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  • 1
    Electronic Resource
    Electronic Resource
    Polyclonal Antibodies to the Glycine Receptor Antagonist Strychnine (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 52 (1989), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Polyclonal antibodies have been raised in rabbits against the glycine receptor antagonist strychnine, coupled through a 2-amino substituent to the antigenic protein keyhole limpet haemocyanin. Strychnine binding of the predominantly immunoglobulin G (IgG) class of antibodies was measured by incubation with [3H]strychnine, followed by adsorption of IgG onto Staphylococcus aureus cells and filtration through glass-fibre filters under vacuum. Only strychnine and structurally related alkaloids or derivatives were able to inhibit [3H]strychnine binding to the IgG. A significant rank correlation was found between the potencies of these compounds to inhibit [3H]strychnine binding to the antibodies and to the glycine receptor in mouse spinal cord membranes. In contrast, preincubation of strychnine antibodies with a variety of ligands at other neurotransmitter, drug, or hormone receptors in the CNS (at 10−4M) failed to inhibit binding significantly. The failure of glycine to inhibit strychnine antibody binding is consistent with previous suggestions that the recognition sites for this amino acid on the CNS receptor may be conformationally distinct from those for the antagonist alkaloid. Strychnine antibodies may now help in the identification and purification of possible endogenous ligands at this alkaloid binding site in the CNS.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1989.tb09197.x
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  • 2
    Electronic Resource
    Electronic Resource
    Uptake of γ-Aminobutyric Acid and Glycine by Synaptosomes from Postmortem Human 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: Synaptosomes prepared from frozen postmortem human brain accumulated the neurotransmitter γ-aminobutyric acid (GABA) and the conformationally restricted GABA analogue cis-3-aminocyclohexanecarboxylic acid (ACHC) by a sodium-dependent, temperature-sensitive, high-affinity transport process into an osmotically sensitive compartment. This transport process could be inhibited by GABA analogues (ACHC, 2,4-di-aminobutyric acid, nipecotic acid, arecaidine, guvacine) that have been shown in studies on other species to be relatively selective for neuronal rather than glial uptake systems, whereas the glial uptake inhibitor β-alanine was ineffective. Synaptosomes prepared from frozen postmortem human medulla and spinal cord, but not cerebral cortex, took up the neurotransmitter glycine by a sodium-dependent high-affinity transport process. The kinetic parameters for the high-affinity uptake of GABA, ACHC. and glycine were Km= 10 ± 3, 49 ± 19, and 35 ± 19 μM; and Vmax= 98 ± 15, 84 ± 25, and 5.5 ± 2.5 nmol/min/100 mg protein, respectively. These results demonstrate the feasibility of using human CNS preparations for studying GABA and glycine uptake, and suggest that such studies may be useful neurochemical markers for transmitter-specific presynaptic terminals in health and disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1986.tb04523.x
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  • 3
    Electronic Resource
    Electronic Resource
    The Synthesis and Activity of cis-and trans-2-(Aminomethyl) cyclopropanecarboxylic Acid as Conformationally Restricted Analogues of GABA (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 34 (1980), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The synthesis of cis-2-(aminomethyl) cyclopropanecarboxylic acid, a new analogue of GABA in a folded conformation, is described, as is also an improved preparation of trans-2-(aminomethyl) cyclopropanecarboxylic acid. When adminstered microelectrophoretically the trans isomer was more potent than GABA as a bicuculline-sensitive depressant of the firing of cat spinal neurons in vivo, whereas the cis-isomer was less potent than GABA and its effects appeared not to be sensitive to bicuculline methochloride. Trans-2-(aminomethyl) cyclopropanecarboxylic acid was a weak inhibitor of the sodium-dependent uptake of GABA by mini slices of rat cerebral cortex and a substrate for the GABA: 2-oxoglutarate aminotransferase activity in extracts of rat brain mitochondria. The cis isomer did not influence GABA uptake or aminotransferase activity and neither isomer reduced glutamate decar-boxylase activity in rat brain homogenates. Both cyclopropane isomers inhibited the sodium-independent binding of GABA to synaptic membranes from rat brain and their relative potencies together with those found for the stereochemically related unsaturated derivatives, cis-and trans-4-aminocrotonic acid, were broadly consistent with the activity observed for these compounds in vivo on cat spinal neurons. These studies reinforce the evidence that extended rather than folded conformations of GABA are active at most GABA recognition sites within the mammalian central nervous system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1980.tb11193.x
