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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Neurochemical research 22 (1997), S. 181-187 
    ISSN: 1573-6903
    Keywords: Glutamate ; [3H]glutamate-binding ; guanine nucleotides ; adenylate cyclase ; G-proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract GMP-PNP, a non-hydrolyzable analog of GTP binds tightly to G-protein in the presence of Mg2+, so that the binding is stable even after exhaustive washings. This property was exploited to prepare membrane samples of rat brain where G-protein GTP-binding sites were saturated with GMP-PNP. Experiments carried out with these membranes showed that GTP, GMP-PNP, GDP-S and GMP (1 mM) inhibit the sodium-independent [3H]glutamate binding by 30–40% [F(4,40) = 5.9; p 〈 .001], whereas only GMP-PNP activates adenylate cyclase activity [F(6,42) = 3.56; p 〈 .01]. The inhibition of sodium-independent [3H]glutamate binding occurred in the absence of Mg2+. These findings suggest that guanine nucleotides may inhibit glutamate binding and activate adenylate cyclase through distinct mechanisms by acting on different sites.
    Type of Medium: Electronic Resource
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