Molecular cloning and expression of the rat EAAT4 glutamate transporter subtype

• Published in: Brain research. Molecular brain research. Vol. 63; no. 1; pp. 174 - 179
• Main Authors: Lin, Chien-Liang Glenn, Tzingounis, Anastassios V, Jin, Lin, Furuta, Akiko, Kavanaugh, Michael P, Rothstein, Jeffrey D
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 10.12.1998; Elsevier
• Subjects: Amino Acid Transport System X-AG; Animals; Biochemistry and metabolism; Biological and medical sciences; cDNA; Central nervous system; Cerebellum; Chloride Channels - genetics; Chloride Channels - metabolism; Chlorides - metabolism; Cloning, Molecular; DNA, Complementary; Electric Stimulation; Electrophysiology; Excitatory Amino Acid Transporter 4; Fundamental and applied biological sciences. Psychology; Gene Expression - physiology; Glutamate Plasma Membrane Transport Proteins; Glutamate transporter; Glutamic Acid - pharmacology; Ion Channel Gating - drug effects; Ligand-gated chloride channel; Ligands; Membrane Potentials - drug effects; Membrane Potentials - physiology; Molecular Sequence Data; Oocytes - physiology; Purkinje cell; Purkinje Cells - chemistry; Purkinje Cells - physiology; Rats; Receptors, Glutamate - genetics; Receptors, Glutamate - metabolism; Sequence Homology, Amino Acid; Symporters; Vertebrates: nervous system and sense organs; Xenopus laevis; Cerebellum; Purkinje cell; cDNA; Ligand-gated chloride channel; Glutamate transporter; Rat; Rodentia; Central nervous system; Purkinje neuron; Ionic channel; Gene expression; Glutamate; Vertebrata; Mammalia; Complementary DNA; Chlorides; Excitatory aminoacid; Neurotransmitter; Molecular cloning; Carrier protein; Aminoacid sequence; Brain (vertebrata)
• ISSN: 0169-328X; 1872-6941
• DOI: 10.1016/S0169-328X(98)00256-3

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.