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  • Glutamate neurotransmission  (1)
  • Glutamate receptors  (1)
  • Neurotransmission  (1)
  • Titanium  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Journal of Organometallic Chemistry 475 (1994), S. 127-137 
    ISSN: 0022-328X
    Keywords: Bis(trimethylsilyl)acetylene ; Bridging ligand ; Magnesium ; Titanium ; X-ray structure
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-6903
    Keywords: Glutamate receptors ; endogenous regulator ; reduced and oxidized glutathione
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A study was made of the effects of reduced (GSH) and oxidized (GSSG) glutathione on the Na+-independent and N-methyl-D-aspartate (NMDA) displaceable bindings of glutamate, on the binding of kainate, 2-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA), and ligands of the brain NMDA receptor-ionophore complex: glycine, dizocilpine (MK-801) and (±)-3-(2-car-boxypiperazin-4-yl)propyl-1-phosphonate (CPP). GSH and GSSG strongly inhibited the binding of glutamate, CPP and AMPA, kainate and glycine binding being less affected. Both peptides enhanced the binding of dizocilpine in a time- and concentration-dependent manner. This activatory effect was not additive to that of saturating concentrations of glutamate or glutamate plus glycine. The activation of dizocilpine binding by GSH and GSSG was prevented by the competitive NMDA and glycine antagonists DL-2-amino-5-phosphonovalerate and 7-chlorokynurenate. GSH and GSSG may be endogenous ligands of AMPA and NMDA receptors, binding preferably to the glutamate recognition site via their γ-glutamyl moieties. In addition to this, at millimolar concentrations they may regulate the redox state of the NMDA receptor-ionophore complex.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-6903
    Keywords: Neurotransmission ; excitatory amino acids ; receptors ; ligand binding ; glutamyl peptides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A number ofD-glutamyl andL-aspartyl dipeptides, glutathione, γ-D-glutamylglycine and γ-D-glutamyltaurine, were tested for their efficacy to displace ligands specific for different subtypes of excitatory amino acid receptors from rat brain synaptic membranes. In general, theL enanthiomorphs of γ-glutamyl peptides were more potent displacers than γ-D-glutamylglycine and-taurine but the latter were more specific for the quisqualate type of receptors. γ-L-glutamyl-L-glutamate was the most effective dipeptide in displacing the binding of glutamate, 2-amino-3-hydroxy-5-methylisoxazole-4-proprionate (AMPA) and 2-amino-5-phosphonoheptanoate (APH), whereas γ-L-glutamyl-L-aspartate was the most effective in the binding of kainate. Both oxidized and reduced glutathione were inhibitory, being most potent in the binding of AMPA. γ-L-Glutamylaminomethylsulphonate was most effective in the binding of APH. The most potent γ-L-glutamyl peptides (glutathione, γ-L-glutamyl-L-glutamate,-L-aspartate, and-glycine) may act as endogenous modulators of excitatory aminoacidergic neurotransmission.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-6903
    Keywords: Glutamate neurotransmission ; taurine peptides ; neuromodulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The in vitro effects of γ-L-glutamyltaurine on different stages of excitatory aminoacidergic neurotransmission were tested with γ-D-glutamyltaurine as reference. γ-L-Glutamyltaurine enhanced the K+-stimulated release of [3H]glutamate from cerebral cortical slices (25% at 0.1 mM) and slightly inhibited the uptake by crude brain synaptosomal preparations (about 10% at 1 mM). γ-L-Glutamyltaurine was also a weak displacer of glutamate and its agonists from their binding sites in brain synaptic membrane preparations, being, however, less selective to quisqualate (QA) sites than γ-D-glutamyltaurine. The basal influx of Ca2+ into cultured cerebellar granular cells was not affected by 1 mM γ-L-glutamyltaurine, but the glutamate- and its agonist-activated influx was significantly inhibited in low-Mg2+ (0.1 mM) and Mg2+-free media. The glutamate-evoked increase in free intracellular Ca2+ and the kainate-activated formation of cGMP in cerebellar slices were both markedly inhibited by 0.1 mM γ-L-giutamyltaurine. We propose that γ-L-glutamyltaurine may act as endogenous modulator in excitatory aminoacidergic neurotransmission.
    Type of Medium: Electronic Resource
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