Biosynthesis of Cerebral Phenolic Amines. I. <i>In Vivo</i> Formation of <i>p</i>-Tyramine, Octopamine, and Synephrine

Boulton, Alan A.; Wu, P.H.

doi:10.1139/o72-037

Cited by 36 publications

(9 citation statements)

References 12 publications

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“…TA are produced by a wide range of organisms from bacteria to plants and vertebrates. In vertebrates, TA can be formed directly by the action of aromatic L-amino acid decarboxylase (AADC) on L-phenylalanine, L-tyrosine, and L-tryptophan, (Boulton and Wu, 1972;Saavedra, 1974;Silkaitis and Mosnaim, 1976;Dyck et al, 1983). TA production in bacteria has been mainly studied in food microorganisms, such as enterococci, lactobacilli, streptococci, lactococci, pediococci, and oenococci which represents the main producers of biogenic amines (Marcobal et al, 2006;Irsfeld et al, 2013;Williams et al, 2014;Barbieri et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

“…In mammalians, TA are synthesized by aromatic L-amino acid decarboxylases (AADC; EC 4.1.1.28) (Boulton and Wu, 1972;Snodgrass and Iversen, 1974;Silkaitis and Mosnaim, 1976;Dyck et al, 1983). Although AADC is widely accepted as the vertebrate synthetic enzyme for PEA, TYM, and TRY, the precursor amino acids are in fact extremely poor substrates for AADC (Christenson et al, 1970;Juorio and Yu, 1985;Gainetdinov et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

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The Neuromodulator-Encoding sadA Gene Is Widely Distributed in the Human Skin Microbiome

et al. 2020

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Trace amines (TA) are endogenously produced in mammals, have a low concentration in the central nervous system (CNS), but trigger a variety of neurological effects and intervene in host cell communication. It emerged that neurotransmitters and TA are produced also by the microbiota. As it has been shown that TA contribute to wound healing, we examined the skin microbiome of probands using shotgun metagenomics. The phyla Actinobacteria, Proteobacteria, Firmicutes, and Bacteroidetes were predominant. Since SadA is a highly promiscuous TA-producing decarboxylase in Firmicutes, the skin microbiome was specifically examined for the presence of sadA-homologous genes. By mapping the reads of certain genes, we found that, although there were less reads mapping to sadA than to ubiquitous housekeeping genes (arcC and mutS), normalized reads counts were still >1000 times higher than those of rare control genes (icaA, icaB, and epiA). At protein sequence level SadA homologs were found in at least 7 phyla: Firmicutes, Actinobacteria, Proteobacteria, Bacteroidetes, Acidobacteria, Chloroflexi, and Cyanobacteria, and in 23 genera of the phylum Firmicutes. A high proportion of the genera that have a SadA homolog belong to the classical skin and intestinal microbiota. The distribution of sadA in so many different phyla illustrates the importance of horizontal gene transfer (HGT). We show that the sadA gene is widely distributed in the human skin microbiome. When comparing the sadA read counts in the probands, there was no correlation between age and gender, but an enormous difference in the sadA read counts in the microbiome of the individuals. Since sadA is involved in TA synthesis, it is likely that the TA content of the skin is correlated with the amount of TA producing bacteria in the microbiome. In this way, the microbiome-generated TA could influence signal transmission in the epithelial and nervous system.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The Neuromodulator-Encoding sadA Gene Is Widely Distributed in the Human Skin Microbiome

et al. 2020

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“…In this regard, p-hydroxyphenylethanolamine (octopamine, OCT) has a wide species distribution and is present in mammalian cns (Molinoff & Axelrod, 1972). The substance accumulates in peripheral adrenergic neurons (Kakimoto & Armstrong, 1962) and various regions of the cns of rats (Boulton & Wu, 1971) following monoamine oxidase inhibition, the accumulated amine can be released by stimulation of adrenergic nerves (Kopin, 1968). p-Hydroxynorephedrine (PHN), a metabolite of amphetamine in some species, is found in heart (Goldstein & Anagnoste, 1965), spleen (Thoenen, Huerlimann & others, 1966) and brain (Groppetti & Costa, 1969;Brodie, Cho & Gessa, 1970;Lewander, 1970) following amphetamine administration and may act as a false transmitter in adrenergic neurons (Brodie & others, 1970).…”

