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PubMed2002

Influence of starter and nonstarter on the formation of biogenic amine in goat cheese during ripening.

Two commercial starters were investigated for their potential ability to decarboxylate amino acids during goat cheese ripening. Two batches of goat cheese were produced with identical pasteurized milk but different starter cultures. One of them contained Lactococcus lactis subsp. lactis and Lactococcus lactis subsp. cremoris and the other Lactococcus lactis subsp. lactis. The amine contents, microbial counts, proteolysis-related parameters, pH, total solids and salt content were studied in raw materials and cheeses. In raw materials, polyamines were the prevailing amines, whereas the main amines in cheeses were putrescine, tryptamine and, in particular, tyramine (94.59 mg/kg). Aerobic mesophilic microorganisms and Lactococcus counts increased throughout ripening, while Enterobacteriaceae were no longer detectable in cheese after 30 days of ripening. Amine concentration rose during cheese ripening in both batches. Moreover, the decarboxylase activity of microorganisms isolated from samples during cheese ripening was assayed and discussed.

Animals↗
PubMed2002

The influence of promoter and of electrode material on the cyclic voltammetry of Pisum sativum plastocyanin.

The reversible cyclic voltammetry of pea plastocyanin (Pisum sativum) was studied with a wide range of electrodes: edge-oriented pyrolytic graphite (PGE), glassy carbon (GCE), gold (Au) and platinum (Pt) electrodes. Plastocyanin was coated onto the electrode surface by exploiting the electrostatic interaction between the negatively charged protein and a wide range of positively charged promoters. The effect of the redox response with an extended range of promoters, including poly-L-lysine, polymyxin B, neomycin, tobramycin, geneticin, spermine and spermidine, were included in this study. The resulting cyclic voltammograms reveal that the observed midpoint potential for plastocyanin can be shifted significantly depending on the choice of promoter. The stability of the negatively charged plastocyanin-promoter layer on an electrode was gauged by the rate of bulk diffusion of the protein from the immobilised film into the solution. Reversible cyclic voltammograms were obtained using edge-oriented pyrolytic graphite (PGE) and glassy carbon electrodes (GCE) with all promoters; however, platinum and gold electrodes were unable to sustain a defined redox response. The combination of pyrolytic graphite electrode/poly-L-lysine/plastocyanin was found to be the most stable combination, with a redox response which remained well defined in solution for more than 1 h at pH 7.0. The midpoint potentials obtained in this manner differed between the two graphite electrodes PGE and GCE using poly-L-lysine as the promoter. This effect was in addition to the expected pH dependence of the midpoint potential for plastocyanin and the results indicated that the pK(a) for plastocyanin on PGE was 4.94 compared to that on GCE of 4.66. It is concluded that both the electrode material and the nature of the promoter can influence the position of the redox potentials for proteins measured in vitro. This study extends the range of biogenic promoters used in combination with electrode materials. Thus, we can begin to develop a more comprehensive understanding of electrode-protein interactions and draw conclusions as to metalloprotein function, in vivo. To support these studies, we have sought information as to the nature of the electrode/promoter/protein interaction using scanning tunneling microscopy (STM) to study both the promoter and the plastocyanin protein on a gold surface.

Biogenic Amines↗
PubMed1991

Molecular features necessary for the uptake of diamines and related compounds by the polyamine receptor of rat lung slices.

