanol withdrawal-induced neurotoxicity. METHODS: Neurotoxicity (measured as fluorescence of the cell death indicator propidium iodide, PI), glutamate release (measured by high-performance liquid chromatography analysis), and polyamine concentrations (by high-performance liquid chromatography) were measured in rat hippocampal slice cultures undergoing withdrawal from chronic (10 day) ethanol exposure (100 mM). In addition, the effects of the polyamine synthesis inhibitor di-fluoro-methyl-ornithine (DFMO, 0.1-100 nM) and NMDAR polyamine-site antagonists ifenprodil, arcaine, and agmatine (1 nM-100 microM) on ethanol withdrawal- and NMDA-induced neurotoxicity were measured. RESULTS: Ethanol withdrawal significantly increased glutamate release (peaking at 18 hr with a 53% increase), increased concentrations of putrescine and spermidine (136% and 139% increases, respectively, at 18 hr), and produced significant cytotoxicity in the CA1 hippocampal region (56% increase in PI staining relative to controls) of the cultures. The cell death produced by ethanol withdrawal was significantly inhibited by ifenprodil (IC(50) = 14.9 nM), arcaine (IC(50) = 37.9 nM), agmatine (IC(50) = 41.5 nM), and DFMO (IC(50) = 0.6 nM). NMDA (5 microM) significantly increased PI staining in the CA1 region of the hippocampal cultures (365% relative to controls), but ifenprodil, arcaine, agmatine, and DFMO all failed to significantly affect this type of toxicity. CONCLUSIONS: These data implicate a role for polyamines in ethanol withdrawal-induced neurotoxicity and suggest that inhibiting the actions of polyamines on NMDARs may be neuroprotective under these conditions.

Animals↗
PubMed1975

Occurrence of polyamines in coliphages T5, phiX174 and in phage-infected bacteria.

The polyamine spermidine and the diamine putrescine have been detected in coliphages T5 and phiX174. Polyamines were identified by thin-layer chromatography and mass-spectrometry of dansyl derivatives, as well as by ion-exchange chromatography. In phiX174 phages, polyamines were sufficient to neutralize 0.5% of DNA phosphates. The polyamine content of T5 phages depended on growth media and purification procedures, but at least 1% of DNA phosphates were neutralized by polyamines. After infection, an increase in cellular polyamine was noticed. This increase paralleled variations in ornithine decarboxylase activity.

Carboxy-Lyases↗
PubMed1997

Cloning and disruption of the ornithine decarboxylase gene of Ustilago maydis: evidence for a role of polyamines in its dimorphic transition.

The gene encoding ornithine decarboxylase (ODC) from Ustilago maydis was cloned. A conserved PCR product amplified from U. maydis DNA was synthesized and used to screen a genomic library of the fungus. Alignment of its deduced protein sequence with those of other cloned ODCs showed a high degree of homology. Gene replacement was obtained by removal of a central part of the gene and insertion of the hygromycin resistance cassette. The null mutant thus obtained displayed no ODC activity and behaved as a polyamine auxotroph. This result is evidence that a single ODC gene exists in the fungus, and that U. maydis utilizes the ODC pathway as the only mechanism for polyamine biosynthesis. When grown in polyamine-containing media, the null mutant accumulated a polyamine pool which further sustained its normal rate of growth in polyamine-free media for approximately 12-16 h. When putrescine concentrations lower than 0.5 mM were employed, the mutant grew at a normal rate but was unable to engage in the dimorphic transition. Under conditions favourable for mycelial growth, the mutant grew with a yeast-like morphology in liquid media, and formed smooth colonies consisting of yeast cells on solid media. Reversion to normal dimorphic phenotype required high concentrations of putrescine or spermidine. These results are evidence that concentrations of polyamines higher than those necessary to sustain vegetative growth are required for the dimorphic transition in U. maydis.

Amino Acid Sequence↗
PubMed2002

Induction of the arginine decarboxylase ADC2 gene provides evidence for the involvement of polyamines in the wound response in Arabidopsis.

