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  • 1
    Electronic Resource
    Electronic Resource
    Increased γ-Aminobutyric Acid Receptor Function in the Cerebral Cortex of Myoclonic Calves with an Hereditary Deficit in Glycine/Strychnine Receptors (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 55 (1990), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Inherited congenital myoclonus (ICM) of Poll Hereford cattle is a neurological disease in which there are severe alterations in spinal cord glycine-mediated neurotransmission. There is a specific and marked decrease, or defect, in glycine receptors and a significant increase in neuronal (synaptosomal) glycine uptake. Here we have examined the characteristics of the cerebral γ-aminobutyric acid (GABA) receptor complex, and demonstrate that the malfunction of the spinal cord inhibitory system is accompanied by a change in the major inhibitory system in the cerebral cortex. In synaptic membrane preparations from ICM calves, both high- and low-affinity binding sites for the GABA agonist [3H]muscimol were found (KD= 9.3 ± 1.5 and 227 ± 41 nM, respectively), whereas only the high-affinity site was detectable in controls (KD= 14.0 ± 3.1 nM). The density and affinity of benzodiazepine agonist binding sites labelled by [3H]diazepam were unchanged, but there was an increase in GABA-stimulated benzodiazepine binding. The affinity for t-[3H]butylbicyclo-o-benzoate, a ligand that binds to the GABA-activated chloride channel, was significantly increased in ICM brain membranes (KD= 148 ± 14 nM) compared with controls (KD= 245 ± 33 nM). Muscimol-stimulated 36Cl- uptake was 12% greater in microsacs prepared from ICM calf cerebral cortex, and the uptake was more sensitive to block by the GABA antagonist picrotoxin. The results show that the characteristics of the GABA receptor complex in ICM calf cortex differ from those in cortex from unaffected calves, a difference that is particularly apparent for the low-affinity, physiologically relevant GABA receptors. Study of the GABA receptor complex in ICM calves may provide a greater insight into the interactions of the various binding sites on the GABA-benzodiazepine receptor protein molecule.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1990.tb04153.x
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  • 2
    Electronic Resource
    Electronic Resource
    γ-Aminobutyric Acid Receptor Ionophore Complexes: Differential Effects of Deltamethrin, Dichlorodiphenyltrichloroethane, and Some Novel Insecticides in a Rat Brain Membrane Preparation (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: The binding of [35S]t-butylbicyclophosphorothionate ([35S]TBPS), a γ-aminobutyric acid (GABA)-activated chloride ionophore ligand; [3H]diazepam, a benzodiazepine agonist; and [3H]muscimol, a GABA receptor probe, were used to assess the effects at 100 μM of deltamethrin, dichlorodiphenyltrichloroethane (DDT), and three experimental insecticides—a DDT-pyrethroid hybrid, GH414 (cycloprothrin), and two DDT-analogues, GH266 and GH149 (EDO), on GABA receptor ionophore complexes in a rat brain membrane preparation. GH266 and GH149 were found to inhibit a greater percentage of [35S]TBPS binding than the same concentration of deltamethrin or DDT, although GH414 had little effect. GH266 and GH149 enhanced [3H]diazepam binding by nearly 200%, in contrast to the inhibitory effects of deltamethrin, DDT, and GH414. GH266 and GH149 also caused a dramatic enhancement of [3H]muscimol binding, 367 and 236% of control, respectively, whereas DDT and deltamethrin caused only a moderate enhancement. The effects of the insecticides on binding affinity and density were examined for each of the ligands. The results show a differential interaction of the insecticides on the various ligand binding sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1987.tb05571.x
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular Properties of 5-Hydroxytryptamine3 Receptor-Type Binding Sites Purified from NG1O8-15 Cells (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 59 (1992), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: 5-Hydroxytryptamine3 (5-HT3) receptor-type binding sites were solubilised from NG108-15 mouse neuro-blastoma X rat glioma hybrid cells using five different detergents (n-octyl-β-D-glucoside, Triton X-100, 3-[3-(cholamidopropyl)dimethylammonio]-1-propanesulphonate (CHAPS), sodium cholate, and deoxycholate) and the solubilisation efficiencies compared. The equilibrium binding, kinetic properties, and pharmacological profile of solubilised binding sites were similar to those of 5-HT3 receptor-type