The influence of 17 putrescine analogues on the uptake of putrescine and/or paraquat by rat lung slices has been determined. Most of these compounds are competitive inhibitors of putrescine and/or paraquat uptake, but three show no inhibiting activity. Apparent Ki values of the putrescine derivatives increase, and thus the inhibitory effects decrease, with increasing N-methylation. Comparison of N-methyl-1,4-diaminobutane (Ki = 8 microM) with N,N'-bis-methyl-1,4-diaminobutane (Ki = 25.5 microM) shows that a single primary amino group is desirable for high inhibiting activity. Dimethylation at one amino function does not greatly decrease inhibitory potential (thus N,N-dimethyl-1,4-diaminobutane has Ki = 11.5 microM). Increasing the size of N-alkyl substituents in putrescine derivatives, decreased their inhibitory action on the uptake of putrescine. Investigation of the effect of conformationally-restricted analogues of putrescine shows that both (E) and (Z) isomers of 1,4-diaminobut-2-ene are poor inhibitors of putrescine uptake. Analogues of putrescine with bulky substituents on the butyl chain, i.e. the meso- and rac-isomers of 1,1-dichloro-2,3-diaminomethylcyclopropane, do not inhibit putrescine uptake. Inhibiting putrescine derivatives which contain aziridine groups are competitive inhibitors of putrescine and paraquat uptake. Surprisingly, N-(4-aminobutyl)aziridine is the most effective inhibitor of putrescine uptake studied, and is a better inhibitor of paraquat uptake than the endogenous polyamine, putrescine. N-(4-Aminobutyl)aziridine binds reversibly to the polyamine transporter and its inhibitory effects do not appear to be due to any cytotoxic activity of the aziridine. The parameter A (mM)-1 defined as 1000/Ki (where Ki units are microM) was taken as a measure of the affinity of a compound for the polyamine receptor in this paper.

Affinity Labels↗
PubMed2000

Interaction of histamine and other bioamines with cytochromes P450: implications for cell growth modulation and chemopotentiation by drugs.

We have characterized microsomal and nuclear histamine sites, designated H(IC), through which this amine acts as an intracellular mediator of platelet aggregation and lymphocyte mitogenesis. A major proportion, at least, of the microsomal H(IC) sites are on cytochromes P450, an important family of microsomal enzymes that are present in all cells, but most abundant in the liver. These enzymes are involved in the metabolism of xenobiotics and natural substrates, including lipid hormones that modulate gene function and cell growth. We have shown that polyamines, hormones (including estrogen, testosterone and progesterone), antihormones (including tamoxifen and flutamide) and various antidepressants and antihistamines, all inhibit histamine binding to P450; we have postulated that, through binding to the heme moiety, intracellular histamine regulates cell function by modulating the catalytic activity of P450 enzymes, an action that may be perturbed by endogenous and exogenous substances. We now demonstrate that, in addition to histamine, melatonin and the biogenic amines dopamine, serotonin and noradrenaline bind to P450 isozymes and to cytochrome C. Thus, heme enzymes in general may represent common targets where multiple bioamines, hormones and drugs interact to influence cell function and growth.

Animals↗
PubMed1994

Allosteric interactions and modulator requirement for NMDA receptor function.

Activation of NMDA receptors by glutamate, glycine and spermine was assessed using non-equilibrium [3H]dizocilpine binding. Glutamate and glycine mutually increased their efficacies and affinities to stimulate [3H]dizocilpine binding, which were further increased by spermine. Enhancement curves by glycine in the presence of increasing concentrations of the glycine antagonist 7-chlorokynurenate revealed that spermine markedly increased the affinity of glycine but not that of 7-chlorokynurenate, and that glycine was also required for [3H]dizocilpine binding in the presence of spermine. Spermine had a biphasic effect on [3H]dizocilpine binding, with a stimulatory phase followed by an inhibitory phase. The potency of spermine for both phases was increased by glutamate, but not by glycine. These observations indicate that there are positive cooperative interactions between the glutamate, the glycine and the stimulatory and inhibitory polyamine sites of the NMDA receptor. Moreover, glutamate and glycine, but not spermine, are required to activate the receptor.

Allosteric Regulation↗
PubMed1989

Stimulus-secretion coupling of arginine-induced insulin release: metabolism of L-arginine and L-ornithine in tumoral islet cells.

The metabolism of L-arginine and L-ornithine was examined in tumoral islet cells of the RINm5F line and compared to the situation previously characterized in normal rat islets. The maximal velocity of arginase in cell homogenates, as well as either the production of 14C-urea or the steady-state content of 14C-labelled ornithine in intact cells exposed to L-[U-14C]arginine were about one order of magnitude lower in tumoral than normal islet cells. The activity of ornithine-glutamate transaminase was similar in both cell types, and this coincided with a comparable rate of 14C-labelled L-glutamate generation by intact cells exposed to L-[1-14C]ornithine. Despite a comparable cell content in 14C-labelled ornithine of normal and tumoral cells exposed to exogenous ornithine, the rate of di- and polyamine generation was about one order of magnitude higher in tumoral than normal islet cells, this coinciding with a much higher activity of ornithine decarboxylase in RINm5F cell than islet homogenates.

