To study interaction of specific antibodies with the GABA receptor/channel, antisera were raised against the extracellular domains of the GABAA receptor/channel β2 subunit, γ2 subunit and the GABAC receptor/channel ρ1 subunit. The specificity of the antibodies was characterized by immunocytochemistry and by Western blotting of transfected FDC-P1 cells expressing recombinant GABA receptor/channel subunits. The effects of the antibodies on whole-cell currents in Xenopus laevis oocytes expressing homomeric recombinant GABA receptor/channel β2, γ2, and ρ1 were studied using two-microelectrode voltage clamp. In the absence of GABA, anti-α2, anti-γ2, and anti-ρ1 antisera elicited whole-cell currents in oocytes expressing β2, γ2, and ρ1 subunits, respectively. The effect of antibody on channel activation was concentration-dependent. The whole-cell currents induced by anti-β2 and anti-γ2 were several-fold greater than those induced by application of 100 μm GABA. In Xenopus oocytes expressing recombinant ρ1 subunits, GABA-induced whole-cell currents were inhibited by the anti-ρ1 antibody. In contrast, the GABA-induced whole-cell currents were potentiated several-fold by anti-β2 and anti-γ2 antibodies in Xenopus oocytes expressing homomeric β2 and γ2 subunits. Our studies indicate that antibodies specific to the N-terminal domain of GABA receptor/channel subunits can modulate the neurotransmitter receptor function.
The Journal of Membrane Biology – Springer Journals
Published: Oct 1, 2001
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