Abstract
A Cl−, HCO3−-ATPase isolated from the plasma membranes of fish brain was reconstituted in artificial proteoliposomes. The original sensitivity to GABAA-ergic ligands was preserved in the reconstituted enzyme. GABA was shown to activate the liposome-embedded enzyme in a concentration range from 10 to 100 μM while picrotoxin (100 μM) removed this activating affect. A Cl−-sensitive fluorescent probe (MEQ) was used to study the ATP-dependent Cl− transport through the membrane of the proteoliposomes. ATP (in concentrations of 1.5 mM and higher) was found to induce Cl−-transport into the proteoliposomes. This ATP-dependent transport was increased in the presence of GABA (100 μM), while the latter effect could also be blocked by picrotoxin (100 μM). It was concluded that the Cl−, HCO3−-ATPase could be involved in ATP-dependent Cl−-transport and regulated by activators and blockers of GABAA receptors.
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