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PubMed2004

Polyamine analysis for chemotaxonomy of thermophilic eubacteria: Polyamine distribution profiles within the orders Aquificales, Thermotogales, Thermodesulfobacteriales, Thermales, Thermoanaerobacteriales, Clostridiales and Bacillales.

Cellular polyamines of 45 thermophilic and 8 related mesophilic eubacteria were investigated by HPLC and GC analyses for the thermophilic and chemotaxonomic significance of polyamine distribution profiles. Spermidine and a quaternary branched penta-amine, N4-bis(aminopropyl)norspermidine, were the major polyamine in Thermocrinis, Hydrogenobacter, Hydrogenobaculum, Aquifex, Persephonella, Sulfurihydrogenibium, Hydrogenothermus, Balnearium and Thermovibrio, located in the order Aquificales. Thermodesulfobacterium and Thermodesulfatator belonging to the order Thermodesulfobacteriales contained another quaternary penta-amine, N4-bis(aminopropyl)spermidine. In the order Thermotogales, Thermotoga contained spermidine, norspermidine, caldopentamine and homocaldopentamine. The latter two linear penta-amines were not found in Marinitoga and Petrotoga. In the order Thermales, Thermus and Marinithermus contained homospermidine, norspermine and the linear penta-amines. Meiothermus lacked penta-amines. Vulcanithermus contained linear penta-amines and hexa-amines but not homospermidine. Oceanithermus contained spermine alone. Within the order Thermoanaerobacteriales, the two quaternary branched penta-amines were found in Thermanaeromonas and Thermoanaerobacter. Caldanaerobacter contained N4-bis(aminopropyl)spermidine. Thermoanaerobacterium lacked penta-amines. Thermaerobacter of the order Clostridiales contained N4-bis(aminopropyl)spermidine and agmatine. Thermosyntropha, Thermanaerovibrio, Thermobrachium ( the order Clostridiales), Sulfobacillus, Alicyclobacillus, Anoxybacillus, Ureibacillus, Thermicanus ( the order Bacillales), Desulfotomaculum, Desulfitobacterium and Pelotomaculum (the family Peptococcaceae) ubiquitously contained spermine. Some thermophiles of Bacillales added linear and branched penta-amines.

Bacteria↗
PubMed1990

[Detection of polyamines by a new enzymatic differential assay. (8) Studies on tissue polyamine concentrations in patients with genitourinary malignant diseases].

Polyamine concentrations of human cancerous and non-cancerous tissues from the kidney, ureter, bladder were measured by a new enzymatic method for isolation and determination of polyamines. In cancerous and non-cancerous tissue of the organs studied, the spermine level was highest followed by the spermidine and diamine levels. The concentrations of diamine, spermidine and spermine in cancerous tissues were significantly higher than those in non-cancerous tissues, but there was no significant difference in the spermidine/spermine ratio between the cancerous and non-cancerous tissues. These data suggest that polyamines are produced above the normal levels in pathological conditions such as renal cell carcinoma, ureteral cancer and bladder cancer.

Biogenic Polyamines↗
PubMed1989

Effects of polyamines on the binding of [3H]MK-801 to the N-methyl-D-aspartate receptor: pharmacological evidence for the existence of a polyamine recognition site.

A heat-stable factor of low molecular weight that increases the binding of [3H]MK-801 to rat brain membranes in the presence of maximally effective concentrations of L-glutamate and glycine was purified from bovine brain by reverse phase and ion-exchange high pressure liquid chromatography. The stimulatory activity was due to the presence of spermidine in the active fractions. Polyamines including spermine and spermidine are found in high concentrations in mammalian tissue. These compounds increase the affinity of N-methyl-D-aspartate (NMDA) receptors for [3H]MK-801 when assays are carried out in the presence of 100 microM L-glutamate and 100 microM glycine. At concentrations of 1 to 300 microM, a number of di- and triamines, including NH2(CH2)3NH2, NH2(CH2)3NH(CH2)2NH2, and NH2(CH2)3NH(CH2)3NH2, have partial or full agonist-like activity similar to that of spermidine. Other polyamines, including putrescine, cadaverine, NH2(CH2)2NH(CH2)2NH2, and CH3NH(CH2)3NHCH3, at concentrations of 1 to 100 microM, inhibited the binding of [3H]MK-801 in the presence of spermine, L-glutamate, and glycine but not in the presence of only L-glutamate and glycine. It is concluded that these compounds are selective antagonists of the effects of spermine at the NMDA receptor. These results suggest that there may be a polyamine recognition site on the NMDA receptor complex.

