Electrogenic uptake of gamma-aminobutyric acid by a cloned transporter expressed in Xenopus oocytes

GAT-1, a gamma-aminobutyric acid (GABA) transporter cloned from rat brain, was expressed in Xenopus oocytes. Voltage-clamp measurements showed concentration-dependent, inward currents in response to GABA (K0.5 4.7 microM). The transport current required extracellular sodium and chloride ions; the Hi...

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Bibliographic Details
Published in:The Journal of biological chemistry 1992-11, Vol.267 (31), p.22007-22009
Main Authors: KAVANAUGH, M. P, ARRIZA, J. L, NORTH, R. A, AMARA, S. G
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Biological Transport, Active
Carrier Proteins - metabolism
Cell physiology
Chlorides - physiology
Cloning, Molecular
Fundamental and applied biological sciences. Psychology
GABA Plasma Membrane Transport Proteins
gamma-Aminobutyric Acid - metabolism
In Vitro Techniques
Membrane and intracellular transports
Membrane Potentials
Membrane Proteins
Membrane Transport Proteins
Molecular and cellular biology
Oocytes
Organic Anion Transporters
Sodium - physiology
Xenopus laevis
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Summary:GAT-1, a gamma-aminobutyric acid (GABA) transporter cloned from rat brain, was expressed in Xenopus oocytes. Voltage-clamp measurements showed concentration-dependent, inward currents in response to GABA (K0.5 4.7 microM). The transport current required extracellular sodium and chloride ions; the Hill coefficient for chloride was 0.7, and that for sodium was 1.7. Correlation of current and [3H]GABA uptake measurements indicate that flux of one positive charge occurs per molecule of GABA transported. Membrane hyperpolarization from -40 to -100 mV increased the transport current approximately 3-fold. The results indicate that the transport of one molecule of GABA involves the co-transport of two sodium ions and one chloride ion.
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(18)41626-2