Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Biogenic Polyamines”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1996

DNA triple helix stabilization by bisguanidinyl analogues of biogenic polyamines.

The polycationic nature of biogenic polyamines such as spermine (SPM, 1) and spermidine (SPD, 2) plays an important role in selective binding to polyanionic nucleic acids. These interactions are mediated by electrostatic and hydrogen bonding forces which led to stabilization of DNA duplexes and triplexes. Transformation of primary amino groups in these molecules into corresponding guanidinium functions is expected to amplify the electrostatic component resulting in improved binding. An easy chemical transformation route as described here gives rise to bisguanidinated derivatives of spermine (SPMG, 3) and spermidine (SPDG, 4). Both enhances DNA duplex stability over the parent polyamines whereas SPMG is more selective for stabilization of DNA triplexes even at pH 7.0. The results have implication for designing of new DNA binding ligands.

Base Sequence↗
PubMed1993

High-performance liquid chromatographic separation of biogenic polyamines using 2-(1-pyrenyl)ethyl chloroformate as a new fluorogenic derivatizing reagent.

The application of a new fluorogenic pre-column derivatizing reagent, 2-(1-pyrenyl)ethyl chloroformate (PEOC), is reported for the separation and detection of biogenic polyamines using column liquid chromatography. The development of the method included the optimization of excitation and emission wavelengths, efficient gradient programming, derivatization temperature, time, and pH. Minimum detection limits, linear ranges, reproducibility, and recovery from analyzed samples were determined. The procedure was applied to hydrolyzed serum samples taken from healthy individuals and cancer patients. Separation of PEOC-derivatized polyamines from the serum hydrolysis by-products was successful and detection limits were more favorable than those previously reported for 9-fluorenyl-methyl chloroformate-derivatized polyamines.

Biogenic Amines↗
PubMed1999

The non-enzymatic hydrolysis of oligoribonucleotides VI. The role of biogenic polyamines.

Single-stranded oligoribonucleotides containing UA and CA phosphodiester bonds can be hydrolyzed specifically under non-enzymatic conditions in the presence of spermidine, a biogenic amine found in a wide variety of organisms. In the present study, the rate of oligonucleotide and tRNA(i)(Met)hydrolysis was measured in the presence of spermidine and other biogenic amines. It was found that spermine [H(3)N(+)(CH(2))(3)(+)NH(2)(CH(2))(4)(+)NH(2)(CH(2))(3)(+)NH(3)] and putrescine [H(3)N(+)(CH(2))(4)(+)NH(3)] can replace spermidine [H(3)N(+)-(CH(2))(4)(+)NH(2)(CH(2))(3)(+)NH(3)] to induce the hydrolysis. For all three polyamines, a bell-shaped cleavage rate versus concentration relationship was observed. The maximum rate of hydrolysis was achieved at 0.1, 1.0 and 10 mM spermine, spermidine and putrescine, respectively. Moreover, we found that the hydrolysis requires at least two linked amino groups since two aminoalcohols, 2-aminoethanol and 3-aminopropanol, were not able to induce the cleavage of the phospho-diester bond. The optimal cleavage rate of the oligo-ribonucleotides was observed when amino groups were separated by tri- or tetramethylene linkers. The methylation of the amino groups reduced the ability of diamines to induce oligoribonucleotide hydrolysis. Non-enzymatic cleavage of tRNA(i)(Met)from Lupinus luteus and tRNA(i)(Met)from Escherichia coli demonstrate that both RNAs hydrolyze as expected from principles derived from oligoribonucleotide models.

Biogenic Polyamines↗
PubMed1996

[New aminooxy analogs of biogenic polyamines].

A series of structural analogs of putrescine, spermidine, and spermine with the aminomethylene fragment substituted by the aminooxy group was suggested. The synthesis of the new aminooxy analogs of spermine was described. Biochemical aspects of the activity of the aminooxy analogs of polyamines were discussed in respect of their selective inhibition of normal and leukemic cells.

Animals↗
PubMed1982

Development of polyamine and biogenic amine systems in brains and hearts of neonatal rats given dexamethasone: role of biochemical alterations in cellular maturation for producing deficits in ontogeny of neurotransmitter levels, uptake, storage and turnover.