Animals↗
PubMed1983

Modulation of the tissue disposition of methylglyoxal bis(guanylhydrazone) in mice by polyamine depletion and by polyamine administration.

Treatment of mice with DL-alpha-difluoromethylornithine (DFMO), an irreversible inhibitor of ornithine decarboxylase (EC 4.1.1.17), produced a significant spermidine depletion in liver, small intestine, and bone marrow among eight tissues studied. The accumulation of methylglyoxal bis(guanylhydrazone) (MGBG) was selectively enhanced in small intestine and in bone marrow cells in response to a prior DFMO treatment. In other tissues studied, i.e., brain, skeletal and cardiac muscle, liver, kidney, and spleen, a preceding treatment with DFMO had no effect on the accumulation of subsequently injected MGBG. When mice, primed with DFMO and then treated with a single injection of MGBG, were given nontoxic doses of spermidine or putrescine through a gastric tube, high concentrations of MGBG in the small intestine and in bone marrow cells were effectively reduced. In spite of the route of administration, bone marrow cells appeared to be more sensitive than intestinal tissue as regards the prevention of the tissue accumulation of MGBG by the polyamines. The different sensitivity of various tissues to the natural polyamines in this respect may offer a means to develop a tissue-specific "polyamine rescue concept" to be used in connection with MGBG treatment.

Animals↗
PubMed1996

Dissociation between effects of polyamines on mitochondrial calcium uptake and mitochondrial permeability transition by elongation of polyamine methylene backbone.

The aliphatic polyamine bis(hexamethylene)triamine, a spermidine analogue, was found to lack the enhancing effect on mitochondrial Ca(2+) accumulation which is typical for the natural polyamines, spermidine and spermine. However, like spermine and spermidine, this compound had a significant inhibitory effect on the Ca(2+) and Pi-induced mitochondrial permeability transition. By chromatographic determination of the amount of polyamines bound to mitochondria after a 2 min incubation, it was found that the binding affinity was spermine > or = bis(hexamethylene)triamine > spermidine. There was no competition between binding of spermine and of bis(hexamethylene)triamine. It is concluded that membrane binding sites of bis(hexamethylene)triamine are different from those of spermine. This different membrane interaction is apparently caused by the elongated hydrophobic spans in bis(hexamethylene)triamine and leads to a loss of the effect on Ca(2+) uptake but leaves intact the inhibitory effect on membrane permeability transition.

Animals↗
PubMed1993

Estimation of polyamine distribution and polyamine stimulation of protein synthesis in Escherichia coli.

