Histamine histidine decarboxylase

Orr, E. Quay, W. B. (1975). Hypothalamic 24-hour rhythms in histamine, histidine, decarboxylase and histamine-N-methyltransferase. Endocrinology 96, 941-5. 

The peak of histidine decarboxylase activity in foetal rat liver coincides. approximately with that of haemopoietic activity . Subsequently, the bone marrow of the adult rat was found to contain a specific histidine decarboxylase Table 4.4), thus supporting the possibility of a connection between haemopoiesis and the formation of histamine . Histidine decarboxylase also occurs in the bone marrow of the guinea-pig this enzyme activity, which was shown to be related to the number of basophils, does not, however, support a relationship between histidine decarboxylase activity and growth, since the basophils in the buffy layer of guinea-pig blood have also a considerable histamine-forming capacity, but contain no cells in mitosis . ... 

Synthesis. Histamine [51-45-6] 2-(4-imidazolyl)ethylarnine (1) is formed by decarboxylation of histidine by the enzyme L-histidine decarboxylase (Fig. 1). Most histamine is stored preformed in cytoplasmic granules of mast cells and basophils. In humans mast cells are found in the loose connective tissue of all organs, especially around blood and lymphatic vessels and nerves. These cells are most abundant in the organs expressing allergic diseases the skin, respiratory tract, and gastrointestinal tract. 

Histamine AND histamine antagonists). It is formed from histidine by the enzyme L-histidine decarboxylase. In the periphery, histamine is stored ia mast cells, basophils, cells of the gastric mucosa, and epidermal cells. In the CNS, histamine is released from nerve cells and acts as a neurotransmitter. The actions of histamine ate terrninated by methylation and subsequent oxidation via the enzymes histamine-/V-methyltransferase and monoamine oxidase. 

Histamine is synthesized from the amino acid histidine via the action of the specific enzyme histidine decarboxylase and can be metabolized by histamine-TV-methyl transferase or diamine oxidase. Interesting, in its role as a neurotransmitter the actions of histamine are terminated by metabolism rather than re-uptake into the pre-synaptic nerve terminals. 

Histamine is synthesised by decarboxylation of histidine, its amino-acid precursor, by the specific enzyme histidine decarboxylase, which like glutaminic acid decarboxylase requires pyridoxal phosphate as co-factor. Histidine is a poor substrate for the L-amino-acid decarboxylase responsible for DA and NA synthesis. The synthesis of histamine in the brain can be increased by the administration of histidine, so its decarboxylase is presumably not saturated normally, but it can be inhibited by a fluoromethylhistidine. No high-affinity neuronal uptake has been demonstrated for histamine although after initial metabolism by histamine A-methyl transferase to 3-methylhistamine, it is deaminated by intraneuronal MAOb to 3-methylimidazole acetic acid (Fig. 13.4). A Ca +-dependent KCl-induced release of histamine has been demonstrated by microdialysis in the rat hypothalamus (Russell et al. 1990) but its overflow in some areas, such as the striatum, is neither increased by KCl nor reduced by tetradotoxin and probably comes from mast cells. 

Figure 13.4 Histamine synthesis, metabolism and receptors. Current knowledge does not justify presentation of a schematic histaminergic synapse. (1) Histidine decarboxylase (2) histamine-A-methyltransferase (3) mono amine oxidase (MAOb)...

Takahashi H, B Kimura, M Yoshikawa, T Fuji (2003) Cloning and sequencing of the histidine decarboxylase genes of Gram-negative, histamine-producing bacteria and their application in detection and identification of these organisms in fish. Appl Environ Microbiol 69 2568-2579. 

Histamine is synthesized in the brain from L-histidine by the enzyme histidine decarboxylase (HDC) (Fig. 2.2C). HDC can be inhibited by application of a-fluoromethylhistidine (a-FMH). Unlike serotonin and the catecholamines, no... 

Histamine, or 2(4-imidazolylethylamine, was first identified in the CNS during the early years of the twentieth century. However, HA was first given the status of a neurotransmitter in the 1970s, after biochemical studies revealed the presence of the HA-synthesizing enzyme L-histidine decarboxylase (HDC)... 

Figure 6.1 Histamine synthesis and metabolism in neurons. L-histidine is transported into neurons by the L-amino acid transporter. Once inside the neuron, L-histidine is converted into histamine by the specific enzyme histidine decarboxylase. Subsequently, histamine is taken up into vesicles by the vesicular monoamine transporter and stored there until released. In the absence of a high-affinity uptake mechanism in the brain, released histamine is rapidly degraded by histamine methyltransferase, which is located postsynaptically and in glia, to telemethylhistamine, a metabolite that does not show any histamine-like activity.