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confidence: 99%

Microiontophoretic studies of the effects of false transmitter candidates and amphetamine on cerebellar Purkinje cells

Kostopoulos

Yarbrough

1975

Journal of Pharmacy and Pharmacology

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The effects of microiontophoretic applications of equivalent doses (ejection times and currents) of noradrenaline, amphetamine, octopamine and p-hydroxynorephedrine on the spontaneous firing of Purkinje and unidentified cells in the cerebellum of rats were examined. In addition, the effects of amphetamine of Purkinje cells were examined in animals pretreated with the tyrosine hydroxylase inhibitor, alpha-methyltyrosine (alpha-MpT) or with a combination of reserpine plus alpha-MpT. The results indicate that the "false transmitters" are weak agonists when compared to noradrenaline in inhibiting the firing of Purkinje cells. The results of the iontophoretic studies with amphetamine are not consistent with a pre-synaptic releasing effect by amphetamine at noradrenergic synapses in the cns since the efficacy of amphetamine on Purkinje cells was unaltered after pretreatment with alpha-MpT or alpha-MpT plus reserpine.

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“…Tyramine, octopamine, synephrine, dopamine, and epinephrine are biogenic amines that exist in a wide range of food products containing proteins or free amino acids such as meat products, dairy products, and fruits. 30,31 They are decarboxylation products derived from the amino acid L-tyrosine through different metabolism pathways, as shown in Figure 1. Many studies showed that these compounds are related to human metabolism and play an important role in stimulating lipolysis, oxidation of fat through increased thermogenesis, and regulating the nervous system.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Sequential Proton Loss Electron Transfer in Deactivation of Iron(IV) Binding Protein by Tyrosine Based Food Components

Tang

Skibsted

2017

J. Agric. Food Chem.

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The iron(IV) binding protein ferrylmyoglobin, MbFe(IV)═O, was found to be reduced by tyrosine based food components in aqueous solution through a sequential proton loss electron transfer reaction mechanism without binding to the protein as confirmed by isothermal titration calorimetry. Dopamine and epinephrine are the most efficient food components reducing ferrylmyoglobin to oxymyoglobin, MbFe(II)O, and metmyoglobin, MbFe(III), as revealed by multivariate curve resolution alternating least-squares with second order rate constants of 33.6 ± 2.3 L/mol/s (ΔH of 19 ± 5 kJ/mol, ΔS of -136 ± 18 J/mol K) and 228.9 ± 13.3 L/mol/s (ΔH of 110 ± 7 kJ/mol, ΔS of 131 ± 25 J/mol K), respectively, at pH 7.4 and 25 °C. The other tyrosine based food components were found to reduce ferrylmyoglobin to metmyoglobin with similar reduction rates at pH 7.4 and 25 °C. These reduction reactions were enhanced by protonation of ferrylmyoglobin and facilitated proton transfer at acidic conditions. Enthalpy-entropy compensation effects were observed for the activation parameters (ΔH and ΔS), indicating the common reaction mechanism. Moreover, principal component analysis combined with heat map were performed to understand the relationship between density functional theory calculated molecular descriptors and kinetic data, which was further modeled by partial least squares for quantitative structure-activity relationship analysis. In addition, a three tyrosine residue containing protein, lysozyme, was also found to be able to reduce ferrylmyoglobin with a second order rate constant of 66 ± 28 L/mol/s as determined by a competitive kinetic method.

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Biosynthesis of Cerebral Phenolic Amines. I. In Vivo Formation of p-Tyramine, Octopamine, and Synephrine

Cited by 36 publications

References 12 publications

The Neuromodulator-Encoding sadA Gene Is Widely Distributed in the Human Skin Microbiome

The Neuromodulator-Encoding sadA Gene Is Widely Distributed in the Human Skin Microbiome

Microiontophoretic studies of the effects of false transmitter candidates and amphetamine on cerebellar Purkinje cells

Sequential Proton Loss Electron Transfer in Deactivation of Iron(IV) Binding Protein by Tyrosine Based Food Components

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