To estimate the polyamine distribution in Escherichia coli, the binding constants (K) for DNA, RNA, phospholipids, and ATP were calculated under the condition of 10 mM Tris-HCl, pH 7.5, 150 mM K+, and 10 mM Mg2+. The binding constants of spermidine for E. coli DNA, E. coli 16S rRNA, phospholipids in E. coli membrane, and ATP were 0.015, 0.066, 0.028, and 0.081 mM-1, respectively. Similarly, those of putrescine were 0.010, 0.010, 0.007, and 0.037 mM-1, respectively. The concentrations of putrescine, spermidine, and ATP and phosphates in DNA, RNA, and phospholipids in E. coli harvested at A600 = 0.3 were 32.2, 6.88, and 2.66 and 96.4, 436, and 57.2 mM, respectively. Accordingly, the percentage of spermidine bound to DNA, RNA, phospholipids, and ATP and that of free spermidine were 5.1, 90, 0.7, 0.8, and 3.8%, respectively. The percentage of putrescine bound to DNA, RNA, phospholipids, and ATP and that of free putrescine were 9.3, 48, 1.4, 2.6, and 39%, respectively. The results indicate that most spermidine exists as a spermidine--RNA complex, and about 40% and 50% of putrescine exists as a free form and a putrescine--RNA complex in cells, respectively. Under the conditions that the synthesis of specific proteins such as RNA replicase is stimulated by polyamines in a cell-free system, the amount of spermidine and putrescine bound to RNA was close to the value estimated in cells. Experiments to demonstrate the polyamine stimulation of MS2 RNA-directed RNA replicase synthesis in vivo were thus performed, and the results were confirmed.

Adenosine Triphosphate↗
PubMed1994

Cellular localization of polyamines: cytochemical and ultrastructural methods providing new clues to polyamine function in ram spermatozoa.

Polyamine binding sites have been localized in ram spermatozoa using biochemical and cytochemical tools. Incubating the cells with 14C-spermine and determining its distribution after sonication and differential centrifugation, revealed that 60% of the radioactive spermine was localized in the head, 21.5% in the tail and about 9% in the plasma membrane. A polyamine specific cytochemical staining by the formaldehyde-fluorescamine method, revealed that most of the polyamines were localized in the midpiece, where the cell mitochondria are located, and in the acrosome region. Two additional studies used electron microscopy, employing polycationic colloidal gold and spermine-ferritin as cytochemical markers. The most sensitive and specific method was the staining of the cells with ferritin-spermine whose synthesis is described in this study. The outer membrane was the preferential site for spermine binding which was densely distributed in a highly orderly pattern. There was a sparse distribution of spermine binding sites on the plasma membrane surrounding the acrosome and none on the post acrosomal region. The role of spermine in the acrosome reaction and Ca2+ fluxes in sperm cells is discussed.

Animals↗
PubMed2001

Influence of polyamine architecture on the transport and topoisomerase II inhibitory properties of polyamine DNA-intercalator conjugates.

An efficient five-step synthetic method was developed to access a series of spermine derivatives containing appended acridine, anthracene, and 7-chloroquinoline motifs. The derivatives were composed of a spermine fragment covalently tethered at its N4 and N9 positions to an aromatic nucleus via an aliphatic chain (e.g., 8: acridine -[C4 aliphatic tether]-spermine-[C4 aliphatic tether]-acridine). The distance separating the spermine and aromatic nuclei was altered via different tethers composed of four or five methylene units. These bis ligands (8, 9, 12, and 13) were shown to inhibit human DNA topoisomerase II (topo II) activity at 5 microM. Enzymatic activity was assessed as the ability to unknot (decatenate) and cleave kinetoplast DNA (kDNA). Polyamine conjugation did not disrupt the ability of the acridine-spermine conjugates 8 and 9 to inhibit topo II activity as compared with the 9-aminoacridine and 9-(N-butyl)aminoacridine controls (at 5 microM). The parent polyamines, spermine (5 microM) and spermidine (10 microM), had little effect on topo II activity. In general, the bis-substituted spermine derivatives (8, 9, 12, and 13) were more efficient topo II inhibitors at 5 microM than their monosubstituted spermidine counterparts (22-25) at 10 microM. Within the bisintercalator spermine series, insertion of an additional methylene unit (i.e., C5 tethers) increased potency 2-fold (8, bis-C4-acridine, 47 h IC(50) = 40 microM; 9, bis-C5-acridine, IC(50) = 17 microM). Comparison of the bis- and monoacridine spermine motifs (8 and 17) revealed a 4-fold increase in potency for the latter architecture (94 h IC(50) for 8, 74 microM; for 17, 17 microM). In general the bisintercalators (8, 9, 12, and 13) behaved as cytostatic agents, while the monosubstituted acridine and anthracene derivatives (22-25) were cytotoxic. Anthracene-containing conjugates were generally more toxic than their acridine counterparts in an L1210 (murine leukemia) cell assay. Of the conjugates tested the (monointercalator)-spermine motif (e.g., 17) had the highest affinity for the L1210 polyamine transporter as revealed by spermidine protection experiments.