Adenoma, Islet Cell↗
PubMedDate not supplied

[Method of determining low-molecular weight oligoamines in various biological materials].

A modified procedure is described for thin-layer chromatography of dansyl-spermine, -spermidine, -cadaverine and -putrescine. Distinct separation of the dansyl derivatives studied from dansyl-ammonium, which usually causes difficulties, was achieved. This procedure enabled to estimate the pyckomolar quantities of biogenic oligoamines. The method does not require radioactive compounds, enables to carry out the measurements without the use of spectrofluorimeter or fluorescent densitometer. The densitometry of the chromatogram photo-prints was successfully used for quantitative estimation of the oligoamines.

Animals↗
PubMed2006

[Development of highly sensitive determination of biogenic compounds by high-performance liquid chromatography with pre-column fluorescence derivatization].

A sensitive fluorescent labeling reagent, 4-(5,6-dimethoxy-2-phthalimidinyl)-2-methoxyphenylsulfonyl chloride (DMS-Cl), for the determination of amino compounds in HPLC was developed. DMS-Cl reacted with amino compounds in the basic medium to produce the corresponding fluorescent sulfonamides (excition 318 nm, emission 406 nm in aqueous acetonitrile). When amino acids were analyzed using reverse-phase HPLC, the detection limits (signal-to-noise ratio = 3) of almost all amino acids labeled with DMS-Cl were less than 5 fmol/injection. DMS-Cl was utilized for highly sensitive determination of amino compounds in biological samples and HPLC methods for determination of prolyl dipeptides, Pro and Hyp, in serum and urine, pipecolic acid in serum, taurine in plasma, and free and N-acetylated polyamine in urine were established. As these proposed methods are highly sensitive and reproducible and require only a small amount of biological sample, they may be useful for clinical and biochemical research.

Amino Acids↗
PubMed1997

Spermine inhibits proinflammatory cytokine synthesis in human mononuclear cells: a counterregulatory mechanism that restrains the immune response.

The local production of proinflammatory cytokines mediates the host response to inflammation, infection, and injury, whereas an overexpression of these mediators can injure or kill the host. Recently, we identified a class of multivalent guanylhydrazone compounds that are effective inhibitors of proinflammatory cytokine synthesis in monocytes/macrophages. The structure of one such cationic molecule suggested a molecular mimicry with spermine, a ubiquitous endogenous biogenic amine that increases significantly at sites of inflammation and infection. Here, we addressed the hypothesis that spermine might counterregulate the innate immune response by downregulating the synthesis of potentially injurious cytokines. When spermine was added to cultures of human peripheral blood mononuclear cells stimulated with lipopolysaccharide (LPS), it effectively inhibited the synthesis of the proinflammatory cytokines tumor necrosis factor (TNF), interleukin-1 (IL-1), IL-6, MIP-1alpha, and MIP-1beta. The inhibition of cytokine synthesis was specific and reversible, with significant inhibition of TNF synthesis occurring even when spermine was added after LPS. The mechanism of spermine-mediated cytokine suppression was posttranscriptional and independent of polyamine oxidase activity. Local administration of spermine in vivo protected mice against the development of acute footpad inflammation induced by carrageenan. These results identify a distinct molecular counterregulatory role for spermine in downregulating the monocyte proinflammatory cytokine response.

Animals↗
PubMed1996

Characterization of the arylalkylamine N-acetyltransferase in Onchocerca volvulus.

The characteristics and kinetic properties of an arylalkylamine N-acetyltransferase were studied in partially purified preparations of the human filarial parasite Onchocerca volvulus. The enzyme, which had a relative molecular mass (M(r)) of 37-38 kDa, catalyzed the acetylation of arylalkylamines but did not accept arylamines or polyamines as substrates. The optimal pH for enzyme activity was found to be 8.5 in TRIS-HCI. The apparent Michaelis constant (K(m)) and maximum velocity (Vmax) determined from Lineweaver-Burk plots for tryptamine were 1.8 microM and 29 nmol min-1 mg protein-1, respectively. Except for the catecholamines, the other arylalkylamines such as 5-hydroxytryptamine (5-HT), tyramine, and octopamine similarly exhibited high affinities and reaction rates. Whereas the enzyme is inhibited by metals and p-chloro-mercuribenzoate, it is inactivated neither by amethopterin nor by cystamine and is thereby distinguished from the mammalian arylamine N-acetyltransferase. Like other N-acetyltransferases whose function is the regulation of intracellular amine levels, the enzyme may have a role in the inactivation of excess biogenic amine in this parasite.

