Molecular cloning and expression of the rat EAAT4 glutamate transporter subtype

  • Chien Liang Glenn Lin
  • , Anastassios V. Tzingounis
  • , Lin Jin
  • , Akiko Furuta
  • , Michael P. Kavanaugh
  • , Jeffrey D. Rothstein

Research output: Contribution to journalArticlepeer-review

54 Scopus citations

Abstract

Glutamate transport is a primary mechanism for the synaptic inactivation of glutamate. Excitatory amino acid transporter 4 (EAAT4) is a novel glutamate transporter with properties of a ligand-gated chloride channel that was recently cloned from human brain. Here we report the cloning of rat EAAT4 (rEAAT4) cDNA from rat cerebellum. The nucleotide sequence of rEAAT4 was 88% identical to the human sequence, and the predicted peptide was 89% identical to the human protein. The transport activity encoded by rEAAT4 has high affinity for L-glutamate. In Xenopus laevis oocytes expressing rEAAT4, L- glutamate and other transporter substrates elicited a current predominantly carried by chloride ions. Like human EAAT4, the rEAAT4 mRNA was largely restricted to cerebellar Purkinje cells; the rEAAT4 protein was localized to Purkinje cell somas and dendrites.

Original languageEnglish
Pages (from-to)174-179
Number of pages6
JournalMolecular Brain Research
Volume63
Issue number1
DOIs
StatePublished - Dec 10 1998

Funding

This study was supported by NIH NS 33958 (J.D.R.) and NS33270 (M.P.K.).

Funder number
NS 33958
R01NS033270

    Keywords

    • Cerebellum
    • Glutamate transporter
    • Ligand-gated chloride channel
    • Purkinje cell
    • cDNA

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