Acridines↗
PubMed1991

Polyamine Metabolism in Ripening Tomato Fruit : II. Polyamine Metabolism and Synthesis in Relation to Enhanced Putrescine Content and Storage Life of a/c Tomato Fruit.

The fruit of the Alcobaca landrace of tomato (Lycopersicon esculentum Mill.) have prolonged keeping qualities (determined by the allele a/c) and contain three times as much putrescine as the standard Rutgers variety (A/c) at the ripe stage (ARG Dibble, PJ Davies, MA Mutschler [1988] Plant Physiol 86: 338-340). Polyamine metabolism and biosynthesis were compared in fruit from Rutgers and Rutgers-a/c-a near isogenic line possessing the allele a/c, at four different stages of ripening. The levels of soluble polyamine conjugates as well as wall bound polyamines in the pericarp tissue and jelly were very low or nondetectable in both genotypes. The increase in putrescine content in a/c pericarp is not related to normal ripening as it occurred with time and whether or not the fruit ripened. Pericarp discs of both normal and a/c fruit showed a decrease in the metabolism of [1,4-(14)C]putrescine and [terminal labeled-(3)H]spermidine with ripening, but there were no significant differences between the two genotypes. The activity of ornithine decarboxylase was similar in the fruit pericarp of the two lines. Arginine decarboxylase activity decreased during ripening in Rutgers but decreased and rose again in Rutgers-a/c fruit, and as a result it was significantly higher in a/c fruit than in the normal fruit at the ripe stage. The elevated putrescine levels in a/c fruit appear, therefore, to be due to an increase in the activity of arginine decarboxylase.

Journal Article↗
PubMed1986

[Urine polyamine in patients with malignant urological diseases using a polyamine-test enzyme kit].

Using a polyamine-test enzyme kit, the urine polyamine concentration was determined in 74 patients with malignant urological disease (12 with renal cell cancer, 13 with pelvic-ureter cancer, 24 with bladder cancer and 25 with prostate cancer), 7 patients with BPH, 20 patients with benign urological disease and 20 normal subjects. The urine polyamine level was significantly elevated in all the patients with any malignant urological disease compared to normal subjects. It was also significantly high in the patients with BPH. Defining the mean +/- 3SD (= 50 mumole/g Cr.) of 20 normal subjects as an upper limit, slightly higher levels not exceeding 100 mumol/g Cr. were frequently observed in the patients with BPH or with benign urological disease. Setting the upper limit at 100 mumole/g Cr., the positive rate amounted to 33% (low stage 17%) in renal cell cancer, 23% (low stage 14%) in pelvic ureter cancer, 13% (low stage 0%) in bladder cancer and 4% (low stage 0%) in prostate cancer. The positive rate was low especially in low stage cases.

Diamines↗
PubMed1979

Inhibition of lymphocyte proliferation by polyamines requires ruminant-plasma polyamine oxidase.

Spermine and spermidine in vitro are potent inhibitors of proliferation of phytohaemagglutinin-stimulated rat thymic lymphocytes, lymphoma cells and human lymphoblastic leukaemia cells, but only in media supplemented by foetal calf serum. This inhibition is shown to be due to a bovine plasma polyamine oxidase, with a high specificity for these polyamines. Spontaneously dividing lymphocytes are not subject to this inhibition. This, plus direct evidence from synchronous cultures of EB2 cells demonstrates that the inhibition is expressed in the late G1 or G1/S interface of the cell cycle. Putrescine was not an inhibitor in the presence of foetal calf serum but became so in the presence of human pregnancy serum, possibly due to the action of diamine oxidase.