Polyamines are small ubiquitous molecules that have been involved in nearly all developmental processes, including the stress response. Nevertheless, no direct evidence of a role of polyamines in the wound response has been described. We have studied the expression of genes involved in polyamine biosynthesis in response to mechanical injury. An increase in the expression of the arginine decarboxylase 2 (ADC2) gene in response to mechanical wounding and methyl jasmonate (JA) treatment in Arabidopsis was detected by using DNA microarray and RNA gel-blot analysis. No induction was observed for the ADC1 gene or other genes coding for spermidine and spermine synthases, suggesting that ADC2 is the only gene of polyamine biosynthesis involved in the wounding response mediated by JA. A transient increase in the level of free putrescine followed the increase in the mRNA level for ADC2. A decrease in the level of free spermine, coincident with the increase in putrescine after wounding, was also observed. Abscisic acid effected a strong induction on ADC2 expression and had no effect on ADC1 expression. Wound-induction of ADC2 mRNA was not prevented in the JA-insensitive coi1 mutant. The different pattern of expression of ADC2 gene in wild-type and coi1 mutant might be due to the dual regulation of ADC2 by abscisic acid and JA signaling pathways. This is the first direct evidence of a function of polyamines in the wound-response, and it opens a new aspect of polyamines in plant biology.

Abscisic Acid↗
PubMed1981

Polyamine requirement for streptomycin action on protein synthesis in bacteria.

The effect of streptomycin on polypeptide synthesis in vivo and in vitro has been investigated using polyamine auxotrophic mutants of Escherichia coli grown in the presence or in the absence of putrescine. We found that streptomycin caused a marked inhibition of protein synthesis in polyamine-supplemented cells whereas bacteria starved for polyamines were less sensitive to the action of the antibiotic. Neomycin, kanamycin and kasugamycin had a behaviour similar to streptomycin while spectinomycin, gentamicin and tetracycline brought about a strong inhibition of protein synthesis both in polyamine-starved and unstarved bacteria. The increase of misreading induced by the addition of streptomycin in vivo was higher in extracts derived from bacteria cultivated in the presence of polyamines. This effect was observed in cell-free systems of streptomycin-sensitive and resistant strains. In contrast, spermidine added in vitro caused an improvement in the accuracy of translocation. Analysis of sodium dodecyl sulphate/polyacrylamide gel electrophoresis of the labelled polypeptides synthesized in vivo seems to indicate that the starvation for polyamine or the presence of streptomycin may lead to premature termination with the appearance of unfinished peptide chains.

Aminoglycosides↗
PubMed1986

Effect of polyamines on translation fidelity in vivo.

Polyamines, when added to cell-free protein-synthesizing systems, have been shown either to reduce mistranslation or to increase it depending upon the composition of the reaction mixture. To study this question under conditions as natural as possible we investigated the effects of polyamines on the fidelity of protein synthesis in intact Escherichia coli bacterial cells, using strains which were auxotrophic for polyamine synthesis. Error was measured in two ways: the incorporation of [3H]histidine into coat protein of bacteriophage MS2, the gene of which does not code for histidine, and the synthesis of a basic variant of MS2 coat protein in which a lysine erroneously replaces an asparagine, causing a change in isoelectric point. We found that when cell cultures were supplemented with polyamines there was no effect on the first type of error and the second type decreased twofold. The measured errors occurred at the level of translation because their frequency increased in the presence of streptomycin and decreased in cells bearing a streptomycin-resistance mutation known to lower the occurrence of translational misreading. The average erroneous incorporation per mol coat protein in the presence of polyamines was 1.43 +/- 0.59 mmol histidine and 25-34 mmol lysine/asparagine substitution. The reason for the different effect of polyamines on the two types of error is not known but could be related to the difference between their corresponding frequencies or to codon-specific effects.

Capsid↗
PubMed1988

Characterization of the inducible polyamine transporter in bovine lymphocytes.

The polyamine uptake system in bovine lymphocytes was activated by concanavalin A. The system was common to putrescine, spermidine and spermine. The Kt values for uptake activities of putrescine, spermidine and spermine were 3.7 microM, 0.38 microM and 0.23 microM in that order. The uptake activity was inhibited by carbonyl cyanide m-chlorophenylhydrazone, gramicidin D or valinomycin in the presence of 20 mM K+ suggesting that polyamine uptake depends on the membrane potential. The uptake activity appeared 10 h after addition of concanavalin A, and the maximum was reached at 28 h indicating that induction of the polyamine transporter precedes the initiation of DNA synthesis. Addition of polyamine antimetabolites, such as alpha-difluoromethylornithine and ethylglyoxal bis(guanylhydrazone), to the medium enhanced at least eightfold the induction of the polyamine transporter. The induction was repressed by addition of 50 microM spermidine or spermine, but not putrescine. We propose here that the induction of the membrane-potential-dependent polyamine transporter is regulated by the intracellular level of spermidine and spermine.

