Functional expression and CNS distribution of a beta-alanine-sensitive neuronal GABA transporter.

Clark JA, Deutch AY, Gallipoli PZ, Amara SG
Neuron. 1992 9 (2): 337-48

PMID: 1497897

The synaptic action of gamma-aminobutyric acid (GABA) is terminated by high affinity, Na(+)-dependent transport processes in both neurons and glia. We have isolated a novel GABA transporter cDNA, GAT-B, which encodes a high affinity (Km = 2.3 microM), Na(+)- and Cl(-)-dependent GABA transport protein that is potently blocked by beta-alanine, a compound generally considered a selective inhibitor of glial transport. However, in situ hybridization studies indicate that GAT-B mRNA is expressed predominantly within neurons. These data indicate that the neuronal-glial distinction of GABA transporters based on inhibitor sensitivities must be reconsidered and suggest a greater diversity of GABA transporters than has been predicted by previous pharmacologic studies.

MeSH Terms (25)

Amino Acid Sequence Animals Base Sequence beta-Alanine Brain Chemistry Carrier Proteins Chlorides DNA GABA Plasma Membrane Transport Proteins Gene Expression Humans Male Membrane Proteins Membrane Transport Proteins Molecular Sequence Data Nerve Tissue Proteins Neuroglia Neurons Nucleic Acid Hybridization Organic Anion Transporters Rats Rats, Inbred Strains RNA, Messenger Sodium Tissue Distribution

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