Animals↗
PubMed1979

Polyamine conjugates and total polyamine concentrations in human amniotic fluid.

A study of the quantitative profile of polyamines in amniotic fluid from the 13th through the 40th week of gestation was undertaken. These experimental observations indicate the absence of free putrescine, spermidine and spermine throughout gestation. Quantities of acid-liberated putrescine, spermidine and spermine are highest in late first and late third trimester. Putrescine is associated with peptide or peptides of molecular weight 1000 to 10 000 throughout gestation. Spermidine is found in amniotic fluid covalently conjugated to peptide or peptides with molecular weight 10 000 to 30 000. Spermine appears to exist in amniotic fluid, both in the higher molecular weight fraction (1000 to 10 000) and as acetylated derivatives. The existance of polyamine conjugates is compatible with an in vivo function in the regulation of embryonic growth and development. Abnormalities in polymines conjugated to peptides or their concentration may be useful in the diagnosis of fetal maldevelopment.

Amniotic Fluid↗
PubMed1992

Changes in regional polyamine profiles in rat brains after transient cerebral ischemia (single versus repetitive ischemia): evidence for release of polyamines from injured neurons.

Reversible cerebral ischemia (of 5 min, 15 min, or 3-times 5 min) was produced in 14 Mongolian gerbils by occluding both common carotid arteries. After 72 h of recirculation, brains were frozen and processed for measuring regional levels of the polyamines putrescine, spermidine and spermine using HPLC and fluorescent detector. Ischemia induced a marked increase in putrescine levels throughout the brain, most pronounced after 3-times 5 min ischemia (P less than or equal to 0.05 - P less than or equal to 0.001). Spermine levels were significantly reduced, in the hippocampal CA1-subfield after 5 min of ischemia and, in addition, in the striatum and thalamus after 3-times 5 min ischemia. It is suggested that polyamines are released from necrotic neurons and cleared into the blood. Spermine, released from neurons into the extracellular compartment, may bind to the N-methyl-D-aspartate (NMDA) receptor of cells located in close vicinity and may thus render neurons vulnerable to otherwise subtoxic levels of excitotoxins.

Animals↗
PubMed1983

Regulation of polyamine-responsive protein kinase by certain highly specific polyamines and charged carbohydrates.

Polyamine-responsive protein kinase, a cyclic nucleotide-independent protein kinase from the cytosol of Morris hepatoma 3924A, was stimulated 8-9 fold by several different polymers of polylysine, polyornithine and random copolymers of lysine-alanine; spermidine, spermine, and mixtures of spermine and spermidine stimulated 2, 3, and 5 fold, respectively. The protein kinase was not stimulated by poly-carboxybenzyl-lysine, random copolymer of lysine-tyrosine, polyhistidine, polymethionine, polyglutamic acid, polyaspartic acid, dipeptide (Lys-Lys), lysine, ornithine, and putresine. The polyamine stimulation of the protein kinase was prevented by certain specific charged carbohydrates: heparin, chondroitin sulfates A, B, and C, dextran sulfate and hyaluronic acid. It was not prevented by noncharged carbohydrates: dextran, glycogen, starch, sucrose, etc; or by sulfate salts: ammonium sulfate, potassium sulfate, sodium thiosulfate, etc. The inhibition was reversed by increased polylysine. Heparin was non-competitive inhibitor of Mg2+-ATP. It would appear that this enzyme is regulated by certain highly specific molecules with certain sizes and charges; plus charge is stimulatory, negative charge prevents the stimulation.

Animals↗
PubMed1984

Catabolism of polyamines in the rat. Polyamines and their non-alpha-amino acid metabolites.

