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 language | English |
|---|---|
| Pages (from-to) | 174-179 |
| Number of pages | 6 |
| Journal | Molecular Brain Research |
| Volume | 63 |
| Issue number | 1 |
| DOIs | |
| State | Published - 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