Animals↗
PubMed1990

Polyamine accumulation and vasogenic oedema in the genesis of late delayed radiation injury of the central nervous system (CNS).

Polyamine (PA) accumulation has been associated with blood-brain barrier (BBB) disruption and vasogenic oedema after cold injury. PAs and water content were measured in a rat spinal cord model of late-delayed radiation injury and were found to be elevated at paralysis. The elevated PA levels could be significantly reduced by treatment with difluoromethylornithine (DFMO). In unirradiated rats DFMO reduced putrescine to undetectable levels after 10-12 weeks. These data suggest that blockade of PA synthesis may be useful in treating the vasogenic oedema of radiation injury and may improve CNS radiation tolerance.

Animals↗
PubMed1998

Crystal structure and mutational analysis of the Escherichia coli putrescine receptor. Structural basis for substrate specificity.

PotF protein is a periplasmic substrate-binding protein of the putrescine transport system in Escherichia coli. We have determined the crystal structure of PotF protein in complex with the substrate at 2.3-A resolution. The PotF molecule has dimensions of 54 x 42 x 30 A and consists of two similar globular domains. The PotF structure is reminiscent of other periplasmic receptors with a highest structural homology to another polyamine-binding protein, PotD. Putrescine is tightly bound in the deep cleft between the two domains of PotF through 12 hydrogen bonds and 36 van der Waals interactions. The comparison of the PotF structure with that of PotD provides the insight into the differences in the specificity between the two proteins. The PotF structure, in combination with the mutational analysis, revealed the residues crucial for putrescine binding (Trp-37, Ser-85, Glu-185, Trp-244, Asp-247, and Asp-278) and the importance of water molecules for putrescine recognition.

Base Sequence↗
PubMed2000

Combined ion-pair extraction and gas chromatography-mass spectrometry for the simultaneous determination of diamines, polyamines and aromatic amines in Port wine and grape juice.

An accurate and very sensitive method which allows for the simultaneous determination of the diamines (1,3-diaminopropane, putrescine and cadaverine), of the polyamines (spermidine and spermine), and of the aromatic amines (beta-phenylethylamine and tyramine) found in Port wines and corresponding grape juices is presented. Sample clean-up consisted of the extraction of the amines with the ion-pairing reagent bis-2-ethylhexylphosphate dissolved in chloroform followed by a back-extraction with 0.1 M HCl. The hydrochloric extract obtained was dried and the amines were further derivatized with heptafluorobutyric anhydride and analyzed by GC-MS in the selected ion-monitoring mode, with a total run time of 18 min. Under the adopted conditions, the extraction of all the studied compounds was almost complete and the obtained extracts were free of potential interferents present in the samples, namely sugars, and most of the amino acids and polyphenols. Via the use of a set of five selected internal standards (amphetamine, [2H8]putrescine, 1,7-diaminoheptane, norspermidine and norspermine), the data obtained from the linearity, repeatability and recovery experiments were very good for all the compounds assayed. The corresponding limits of detection were invariably below 10 microg l(-1). The method was successfully applied to measure the content of biogenic amines in twelve young and five aged Port wine samples, eleven grape juice samples as well as in ten Portuguese red and white table wines. Results are presented and briefly discussed.

Amines↗
PubMed1991

Protection from chlordecone-amplified carbon tetrachloride toxicity by cyanidanol: regeneration studies.