The metabolic fate of stable isotopically labeled polyamines was investigated after their first and second intraperitoneal injection in rats. Using gas chromatographic and mass fragmentographic analyses of acid-hydrolyzed 24-h urines, some aspects of the polyamine metabolism could be elucidated. After the injections with hexadeutero-1,3-diaminopropane, only labeled 1,3-diaminopropane was recovered from the urine samples. The rat injected with tetradeuteroputrescine excreted labeled putrescine, gamma-amino-n-butyric acid, 2-hydroxyputrescine and spermidine, while the urine samples of the rat after the injections with tetradeuterocadaverine contained labeled cadaverine and delta-aminovaleric acid. The injections of hexadeuterospermidine led to the appearance of labeled spermidine, isoputreanine, putreanine, N-(2-carboxyethyl)-4-amino-n-butyric acid, putrescine, gamma-amino-n-butyric acid, 1,3-diaminopropane, beta-alanine and spermine. After the injections with bis(2-carboxyethyl)-1,4-diaminobutane, spermidine, isoputreanine, putreanine, N-(2-carboxyethyl)-4-amino-n-butyric acid, putrescine, 1,3-diaminopropane, beta-alanine, 2-hydroxyputrescine and possibly gamma-amino-n-butyric acid were recovered. Clear differences between the metabolism after the first and second injection were noted for putrescine, spermidine and spermine, which is suggestive for enzyme induction and/or the existence of salvage pathways.

Animals↗
PubMed1983

Polyamine starvation causes parallel increase in nuclear and chromosomal aberrations in a polyamine-dependent strain of CHO.

Deprivation of polyamines and ornithine causes in a polyamine-dependent CHO strain aneuploidy and alterations in nuclear morphology including micronuclei, macronuclei, framented and bulged nuclei. There is also formation of multinucleate cells. The number of micronuclei and certain other nuclear aberrations increase concomitantly with chromosome abberrations.

Aneuploidy↗
PubMed2006

Alpha-methyl polyamines: efficient synthesis and tolerance studies in vivo and in vitro. First evidence for dormant stereospecificity of polyamine oxidase.

Efficient syntheses of metabolically stable alpha-methylspermidine 1, alpha-methylspermine 2, and bis-alpha,alpha'-methylated spermine 3 starting from ethyl 3-aminobutyrate are described. The biological tolerance for these compounds was tested in wild-type mice and transgenic mice carrying the metallothionein promoter-driven spermidine/spermine N(1)-acetyltransferase gene (MT-SSAT). The efficient substitution of natural polyamines by their derivatives was confirmed in vivo with the rats harboring the same MT-SSAT transgene and in vitro with the immortalized fibroblasts derived from these animals. Enantiomers of previously unknown 1-amino-8-acetamido-5-azanonane dihydrochloride 4 were synthesized starting from enantiomerically pure (R)- and (S)-alaninols. The studies with recombinant human polyamine oxidase (PAO) showed that PAO (usually splits achiral substrates) strongly favors the (R)-isomer of 4 that demonstrates for the first time that the enzyme has hidden potency for stereospecificity.

Animals↗
PubMed1983

Polyamine starvation causes accumulation of cadaverine and its derivatives in a polyamine-dependent strain of Chinese-hamster ovary cells.

Starvation of the polyamine-dependent Chinese-hamster ovary cells for ornithine or ornithine-derived polyamines in serum-free culture resulted in the formation of cadaverine and its aminopropyl derivatives, N-(3-aminopropyl)cadaverine and NN'-bis(3-aminopropyl)cadaverine. The synthesis of these unusual amines was inhibited by treatment of the cells with DL-2-difluoromethylornithine, a specific inhibitor of ornithine decarboxylase (EC 4.1.1.17). In the absence of ornithine (the normal substrate), ornithine decarboxylase thus appeared to catalyse the decarboxylation of lysine to cadaverine. Cell proliferation was markedly inhibited by ornithine deprivation of the cells, and further depressed by exposure of the cultures to difluoromethylornithine.

Animals↗