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  • 1
    Electronic Resource
    Electronic Resource
    Characteristics of the β-Adrenoreceptor from Neuronal and Glial Cells in Primary Cultures of Rat Brain (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 47 (1986), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract The cellular characteristics of the β-adrenoreceptor in glial and neuronal cells from the newborn rat brain were determined by (−)-[125I]iodocyanopindolol binding. In membranes from both cell types, the binding was saturable and from competition assays the potency series of (−)-isoproterenol 〉 (−)-epinephrine = (−)-norepinephrine 〉 (+)-isoproterenol was observed. 5′-GuanylyI-imidodiphosphate reduced the affinity of (−)-isoproterenol for the β-adrenoreceptor from glial cells but had no effect on agonist affinity in neuronal cells. Chronic treatment of both cell types with (−)-isoproterenol reduced the receptor content and the capacity of the agonist to increase the cellular cyclic AMP content. However, the receptor recovery after chronic agonist treatment was faster in glial cells (72 h) than neuronal cells (120 h) and was blocked by cycloheximide. Treatment of both types with the irreversible β-blocker bromoacetylalprenololmentane (2 μM) reduced the receptor content by 78% but no receptor recovery was observed for 120 h after the initial receptor loss. The data indicated that the majority of β-adrenoreceptors in both cell types are the β−1 subtype, but show some differences in receptor-agonist interactions. Furthermore, these CNS cells may be useful models for regulatory studies on the β-adrenoreceptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1986.tb00757.x
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  • 2
    Electronic Resource
    Electronic Resource
    Irreversible Binding and Recovery of the Norepinephrine Uptake System Using an Alkylating Derivative of Norepinephrine (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 50 (1988), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The effects of bromoacetylaminomenthylnorepinephrine (BAAN) on the sodium-dependent, high-affinity norepinephrine (NE) uptake system in rat brain synaptosomes and CNS neuronal cultures were investigated. BAAN inhibited [3H]NE uptake into synaptosomes in a dose- and time-dependent manner (IC50. 6.5 μM). Pretreatment of cortical synaptosomes or neuronal cells with BAAN alone, followed by washing to remove free drug, reduced the Vmax but did not alter the Km value for [3H]NE uptake. The BAAN-induced reduction in Vmax was attenuated by concurrent pretreatment with desipramine and blocked by the reaction of BAAN with dithiothreitol or cysteine. In contrast, BAAN was 19-fold less potent at inhibiting [3H]dopamine uptake in striatal synaptosomes, and no change in the Vmas or Km value for [3H]dopamine uptake was observed after a pretreatment with BAAN followed by washing. Furthermore, the irreversible β-antagonist, bromoacetylalprenololmentane, was equipotent to BAAN for inhibiting [3H]NE uptake into cortical synapto somes, but did not alter the Vmax or Km for [3H]NE after pretreatment. In neuronal cultures, BAAN inhibited sodium-dependent uptake of [3H]NE (IC50, 5.6 μM) with no effect on sodium-independent uptake. After pretreatment of cultures with 30 μM BAAN followed by washing, there was a 74% decrease in the Vmax for [3H]NE uptake. Following a 24-h lag period, uptake recovered to the control level within 48 h; however, recovery was completely blocked by cycloheximide. The data indicate that BAAN irreversibly binds to the [3H]NE uptake system in both CNS synaptosomes and neuronal cultures and may be a useful probe for studying the turnover of the [3H]NE uptake system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1988.tb10571.x
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  • 3
    Electronic Resource
    Electronic Resource
    Histone methylation at gene promoters is associated with developmental regulation and region-specific expression of ionotropic and metabotropic glutamate receptors in human brain (2005)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 94 (2005), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Glutamatergic signaling is regulated, in part, through differential expression of NMDA and AMPA/KA channel subunits and G protein-coupled metabotropic receptors. In human brain, region-specific expression patterns of glutamate receptor genes are maintained over the course of decades, suggesting a role for molecular mechanisms involved in long-term regulation of transcription, including methylation of lysine residues at histone N-terminal tails. Using a native chromatin immunoprecipitation assay, we studied histone methylation marks at proximal promoters of 16 ionotropic and metabotropic glutamate receptor genes (GRIN1,2A–D; GRIA1,3,4; GRIK2,4,5; GRM1,3,4,6,7 ) in cerebellar cortex collected across a wide age