Abstract
Different combinations of cloned rat brain subunits of the GABA A receptor were expressed in Xenopus oocytes. The effect of the phorbol ester PMA, an activator of protein kinase C, on the expressed GABA-gated ion current was determined. Ion currents were diminished by β-PMA, but not by the control substance α-PMA, irrespective of the subunit combination studied. The mechanism of current decrease was investigated in more detail for the subunit combination α5β2γ2. The reversal potential of the current remained unaffected, while the maximal current amplitude was decreased and the apparent K a for GABA-dependent channel gating was shifted to higher concentrations.
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