Excessive levels of glucocorticoids are thought to interfere with synaptic development in the central nervous system. In the present study, dexamethasone given to newborn rats produced deficits in brain growth associated with shifts in the developmental pattern of the ornithine decarboxylase/polyamine system consistent with delays in cellular maturation. The effects on the brain were of smaller magnitude and shorter duration than those on the heart or on general growth and were indicative of "brain sparing." Although some biochemical indices of synaptic development of central noradrenergic systems ([3H]norepinephrine uptake into synaptosomes) were quantitatively deficient on a whole-brain basis, the reductions never exceeded the magnitude of effect on brain weight; for other indices (transmitter levels, [3H]norepinephrine into synaptic vesicles), there were little or no apparent developmental deficits. Thus, the effects of dexamethasone on synaptic development in the brain may not reflect a specific action of glucocorticoids over and above their more general effects on cellular maturation. In contrast to the lack of specific action on biochemical indices of synaptic outgrowth, neonatal dexamethasone did cause alterations in norepinephrine synthesis and turnover in both central and peripheral sympathetic neurons which could contribute to the physiological and behavioral abnormalities associated with glucocorticoid treatment during development.

Animals↗
PubMed1974

Enzymatic methylations: III. Cadaverine-induced conformational changes of E. coli tRNA fMet as evidenced by the availability of a specific adenosine and a specific cytidine residue for methylation.

A partially purified tRNA methylase fraction from rat liver, containing m(2)G- m(1)A- and m(5)C-methylase, was used to study the influence of Mg(++) and of the biogenic polyamine cadaverine on the enzymatic methylation of E.coli tRNA(fMet)in vitro. In presence of 1 or 10 mM Mg(++), guanosine no. 27 was methylated to m(2)G. In 1 mM Mg(++) plus 30 mM cadaverine, guanosine in position 27 and adenosine in position 59 were methylated. In presence of 30 mM cadaverine alone tRNA(fMet) accepted three methyl groups: in addition to guanosine no. 27 and adenosine no. 59 cytidine no. 49 was methylated. In order to correlate tRNA(fMet) tertiary structure changes with the methylation patterns, differentiated melting curves of tRNA(fMet) were measured under the methylation conditions. It was shown that the thermodynamic stability of tRNA(fMet) tertiary structure is different in presence of Mg(++), or Mg(++) plus cadaverine, or cadaverine alone. From the differentiated melting curves and from the methylation experiments one can conclude that at 37 degrees in the presence of Mg(++) tRNA(fMet) has a compact structure with the extra loop and the TpsiC-loop protected by tertiary structure interactions. In Mg(++) plus cadaverine, the TpsiC-loop is available, while the extra loop is yet engaged in teritary structure (G-15: C-49) interactions. In cadaverine alone, the TpsiC-loop and the extra loop are free; hence under these conditions the open tRNA(fMet) clover leaf may be the substrate for methylation. In general, cadaverine destabilizes tRNA tertiary structure in the presence of Mg(++), and stabilizes tRNA(fMet) tertiary structure in the absence of Mg(++). This may be explained by a competition of cadaverine with Mg(++) for specific binding sites on the tRNA. On the basis of these experiments a possible role of biogenic polyamines in vivo may be discussed: as essential components of procaryotic and eucaryotic ribosomes they may together with ribosomal factors facilitate tRNA-ribosome binding during protein biosynthesis by opening the tRNA tertiary structure, thus making the tRNA's TpsiC-loop available for interaction with the complementary sequence of the ribosomal 5S RNA.

Adenosine↗
PubMed1989

Polyamines induce precocious development in rats. Possible interaction with growth factors.

The study reports the effects of daily subcutaneous injections of the biogenic polyamines putrescine, spermidine and spermine (10 mg/kg each) given for a short postnatal period, on growth and development of rats. Polyamine treatment, while only slightly enhancing normal body weight gain, prevented the weight loss caused by surgical injury of 5-day-old animals. The treatment resulted in earlier eyelid and ear opening and in earlier maturation of righting and gripping responses. Increased number of neurons in the superior cervical ganglion that is caused by polyamine treatment, could not be prevented by castration of newborn rats, thus excluding the testes as a site through which polyamines may exert their action. An apparent increase in immunohistochemically detectable nerve growth factor was evident in iris and submaxillary salivary gland of polyamine-treated animals, but no change in epidermal growth factor immunohistochemistry was detected in the salivary gland. We conclude: (1) treatment of newborn rats with polyamines can accelerate somatic and neurobehavioral development; (2) further studies are required in order to verify and quantitate the effects of polyamines on growth factors, and (3) the results imply that exogenous polyamines may exert their growth-promoting effects on a number of cell types when these cells experience periods of polyamine dependence.

Animals↗
PubMed1978

Polyamine interaction with pregnancy serum in suppression of lymphocyte transformation.