Animals↗
PubMed1992

Regulation of plant cell-wall pectin methyl esterase by polyamines--interactions with the effects of metal ions.

The kinetic study of the de-esterification of natural pectin by soya bean or orange pectin methyl esterase shows that the rate of the reaction is highly controlled by the presence of polyamines. The reaction rate versus the polyamine concentration is a bell-shaped curve similar to that which is obtained when the concentration of salts is varied in the reaction mixture. However polyamines, in particular the largest ones, are more efficient than salts. The results may be interpreted by assuming that polyamines mainly interact with the negative charges of the pectic substrate which condition the binding of the pectin methyl esterase. Activating effects were observed at polyamine concentrations that have been shown to exist in the plant cell wall in vivo. Thus, polyamines may act as efficient regulators of the cell-wall pH via the control of the electrostatic cell-wall potential. If such is the case, they might have a role in all regulatory mechanisms in which cell-wall enzymes are involved.

Cadaverine↗
PubMed1998

Facilitation of currents through rat Ca2+-permeable AMPA receptor channels by activity-dependent relief from polyamine block.

1. In outside-out patches excised from human embryonic kidney (HEK) 293 cells expressing Ca2+-permeable alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptor (AMPAR) channels, currents activated by 1 ms glutamate pulses at negative membrane potentials facilitated during and following a repetitive (2 to 100 Hz) agonist application. The degree of facilitation depended on subunit type, membrane potential and stimulation frequency being antagonized by a slow recovery from desensitization. 2. Activity-dependent current facilitation occurred in Ca2+-permeable but not in Ca2+-impermeable AMPAR channels. Current facilitation, however, does not depend on Ca2+ flux. Rather it reflects a relief from the block of Ca2+-permeable AMPARs by intracellular polyamines since facilitation occurred only in the presence of polyamines and since facilitated currents had a nearly linear current-voltage relation (I-V). 3. Relief from polyamine block was use dependent and occurred mainly in open channels. The relief mechanism was determined primarily by membrane potential rather than by current flow. 4. In closed channels the degree of polyamine block was independent of membrane potential. The voltage dependence of the rate of relief from the block in open channels rather than the voltage dependence of the block underlies the inwardly rectifying shape of the I-V at negative potentials. 5. Currents through native Ca2+-permeable AMPAR channels in outside-out or nucleated patches from either hippocampal basket cells or a subtype of neocortical layer II nonpyramidal cells also showed facilitation. 6. It is concluded that a use-dependent relief from polyamine block during consecutive AMPAR channel openings underlies current facilitation. This polyamine-AMPAR interaction may represent a new activity-dependent postsynaptic mechanism for control of synaptic signalling.

Animals↗
PubMed1983

Biosynthesis of polyamines in mouse brain: effects of methionine sulfoximine and adenosylhomocysteine.

This study examines the consequences on cerebral polyamine biosynthesis of increases and decreases in cerebral methylation. Increases were elicited by administering the convulsant agent methionine sulfoximine (MSO) and decreases by elevating in vivo the cerebral levels of the methylation inhibitor S-adenosylhomocysteine. Following the intraventricular (i.vt.) administration of one of the two possible polyamine precursors, [1,4-14C]putrescine, the specific radioactivity (sra) of the newly formed [14C]spermidine remained unchanged. Conversely, after i.vt. L-[3,4-14C]methionine, the other polyamine precursor, significantly higher sra values for [14C]spermidine and [14C]spermine were recorded in the brains of the MSO-treated animals. [14C]S-adenosylmethionine in the brain of the MSO-treated animals was also more highly labeled following [1-14C]-methionine, indicating its accelerated formation relative to controls. We also investigated the effect of the administration of adenosine + homocysteine, a treatment that results in elevated brain adenosylhomocysteine levels, on polyamine biosynthesis from [3,4-14C]-methionine. The results of these experiments show both significantly lower sra values for [14C]spermidine and [14C]spermine and significantly higher than control endogenous methionine levels, a clear sign of the existence of a retardation in the conversion of methionine to polyamines under these conditions. In conclusion, the present study demonstrates that while interference with cerebral methylation results in significant alterations of the rate of formation of the methionine moiety of spermidine and spermine, it has no effect on the entry of the putrescine moiety into the two polyamine molecules.

