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  • 1
    Electronic Resource
    Electronic Resource
    A Simple and Rapid Method for the Purification of Ovine Pineal Arylalkylamine N-Acetyltransferase (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 48 (1987), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: A two-step chromatographic procedure has been developed for the purification of ovine pineal arylalkylamine N-acetyltransferase (EC 2.3.1.87), based on the principles of disulfide exchange and anion exchange. The enzyme from 20 ovine pineal glands can be purified about 500-fold in a day; recovery is about 5%. Polyacrylamide gel electrophoretic analysis of the final preparation shows four major bands; one appears to be arylalkylamine N-acetyl-transferase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1987.tb04132.x
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  • 2
    Electronic Resource
    Electronic Resource
    Selective Adrenergic/Cyclic AMP-Dependent Switch-Off of Proteasomal Proteolysis Alone Switches on Neural Signal Transduction (2000)
    Oxford UK : Blackwell Science Ltd.
    Journal of neurochemistry 75 (2000), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The molecular processes underlying neural transmission are central issues in neurobiology. Here we describe a novel mechanism through which noradrenaline (NA) activates its target cells, using the mammalian pineal organ as a model. In this neuroendocrine transducer, NA stimulates arylalkylamine N-acetyltransferase (AANAT; EC 2.3.1.87), the key enzyme regulating the nocturnal melatonin production. In rodents, AANAT protein accumulates as a result of enhanced transcription, but in primates and ungulates, the AANAT mRNA level fluctuates only marginally, indicating that other mechanisms regulate AANAT protein and activity. These were investigated in cultured bovine pinealocytes. AANAT mRNA was readily detectable in unstimulated pinealocytes, and levels did not change following NA treatment. In contrast, NA increased AANAT protein levels in parallel with AANAT activity, apparently through a cyclic AMP-mediated mechanism. Immunocytochemistry revealed that the changes in AANAT protein levels occurred in virtually all pinealocytes. Inhibition of AANAT degradation by proteasomal proteolysis alone was found to switch-on enzyme activity by increasing AANAT protein levels five- to 10-fold. Accordingly, under unstimulated conditions AANAT protein is continually synthesized and immediately destroyed by proteasomal proteolysis. NA appears to act via cyclic AMP to protect AANAT from proteolytic destruction, resulting in accumulation of the protein. These findings show that tightly regulated control of proteasomal proteolysis of a specific protein alone can play a pivotal role in neural regulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2000.0752123.x
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  • 3
    Electronic Resource
    Electronic Resource
    PINEAL SEROTONIN N-ACETYLTRANSFERASE ACTIVITY: PROTECTION OF STIMULATED ACTIVITY BY ACETYL-CoA AND RELATED COMPOUNDS (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: —Rat pineal serotonin N—acetyltransferase activity increases 30–70-fold at night in the dark and then decreases rapidly when animals are exposed to light. Activity of the enzyme is also stimulated by l-norepinephrine in organ culture. When homogenates of glands stimulated by dark in vivo or NE in vitro are incubated at 37°C, enzyme activity will also rapidly decrease. This decrease can be prevented by one of the cosubstrates of the enzyme, acetyl–CoA. Protection can also be conferred by cysteamine (β-mercaptoethylamine, HS–CH2–CH2–NH2) which is the terminal portion of the CoA molecule. This protection mechanism could be involved in the physiological control of enzyme activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb04435.x
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  • 4
    Electronic Resource
    Electronic Resource
    POSTSYNAPTIC ADRENERGIC-CYCLIC AMP CONTROL OF THE SEROTONIN CONTENT OF CULTURED RAT PINEAL GLANDS (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— This investigation was designed to determine whether the amount of serotonin (5-HT) in cultured pineal glands can be altered by norepinephrine (NE). Treatment with l-NE (10−5-10−7m) for 4-6 h caused a gradual decrease in the concentration of 5-HT to a value that was less than 30% of that in the untreated control gland. This effect was observed using chronically denervated pineal glands. d-Norepinephrine (10−6-10−7m) and dopamine (10−4m) were ineffective in lowering 5-HT. The effect of l-NE was completely blocked by a β-adrenergic receptor blocker, propranolol and was only slightly decreased by α-adrenergic receptor blockers. These observations indicate that l-NE acts post-synaptically via a highly specific β-adrenergic mechanism. The effect of l-norepinephrine was mimicked by theophylline and N6, 2′0-dibutyryl adenosine 3′,5′-monophosphate, an indication that adenosine 3′,5′-monophosphate is involved in the effect of l-NE on 5-HT. Treatment with cycloheximide, which by itself caused a decrease in pineal 5-HT, also blocked any further decrease caused by treatment with l-NE, an indication that protein synthesis is necessary for maintenance of baseline levels of serotonin and for the effect of l-NE to be observed. The total amount of l-[3H]NE and degradation products of L-[3H]NE in the gland after 6 h of treatment with l-[3H]NE was less than 3 pmol. This amount of l-NE and degradation products of l-NE could not account for the decrease of 100-200 pmol of 5-HT on the basis of a mole for mole replacement of 5-HT by l-NE. These findings are consistent with the hypothesis that non-neuronal pineal 5-HT is physiologically regulated by the release of l-NE from the sympathetic nerve network.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1973.tb07580.x
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  • 5
    Electronic Resource
    Electronic Resource
