The displacement of [(3)H]GABA binding to GABA receptors of bovine brain cortical membranes by some sulfur-containing compounds (homothiotaurine, thiotaurine and carboxymethylcysteamine) was investigated and their potency was compared to that of other known sulfur-containing analogues of GABA, such as homotaurine, homohypotaurine and taurine. Displacement studies showed homotaurine to be more effective as a GABA displacer than homohypotaurine and homothiotaurine (IC(50): 3.9 x 10(?8), 6.7 x 10(?7) and 6.8 x 10(?7) M, respectively). Saturation experiments showed that the effect of taurine, homothiotaurine, homotaurine and homohypotaurine was due to a loss of high-affinity GABA sites (K(d) = 10.7 nM). Homotaurine seems also to interact with low-affinity sites, decreasing the affinity constant, whereas the number of binding sites remains unchanged.

Displacement of [3H]GABA binding to bovine brain receptors by sulfur containing analogues / Costa, Mara; Vesci, L; Fontana, Mario; Solinas, Sp; Dupre', Silvestro; Cavallini, Doriano. - In: NEUROCHEMISTRY INTERNATIONAL. - ISSN 0197-0186. - STAMPA. - 17(1990), pp. 547-551. [10.1016/0197-0186(90)90042-R]

Displacement of [3H]GABA binding to bovine brain receptors by sulfur containing analogues.

COSTA, Mara;FONTANA, Mario;DUPRE', Silvestro;CAVALLINI, Doriano
1990

Abstract

The displacement of [(3)H]GABA binding to GABA receptors of bovine brain cortical membranes by some sulfur-containing compounds (homothiotaurine, thiotaurine and carboxymethylcysteamine) was investigated and their potency was compared to that of other known sulfur-containing analogues of GABA, such as homotaurine, homohypotaurine and taurine. Displacement studies showed homotaurine to be more effective as a GABA displacer than homohypotaurine and homothiotaurine (IC(50): 3.9 x 10(?8), 6.7 x 10(?7) and 6.8 x 10(?7) M, respectively). Saturation experiments showed that the effect of taurine, homothiotaurine, homotaurine and homohypotaurine was due to a loss of high-affinity GABA sites (K(d) = 10.7 nM). Homotaurine seems also to interact with low-affinity sites, decreasing the affinity constant, whereas the number of binding sites remains unchanged.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11573/467888
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