binding sites (5-HT3R) in membrane preparations determined using [3H]GR65630. The solubilised binding sites were purified using an affinity column constructed by coupling the high-affinity antagonist GR1 19566X to an Affi-Gel 15 resin. The affinity of purified 5-HT3R for [3H]GR65630 was reduced threefold compared to the crude soluble preparation, but the pharmacological profile was similar. The sedimentation coefficient of the purified protein (US, detergent: CHAPS) was determined by sucrose density gradient centrifugation. The apparent molecular mass of the detergent/binding site complex (370 kDa) was determined by size exclusion chromatography in the presence of n-dodecyl-β-D-maltoside. Gel electrophoresis of the purified protein revealed bands at apparent molecular masses of 36, 40, 50, and 76 kDa. Electron microscopy of the negatively stained purified protein showed the presence of round particles of 8–9 nm diameter with a 2-nm stained pit in the centre, closely resembling the doughnut shapes described for nicotinic acetylcholine receptors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1992.tb11000.x
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  • 4
    Electronic Resource
    Electronic Resource
    Cis – trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel (2005)
    [s.l.] : Nature Publishing Group
    Nature 438 (2005), S. 248-252 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] 5-Hydroxytryptamine type 3 (5-HT3) receptors are members of the Cys-loop receptor superfamily. Neurotransmitter binding in these proteins triggers the opening (gating) of an ion channel by means of an as-yet-uncharacterized conformational change. Here we show that a ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature04130
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  • 5
    Electronic Resource
    Electronic Resource
    Pharmacology of insect GABA receptors (1991)
    Springer
    Neurochemical research 16 (1991), S. 363-374 
    Details
    ISSN: 1573-6903
    Keywords: GABA receptor ; chloride channel ; insect ; physiology ; biochemistry ; molecular biology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A GABA-operated Cl− channel that is bicuculline-insensitive is abundant in the nervous tissue of cockroach, in housefly head preparations and thorax/abdomen preparations, and in similar preparations from several insect species. Bicuculline-insensitive GABA-operated Cl− channels, which are rare in vertebrates, possess sites of action of benzodiazepines, steroids and insecticides that are pharmacologically-distinct from corresponding sites on vertebrate GABAA receptors. The pharmacological profile of the benzodiazepine-binding site linked to an insect CNS GABA-operated Cl− channel resembles more closely that of vertebrate peripheral benzodiazepine-binding sites. Six pregnane steroids and certain polychlorocycloalkane insecticides, which are active att-butylbicy-clophosphorothionate (TBPS)-binding sites, also differ in their effectiveness on vertebrate and insect GABA receptors. Radioligand binding and physiological studies indicate that in insects there may be subtypes of the GABA receptor. Molecular biology offers experimental approaches to understanding the basis of this diversity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00966100
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  • 6
    Electronic Resource
    Electronic Resource
    [N-Methyl-3H]Scopolamine binding sites in the central nervous system of the cockroach Periplaneta americana (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 339-347 
    Details
    ISSN: 0739-4462
    Keywords: Muscarinic acetylcholine receptors ; cockroach CNS ; [N-methyl-3H]scopolamine ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The binding of [N-methyl-3H]scopolamine to a cockroach nerve cord preparation has been investigated. Specific [N-methyl-3H]scopolamine binding was found to be saturable and of high affinity (Kd = 13.9 nM). Muscarinic ligands were found to displace [N-methyl-3H]scopolamine binding more effectively than nicotinic ligands. The distribution of these [N-methyl-3H]scopolamine binding sites was examined in the metathoracic ganglion at the light microscope level by autoradiographical techniques. Specific binding was found to be localized to distinct regions of the neuropile. This pattern showed certain similarities to that seen when the ganglion was stained for acetylcholinesterase, suggesting a functional role for these insect muscarinic acetylcholine receptors.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940030403
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