Previous work has shown that chlordecone (CD)-amplified CCl4 hepatotoxicity and lethality can be mitigated by pretreatment with cyanidanol. These studies also revealed that stimulated hepatocellular regeneration might play an important role in the cyanidanol protection of CD-amplified CCl4 toxicity. The present studies conducted over a time course of 0 to 120 hr after CCl4 challenge describe sequential changes in hepatic [3H]thymidine incorporation into hepatocellular nuclear DNA, polyamines and related enzymes, and histomorphometry of liver sections from variously treated rats. Male Sprague-Dawley rats (125-150 g) were maintained on a control diet or on a diet contaminated with CD (10 ppm) for 15 days and/or pretreated with cyanidanol (250 mg/kg, ip) at 48, 24, and 2 hr before a single ip injection of either a standard protocol dose (100 microliters/kg) or a low dose (50 microliters/kg, L) of CCl4 on Day 16 of the dietary protocol. Cyanidanol pretreatment significantly stimulated the hepatic [3H]thymidine incorporation into hepatocellular nuclear DNA of control rats irrespective of CD pretreatment. Similarly, polyamine metabolism was altered favorably for cell division, although mitotic index (metaphase) was not increased. Cyanidanol-stimulated [3H]thymidine incorporation was highly suppressed in rats receiving the CD + CCl4 standard dose combination treatment up to 36 hr, but after this time point a marked increase was observed. Hepatocellular regeneration, quantified histomorphometrically as volume density of cells in metaphase, was progressively increased in rats protected from CD + CCl4 interaction by cyanidanol, starting at 36 hr and lasting until 72 hr. Favorably altered polyamine metabolism was evident from the stimulated ornithine decarboxylase, as well as from the stimulated interconversion of the higher polyamines to maintain increased concentration of putrescine. Challenge by the same dose of CCl4 (100 microliters/kg) to CD-pretreated rats not protected by cyanidanol failed to cause any increase in [3H]thymidine incorporation up to 36 hr and resulted in animal death starting at 36 hr. In the surviving rats, [3H]thymidine incorporation at 48 hr was increased, but was less than 50% of the increase observed in the cyanidanol group. In these rats, attenuation in the stimulation of cell division and insufficiently increased putrescine levels were observed, which are consistent with the inadequate level of hepatocellular regeneration. With rats receiving CD + CCl4(L) combination, the [3H]thymidine incorporation at 48 hr was less than 50% of the increase of cyanidanol-protected rats. Cyanidanol pretreatment to the CD + CCl4 group of rats prevented the decrease in the hepatic DNA levels.(ABSTRACT TRUNCATED AT 400 WORDS)

Adenosylmethionine Decarboxylase↗
PubMed1995

Purification and kinetic characterization of gamma-aminobutyraldehyde dehydrogenase from rat liver.

Oxidative deamination of putrescine, the precursor of polyamines, gives rise to gamma-aminobutyraldehyde (ABAL). In this study an aldehyde dehydrogenase, active on ABAL, has been purified to electrophoretic homogeneity from rat liver cytoplasm and its kinetic behaviour investigated. The enzyme is a dimer with a subunit molecular weight of 51,000. It is NAD(+)-dependent, active only in the presence of sulphhydryl compounds and has a pH optimum in the range 7.3-8.4. Temperatures higher than 28 degrees C promote slow activation and the process is favoured by the presence of at least one substrate. Km for aliphatic aldehydes decreases from 110 microM for ABAL and acetaldehyde to 2-3 microM for capronaldehyde. The highest relative V-values have been observed with ABAL (100) and isobutyraldehyde (64), and the lowest with acetaldehyde (14). Affinity for NAD+ is affected by the aldehyde present at the active site: Km for NAD+ is approximately 70 microM with ABAL, approximately 200 microM with isobutyraldehyde and capronaldehyde, and > 800 microM with acetaldehyde. The kinetic behaviour at 37 degrees C is quite complex; according to enzymatic models, NAD+ activates the enzyme (Kact approximately 500 microM) while NADH competes for the regulatory site (Kin approximately 70 microM). In the presence of high NAD+ concentrations (4 mM), ABAL promotes further activation by binding to a low-affinity regulatory site (Kact approximately 10 mM). The data show that the enzyme is probably an E3 aldehyde dehydrogenase, and suggest that it can effectively metabolize aldehydes arising from biogenic amines.

