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  • 1975-1979  (15)
  • 1970-1974  (14)
  • 1
    Electronic Resource
    Electronic Resource
    THE SUBCELLULAR LOCALIZATION OF HISTIDINE DECARBOXYLASE IN VARIOUS REGIONS OF RAT BRAIN (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 21 (1973), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1111/j.1471-4159.1973.tb07583.x
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  • 2
    Electronic Resource
    Electronic Resource
    HISTAMINE SYNTHESIZING AFFERENTS TO THE HIPPOCAMPAL REGION (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 26 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —Histidine decarboxylase activity is found in all parts of the hippocampal formation (subiculum, CA1, CA3 and area dentata), and a major portion of the enzyme is localized in a subcellular fraction containing the nerve terminal particles. The almost complete disppearance of HD (and histamine) after deafferentation of the hippocampal formation suggests that histamine synthesis in this region resides in terminals of extrinsic fibres. The results after selective lesions indicate that these alleged histaminergic fibres enter the hippocampus, like the monaminergic fibres, through a dorsal route (comprising fimbria, fornix superior and cingulum) as well as through a ventral route (via the amygdaloid area). The former was tentatively estimated to represent about 60% of the total hippocampal supply of alleged histaminergic fibres.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb04474.x
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  • 3
    Electronic Resource
    Electronic Resource
    STUDIES ON S-ADENOSYLHOMOCYSTEINE INHIBITION OF HISTAMINE TRANSMETHYLATION IN BRAIN (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 20 (1973), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1111/j.1471-4159.1973.tb12099.x
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  • 4
    Electronic Resource
    Electronic Resource
    Histamine formation in rat brain during development (1971)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 18 (1971), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1971.tb03757.x
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  • 5
    Electronic Resource
    Electronic Resource
    [3H]GLYCOGEN HYDROLYSIS IN BRAIN SLICES: RESPONSES TO NEUROTRANSMITTERS AND MODULATION OF NORADRENALINE RECEPTORS (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 30 (1978), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Different agents have been investigated for their effects on [C3H]glycogen synthesized in mouse cortical slices. Of these noradrenaline, serotonin and histamine induced clear concentration-dependent glycogenolysis.[C3H]Glycogen hydrolysis induced by noradrenaline appears to be mediated by beta-adrenergic receptors because it is completely prevented by timolol, while phentolamine is ineffective. It seems to involve cyclic AMP because it is potentiated in the presence of isobutylmethylxanthine; in addition dibutyryl cyclic AMP (but not dibutyryl cyclic GMP) promotes glycogenolysis.Lower concentrations of noradrenaline were necessary for [C3H]glycogen hydrolysis (EC50= 0.5μM) than for stimulation of cyclic AMP accumulation (EC50= 8μM).After subchronic reserpine treatment the concentration-response curve to noradrenaline was significantly shifted to the left (EC50= 0.09 ± 0.02 μM as compared with 0.49 ± 0.08 μM in saline-pretreated mice) without modifications of either the basal [C3H]glycogen level, maximal glycogenolytic effect, or the dibutyryl cAMP-induced glycogenolytic response.In addition to noradrenaline, clear concentration-dependent [3H]glycogen hydrolysis was observed in the presence of histamine or serotonin. In contrast to the partial [3H]glycogen hydrolysis elicited by these biogenic amines, depolarization of the slices by 50 mM K+ provoked a nearly total [C3H)glycogen hydrolysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1978.tb10464.x
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  • 6
    Electronic Resource
    Electronic Resource
    HISTAMINE FORMATION IN RAT BRAIN IN VIVO: EFFECTS OF HISTIDINE LOADS (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 19 (1972), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1111/j.1471-4159.1972.tb01394.x
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  • 7
    Electronic Resource
    Electronic Resource
    PROPERTIES AND REGIONAL DISTRIBUTION OF HISTIDINE DECARBOXYLASE IN RAT BRAIN (1970)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 17 (1970), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1111/j.1471-4159.1970.tb03722.x
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  • 8
    Electronic Resource
    Electronic Resource
    RADIOIMMUNOASSAY OF METHIONINE-AND LEUCINE-ENKEPHALINS IN REGIONS OF RAT BRAIN AND COMPARISON WITH ENDORPHINS ESTIMATED BY A RADIORECEPTOR ASSAY (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 31 (1978), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Radioimmunoassays (RIAs) selective for methionine-enkephalin (Met-ENK) and leucineenkephalin (Leu-ENK) have been developed using competition towards binding of 10 pM 125I-enkephalins to antibodies raised in rabbits against ENKs coupled to ovalbumin with carbodiimide. The high sensitivity of the RIAs (IC50 0.57 nm and 0.55 nm for Met- and Leu-ENK, respectively) allowed estimation of the enkephalin content in extracts of all rat brain regions. Regional levels are compared with those determined on the same extracts by a radioreceptor assay (RRA) using competition towards binding of 5 nm [3H]Leu-ENK to rat striatal membranes. Optimal conditions for killing the animals and extracting the endorphins have been carefully investigated: killing by rapid microwave irradiation was not found necessary as long as brain regions were homogenized into 0.1 n-HCl before deproteinization.Marked differences both in total endorphins (RRA) and ENKs (RIA) between regions are observed with similar ranking of the various regions: highest levels are found in striatum and hypothalamus and lowest in cerebellum and hippocampus. In each region the total ENK levels (RIA) represent only 2–13% of the total endorphins (RRA) suggesting the presence of large amounts of endorphins other than the ENKs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1978.tb12429.x
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  • 9
    Electronic Resource
    Electronic Resource
    High-affinity enkephalin-degrading peptidase in brain is increased after morphine (1978)
    [s.l.] : Nature Publishing Group
    Nature 276 (1978), S. 523-526 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Enkephalin-hydrolysing activity exhibits a considerable heterogeneity in rat brain subtractions8. Starting from the hypothesis that a specific peptidase involved in the control of enkephalin concentration in the synaptic cleft should be membrane-bound and should exhibit a high affinity for the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/276523a0
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  • 10
    Electronic Resource
    Electronic Resource
    Enkephalin receptors on dopaminergic neurones in rat striatum (1977)
    [s.l.] : Nature Publishing Group
    Nature 268 (1977), S. 745-747 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] 3H-Leu-enkephalin binds to a particulate fraction from rat striatum and the saturation kinetics at equilibrium evidence two distinct sites; the first one, exhibiting a high affinity (K& around 3 nM) and recognised by morphine or naloxone, has been identified as the 'opiate receptor' whereas the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/268745a0
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