Biogenic amines are low molecular weight organic nitrogen compounds. They are formed by the decarboxylation of amino acids or by amination and transamination of aldehydes and ketones during normal metabolic processes in living cells and therefore are ubiquitous in animals, plants, microorganisms, and humans. In food and beverages, they are formed by the enzymes of raw materials or are generated by microbial decarboxylation of amino acids. The structure of a biogenic amine can be aromatic and heterocyclic amines (histamine, tryptamine, tyramine, phenylethylamine, and serotonin); aliphatic di-, tri-, and polyamines (putrescine, cadaverine, spermine, spermidine, and agmatine); and aliphatic volatile amines (ethylamine, methylamine, isopentylamine, and ethanolamine). Many of them possess a strong pharmacologic effect, and others are important as precursors of hormones and components of coenzymes. The biogenic amine intoxication leads to toxicological risks and health hazards that trigger psychoactive, vasoactive, and hypertensive effects resulting from consumption of high amounts of biogenic amines in foods. The toxicological effects of biogenic amines increase when the mono- and diaminoxidase enzymes are deficient or drugs that inhibit these enzymes (pain reliever, stress, and depression drugs) are used. In this chapter, biosynthesis of biogenic amines, their toxic effects as well as their physiological functions, and their effect on health will be described.
Many possible factors influence the accumulation of biogenic amines in wines, correlated both to agronomical practices in the vineyard and during the winemaking process. In the literature, it is reported that the quantities of biogenic amines found in many wines are not alarming, especially with regard to those of toxicological interest (histamine and tyramine). For subjects in specific physiological conditions (histamine intolerance, taking class of drugs that inhibit monoamine oxidase enzymes), the risk of creating toxic reactions is related to the composition of the whole meal, not only the consumption of wine. It would be desirable to establish a regulatory system, as already existing for sulphites, allowing to read a label with the claim specifying their absence (e.g., histamine free) in order to enhance the quality of wines that would be a priori forbidden.
Biogenic amines are low-molecular-mass substances, essential for proper health for all organisms. These compounds could be detrimental to human health with various toxicological effects when they are present in high concentrations. Therefore, biogenic amines monitoring in food samples is a matter of utmost importance, and their accurate determination is considered indispensable. Under this context, we provide an overview over the most widely employed analytical techniques for biogenic amines determination such as chromatographic techniques and biosensors, emphasizing on new approaches. A critical comparison of the techniques is also given, presenting their advantages and drawbacks regarding important analytical characteristics such as sensitivity. Finally, we focus on foods in which biogenic amines mainly occur such as fish, meat and wine and other fermented products.
Histamine is a biogenic amine involved in important physiological activities in the organism, but its ingestion through food is associated with the onset of health disorders. Histamine intoxication, previously known as scombroid fish poisoning, is caused by the intake of foods with high levels of histamine. According to official European Union reports, more than 90% of the outbreaks registered in the last years were caused by the consumption of fish and seafood products. Histamine intolerance, on the other hand, arises when histamine degradation is impaired, mainly by a lower diamine oxidase (DAO) activity. Some of the uncertainties classically associated with histamine intoxication may be explained by this enzymatic deficit in a sensitive population. This chapter reviews the adverse effects of histamine from food within a risk analysis framework, focusing specifically on the components of risk assessment and management.
are applied, the detoxification process is disturbed and BAs accumulate in the body.Knowing the concentration of BAs is essential because they can affect human health, and also because they can be used as freshness indicators to estimate the degree of food spoilage.
Biogenic amines are low molecular weight organic nitrogen compounds. They are formed by the decarboxylation of amino acids or by amination and transamination of aldehydes and ketones during normal metabolic processes in living cells and therefore are ubiquitous in animals, plants, microorganisms, and humans. In food and beverages, they are formed by the enzymes of raw materials or are generated by microbial decarboxylation of amino acids. The structure of a biogenic amine can be aromatic and heterocyclic amines (histamine, tryptamine, tyramine, phenylethylamine, and serotonin); aliphatic di-, tri-, and polyamines (putrescine, cadaverine, spermine, spermidine, and agmatine); and aliphatic volatile amines (ethylamine, methylamine, isopentylamine, and ethanolamine). Many of them possess a strong pharmacologic effect, and others are important as precursors of hormones and components of coenzymes. The biogenic amine intoxication leads to toxicological risks and health hazards that trigger psychoactive, vasoactive, and hypertensive effects resulting from consumption of high amounts of biogenic amines in foods. The toxicological effects of biogenic amines increase when the mono- and diaminoxidase enzymes are deficient or drugs that inhibit these enzymes (pain reliever, stress, and depression drugs) are used. In this chapter, biosynthesis of biogenic amines, their toxic effects as well as their physiological functions, and their effect on health will be described.
Methoctramine and its analogues are polymethylene tetramines that selectively bind to a variety of receptor sites. Although these compounds are widely used as pharmacological tools for receptor characterization, the toxicological properties of these polyamine-based structures are largely unknown. We have evaluated the cytotoxic effects of methoctramine and related symmetrical analogues differing in polymethylene chain length between the inner nitrogens against a panel of cell lines. Methoctramine caused cell death only at high micromolar concentrations, whereas its pharmacological action is exerted at nanomolar level. Increasing the spacing between the inner nitrogen atoms resulted in a significative increase in cytotoxicity. In particular, an elevated cytotoxicity is associated to a methylene chain length of 12 units dividing the inner amine functions (compound 5). H9c2 cardiomyoblasts were the most sensitive cells, followed by SH-SY5Y neuroblastoma, whereas HL60 leukaemia cells were much more resistant. Methoctramine and related compounds down-regulated ornithine decarboxylase, the first enzyme of polyamine biosynthesis even at non-toxic concentration. Further, methoctramine and compound 5 caused a limited up-regulation of spermine/spermidine N-acetyltransferase, suggesting that interference in polyamine metabolism is not a primary mechanism of toxicity. Methoctramine and its analogues bound to DNA with a higher affinity than spermine, but the correlation with their toxic effect was poor. The highly toxic compound 5 killed the cells in the absence of caspase activation and caused an increase in p53 expression and ERK1/2 phosphorylation. Compound 5 was directly oxidized by cell homogenates producing hydrogen peroxide and its toxic effect was partially subdued by the inhibition of its uptake, by the NMDA ligand MK-801, and by the antioxidant N-acetylcysteine, suggesting that compound 5 can act at different cellular levels and lead to oxidative stress.