Ohtsu, H. Watanabe, T. (2003). New functions of histamine found in histidine decarboxylase gene knockout mice. Biochem. Biophys. Res. Commun. 305, 443-7. 

Takeda, N., Inagaki, S., Taguchi, Y. et al. (1984). Origins of histamine-containing fibers in the cerebral cortex of rats studied by immunohistochemistry with histidine decarboxylase as a marker and transection. Brain Res. 323, 55-63. 

Specific enzymes control histamine synthesis and breakdown 253 Several forms of histidine decarboxylase may derive from a single gene 254... 

Histamine synthesis in the brain is controlled by the availability of L-histidine and the activity of histidine decarboxylase 254 Histamine is stored within and released from neurons but a neuronal transporter for histamine has not been found 254 In the vertebrate brain, histamine metabolism occurs predominately by methylation 254... 

Biosynthesis is performed in one step by the enzyme L-histidine decarboxylase (HDC, E.C. 4.1.1.22). Histamine metabolism occurs mainly by two pathways. Oxidation is carried out by diamine oxidase (DAO, E.C. 1.4.3.6), leading to imidazole acetic acid (IAA), whereas methyla-tion is effected by histamine N-methyltransferase (HMT, E.C. 2.1.1.8), producing fe/e-methylhistamine (t-MH). IAA can exist as a riboside or ribotide conjugate. t-MH is further metabolized by monoamine oxidase (MAO)-B, producing fe/e-methylimidazole acetic acid (t-MIAA). Note that histamine is a substrate for DAO but not for MAO. Aldehyde intermediates, formed by the oxidation of both histamine and t-MH, are thought to be quickly oxidized to acids under normal circumstances. In the vertebrate CNS, histamine is almost exclusively methylated... 

FIGURE 14-3 Synthesis and metabolism of histamine. Solid lines indicate the pathways for histamine formation and catabolism in brain. Dashed lines show additional pathways that can occur outside the nervous system. HDC, histidine decarboxylase HMT, histamine methyltransferase DAO, diamine oxidase MAO, monoamine oxidase. Aldehyde intermediates, shown in brackets, have been hypothesized but not isolated. 

Histamine synthesis in the brain is controlled by the availability of L-histidine and the activity of histidine decarboxylase. Although histamine is present in plasma, it does not penetrate the blood-brain barrier, such that histamine concentrations in the brain must be maintained by synthesis. With a value of 0.1 mmol/1 for L-histidine under physiological conditions, HDC is not saturated by histidine concentrations in the brain, an observation that explains the effectiveness of large systemic doses of this amino acid in raising the concentrations of histamine in the brain. The essential amino acid L-histidine is transported into the brain by a saturable, energy-dependent mechanism [5]. Subcellular fractionation studies show HDC to be localized in cytoplasmic fractions of isolated nerve terminals, i.e. synaptosomes. 

Parmentier, R., Ohtsu, H., Djebbara-Hannas, Z., Valatx, J. L., Watanabe, T. and Lin, J. S. Anatomical, physiological, and pharmacological characteristics of histidine decarboxylase knock-out mice evidence for the role of brain histamine in behavioral and sleep-wake control. /. Neurosci. 22 7695-7711,2002. 

Figure 3.5. Biosynthesis of histamine. Histamine is generated from histidine by the action of L-histidine decarboxylase.

Histamine (2-[4-imidazole] ethylamine) is a low-molecular-weight amine synthesized from L-histidine exclusively by histidine decarboxylase. It is produced by various cells throughout the body, including central nervous system neurons, gastric mucosa parietal cells, mast cells, basophils and lymphocytes [1-4]. Since its discovery as a uterine... 

Histamine is synthesized by decarboxylation of histidine by L-histidine decarboxylase (HDC), which is dependent on the cofactor pyridoxal-5 -phosphate [21]. Mast cells and basophils are the major source of granule-stored histamine, where it is closely associated with the anionic proteoglycans and chondroitin-4-sulfate. Histamine is released when these cells degranulate in response to various immunologic and non-immunologic stimuli. In addition, several myeloid and lymphoid cell types (DCs and T cells), which do not... 