Biogenic polyamines interacting with pregnancy serum elicit potent suppression of lymphocyte transformation in vitro. Within the assay limits, activity was first shown after about 15 weeks' gestation and reached its highest level at about 28 weeks. This level was maintained until term. It is thought that specific humoral amine oxidases were the cause. Fetal-cord serum and non-pregnancy serum were inactive. This system may have an immunoregulatory function in pregnancy.

Animals↗
PubMed1998

Effects of polyamine levels on the degradation of short-lived and long-lived proteins in cultured L-132 human lung cells.

Biogenic polyamines have important regulatory functions in various biological processes and it has also been suggested that they could modulate intracellular protein degradation. For an overall assessment of the role of polyamines in this process, we have investigated the effect that the decrease in intracellular polyamine levels caused by inhibitors of polyamine biosynthesis brings about on the degradation of the pools of short- and long-lived proteins in cultured L-132 human lung cells. Treatment of cells with 100 microM (2R,5R)-delta-methyl acetylenic putrescine (MAP), a potent enzyme-activated irreversible inhibitor of ornithine decarboxylase, or with 100 microM MAP plus 50 microM N-butyl 1,3-diaminopropane, a specific inhibitor of spermine synthase, caused a similar decrease (65-70% of control) in the total intracellular levels of polyamines, although they affected the concentrations of spermidine and spermine differently. The effect of the two treatments on protein degradation was essentially the same. In polyamine-depleted cells we observed an inhibition of degradation in long-lived proteins of 16% (P<0.05), with a significant increase in the half-life (t12) of this pool from 100.5 to 120.1 h. This was concomitant with an increase of 26% (P<0. 05) in degradation in short-lived proteins, with a significant decrease in the t12 of this pool from 0.85 to 0.67 h. Recovery of polyamine levels by the addition of 50 microM spermidine to polyamine-depleted cells resulted in a restoration of the degradation rates in both pools of proteins. The way(s) by which polyamines could modulate proteolysis are discussed.

Alkynes↗
PubMed1988

Early polyamine treatment enhances survival of sympathetic neurons after postnatal axonal injury or immunosympathectomy.

We have recently demonstrated that following injury of their axon, sympathetic neurons of the rat superior cervical ganglion become dependent on polyamine synthesis for their survival. In addition we have observed that the treatment of newborn rats with biogenic polyamines can prevent the naturally occurring reduction in the number of neurons in the ganglion. In the present study groups of newborn rats were subjected to either postganglionic nerve crush (axotomy) or to treatment with antiserum to nerve growth factor (immunosympathectomy), two treatments which result in a massive loss of neurons in the ganglion. Daily injections of the polyamines putrescine, spermidine and spermine (10 mg/kg each), for 7 days after the operation to the axotomized group, and for 9 days starting with the first antiserum injection to the immunosympathectomized group, attenuated the nerve cell loss. The polyamine treatment also attenuated the reduction in the activity of the neurotransmitter-synthesizing enzyme tyrosine hydroxylase observed after both axotomy and immunosympathectomy in the ganglion. These results further indicate that polyamines are important for the survival of sympathetic neurons and, while their mechanism of action is unknown, an interaction with nerve growth factor regulation cannot be excluded. In the iris, the reduction observed in [3H]norepinephrine uptake after the two noxious treatments was unproportionately small when compared to the large drop in the number of parent neurons in the ganglion. This suggests that compensatory mechanisms exist which act to adjust the number of functional axon terminals per neuron so that the number of terminals innervating the target remains relatively constant.

Animals↗
PubMedDate not supplied

Biomechanical signals in the coronary artery triggering the metabolic processes during cardiac overload.

Peculiarities in structure and deformability of epicardial conduit coronary arteries are described. The thin wall of animal coronary artery contrasts the human coronary artery in which the remarkable wall thickness is due namely by the intima thickness. Deformation in length and diameter of conduit coronary arteries, due to the left and right ventricle volume increase, has been defined in non-beating canine heart. Ramus interventricularis anterior being firmly tethered to the myocardium undergoes about 3 times larger deformation than ramus circumflexus. In anaesthetized dogs a 30% increase in blood pressure, elicited by aortic constriction, induces an increase in diameter of coronary artery, in segment length, in blood flow and consequently in shear stress which represents a load for circumferentially running smooth muscle bundles, longitudinally running smooth muscle bundles, as well as for the endothelium. The above load lasting 4 h is already reflected by an increase in total RNA content and [14C] leucin incorporation in the left ventricle myocardium in the wall of ramus interventricularis anterior, not in ramus circumflexus. The findings fit completely with the different range of deformation of both the above coronary branches and indicates an increase in proteosynthesis not only in myocardium, but in ramus interventricularis anterior as well. An increase in ornithindecarboxylase activity in coronary wall leading to an increase in biogenic polyamines, is present in the case only, when blood pressure increase is induced by infusion of noradrenaline.