    DEVELOPMENT OF A CIRCADIAN RHYTHM IN THE ACTIVITY OF PINEAL SEROTONIN N-ACETYLTRANSFERASE (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— Pineal serotonin N-acetyltransferase (EC 2.3.1.5) is a neurally regulated enzyme. It is detectable in the rat as early as 4 days prior to birth. A circadian rhythm in enzyme activity appears on the fourth day after birth. It develops most rapidly during the second week and achieves an adult magnitude by the end of the third week at which time nocturnal values are more than 30-fold greater than daytime values. Norepinephrine, which appears to be the neurotransmitter regulating this enzyme, can cause a 2- to 3-fold stimulation of N-acetyltransferase in organ cultures of pineal glands from 4-day-old animals and a 17-fold increase in the activity of glands from 15-day-old animals. Apparently the norepinephrinesensitive system controlling pineal N-acetyltransferase activity also develops most rapidly during the first few weeks of life. The circadian rhythm in the activity of serotonin N-acetyltransferase develops in the pineal glands of both male and female rats at the same rate. A similar rhythm for the enzyme was not observed in twelve other tissues of the rat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1972.tb01458.x
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  • 6
    Electronic Resource
    Electronic Resource
    A COMPARATIVE STUDY OF PINEAL ACETYL-CoA HYDROLASE AND N-ACETYLTRANSFERASE ACTIVITIES (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 32 (1979), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: pineal acetyl-CoA hydrolase is measurable at 4 days before birth. It increases rapidly to a maximum of 0.37 nmol/min/0.1 mg protein during the first week after birth, thereafter gradually decreasing and stabilizing at adult levels (0.27 nmol/min/0.1 mg protein) 3-4 weeks after birth. Unlike A/-acetyltransferase, the activity of acetyl-CoA hydrolase does not increase following treatment with isoproterenol, does not exhibit a circadian rhythm and is not inactivated on exposure of the animals to light at night. In addition, denervation of the pineal gland does not alter acetyl-CoA hydrolase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1979.tb04506.x
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  • 7
    Electronic Resource
    Electronic Resource
    RADIOMETRIC ASSAY OF TOTAL TRYPTOPHAN HYDROXYLATION BY INTACT CULTURED PINEAL GLANDS (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 23 (1974), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— A new method is described for the analysis of total tryptophan hydroxylation by intact tissue in culture. This method differs from classical measurements of tryptophan hydroxylase because it allows the detection of changes in tryptophan hydroxylation due to alterations in tryptophan transport, cofactor regeneration and protein synthesis. The rat pineal gland was studied. It was found to hydroxylate tryptophan linearly for a 48-h period. A direct proportional relationship between the concentration of tryptophan in the culture medium and the amount of tryptophan hydroxylated persists between 0.05 and 0.5 mm. As the medium concn of tryptophan is increased above 0.5 mm the amount of tryptophan hydroxylated decreases. Tryptophan hydroxylation is substantially inhibited by 1 mm p-chlorophenylalanine and 0.03 mm cycloheximide. No difference in the total amount of tryptophan hydroxylated was detected between male and female rat pineal glands, between chronically denervated and normal rat pineal glands, or between control glands and glands treated with 0.1-0.001 mm norepinephrine, 0.01 mm isoproterenol, or 0.01 mm mescaline.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1974.tb06923.x
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  • 8
    Electronic Resource
    Electronic Resource
    Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation (2003)
    [s.l.] : Nature Publishing Group
    Nature structural biology 10 (2003), S. 1054-1057 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Serotonin N-acetyltransferase (arylalkylamine N-acetyltransferase, AANAT) controls daily changes in the production and circulating levels of melatonin. Here, the significance of the phosphorylation of AANAT was studied using a semisynthetic enzyme in which a nonhydrolyzable phosphoserine/threonine ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsb1005
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  • 9
    Electronic Resource
    Electronic Resource
    Dark induced increase in pineal serotonin N-acetyltransferase activity: A refractory period (1973)
    Springer
    Cellular and molecular life sciences 29 (1973), S. 1339-1340 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Nachweis, dass Ratten, aus normaler Lichtperiode abrupt in Dunkelheit versetzt, keine Zunahme der NATase-Aktivität im Pinealorgan zeigen und dass Isoproterenol-Injektion die Zunahme der NATase auslöst.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01922804
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  • 10
    Electronic Resource
    Electronic Resource
    In vitro [35S]methionine-labeled protein synthesis in microdissected discrete brain areas: Marked regional differences revealed by two-dimensional gel electrophoresis (1984)
    Weinheim : Wiley-Blackwell
    Electrophoresis 5 (1984), S. 116-121 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A method is presented for the incorporation of [35S]methionine into proteins from freshly microdissected brain tissue samples. Rats were killed by decapitation, the brain was rapidly removed and sectioned without freezing using a vibratome. Hypothalamic nuclei and circumventricular organs of interest were removed by microdissection and incubated in a media containing [35S]methionine for six hours. Proteins within these tissue samples were then separated by two-dimensional polyacrylamide gel electrophoresis. The gels were stained with silver, photographed, dried and exposed to autoradiographic film. The results suggest that 1) this technique will prove useful in examining the uptake of radiolabeled amino acids into proteins from discrete nuclei and other brain areas, and 2) there is considerable regional heterogeneity in the uptake of [35S]methionine by proteins from the different brain regions examined in this study.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150050210
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