Most people have heard of antihistamines, even if they have little concept of the nature of histamine. Histamine is the decarboxylation product from histidine, and is formed from the amino acid by the action of the enzyme histidine decarboxylase. The mechanism of this pyridoxal phosphate-dependent reaction will be studied in more detail later (see Section 15.7). 

An important example of PLP-dependent amino acid decarboxylation is the conversion of histidine into histamine. Histamine is often involved in human allergic responses, e.g. to insect bites or pollens. Stress stimulates the action of the enzyme histidine decarboxylase and histamine is released from mast cells. Topical antihistamine creams are valuable for pain relief, and oral antihistamines are widely prescribed for nasal allergies such as hay fever. Major effects of histamine include dilation of blood vessels, inflammation and swelling of tissues, and narrowing of airways. In serious cases, life-threatening anaphylactic shock may occur, caused by a dramatic fall in blood pressure. 

HISTAMINE N-METHYLTRANSFERASE HISTIDINE AMMONIA-LYASE DEHYDROALANINE HISTIDINE DECARBOXYLASE Histidine decarboxylase reduction, BOROHYDRIDE REDUCTION HISTIDINOL DEHYDROGENASE... 

The principal pathways for the biogenesis and metabolism of histamine are well known. Histamine is formed by decarboxylation of the amino acid, L-histidine, a reaction catalyzed by the enzyme, histidine decarboxylase. This decarboxylase is found in both mammalian and non-mammalian species. The mammalian enzyme requires pyridoxal phosphate as a cofactor. The bacterial enzyme has a different pH optimum and utilizes pyruvate as a cofactor (26.27). 

Amine build-up in fish muscle usually results from decarboxylation of amino acids in the muscle by enzymes of bacterial origin. This review will present information on the activity of bacterial decarboxylases and the formation of amines in fish. Mechanisms of decarboxylase action and production of bacterial decarboxylases in fish muscle are discussed. Emphasis is placed upon studies dealing with formation of histidine decarboxylase and histamine. Histamine, because of its involvement in Scombroid food poisoning, has been extensively studied with regard to its formation in fish and fishery products. 

Because amine formation in fish muscle and other foods usually results from bacterial growth with concomitant production of a bacterial decarboxylase, this paper will concentrate on the mechanisms of bacterial decarboxylation and factors influencing the production and activity of the enzymes. Also, because of the overall scope of the subject, the availability of excellent reviews on bacterial decarboxylation (2, 3) and the public health importance of histamine in fish and fishery products, this paper will primarily be limited to a discussion of histidine decarboxylase (EC 4.1.1.22) and the formation of histamine in fish muscle. 

Non-pyridoxal Phosphate Dependent. Figure 2 depicts the postulated mechanism for a non-pyridoxal phosphate catal) zed decarboxylation of histidine to histamine involving a pyruvoyl residue instead of pyridoxal -5 - phosphate (20). Histidine decarboxylases from Lactobacillus 30a and a Micrococcus sp. have been shown to contain a covalently bound pyruvoyl residue on the active site. The pyruvoyl group is covalently bound to the amino group of a phenylalanine residue on the enzyme, and is derived from a serine residue (21) of an inactive proenzyme (22). The pyruvoyl residue acts in a manner similar to pyridoxal phosphate in the decarboxylation reaction. 

Bacteria that Produce Histidine Decarboxylase. Early studies demonstrated that histidine decarboxylase is widely distributed in the genera Escherichia, Salmonella, Clostridium, Bacillus and Lactobacillus (24). Evidence for the enzyme in E, coli included the finding by Gale (7) that 14 of 155 cultures possessed histidine decarboxylase. A study by Hanke and Koessler (25) found that six of 20 coliform cultures synthesized the enzyme. Havelka (26) found that 71.4% of all Enterobacteriacae isolated from imported marine fish produced histamine. Eggerth (27) found 40 strains of bacteria of intestinal origin capable of decarboxylating histidine. Rodwell (11) found various... 

Relationship of Bacterial Histidine Decarboxylase Production to Histamine Formation. Many studies have been completed with the objective of understanding factors such as storage time and temperature that influence production of histamine in fish. The majority of the investigations have considered only the histamine content of the product, and, consequently, only limited information is available concerning the relationship of histidine decarboxylase formation by the microflora to histamine build-up. 

Edmunds and Eitenmiller (38) in a study of the effect of storage time and temperature on histamine content and histidine decarboxylase activity of several fresh water and marine species... 

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