Abstract
A Cl−, HCO −3 -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−, HCO −3 -ATPase could be involved in ATP-dependent Cl−-transport and regulated by activators and blockers of GABAA receptors.
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Abbreviations
- GABA:
-
γ-aminobutyric acid
- PMSF:
-
phenylmethylsulfonyl fluoride
- MEQ:
-
6-methoxy-N-ethylquinolinium iodide
- TCA:
-
trichloroacetic acid
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Original Russian Text © S.A. Menzikov, O.V. Menzikova, 2007, published in Neirokhimiya, 2006, Vol. 23, No. 2, pp. 106–111.
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Menzikov, S.A., Menzikova, O.V. Effects of GABAA-ergic ligands on Cl− transport induced by the Cl−, HCO −3 -ATPase from carp (Cyprinus carpio L.) brain reconstituted in proteoliposomes. Neurochem. J. 1, 31–36 (2007). https://doi.org/10.1134/S1819712407010047
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DOI: https://doi.org/10.1134/S1819712407010047