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  • 4
    Electronic Resource
    Electronic Resource
    ACTION OF THE NEUROTOXIN KAINIC ACID ON HIGH AFFINITY UPTAKE OF l-GLUTAMIC ACID IN RAT BRAIN SLICES (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: Kainic acid is a linear competitive inhibitor (Kis 250 μm) of the ‘high affinity’ uptake of l-glutamic acid into rat brain slices. Kainic acid inhibits the ‘high affinity’ uptake of l-glutamic, d-aspartic and l-aspartic acids to a similar extent. Kainic acid is not actively taken up into rat brain slices and is thus not a substrate for the ‘high affinity’ acidic amino acid transport system or any other transport system in rat brain slices. Kainic acid (300 μm) does not influence the steady-state release or potassium-stimulated release of preloaded d-aspartic acid from rat brain slices.Kainic acid binds to rat brain membranes in the absence of sodium ions in a manner indicating binding to a population of receptor sites for l-glutamic acid. Only quisqualic and l-glutamic acid inhibit kainic acid binding in a potent manner. The affinity of kainic acid for these receptor sites appears to be some 4 orders of magnitude higher than for the ‘high affinity’l-glutamic acid transport carrier.Dihydrokainic acid is approximately twice as potent as kainic acid as an inhibitor of ‘high affinity’l-glutamic acid uptake but is some 500 times less potent as an inhibitor of kainic acid binding and at least 1000 times less potent as a convulsant of immature rats on intraperitoneal injection. Dihydrokainic acid might be useful as a ‘control uptake inhibitor’ for the effects of kainic acid on ‘high affinity’l-glutamic acid uptake since it appears to have little action on excitatory receptors. N-Methyl-d-aspartic acid is a potent convulsant of immature rats, but does not inhibit kainic acid binding or ‘high affinity’l-glutamic acid uptake. N-Methyl-d-aspartic acid might be useful as a ‘control excitant’ that activates different excitatory receptors to kainic acid and does not influence ‘high affinity’l-glutamic acid uptake.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1979.tb04518.x
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  • 5
    Electronic Resource
    Electronic Resource
    d-ASPARTATE OXIDASE ACTIVITY IN EXTRACTS OF MAMMALIAN CENTRAL NERVOUS TISSUE (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 25 (1975), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— d-Aspartate oxidase activity has been measured in water extracts of acetone powders prepared from cat forebrain, cerebellum and spinal cord, rat brain, hog brain and sheep brain stem, and compared with that found in rabbit and cat kidney. The results suggest that the brain enzyme has very similar properties to the n-aspartate oxidase (d-aspartate: oxygen oxidorcductase (deaminating), EC 1.4.3.1) of kidney. Crude extracts (ammonium sulphate fractions of water extracts of acetone powders) displayed little activity without added FAD. FMN could not replace FAD. With oxygen as electron acceptor, the enzyme oxidized d-aspartate much more rapidly than d-glutamate, and displayed quite high activities with N-substituted derivatives of d-aspartate as substrates. Those amino acids susceptible to oxidation by d-amino acid oxidase were not oxidized by the d-aspartate oxidase. The regional distribution of the d-aspartate oxidase activity within the CNS differed from that of d-amino acid oxidase. As has been previously observed for kidney d-aspartate oxidase activity, dicarboxylic acids competitively inhibited this enzymic activity in brain extracts, while sodium benzoate and sodium barbitone, inhibitors of d-amino acid oxidase, were without effect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1975.tb06970.x
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  • 6