Animals↗
PubMed1997

New findings concerning vertebrate porin.

Eukaryotic porin can be considered to be a good candidate for forming the channel component of the protein complex which, depending on the approach used, may realize its expression either as the outwardly-rectifying depolarization-induced chloride channel or as the volume-sensitive organic osmolyte-anion channel. As a basis for this proposition, we point to a series of correspondences in properties between mammalian porin and the ORDIC channel complex. Specifically, mammalian porin is expressed in the plasmalemma of different cells and chloride channels can be blocked by anti-human porin antibodies in astrocytes and endothelial cells. There is an indication of colocalisation of human porin and the cystic fibrosis (CF) gene product, CFTR, in the apical region of epithelial cells. The primary structure of porin from a CF patient was found to be normal. Cytosol and amniotic fluid fractions influence the channel characteristics of mammalian porin. Channel-active mammalian porin binds ATP and the stilbene disulphonate grouping of the chloride channel inhibitor DIDS. Human porin in black membranes is a pathway for taurine, and biogenic polyamines reduce the voltage dependence of human porin. Assuming the relationship between human porin and the ORDIC channel/VSOAC complex, studies on plasmalemma-integrated human porin have a relevance for CF research. In addition, we refer to a case study on a child with encephalomyopathy in which porin could not be detected using monoclonal anti-human porin antibodies. Our studies were based on purified and sequenced human porin from different cells and from different cell compartments. In addition, we raised antibodies against mature human porin or synthetic parts of the molecule. This provided a firm foundation for our topochemical work with which we were able to establish the multi-topological expression of eukaryotic porin channels. The data are summarized and discussed.

Amino Acid Sequence↗
PubMed1999

Spermine inhibition of monocyte activation and inflammation.

The innate immune system functions as a defensive front line against pathogenic invasion, but the proinflammatory products of activated monocytes and macrophages (e.g., TNF and NO) can also injure normal cells. Anti-inflammatory mediators restrain the innate immune response and prevent excessive collateral tissue damage. Spermine, a ubiquitous biogenic polyamine, specifically and reversibly suppresses the synthesis of monocyte proinflammatory cytokines. This may provide a counterregulatory mechanism to restrain monocyte activation in injured or infected tissues and in tumors where spermine levels are significantly increased. Here we show that monocyte spermine uptake was significantly increased following lipopolysaccharide stimulation. The polyamine analogue 1, 4-bis(3-aminopropyl)-piperazine (BAP) inhibited LPS-stimulated monocyte spermine uptake via the "nonselective" polyamine transporter. BAP fully restored macrophage TNF synthesis despite the presence of spermine, indicating that the mechanism of monocyte deactivation by spermine is dependent on spermine uptake. Administration of BAP in vivo significantly augmented the development of carrageenan-induced paw edema and nitric oxide release. Thus, endogenous spermine normally inhibits the innate inflammatory response by restraining macrophages.

Animals↗
PubMed1980

[Alteration of biogenic amines, serotonin, histamine and polyamines, in cases of diarrhea induced by various cathartics (author's transl)].

Effects of various cathartics on charcoal transport, permeability of blood vessels and biogenic amines (serotonin (5-HT), histamine (His), polyamines) in the small intestine of mice were investigated. Diarrhea was induced in mice by oral administration of magnesium sulfate, mannitol, dioctyl sodium sulfosuccinate (DSS), castor oil and pilocarpine. In diarrhea following ingestion of magnesium sulfate and mannitol, vascular permeability in the intestinal membrane accompanied release of His from the small intestine, but such was not so when diarrhea was induced by DSS and castor oil. In diarrhea induced by various cathartics, 5-HT and His were apparently not related to intestinal motility. Thus, alteration in polyamine metabolism in the small intestine may exert an influence on transport of substances in cases of diarrhea in mice.

Animals↗
PubMed1999

Polyamines. An overview.

The polyamines spermine, spermidine, and putrescine are small organic molecules one or more of which are present in all living organisms. Many natural products contain polyamine residues. Polyamines are synthesized by a highly regulated pathway from arginine or ornithine and also can be transported in and out of cells. Polyamines are degraded to a variety of compounds the functions of which are largely unknown. Polyamines influence the transcriptional and translational stages of protein synthesis, stabilize membranes, and, in mammalian systems, modulate neurophysiological functions and may act as intracellular messengers. However, at the molecular level the mode of action of the polyamines is largely unknown.

Animals↗