Adenine Nucleotides↗
PubMed1990

Polyamine regulation of heat-shock-induced spermidine N1-acetyltransferase activity.

The enzyme spermidine/spermine N1-acetyltransferase (N1-SAT) is rapidly induced by heat shock in CHO and A549 cells, with activity declining by 24 h. Depletion of intracellular polyamines by alpha-difluoromethylornithine, an inhibitor of ornithine decarboxylase, blocks this induction. Re-addition of putrescine to these cultures restores the response to heat shock, with a concomitant increase in intracellular N1-acetylspermidine. Diaminopropane is more than twice as effective as the naturally occurring diamine putrescine, suggesting that the propylamine moiety of spermidine is involved in the regulation of N1-SAT induction. Inhibitor studies indicate transcriptional activation and that the enzyme has an apparent half-life of 30-60 min. A second heat shock rapidly inhibits induced N1-SAT activity, which decays with a half-life of 2-3 min. Despite its induction by heat, N1-SAT is not a stable enzyme, suggesting that the activity observed is not due to a modification of an existing peptide, but is due to a transcriptional event, which may justify the inclusion of this enzyme in the family of heat-shock proteins.

Acetyltransferases↗
PubMed2000

Interactive binding at cytochrome P-450 of cell growth regulatory bioamines, steroid hormones, antihormones, and drugs.

The virtually universal family of P-450 isozymes contribute to the regulation of cell growth by modulating the levels of steroids and other lipid messengers for cytoplasmic and nuclear processes, including gene expression. In microsomes from rat liver cells, the concentration ( approximately 1 nmole/mg protein) of cytochromes P-450 approximates that of intracellular binding sites (K(d) 1.0-50 microM) for histamine. The potencies of certain therapeutic drugs to inhibit catalytic activity of, and histamine binding to, cytochromes P-450 in vitro were previously shown by us to be predictive of relative propensities to modulate tumor growth in rodents. Also, we demonstrated that growth-regulating polyamines potently interact with histamine at P-450. We now show that several classes of steroid hormones, antiestrogens, and antiandrogens, as well as various arylalkylamine drugs, all potently inhibit (3)H-histamine binding to cytochrome P-450 (K(i) values: testosterone 0.28 microM, progesterone 0.56 microM, flutamide 1.7 microM, tamoxifen 9.0 microM). Furthermore, all the various hormone and drug ligands are mutually inhibitory in their binding to cytochrome P-450; e.g., K(i) values of androstenedione and progesterone, to inhibit imipramine binding to P-450 (determined by spectral analysis), are 11 nM and 26 nM, respectively. The K(i) value of imiprimine to inhibit binding of androstenedione to P-450 is 3.5 microM. We estimate the total P-450 content in microsomes to be greater in male than in female rats and correlated with the number of binding sites for histamine, but not for steroids and drugs that appear to be more selective for P-450 isozymes. Thus, for at least some isozymes, the homeostatic role of the monooxygenases may be governed by histamine, modulated by endogenous ligands, and perturbed by many foreign molecules.

Animals↗
PubMed1996

Motor actions of eliprodil in the normal and monoamine-depleted mouse: a role in the treatment of Parkinson's disease?

The non-competitive NMDA polyamine site antagonist, eliprodil, was examined for its effects on exploratory activity in non-habituated mice and for its antiakinetic potential in reserpine-treated mice. A low dose of eliprodil (5 mg/kg) weakly stimulated locomotion in naive animals, whilst higher doses depressed rearing (20-40 mg/kg) and grooming (40 mg/kg), consistent with a sedative action. At no dose did eliprodil cause ataxia. In 24 h reserpine-treated mice, eliprodil (10-40 mg/kg) reversed akinesia, but this effect was subject to considerable inter-animal variation and was not statistically significant. Eliprodil did not alter the motor recovery elicited by the dopamine D1 agonist SKF 38393, or the dopamine D2 agonist RU 24213, and suppressed the motor stimulation induced by L-DOPA. These results indicate that eliprodil displays a far lower propensity than many other NMDA receptor antagonists for disturbing posture and gait, but lacks the essential motor stimulant action required to make it a safe and effective antiparkinsonian agent, at least in the reserpine-treated mouse model of Parkinson's disease.

2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-ben↗