    Electronic Resource
    Electronic Resource
    HIGH AFFINITY UPTAKE OF l-GLUTAMINE IN RAT BRAIN SLICES (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 24 (1975), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —l-Glutamine is taken up into rat brain slices by a specific‘high affinity’uptake system (Km 52 μm) which is not influenced by high concentrations of l-glutamate and l-asparagine. The uptake system appears to be associated with cellular structures that do not survive homogenization under conditions which yield synaptosomes. The‘high affinity’uptake of glutamine is dependent on the external sodium ion concentration and can be inhibited by p-chloromercuriphenylsulphonate, amino-oxyacetic acid, ouabain, dibenamine and allylglycine. The effects of several inhibitors indicate that l-asparagine uptake is mediated by a system different from the‘high affinity’system mediating l-glutamine uptake.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1975.tb03650.x
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  • 7
    Electronic Resource
    Electronic Resource
    GABA UPTAKE IN RAT BRAIN SLICES: INHIBITION BY GABA ANALOGUES AND BY VARIOUS DRUGS (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— 2-Hydroxy-, 2-chloro-, 2- and Cmethyl-GABA are linear competitive inhibitors of GABA uptake in rat brain slices. These analogues are thus potential substrates for the GABA transport system and possible‘false transmitters'. 2-Hydroxy-GABA is the most potent inhibitor of GABA uptake yet described. No specific inhibitor of GABA uptake was revealed amongst the drugs tested.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1973.tb12131.x
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  • 8
    Electronic Resource
    Electronic Resource
    GLUTAMATE AND RELATED AMINO ACIDS IN CAT SPINAL ROOTS, DORSAL ROOT GANGLIA AND PERIPHERAL NERVES (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: Of the free amino acids found in extracts of cat spinal roots, dorsal root ganglia and peripheral nerves, only glutamate was present in disproportionately high concentrations in those parts of the dorsal roots between ganglia and spinal cord. This distribution suggests that the high dorsal root levels of glutamate may result from synthesis in dorsal root ganglia and subsequent transport towards the spinal cord. Four excitant amino acids were detected in the extracts: aspartate, cysteate, cysteine sulphinate and glutamate. The unique regional distribution of glutamate is consistent with the proposed role of this amino acid as an excitatory transmitter at the terminals of primary afferent fibres.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1970.tb03369.x
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  • 9
    Electronic Resource
    Electronic Resource
    Uptake and Release of N-Methyl-d-Aspartate by Rat Brain Slices (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 36 (1981), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The excitant amino acid, N-methyl-d-aspartate, was actively taken up by slices of rat cerebral cortex. This uptake was Na+ - and temperature-dependent, but was relatively inefficient (Km 3 MM, Vmax 0.07 μmol/g/min) compared with that of other acidic amino acids. The uptake of N-methyl-d-aspartate does not appear to have a rate-limiting influence on the time course of N-methyl-d-aspartate-induced excitation since potent uptake inhibitors, such as threo-3-hydroxy-l-aspartate, do not influence the excitant action of N-methyl-d-aspartate. The relatively prolonged excitant action of this acidic amino acid may be the result of relatively slow dissociation of the activated receptor complex. Reloaded N-methyl-d-aspartate can be released from rat brain slices by stimulation with K+ ions. Such K+-stimulated release appeared to be Ca2+-independent, unlike the K+-stimulated release of preloaded d-aspartate. These findings suggest that N-methyl-d-aspartate may be a weak but selective substrate for a glial acidic amino acid uptake system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb01676.x
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  • 10
    Electronic Resource
    Electronic Resource
    Potentiation of L-Glutamate and L-Aspartate Excitation of Cat Spinal Neurones by the Stereoisomers of threo-3-Hydroxyaspartate (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 34 (1980), 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.1471-4159.1980.tb04650.x
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