Animals↗
PubMed1992

Neomycin is an agonist at a polyamine site on the N-methyl-D-aspartate receptor.

Neomycin appears as a full agonist and spermidine as a partial agonist at the site where polyamines enhance 1-[1-(2-thienyl)cyclohexyl][3H]piperidine ([3H]TCP) binding on the N-methyl-D-aspartate (NMDA) receptor. Other aminoglycosides also enhance [3H]TCP binding with efficacies roughly proportional to the number of primary amine groups. The polyamine antagonists ifenprodil and arcaine inhibit enhancement of [3H]TCP binding by spermidine or neomycin. The inhibition of [3H]TCP binding by arcaine is apparently competitively reduced by neomycin and spermidine, supporting a common site. Diethylenetriamine (previously described as a polyamine antagonist) may be a partial agonist. Enhancement by neomycin or spermidine is not additive to that of Mg2+, consistent with competition of Mg2+ and spermidine or neomycin at the site where these compounds enhance [3H]TCP binding. Polyamines also enhance the binding of the competitive antagonist 2-(2-carboxypiperazin-4-yl)[3H]propyl-1-phosphonic acid ([3H]CPP). Neomycin, which does not enhance [3H]CPP binding, inhibits the enhancement by spermidine. That this site is distinct from the site where spermidine and neomycin increase [3H]TCP binding is supported by different pharmacology. Arcaine and diethylenetriamine do not inhibit spermidine enhancement of [3H]CPP binding. Mg2+ also does not compete with the spermidine enhancement of [3H]CPP binding. Ifenprodil inhibits the spermidine enhancement of [3H]CPP binding. The data suggest two or more polyamine sites, with arcaine selective for the site that enhances [3H]TCP binding. Neomycin is an agonist at one polyamine site and antagonist to the second.

Adrenergic alpha-Antagonists↗
PubMed2005

Albumin stimulates cell growth, l-arginine transport, and metabolism to polyamines in human proximal tubular cells.

BACKGROUND: Pure albumin stimulates proximal tubular epithelial cell (PTEC) proliferation, and may have a role in homeostasis in health, as well as in disrupted PTEC turnover in proteinuric nephropathies. We investigated a role for arginine and its metabolites, the polyamines, in this process, given the ability of polyamines to trigger proliferation in other mammalian cells. METHODS: [(3)H]-L-arginine uptake was examined after incubation with 20 mg/mL recombinant human serum albumin (rHSA) in HK-2 PTEC monolayers. Nitric oxide synthase (NOS) and arginase activity was measured; NOS, arginase, and ornithine decarboxylase (ODC) expression was identified by semiquantitative reverse transcription-polymerase chain reaction (RT-PCR). Polyamine synthesis and intracellular amino acid concentrations were compared using high-performance liquid chromatography, and cell growth measured by [(3)H]-thymidine incorporation. RESULTS: In HK-2 PTEC exposed to 20 mg/mL rHSA for 24 hours, cell proliferation as determined by [(3)H]-thymidine incorporation was increased. In parallel, L-arginine transport capacity was increased in a dose- and time-dependent manner. This effect was specific to rHSA, and was not seen with transferrin or immunoglobulin G. The intracellular concentration of L-arginine remained unchanged, although L-ornithine was increased with rHSA incubation. rHSA up-regulated type II arginase mRNA, and increased arginase activity, although no difference in nitric oxide synthase expression or activity was seen. ODC mRNA was increased, as were intracellular polyamine concentrations. alpha-Difluoromethylornithine (DFMO), an ODC inhibitor, reduced intracellular polyamine concentrations and rHSA-induced cell proliferation to control levels. CONCLUSION: The arginine-ornithine-polyamine pathway appears enhanced in PTEC incubated with rHSA and is involved in cellular proliferation; this may offer novel approaches to understanding progressive proteinuric nephropathies.

Arginase↗