Objectives: ryptophan hydroxylase (TPH) is the first and rate-limiting enzyme in the biosynthesis of serotonin. In 2003, the brain-specific isozyme of TPH (TPH2) was discovered. We investigated the enzymatic properties of recombinant human TPH2 with maltose-binding protein (MBP). We also produced anti-TPH2 antibody, and examined the distribution of TPH2 in the brain by Western blot analysis. Methods: MBP-hTPH2 was expressed in E.coli, and purified by amylose resin and gel permeation chromatography. The activity of the purified MBP-hTPH2 was measured by HPLC-fluorescence detection. Antisera were raised against purified MBP-hTPH2. Results: We found that the MBP-hTPH2 showed maximum activity in the presence of 20 μM ferrous ion, and was strongly inhibited by the addition of ferric ion. MBP-hTPH2 activity was also inhibited by high concentrations of the substrate L-Trp, but not by its cofactor BH4. From the Western blot analysis, TPH2 was detected not only in the pons and medulla oblongata but also in a wide area of the mouse brain. Its molecular weight was estimated to be 52 kDa, whereas the calculated molecular mass was 56 kDa. CONCLUSION: These data suggest that hTPH2 may be highly dependent on the concentration of ferrous ions in the cell and that the TPH2 protein in the brain may be easily degraded by proteolytic digestion.
The influence of medicinal plants on hypobaric hypoxia was assessed by behavioral, electroencephaloghaphic study and brain monoamines estimation. Holtzman strain rats were divided into 3 groups: Control, hypobaric hypoxia and Moringa oleifera (MO) treated hypobaric hypoxia. Rats exposed to hypobaric hypoxia 412.0mm Hg (18,000 ft) for 21 days showed loss of memory as evidenced by increase in latency period and decrease in number of correct choices in daily trials in radial maze learning task. Biochemical studies showed decrease in norepinephrine (NE) level in cerebral cortex (CC), cerebellum (CB), midbrain (MB) and increase in caudate nucleus (CN). Dopamine (DA) level was decreased in CC and CN but increased in CB and MB, while serotonin (5-HT) level was decreased in CC but increased in CB, MB, and CN. The EEG studies showed persistent, high voltage fast wave discharges with a few β waves. Pretreatment with MO leaf extract (250 mg/kg), hypobaric hypoxic group showed an increase in correct choices and decrease in latency period. The EEG studies showed abolition of high voltage fast wave discharges and increase in β and a waves. NE level was significantly increased in CB and MB and decreased in CN whereas 5-HT level was decreased in CB and MB while increased in CN. The results suggest that MO improves maze-learning task possibly by specific brain monoamines on exposure to hypobaric hypoxia simulating at high altitude.
From Volume 20 (2006), this title is published by Society of Integrated Sciences (International Medart, PO Box 37, 814 99 Bratislava 1, Slovak Republic, E-mail: publisher@nel.edu, Fax: +41 13553207).
From Volume 20 (2006), this title is published by Society of Integrated Sciences (International Medart, PO Box 37, 814 99 Bratislava 1, Slovak Republic, E-mail: publisher@nel.edu, Fax: +41 13553207).
The effect of a lack of the gene encoding monoamine oxidase A (MAO A) in transgenic Tg8 mice on the levels of norepinephrine (NE), dopamine (DA) and 3,4-dihydroxyphenylacetic acid (DOPAC) in the midbrain, hypothalamus, hippocampus, striatum, amygdala, and frontal cortex was studied. It was shown that mice with a genetic MAO A knockout differed from those of the initial C3H/HeJ strain by a higher level of NE in all brain regions but the frontal cortex. The increased dopamine level in the striatum, a lower level of its metabolite DOPAC and decreased DOPAC/DA ratio in the midbrain, hypothalamus, hippocampus, and striatum of Tg8 mice was found. There were no changes in the DOPAC level or in the DOPAC/DA ratio in the frontal cortex and amygdala.The substantial (2.4 to 4.8-fold) decrease in the level of DOPAC in the midbrain, hypothalamus, hippocampus, and striatum shows significant impairment of dopamine oxidative deamination in MAO A-knockout mice. At the same time, the lack of any changes in the dopamine level in most of brain regions studied indicates rather effective compensation of the deficit in DA metabolism in Tg8 mice and explains the lack of severe behavioral and pathological consequences in MAO A genetic deficiency. The data show that DA and NE metabolism in brain regions is differently affected by the MAO A deficiency, and that catecholamines in the mouse frontal cortex are unaffected by the lack of MAO A. The results suggest that in different brain regions the relative roles of MAO A, MAO B and COMT in metabolism of catecholamines are different.
From Volume 20 (2006), this title is published by Society of Integrated Sciences (International Medart, PO Box 37, 814 99 Bratislava 1, Slovak Republic, E-mail: publisher@nel.edu, Fax: +41 13553207).
From Volume 20 (2006), this title is published by Society of Integrated Sciences (International Medart, PO Box 37, 814 99 Bratislava 1, Slovak Republic, E-mail: publisher@nel.edu, Fax: +41 13553207).