range from midgestation to 90 years old. Levels of di- and trimethylated histone H3-lysine 4, which are associated with open chromatin and transcription, showed significant differences between promoters and a robust correlation with corresponding mRNA levels in immature and mature cerebellar cortex. In contrast, levels of trimethylated H3-lysine 27 and H4-lysine 20, two histone modifications defining silenced or condensed chromatin, did not correlate with transcription but were up-regulated overall in adult cerebellum. Furthermore, differential gene expression patterns in prefrontal and cerebellar cortex were reflected by similar differences in H3-lysine 4 methylation at promoters. Together, these findings suggest that histone lysine methylation at gene promoters is involved in developmental regulation and maintenance of region-specific expression patterns of ionotropic and metabotropic glutamate receptors. The association of a specific epigenetic mark, H3-(methyl)-lysine 4, with the molecular architecture of glutamatergic signaling in human brain has potential implications for schizophrenia and other disorders with altered glutamate receptor function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.2005.03190.x
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  • 4
    Electronic Resource
    Electronic Resource
    Carbostyril derivatives having potent .beta.-adrenergic agonist properties (1987)
    s.l. : American Chemical Society
    Journal of medicinal chemistry 30 (1987), S. 1563-1566 
    Details
    ISSN: 1520-4804
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jm00392a006
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  • 5
    Electronic Resource
    Electronic Resource
    Substituted 1,3-Dipropylxanthines as Irreversible Antagonists of A1 Adenosine Receptors (1994)
    s.l. : American Chemical Society
    Journal of medicinal chemistry 37 (1994), S. 2704-2712 
    Details
    ISSN: 1520-4804
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jm00043a010
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  • 6
    Electronic Resource
    Electronic Resource
    Carbostyril-based beta-adrenergic agonists: evidence for long lasting or apparent irreversible receptor binding and activation of adenylate cyclase activity in vitro (1989)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 339 (1989), S. 129-137 
    Details
    ISSN: 1432-1912
    Keywords: Rat reticulocytes ; Beta-adrenoreceptors ; Apparent irreversible ligand ; Carbostyril derivatives
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The interaction of the carbostyril derivatives 5-[2-[[1-(4-aminophenyl)-2-methyl-prop-2-yl]amino]-1-hydroxyethyl]-8-hydroxycarbostyril (carbo-amine) and 5-[2[[3-[4-(bromoacetamido)phenyl]-2-methylprop-2-yl]amino]1-hydroxyethyl]-8-hydroxycarbostryril (carbo-Br) with the rat reticulocyte beta-adrenoreceptor system has been partially characterized. In the absence of a guanine nucleotide, the concentration of carbo-amine, carbo-Br and (−)isoprenaline that inhibited (−)-[125I]iodocyanopindolol ([125I]CYP) binding by 50% (IC50) was 5.9 ± 0.2, 3.3 ± 0.3 and 49 ± 3 nM, respectively. In the presence of a guanine nucleotide, the (IC50) values were carbo-amine, 21 ± 0.6 nM; carbo-Br, 7.6 ± 0.3 nM and (−)isoprenaline, 813 ± 66 nM. Preincubation of membranes with either of the carbostyril congeners followed by washing reduced specific [125I]CYP binding capacity without changing the K D value for the remaining receptors. The beta-antagonist nadolol largely prevented the receptor reduction induced by the carbostyril compounds. Incubation of membranes for 18 It at 25°C resulted in an 11 % recovery of the carbo-amine-induced receptor loss and no recovery of the receptors lost by preincubation with carbo-Br. However, the carbo-amine induced receptor loss could be largely reversed (80%) by membrane heating at 45°C whereas little reversal (〈 10%) was observed with the carbo-Br pretreated membranes. The concentration of carbo-amine, carbo-Br and (−)isoprenaline that stimulated halt-maximal cAMP formation in reticulocyte membranes was 17.8 ± 3.1, 8.2 ± 2.1 and 241 ± 17 nM, respectively, and all 3 agonists produced the same maximal response. Initial cAMP formation stimulated by the carbostyril derivatives and (−)isoprenaline was blocked by concurrent addition of propranolol. However, the addition of propranolol after 7 min of incubation with either of the two carbostyril derivatives did not affect further cAMP production whereas with (−)isoprenaline further cAMP production was blocked. The data indicate that both carbostyril-derivatives are potent, full beta-adrenoreceptor agonists and the carbo-amine bound to the beta-adrenoreceptor in a tight, slowly dissociating manner whereas carbo-Br binding shows an apparent irreversible interaction with the receptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00165134
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