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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Cardiovascular drug reviews 18 (2000), S. 0 
    ISSN: 1527-3466
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 53 (1989), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Serum albumin conjugates of histamine or tele-methylhistamine, a major catabolite, were prepared using 1,4-benzoquinone as the coupling agent and used to raise polyclonal antibodies in rabbits. The same reagent was used to prepare the [125I]iodinated tracer and treat tissue extracts submitted to the radioimmunoassays. The IC50 values of prederivatized histamine and tele-methylhistamine in the radioimmunoassays were 0.3 nM and 0.5 nM, respectively, whereas nonderivatized histamine or tele-methylhistamine, histidine, a variety of histamine derivatives, amines, etc., had at least 1,000-fold higher IC50 values. Application of the radioimmunoassays to nonpurified extracts of rat brain allowed the quantification of the two amine immunoreactivities in samples corresponding to less than 1 mg of hypothalamus. The tissue immunoreactivity corresponded to authentic histamine or tele-methylhistamine, as shown by (a) the parallel 125I-tracer displacement curves, (b) the similar elution patterns from HPLC columns, (c) the regional levels of histamine and tele-methylhistamine in brain, similar to those obtained with other methods, and (d) the clearcut effects of treatments with inhibitors of l-histidine decarboxylase or monoamine oxidase. The two radioimmunoassays appear as simple and sensitive tools to evaluate steady-state levels and turnover rates of histamine and tele-methylhistamine
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford UK : Blackwell Science Ltd
    Journal of neurochemistry 74 (2000), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Changes in various histamine (HA) H3 receptor-mediated responses and H3 receptor binding in brain were investigated in mice receiving single or repeated administration of ciproxifan, a potent brain-penetrating and selective H3 receptor antagonist. Blockade of the H3 autoreceptor was nearly as effective in enhancing levels of tele-methylhistamine (t-MeHA), a major HA metabolite, in brain areas when ciproxifan was administered once either at 7 a.m. or 8 p.m., in spite of the large differences of basal levels at these two phases of the circadian cycle. Blockade after a single ciproxifan administration was, however, followed by a transient decrease in striatal t-MeHA levels, possibly reflecting rapid development of autoreceptor hypersensitivity. Following a 5-day administration of ciproxifan and a 2-day drug-free period, basal t-MeHA levels were significantly decreased (approximately -20%) in three brain areas, and the ED50 values of the drug to enhance t-MeHA levels were increased by 5-15 times without significant change in maximal response, indicating that H3 autoreceptor hypersensitivity had developed. However, in synaptosomes from the cerebral cortex of these animals, the H3 receptor-mediated inhibition of K+-induced [3H]HA release was not significantly modified. Subchronic administration of ciproxifan for 10 days also resulted in an increased binding of [125I]iodoproxyfan to the H3 receptor of striatal and hypothalamic membranes by 40-54%. Hypersensitivity at H3 somatodendritic autoreceptors and at heteroreceptors attributable to an increased number of HA binding sites could account for the various changes observed in this study.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 21 (1973), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The subcellular distribution of histidine decarboxylase (assayed by two different isotopic methods) and several biochemical markers (lactate dehydrogenase, DOPA decarboxylase and protein) was determined in rat cerebral cortex. After differential centrifugation, the enzyme activity was found mainly in the crude mitochondrial and soluble fractions. Further separation of the former on discontinuous sucrose gradients showed that the particulate histidine decarboxylase (HD) was found in the synaptosomal fraction. After osmotic shock, HD activity appeared in the supernatant fraction suggesting that a major portion of the enzyme is localized in the cytoplasm of cortical nerve endings. By analogy with other brain amines, this finding, together with the presence of histamine in synaptic vesicles (Kataoka and de Robertis, 1967), can be taken as further support for the hypothesis of a role as neurotransmitter for histamine.Various brain regions were homogenized under conditions leading to synaptosome formation. The distribution of HD between ‘particulate’ and soluble fractions differed from one region to the other, but did not give any clear-cut indication of regions rich in cell bodies or nerve terminals.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 20 (1973), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The mechanism of histamine methyltransferase (HMT) inhibition by S-adenosylhomocysteine (SAH) has been investigated on a partially purified enzyme from guinea-pig brain. The kinetic data indicated that this inhibition was competitive with respect to S-adenosylmethionine (SAMe) and noncompetitive with respect to histamine. The Kt, values (about 5 ± 10−6 M in both cases) indicated that SAH had a higher affinity than SAHe or histamine for the enzyme.In rats, after administration of a small dose of SAH, methylation of intracisternally injected [3H]histamine was not modified.However, treatment with l-DOPA or pyrogallol induced a decrease in [3H]histamine methylation, presumably due to a modification in the SAMe/SAH ratio in the brain. Hence, histamine methylation in brain could be regulated according to the value of this ratio and thus related to methylation of other biogenic amines.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 18 (1971), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 19 (1972), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Administration of l-histidine at the rate of 500 mg/kg induced an increase of nearly 50 per cent in the level of histamine in rat brain which lasted several hours. The augmentation of histamine level was not significant 3 h after lower doses or after d-histidine α-methyl DOPA and Ro 4-4602 neither affected the cerebral level of histamine nor its elevation induced by l-histidine. Brocresine, a known histidine decarboxylase inhibitor not only prevented the effect of histidine load but also induced a prompt fall in the amine level. These results confirm those from earlier experiments in vitro indicating that histamine synthesis in rat brain depends on a specific decarboxylase (EC 4, 1.1.22) which is not normally saturated by the endogenous level of its substrate.When histamine levels were enhanced by histidine treatment, histidine decarboxylase activity, as evaluated on hypothalamus homogenates, was significantly reduced; intracisternal administration of cycloheximide, an inhibitor of protein synthesis, had similar effects. On the other hand, enzyme activity was not altered by the addition of histamine to hypothalamus homogenates. These results are compatible with the existence of a regulation mechanism of histidine decarboxylase involving repression by its end-product.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 17 (1970), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —Properties of the histamine-forming enzyme in rat brain were studied, utilizing a sensitive fluorometric assay. The optimum pH was related to substrate concentration and found to be6·4 at 10−2m-histidine; the apparent Km was about 4·10−4m; enzyme activity was inhibited by α-hydrazino -histidine and brocresine but was not affected by α-methyl DOPA or benzene. These different data suggest that the 'specific’histidine decarboxylase (EC 4.1.1.22)—and not the aromatic l-aminoacid decarboxylase—is involved. Determination of enzyme activity and histamine level in different areas of the rat brain revealed important regional differences, the two values being roughly parallel.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 24 (1985), S. 5938-5943 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 28 (1972), S. 904-905 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Résumé On a mis en évidence chez le Rat une formation de méthylhistamine-3H par décarboxylation de lal-3-méthylhistidine-3H. Cette réaction se produit in vitro et in vivo dans des tissus riches en histidine décarboxylase et elle est prévenue par un inhibiteur de cette enzyme. Les implications biologiques de l'existence de cette nouvelle voie métabolique sont envisagées.
    Type of Medium: Electronic Resource
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